NUMBER	SwissProt ID (E3)	SwissProt ID (Substrate)	SwissProt AC (E3)	SwissProt AC (Substrate)	Gene Symbol (E3)	Gene Symbol (Substrate)	SOURCE	SOURCEID	SENTENCE	E3TYPE	COUNT	type	species
1	ADO1_ARATH	APRR1_ARATH	Q94BT6	Q9LKL2	ADO1	APRR1	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
2	AIP2_ARATH	AIP2_ARATH	Q8RXD3	Q8RXD3	AIP2	AIP2	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
3	AIP2_ARATH	ABI3_ARATH	Q8RXD3	Q01593	AIP2	ABI3	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
4	ATL55_ARATH	ATL55_ARATH	Q9LX93	Q9LX93	ATL55	ATL55	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
5	BPM3_ARATH	P2C77_ARATH	O22286	O04719	BPM3	ABI2	MEDLINE	31308219	The MATH-BTB <span class="match term0">BPM3</span> and BPM5 subunits of Cullin3-RING E3 ubiquitin ligases target PP2CA and other clade A PP2Cs for degradation.	Other	1	Other	A.thaliana
6	BPM3_ARATH	P2C56_ARATH	O22286	P49597	BPM3	ABI1	MEDLINE	31308219	The MATH-BTB <span class="match term0">BPM3</span> and BPM5 subunits of Cullin3-RING E3 ubiquitin ligases target PP2CA and other clade A PP2Cs for degradation.	Other	1	Other	A.thaliana
7	BPM3_ARATH	P2C16_ARATH	O22286	Q9CAJ0	BPM3	HAB1	MEDLINE	31308219	UbiNet 2.0	Other	1	Other	A.thaliana
8	BPM3_ARATH	P2C37_ARATH	O22286	P49598	BPM3	PP2CA	MEDLINE	31308219	UbiNet 2.0	Other	1	Other	A.thaliana
9	BPM5_ARATH	P2C56_ARATH	Q1EBV6	P49597	BPM5	ABI1	MEDLINE	31308219	The MATH-BTB BPM3 and <span class="match term0">BPM5</span> subunits of Cullin3-RING E3 ubiquitin ligases target PP2CA and other clade A PP2Cs for degradation.	Other	1	Other	A.thaliana
10	BPM5_ARATH	P2C16_ARATH	Q1EBV6	Q9CAJ0	BPM5	HAB1	MEDLINE	31308219	UbiNet 2.0	Other	1	Other	A.thaliana
11	BPM5_ARATH	P2C37_ARATH	Q1EBV6	P49598	BPM5	PP2CA	MEDLINE	31308219	UbiNet 2.0	Other	1	Other	A.thaliana
12	BPM5_ARATH	P2C77_ARATH	Q1EBV6	O04719	BPM5	ABI2	MEDLINE	31308219	The MATH-BTB BPM3 and <span class="match term0">BPM5</span> subunits of Cullin3-RING E3 ubiquitin ligases target PP2CA and other clade A PP2Cs for degradation.	Other	1	Other	A.thaliana
13	CHIP_ARATH	FTSH1_ARATH	Q9SRS9	Q39102	CHIP	FTSH1	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
14	CHIP_ARATH	CLPP4_ARATH	Q9SRS9	Q94B60	CHIP	CLPP4	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
15	CIP8_ARATH	HY5_ARATH	Q9SPL2	O24646	CIP8	HY5	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
16	COI1_ARATH	TI10A_ARATH	O04197	Q9LMA8	COI1	TIFY10A	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
17	COI1_ARATH	TIF6B_ARATH	O04197	Q9LVI4	COI1	TIFY6B	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
18	COP1_ARATH	MYB21_ARATH	P43254	Q9LK95	COP1	MYB21	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
19	COP1_ARATH	PHYA_ARATH	P43254	P14712	COP1	PHYA	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
20	COP1_ARATH	HFR1_ARATH	P43254	Q9FE22	COP1	HFR1	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
21	COP1_ARATH	CRY1_ARATH	P43254	Q43125	COP1	CRY1	MEDLINE	11752373	The signaling mechanism of Arabidopsis <span class="match term1">CRY1</span> involves direct interaction with <span class="match term0">COP1</span>.	Other	1	Other	A.thaliana
22	COP1_ARATH	PIF5_ARATH	P43254	Q84LH8	COP1	PIF5	MEDLINE	30144338	Furthermore, <span class="match term0">COP1</span> and SPA proteins stabilize <span class="match term1">PIF5</span> in the dark, but promote the ubiquitination and degradation of <span class="match term1">PIF5</span> in response to red light through the 26S proteasome pathway	Other	1	Other	A.thaliana
23	COP1_ARATH	GIGAN_ARATH	P43254	Q9SQI2	COP1	GI	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
24	COP1_ARATH	HY5_ARATH	P43254	O24646	COP1	HY5	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
25	COP1_ARATH	CONS_ARATH	P43254	Q39057	COP1	CO	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
26	COP1_ARATH	PIF1_ARATH	P43254	Q8GZM7	COP1	PIF1	MEDLINE	26037329	UbiNet 2.0	Other	1	Other	A.thaliana
27	COP1_ARATH	HYH_ARATH	P43254	Q8W191	COP1	HYH	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
28	COP1_ARATH	LAF1_ARATH	P43254	Q9M0K4	COP1	LAF1	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
29	O22809_ARATH	RGL2_ARATH	O22809	Q8GXW1	CRL1	RGL2	MEDLINE	29462139	We provide genetic evidence to demonstrate that the germination phenotype of csn1-10 is caused by over-accumulation of <span class="match term1">RGL2</span>, a substrate of the SCF (<span class="match term0">CRL1</span>) ubiquitin E3 ligase, while the csn5a-1 phenotype is caused by over-accumulation of RGL2 as well as ABI5	Other	1	Other	A.thaliana
30	DRIP1_ARATH	DRE2A_ARATH	Q9M9Y4	O82132	DRIP1	DREB2A	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
31	DRIP2_ARATH	DRE2A_ARATH	Q94AY3	O82132	DRIP2	DREB2A	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
32	DWA2_ARATH	ABI5_ARATH	Q6NPN9	Q9SJN0	DWA2	ABI5	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
33	EBF1_ARATH	CUL1_ARATH	Q9SKK0	Q94AH6	EBF1	CUL1	MEDLINE	29643073	The ubiquitin E3 ligase complex containing Skp1, Cullin1, and the F-box protein <span class="match term0">EBF1</span> or EBF2 (SCFEBF1/2) target the degradation of EIN3, the master transcription factor in ethylene signaling	Other	1	Other	A.thaliana
34	EBF2_ARATH#EBF1_ARATH	EIN3_ARATH	Q708Y0#Q9SKK0	O24606	EBF2#EBF1	EIN3	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
35	ETO1_ARATH	1A15_ARATH	O65020	Q37001	ETO1	ACS5	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
36	FBL17_ARATH	CDKA1_ARATH	Q8W104	P24100	FBL17	CDKA-1	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
37	GID2_ARATH	RGL2_ARATH	Q9STX3	Q8GXW1	GID2	RGL2	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
38	GID2_ARATH	RGA_ARATH	Q9STX3	Q9SLH3	GID2	RGA	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
39	GID2_ARATH	GAI_ARATH	Q9STX3	Q9LQT8	GID2	GAI	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
40	HOS1_ARATH	ICE1_ARATH	Q84JU6	Q9LSE2	HOS1	SCRM	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
41	BRE1A_ARATH	H2B6_ARATH	Q8RXD6	O23629	HUB1	H2B	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
42	BRE1B_ARATH	H2B6_ARATH	Q9C895	O23629	HUB2	H2B	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
43	KEG_ARATH	ABI5_ARATH	Q9FY48	Q9SJN0	KEG	ABI5	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
44	LOFG2_ARATH	P2C56_ARATH	Q9S752	P49597	LOG2	ABI1	MEDLINE	33077597	Both UBC27 and AIRP3 interact with <span class="match term1">ABI1</span> and affect the ubiquitination and degradation of <span class="match term1">ABI1</span>	RING	1	Other	A.thaliana
45	MIEL1_ARATH	MYB30_ARATH	Q8VZK0	Q9SCU7	MIEL1	MYB30	MEDLINE	30923370	Addendum: Arabidopsis ubiquitin ligase <span class="match term0">MIEL1</span> mediates degradation of the transcription factor <span class="match term1">MYB30</span> weakening plant defence.	RING	1	Other	A.thaliana
46	ORTH3_ARATH	DNMT1_ARATH	Q9FVS2	P34881	ORTH3	DMT1	MEDLINE	32769133	We demonstrate that VIM5 is a ubiquitin E3 ligase and directly targets DNA methyltransferases MET1 and CMT3 for degradation by the ubiquitin 26S proteasome proteolytic pathway	RING	1	Other	A.thaliana
47	ORTH3_ARATH	CMT3_ARATH	Q9FVS2	Q94F88	ORTH3	CMT3	MEDLINE	32769133	We demonstrate that VIM5 is a ubiquitin E3 ligase and directly targets DNA methyltransferases MET1 and <span class="match term1">CMT3</span> for degradation by the ubiquitin 26S proteasome proteolytic pathway	RING	1	Other	A.thaliana
48	PEX12_ARATH	PEX5_ARATH	Q9M841	Q9FMA3	PEX12	PEX5	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
49	PRL1_ARATH	KIN10_ARATH	Q42384	Q38997	PRL1	KIN10	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
50	PUB13_ARATH	FLS2_ARATH	Q9SNC6	Q9FL28	PUB13	FLS2	MEDLINE	29868071	The Arabidopsis <span class="match term0">PUB13</span> has been shown to attenuate the pattern recognition receptor <span class="match term1">FLS2</span>-mediated immune signaling by ubiquitinating <span class="match term1">FLS2</span> and consequently promoting its degradation by the 26S proteasome	Other	1	Other	A.thaliana
51	PUB22_ARATH	PSD8A_ARATH	Q9SVC6	Q9SGW3	PUB22	RPN12A	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
52	PUB23_ARATH	PSD8A_ARATH	Q84TG3	Q9SGW3	PUB23	RPN12A	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
53	PUB25_ARATH	MYB15_ARATH	Q9LT79	Q9LTC4	PUB25	MYB15	MEDLINE	31543444	Both <span class="match term0">PUB25</span> and PUB26 poly-ubiquitinate <span class="match term1">MYB15</span>, a transcriptional repressor of the CBF-dependent cold signaling pathway, leading to <span class="match term1">MYB15</span> degradation and thus enhanced CBF expression under cold stress	Other	1	Other	A.thaliana
54	RGLG1_ARATH	M3K18_ARATH	Q9SS90	Q9ZVP5	RGLG1	MAPKKK18	MEDLINE	32970364	Ubiquitin ligases <span class="match term0">RGLG1</span> and RGLG2 ubiquitinated <span class="match term1">MAPKKK18</span> at lysine residue K32 and K154, and promoted its degradation	RING	1	Other	A.thaliana
55	RGLG2_ARATH	M3K18_ARATH	Q9LY87	Q9ZVP5	RGLG2	MAPKKK18	MEDLINE	32970364	Ubiquitin ligases RGLG1 and <span class="match term0">RGLG2</span> ubiquitinated <span class="match term1">MAPKKK18</span> at lysine residue K32 and K154, and promoted its degradation	RING	1	Other	A.thaliana
56	RHA2B_ARATH	MYB30_ARATH	Q9ZU51	Q9SCU7	RHA2B	MYB30	MEDLINE	30030326	The Ubiquitin E3 Ligase <span class="match term0">RHA2b</span> Promotes Degradation of <span class="match term1">MYB30</span> in Abscisic Acid Signaling	RING	1	Other	A.thaliana
57	RKP_ARATH	KRP1_ARATH	Q9SIZ8	Q67Y93	RKP	KRP1	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
58	RKP_ARATH	KRP2_ARATH	Q9SIZ8	Q9SCR2	RKP	KRP2	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
59	RMA1_ARATH	PIP21_ARATH	O64425	P43286	RMA1	PIP2-1	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
60	RMA2_ARATH	ABP1_ARATH	P93030	P33487	RMA2	ERABP1	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
61	SAP5_ARATH	ENO2_ARATH	Q9LHJ8	P25696	SAP5	ENO2	MEDLINE	23952686	UbiNet 2.0	Other	1	Other	A.thaliana
62	SAP5_ARATH	DRIP1_ARATH	Q9LHJ8	Q9M9Y4	SAP5	DRIP1	MEDLINE	29089392	The E3 Ligase TaSAP5 Alters Drought Stress Responses by Promoting the Degradation of DRIP Proteins.	Other	1	Other	A.thaliana
63	SAP5_ARATH	DRIP2_ARATH	Q9LHJ8	Q94AY3	SAP5	DRIP2	MEDLINE	29089392	The E3 Ligase TaSAP5 Alters Drought Stress Responses by Promoting the Degradation of DRIP Proteins.	Other	1	Other	A.thaliana
64	SAP5_ARATH	HS905_ARATH	Q9LHJ8	Q9SIF2	SAP5	HSP90-5	MEDLINE	31481192	UbiNet 2.0	Other	1	Other	A.thaliana
65	SINA5_ARATH	NAC22_ARATH	Q8S3N1	Q84TE6	SINAT5	NAC021	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
66	-	IF4A1_ARATH	-	P41376	TaMAB2	EIF4A1	MEDLINE	31824527	UbiNet 2.0	Other	1	Other	A.thaliana
67	-	IF2C_ARATH	-	Q9SHI1	TaMAB2	At1g17220	MEDLINE	31824527	UbiNet 2.0	Other	1	Other	A.thaliana
68	-	F4J6A1_ARATH	-	F4J6A1	TaMAB2	EIF3G1	MEDLINE	31824527	UbiNet 2.0	Other	1	Other	A.thaliana
69	-	EIF3C_ARATH	-	O49160	TaMAB2	TIF3C1	MEDLINE	31824527	UbiNet 2.0	Other	1	Other	A.thaliana
70	-	EIF3A_ARATH	-	Q9LD55	TaMAB2	TIF3A1	MEDLINE	31824527	UbiNet 2.0	Other	1	Other	A.thaliana
71	-	RR9_ARATH	-	Q9XJ27	TaMAB2	RPS9	MEDLINE	31824527	UbiNet 2.0	Other	1	Other	A.thaliana
72	THOC6_ARATH	ABI5_ARATH	Q8L4M1	Q9SJN0	THO6	ABI5	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
73	TIR1_ARATH	IAA12_ARATH	Q570C0	Q38830	TIR1	IAA12	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
74	TIR1_ARATH	IAA3_ARATH	Q570C0	Q38822	TIR1	IAA3	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
75	TIR1_ARATH	IAA7_ARATH	Q570C0	Q38825	TIR1	IAA7	MEDLINE	22199232	E3Net	Other	1	Other	A.thaliana
76	UPL5_ARATH	WRK53_ARATH	Q9SU29	Q9SUP6	UPL5	WRKY53	MEDLINE	22199232	E3Net	HECT	1	Other	A.thaliana
77	XB32_ARATH	1A14_ARATH	Q6NLQ8	Q43309	XBAT32	ACS4	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
78	XB32_ARATH	1A17_ARATH	Q6NLQ8	Q9STR4	XBAT32	ACS7	MEDLINE	22199232	E3Net	RING	1	Other	A.thaliana
79	XB35_ARATH	ELF3_ARATH	Q4FE47	O82804	XBAT35	ELF3	MEDLINE	33963671	<span class="match term0">XBAT35</span> interacts with <span class="match term1">ELF3</span> and ubiquitinates <span class="match term1">ELF3</span>	RING	1	Other	A.thaliana
80	BACD1_BOVIN	RHOA_BOVIN	Q2T9W0	P61585	KCTD13	RHOA	MEDLINE	22199232	E3Net	BTB_OTHER	1	Other	B.taurus
81	KLH21_BOVIN	AURKB_BOVIN	Q08DS0	Q7YRC6	KLHL21	AURKB	MEDLINE	22199232	E3Net	BTB_3	1	Other	B.taurus
82	MARH5_BOVIN	FIS1_BOVIN	Q3ZC24	Q3T0I5	MARCHF5	FIS1	MEDLINE	22199232	E3Net	RING	1	Other	B.taurus
83	PAXI1_BOVIN	PCNA_BOVIN	A0JNA8	Q3ZBW4	PAXIP1	PCNA	MEDLINE	22199232	E3Net	Other	1	Other	B.taurus
84	RN220_BOVIN	RN220_BOVIN	Q08DV5	Q08DV5	RNF220	RNF220	MEDLINE	22199232	E3Net	RING	1	Other	B.taurus
85	SPOP_BOVIN	BMI1_BOVIN	Q0VCW1	Q32KX7	SPOP	BMI1	MEDLINE	22199232	E3Net	Other	1	Other	B.taurus
86	TRI17_BOVIN	TRI17_BOVIN	Q2T9Z0	Q2T9Z0	TRIM17	TRIM17	MEDLINE	22199232	E3Net	RING	1	Other	B.taurus
87	RO52_BOVIN	UBP4_BOVIN	Q7YRV4	A6QR55	TRIM21	USP4	MEDLINE	22199232	E3Net	RING	1	Other	B.taurus
88	RO52_BOVIN	IKKB_BOVIN	Q7YRV4	Q95KV0	TRIM21	IKBKB	MEDLINE	22199232	E3Net	RING	1	Other	B.taurus
89	BARD1_CAEEL	H2A_CAEEL	Q21209	P09588	brd-1	his-68	MEDLINE	30804228	30804228	RING	1	Other	C.elegans
90	G5ECY6_CAEEL	PK3C3_CAEEL	G5ECY6	Q9TXI7	chn-1	vps-34	MEDLINE	29092895	We found that UBC-13 functions with UEV-1, a noncatalytic E2 variant, and <span class="match term0">CHN-1</span>, a U-box-containing E3 ubiquitin ligase, to catalyze K63-linked poly-ubiquitination on <span class="match term1">VPS-34</span> both in vitro and in Caenorhabditis elegans Loss of ubc-13, uev-1, or <span class="match term0">chn-1</span> disrupts ubiquitin modification of <span class="match term1">VPS-34</span> and causes significantly reduced <span class="match term1">VPS-34</span> protein levels	UBOX	1	Other	C.elegans
91	G5ECY6_CAEEL	INSR_CAEEL	G5ECY6	Q968Y9	chn-1	daf-2	MEDLINE	28431247	28431247	UBOX	1	Other	C.elegans
92	O61899_CAEEL	RAPSN_CAEEL	O61899	Q09485	Deleted	rpy-1	MEDLINE	22199232	E3Net	Other	1	Other	C.elegans
93	Q9BMU2_CAEEL	Q09981_CAEEL	Q9BMU2	Q09981	Deleted	Deleted	MEDLINE	22199232	E3Net	Other	1	Other	C.elegans
94	Q9GUP2_CAEEL	SKN1_CAEEL	Q9GUP2	P34707	eel-1	skn-1	MEDLINE	22199232	E3Net	HECT	1	Other	C.elegans
95	Q9GUP2_CAEEL	OGT1_CAEEL	Q9GUP2	O18158	eel-1	ogt-1	MEDLINE	30858176	30858176	HECT	1	Other	C.elegans
96	FBXL_CAEEL	RIM_CAEEL	P34284	Q22366	fbxl-1	unc-10	MEDLINE	30460068	30460068	F-box	1	Other	C.elegans
97	FEM1_CAEEL	TRA1_CAEEL	P17221	P34708	fem-1	tra-1	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	C.elegans
98	SKP1B_DICDI	SKR1_CAEEL	Q557E4	G5ECU1	fpaB1	skr1	MEDLINE	28739890	28739890	Other	1	Other	C.elegans
99	APC1_CAEEL	CCNB3_CAEEL	O18191	Q10654	mat2	cyb3	MEDLINE	31588029	31588029	Other	1	Other	C.elegans
100	CDC23_CAEEL	SAS5_CAEEL	Q19294	Q20010	mat3	sas5	MEDLINE	29030390	29030390	Other	1	Other	C.elegans
101	MEL26_CAEEL	KTNA1_CAEEL	Q94420	P34808	mel-26	mei-1	MEDLINE	22199232	E3Net	Other	1	Other	C.elegans
102	MEL26_CAEEL	FIGL1_CAEEL	Q94420	O16299	mel-26	figl-1	MEDLINE	22199232	E3Net	Other	1	Other	C.elegans
103	Q9U2C5_CAEEL	LIN12_CAEEL	Q9U2C5	P14585	mib1	lin12	MEDLINE	29531012	29531012	RING	1	Other	C.elegans
104	Q9U2C5_CAEEL	GLP1_CAEEL	Q9U2C5	P13508	mib1	glp1	MEDLINE	29531012	29531012	RING	1	Other	C.elegans
105	RPM1_CAEEL	Q18909_CAEEL	Q17551	Q18909	rpm1	cebp1	MEDLINE	28673818	Previous studies revealed that the levels of cebp-1 mRNA in neurons depend on its 3' UTR and are also negatively regulated by the E3 ubiquitin ligase RPM-1	RING	1	Other	C.elegans
106	RPM1_CAEEL	UNC51_CAEEL	Q17551	Q23023	rpm-1	unc-51	MEDLINE	31676756	31676756	RING	1	Other	C.elegans
107	RPM1_CAEEL	DLK1_CAEEL	Q17551	O01700	rpm-1	dlk-1	MEDLINE	22199232	E3Net	RING	1	Other	C.elegans
108	SEL10_CAEEL	LIN41_CAEEL	Q17389	Q9U489	sel-10	lin-41	MEDLINE	30206186	Elimination of <span class="match term1">LIN-41</span> requires the activities of CDK-1 and multiple SCF (Skp1, Cul1, and F-box protein)-type E3 ubiquitin ligase subunits, including the conserved substrate adaptor protein SEL-10/Fbw7/Cdc4, suggesting that <span class="match term1">LIN-41</span> is a target of ubiquitin-mediated protein degradation	F-box	1	Other	C.elegans
109	HRD1_CAEEL	Q9BMU4_CAEEL	Q20798	Q9BMU4	sel-11	atln-1	MEDLINE	32916628	32916628	RING	1	Other	C.elegans
110	Q19019_CAEEL	SRC1_CAEEL	Q19019	G5EE56	sli-1	src-1	MEDLINE	29498112	29498112	RING	1	Other	C.elegans
111	H2KYH3_CAEEL	H2A_CAEEL	H2KYH3	P09588	spat3	his68	MEDLINE	29386386	29386386	Other	1	Other	C.elegans
112	Q9XYW6_DROME	INSR_CAEEL	Q9XYW6	Q968Y9	STUB1	daf-2	MEDLINE	28959501	28959501	UBOX	1	Other	C.elegans
113	UBR1_CAEEL	LIN28_CAEEL	P91133	P92186	ubr-1	lin-28	MEDLINE	28602583	We show that CED-3 caspase and the E3 ubiquitin ligase <span class="match term0">UBR-1</span> form a complex that couples their in vivo activities, allowing for recognition and rapid degradation of <span class="match term1">LIN-28</span> and thus facilitating a switch in developmental programs	UBOX	1	Other	C.elegans
114	UBE4_CAEEL	MYO3_CAEEL	Q09349	P12844	ufd-2	myo-3	MEDLINE	29396393	29396393	UBOX	1	Other	C.elegans
115	VHL_CAEEL	O45486_CAEEL	Q19213	O45486	vhl-1	Deleted	MEDLINE	22199232	E3Net	Other	1	Other	C.elegans
116	Q9N2Z7_CAEEL	PQE1_CAEEL	Q9N2Z7	Q10124	wwp1	pqe1	MEDLINE	30194090	30194090	HECT	1	Other	C.elegans
117	Q9N2Z7_CAEEL	RPB1_CAEEL	Q9N2Z7	P16356	wwp-1	ama-1	MEDLINE	22199232	E3Net	HECT	1	Other	C.elegans
118	Q9N2Z7_CAEEL	Q9XUK2_CAEEL	Q9N2Z7	Q9XUK2	wwp-1	zip-3	MEDLINE	30850535	Mitochondrial UPR repression during	HECT	1	Other	C.elegans
119	BRE1_DROME	H2B_DROME	Q9VRP9	P02283	Bre1	His2B	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
120	Q9VSK2_DROME	SRC42_DROME	Q9VSK2	Q9V9J3	Cbl	Src42A	MEDLINE	29498112	29498112	RING	1	Other	D.melanogaster
121	Q9VGE3_DROME	YAP1_DROME	Q9VGE3	Q45VV3	DCAF12	yki	MEDLINE	31857346	CDK7 regulates organ size and tumor growth by safeguarding the Hippo pathway effector <span class="match term1">Yki</span>/Yap/Taz in the nucleus.	DWD	1	Other	D.melanogaster
122	DIAP1_DROME	DIAP1_DROME	Q24306	Q24306	Diap1	Diap1	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
123	DIAP1_DROME	DRONC_DROME	Q24306	Q9XYF4	Diap1	Dronc	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
124	DIAP1_DROME	RPR_DROME	Q24306	Q24475	Diap1	rpr	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
125	DIAP2_DROME	DIAP1_DROME	Q24307	Q24306	Diap2	Diap1	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
126	A1Z971_DROME	Q8IPM1_DROME	A1Z971	Q8IPM1	dRNF34	srl	MEDLINE	30247505	RNF34 modulates the mitochondrial biogenesis and exercise capacity in muscle and lipid metabolism through ubiquitination of PGC-1 in Drosophila.	RING	1	Other	D.melanogaster
127	O18402_DROME	ORC1_DROME	O18402	O16810	fzr	Orc1	MEDLINE	22199232	E3Net	Other	1	Other	D.melanogaster
128	Q9W4H9_DROME	WARTS_DROME	Q9W4H9	Q9VA38	fzr	wts	MEDLINE	31000600	31000600	CDC20	1	Other	D.melanogaster
129	Q24044_DROME	CCNB_DROME	Q24044	P20439	fzy	CycB	MEDLINE	22199232	E3Net	CDC20	1	Other	D.melanogaster
130	Q24044_DROME	Q7JX41_DROME	Q24044	Q7JX41	fzy	geminin	MEDLINE	22199232	E3Net	CDC20	1	Other	D.melanogaster
131	HIW_DROME	Q9VC03_DROME	Q9NB71	Q9VC03	hiw	Nmnat	MEDLINE	29997255	29997255	RING	1	Other	D.melanogaster
132	Q6GKZ1_DROME	Q9VH01_DROME	Q6GKZ1	Q9VH01	klhl10	Bruce	MEDLINE	20643358;17880263	20643358;17880263	BTB_3	1	Other	D.melanogaster
133	Q9VGE5_DROME	Q9VES0_DROME	Q9VGE5	Q9VES0	KLHL18	Dmel\CG10324	MEDLINE	22199232	E3Net	BTB_3	1	Other	D.melanogaster
134	Q9VGE5_DROME	Q9XYZ6_DROME	Q9VGE5	Q9XYZ6	KLHL18	UKL	MEDLINE	22199232	E3Net	BTB_3	1	Other	D.melanogaster
135	Q9VGE5_DROME	Q9VIZ3_DROME	Q9VGE5	Q9VIZ3	KLHL18	l(2)37Cb	MEDLINE	22199232	E3Net	BTB_3	1	Other	D.melanogaster
136	L2DTL_DROME	E2F1_DROME	Q24371	Q27368	l(2)dtl	E2f1	MEDLINE	22199232	E3Net	Other	1	Other	D.melanogaster
137	DCAF1_DROME	LATS1_MOUSE	Q9W2F2	Q8BYR2	mahj	Lats1	MEDLINE	31170139	UbiNet 2.0	DWD	1	Other	D.melanogaster
138	MIB_DROME	SERR_DROME	Q9VUX2	P18168	mib1	Ser	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
139	MIB_DROME	DL_DROME	Q9VUX2	P10041	mib1	Dl	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
140	B7Z0L8_DROME	E2F1_DROME	B7Z0L8	Q27368	moi	E2f1	MEDLINE	19081076	UbiNet 2.0	Other	1	Other	D.melanogaster
141	NEDD4_DROME	Q9W213_DROME	Q9VVI3	Q9W213	Nedd4	robo1	MEDLINE	30893602	Ndfip proteins recruit <span class="match term0">Nedd4</span> E3 ubiquitin ligases to promote <span class="match term1">Robo1</span> ubiquitylation and degradation	HECT	1	Other	D.melanogaster
142	NEDD4_DROME	COMM_DROME	Q9VVI3	Q24139	Nedd4	comm	MEDLINE	22199232	E3Net	HECT	1	Other	D.melanogaster
143	NEDD4_DROME	NOTCH_DROME	Q9VVI3	P07207	Nedd4	N	MEDLINE	15620649	UbiNet 2.0	HECT	1	Other	D.melanogaster
144	NEDD4_DROME	Q9NCC3_DROME	Q9VVI3	Q9NCC3	Nedd4	SH3PX1	MEDLINE	30518551	30518551	HECT	1	Other	D.melanogaster
145	NEUR_DROME	SERR_DROME	P29503	P18168	neur	Ser	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
146	NEUR_DROME	DL_DROME	P29503	P10041	neur	Dl	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
147	Q7KTX7_DROME	MARF_DROME	Q7KTX7	Q7YU24	park	Marf	MEDLINE	30219582	This genetic interaction was explained by the subsequent discovery that <span class="match term0">Parkin</span> physically interacts with and ubiquitinates <span class="match term1">Marf (dMfn)</span>, fly homologue of mammalian Mitofusins, to control its steady state levels	RING	1	Other	D.melanogaster
148	Q7KTX7_DROME	VDAC_DROME	Q7KTX7	Q94920	park	porin	MEDLINE	32047033	32047033	RING	1	Other	D.melanogaster
149	M9PB68_DROME	Q0KIB3_DROME	M9PB68	Q0KIB3	poe	Hat1	MEDLINE	31365869	31365869	Other	1	Other	D.melanogaster
150	RDX_DROME	Q9VHV8_DROME	Q9VFP2	Q9VHV8	rdx	puc	MEDLINE	22199232	E3Net	Other	1	Other	D.melanogaster
151	RDX_DROME	CI_DROME	Q9VFP2	P19538	rdx	ci	MEDLINE	22199232	E3Net	Other	1	Other	D.melanogaster
152	B7Z078_DROME	AXN_DROME	B7Z078	Q9V407	Rnf146	Axn	MEDLINE	30796047	30796047	RING	1	Other	D.melanogaster
153	RING1_DROME	H2AV_DROME	Q9VB08	P08985	Sce	His2Av	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
154	SINA_DROME	TTKA_DROME	P21461	P42282	sina	ttk	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
155	O44382_DROME	PLK4_DROME	O44382	O97143	slmb	SAK	MEDLINE	22199232	E3Net	Other	1	Other	D.melanogaster
156	Q9VDE3_DROME	Q9V3B8_DROME	Q9VDE3	Q9V3B8	slmb	nerfin-1	MEDLINE	29154825	Mechanistically, Slimb associates with <span class="match term1">Nerfin-1</span> and promotes it ubiquitination and degradation in Drosophila S2R+ cells	F-box	1	Other	D.melanogaster
157	-	O46122_DROME	-	O46122	SPOP	puc	MEDLINE	19164706	UbiNet 2.0	Other	1	Other	D.melanogaster
158	-	Q9VHV8_DROME	-	Q9VHV8	SPOP	puc	MEDLINE	19164706	UbiNet 2.0	Other	1	Other	D.melanogaster
159	Q9XYW6_DROME	INSR_DROME	Q9XYW6	P09208	STUB1	InR	MEDLINE	28431247	The Ubiquitin Ligase <span class="match term0">CHIP</span> Integrates Proteostasis and Aging by Regulation of Insulin Receptor Turnover.	UBOX	1	Other	D.melanogaster
160	B7YZY9_DROME	DTX_DROME	B7YZY9	Q23985	Su(dx)	dx	MEDLINE	30213861	30213861	Other	1	Other	D.melanogaster
161	SUDX_DROME	DTX_DROME	Q9Y0H4	Q23985	Su(dx)	dx	MEDLINE	30213861	30213861	HECT	1	Other	D.melanogaster
162	A1Z7P5_DROME	Q7KJV5_DROME	A1Z7P5	Q7KJV5	Su(var)210	Aos1	MEDLINE	31901446	31901446	RING	1	Other	D.melanogaster
163	TOPRS_DROME	HAIR_DROME	Q9V8P9	P14003	Topors	h	MEDLINE	22199232	E3Net	RING	1	Other	D.melanogaster
164	Q9VTH1_DROME	Q9VXF9_DROME	Q9VTH1	Q9VXF9	Ube3a	rngo	MEDLINE	31130875	31130875	SINGLE_OTHER	1	Other	D.melanogaster
165	Q9VTH1_DROME	ATNA_DROME	Q9VTH1	P13607	Ube3a	Atpalpha	MEDLINE	28888970	Here we expand on previous work showing that the Na+/K+ pump <span class="match term1">ATPalpha</span> is a direct ubiquitin ligase substrate of <span class="match term0">Dube3a</span>	Other	1	Other	D.melanogaster
166	DTL_DANRE	Q8JFE3_DANRE	Q5RHI5	Q8JFE3	dtl	tp63	MEDLINE	31591562	31591562	DWD	1	Other	D.rerio
167	A0A2I4KBP1_DANRE	SHH_DANRE	A0A2I4KBP1	Q92008	gan	shha	MEDLINE	31503551	31503551	Other	1	Other	D.rerio
168	KLH12_DANRE	-	Q5U374	-	klhl12	DSH	MEDLINE	16547521	UbiNet 2.0	BTB_3	1	Other	D.rerio
169	MDM2_DANRE	P53_DANRE	O42354	P79734	mdm2	tp53	MEDLINE	32278060	32278060	RING	1	Other	D.rerio
170	MIB1_DANRE	JAG1B_DANRE	Q804S5	Q90Y54	mib1	jag1b	MEDLINE	22199232	E3Net	RING	1	Other	D.rerio
171	MIB1_DANRE	DLLB_DANRE	Q804S5	O57409	mib1	dlb	MEDLINE	22199232	E3Net	RING	1	Other	D.rerio
172	MIB1_DANRE	DLLD_DANRE	Q804S5	Q8UWJ4	mib1	dld	MEDLINE	22199232	E3Net	RING	1	Other	D.rerio
173	MIB1_DANRE	STING_DANRE	Q804S5	E7F4N7	mib1	sting1	MEDLINE	30508673	30508673	RING	1	Other	D.rerio
174	MIB1_DANRE	JAG1A_DANRE	Q804S5	Q90Y57	mib1	jag1a	MEDLINE	22199232	E3Net	RING	1	Other	D.rerio
175	MIB1_DANRE	DLLC_DANRE	Q804S5	Q9IAT6	mib1	dlc	MEDLINE	22199232	E3Net	RING	1	Other	D.rerio
176	MIB1_DANRE	DLLA_DANRE	Q804S5	Q6DI48	mib1	dla	MEDLINE	22199232	E3Net	RING	1	Other	D.rerio
177	RAG1_DANRE	H33_DANRE	O13033	Q6PI20	rag1	h3f3a	MEDLINE	22199232	E3Net	RING	1	Other	D.rerio
178	RAG1_DANRE	H32_DANRE	O13033	Q4QRF4	rag1	zgc:113984	MEDLINE	22199232	E3Net	RING	1	Other	D.rerio
179	A0A2R8Q387_DANRE	Q803T0_DANRE	A0A2R8Q387	Q803T0	rnf4	dnmt1	MEDLINE	29634367	<span class="match term0">RNF4</span> regulates zebrafish granulopoiesis through the <span class="match term1">DNMT1</span>-C/EBPalpha axis.	Other	1	Other	D.rerio
180	SIAH1_DANRE	G1K2I7_DANRE	Q7ZVG6	G1K2I7	siah1	cdhr1a	MEDLINE	33330480	Proteasome-Mediated Regulation of <span class="match term1">Cdhr1a</span> by <span class="match term0">Siah1</span> Modulates Photoreceptor Development and Survival in Zebrafish.	RING	1	Other	D.rerio
181	SMUF2_DANRE	P53_DANRE	A9JRZ0	P79734	smurf2	tp53	MEDLINE	32278060	32278060	HECT	1	Other	D.rerio
182	SYVN1_DANRE	SYVN1_DANRE	Q803I8	Q803I8	syvn1	syvn1	MEDLINE	22199232	E3Net	RING	1	Other	D.rerio
183	E7EYR3_DANRE	CCND1_DANRE	E7EYR3	Q90459	ttc3	ccnd1	MEDLINE	33067265	RNA-Binding RING E3-Ligase DZIP3/hRUL138 Stabilizes Cyclin D1 to Drive Cell-Cycle and Cancer Progression.	Other	1	Other	D.rerio
184	RSP5_EMENI	UAPA_EMENI	Q5BDP1	Q07307	hulA	uapA	MEDLINE	22199232	E3Net	Other	1	Other	E.nidulans
185	-	FBXW7_HUMAN	-	Q969H0	TRP120	FBXW7	MEDLINE	32353058	UbiNet 2.0	Other	1	Other	Ehrlichia chaffeensis
186	HAKAI_CHICK	CADH1_CHICK	Q5ZHZ4	P08641	CBLL1	CDH1	MEDLINE	22199232	E3Net	RING	1	Other	G.gallus
187	RAG1_CHICK	H33_CHICK	P24271	P84247	RAG1	H3IX	MEDLINE	22199232	E3Net	RING	1	Other	G.gallus
188	RAG1_CHICK	H32_CHICK	P24271	P84229	RAG1	H3I	MEDLINE	22199232	E3Net	RING	1	Other	G.gallus
189	E1C049_CHICK	MYD88_CHICK	E1C049	A5HNF6	SPOP	MYD88	MEDLINE	32365080	UbiNet 2.0	Other	1	Other	G.gallus
190	AHR_HUMAN	ESR1_HUMAN	P35869	P03372	AHR	ESR1	MEDLINE	21397018	UbiNet 2.0	Other	1	Training data	H.sapiens
191	AHR_HUMAN	PPARG_HUMAN	P35869	P37231	AHR	PPARG	MEDLINE	31653699	UbiNet 2.0	Other	1	Other	H.sapiens
192	AMRA1_HUMAN	BECN1_HUMAN	Q9C0C7	Q14457	AMBRA1	BECN1	MEDLINE	23974797	<span class="match term0">Ambra1</span> is an E3 ligase for lysine 63-linked ubiquitination of <span class="match term1">Beclin 1</span> that is required for starvation-induced autophagy	DWD	1	Other	H.sapiens
193	AMFR2_HUMAN	APOB_HUMAN	Q9UKV5	P04114	AMFR	APOB	MEDLINE	12670940	Finally, using an in vitro translation system, we demonstrated that <span class="match term0">gp78</span> led to increased ubiquitinylation and proteasomal degradation of apoB48	RING	1	Training data	H.sapiens
194	AMFR2_HUMAN	CD3D_HUMAN	Q9UKV5	P04234	AMFR	CD3D	MEDLINE	11724934	Importantly, <span class="match term0">gp78</span> can also mediate degradation of <span class="match term1">CD3-delta</span>, a well-characterized ERAD substrate	RING	1	Training data	H.sapiens
195	AMFR_HUMAN	SODC_HUMAN	Q9UKV5	P00441	AMFR	SOD1	MEDLINE	19661182	UbiNet 2.0	RING	1	Other	H.sapiens
196	AMFR2_HUMAN	CP3A4_HUMAN	Q9UKV5	P08684	AMFR	CYP3A4	MEDLINE	19095658	To determine whether phosphorylation enhances <span class="match term1">CYP3A4</span> degradation by enhancing its ubiquitination, <span class="match term1">CYP3A4</span> ubiquitination was examined in an in vitro UBC7/<span class="match term0">gp78</span>-reconstituted system with and without cAMP-dependent protein kinase A and PKC, two liver cytosolic kinases involved in <span class="match term1">CYP3A4</span> phosphorylation	RING	1	Training data	H.sapiens
197	AMFR2_HUMAN	HMDH_HUMAN	Q9UKV5	P04035	AMFR	HMGCR	MEDLINE	17681147	The membrane-anchored ubiquitin ligase <span class="match term0">gp78</span> promotes degradation of misfolded endoplasmic reticulum (ER) proteins and sterol-regulated degradation of <span class="match term1">HMG-CoA</span> reductase	RING	1	Training data	H.sapiens
198	AMFR2_HUMAN	A1AT_HUMAN	Q9UKV5	P01009	AMFR	SERPINA1	MEDLINE	16979136	Here we report that <span class="match term0">gp78</span>, a ubiquitin ligase (E3) pairing with mammalian Ubc7 for ERAD, ubiquitinates and facilitates degradation of ATZ, the classic deficiency variant of <span class="match term1">AAT</span> having a Z mutation (Glu 342 Lys)	RING	1	Training data	H.sapiens
199	AMFR2_HUMAN	INSI1_HUMAN	Q9UKV5	O15503	AMFR	INSIG1	MEDLINE	17043353	Here, we report that the ubiquitin ligase <span class="match term0">gp78</span>, which binds with much higher affinity to Insig-1 than Insig-2, is required for ubiquitination and degradation of Insig-1 in sterol-depleted cells	RING	1	Training data	H.sapiens
200	AMFR_HUMAN	CXB1_HUMAN	Q9UKV5	P08034	AMFR	GJB1	MEDLINE	30737405	Ultimately, the E3 ligase <span class="match term0">gp78</span> ubiquitinates <span class="match term1">Cx32</span> proteins, targeting them for degradation	RING	1	Other	H.sapiens
201	AMFR_HUMAN	HERP1_HUMAN	Q9UKV5	Q15011	AMFR	HERPUD1	MEDLINE	17310145	UbiNet 2.0	RING	1	Other	H.sapiens
202	AMFR2_HUMAN	CFTR_HUMAN	Q9UKV5	P13569	AMFR	CFTR	MEDLINE	18216283	<span class="match term0">Gp78</span> cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508	RING	1	Training data	H.sapiens
203	AMFR_HUMAN	MFN1_HUMAN	Q9UKV5	Q8IWA4	AMFR	MFN1	MEDLINE	23427266	UbiNet 2.0	RING	1	Training data	H.sapiens
204	AMFR_HUMAN	MFN2_HUMAN	Q9UKV5	O95140	AMFR	MFN2	MEDLINE	23427266	UbiNet 2.0	RING	1	Training data	H.sapiens
205	AMFR2_HUMAN	CD82_HUMAN	Q9UKV5	P27701	AMFR	CD82	MEDLINE	18037895	The ubiquitin ligase <span class="match term0">gp78</span> promotes sarcoma metastasis by targeting <span class="match term1">KAI1</span> for degradation	RING	1	Training data	H.sapiens
206	AMFR_HUMAN	UBL4A_HUMAN	Q9UKV5	P11441	AMFR	UBL4A	MEDLINE	24424410	Here we demonstrate that the ERAD E3 <span class="match term0">gp78</span> can ubiquitinate not only ERAD substrates, but also the machinery protein <span class="match term1">Ubl4A</span>, a key component of the Bag6 chaperone complex	RING	1	Other	H.sapiens
207	AMFR_HUMAN	NEUS_HUMAN	Q9UKV5	Q99574	AMFR	SERPINI1	MEDLINE	21507957	UbiNet 2.0	RING	1	Training data	H.sapiens
208	APC11_HUMAN	PTTG1_HUMAN	Q9NYG5	O95997	ANAPC11	PTTG1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
209	APC11_HUMAN	ANLN_HUMAN	Q9NYG5	Q9NQW6	ANAPC11	ANLN	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
210	APC11_HUMAN	GEMI_HUMAN	Q9NYG5	O75496	ANAPC11	GMNN	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
211	APC11_HUMAN	CCNB1_HUMAN	Q9NYG5	P14635	ANAPC11	CCNB1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
212	ANC2_HUMAN	PTTG1_HUMAN	Q9UJX6	O95997	ANAPC2	PTTG1	MEDLINE	12956947	UbiNet 2.0	Other	1	Other	H.sapiens
213	-	IRS2_HUMAN	-	Q9Y4H2	APC/C	IRS2	MEDLINE	32554797	UbiNet 2.0	Other	1	Other	H.sapiens
214	-	PININ_HUMAN	-	Q9H307	APC/C	PNN	MEDLINE	32203416	UbiNet 2.0	Other	1	Other	H.sapiens
215	ARI1B_HUMAN	ARI1B_HUMAN	Q8NFD5	Q8NFD5	ARID1B	ARID1B	MEDLINE	20086098	UbiNet 2.0	Other	1	Training data	H.sapiens
216	ARI1_HUMAN	IF4E2_HUMAN	Q9Y4X5	O60573	ARIH1	EIF4E2	MEDLINE	14623119	UbiNet 2.0	RING	1	Training data	H.sapiens
217	ARI1_HUMAN	SIM2_HUMAN	Q9Y4X5	Q14190	ARIH1	SIM2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
218	ARI2_HUMAN	IKBB_HUMAN	O95376	Q15653	ARIH2	NFKBIB	MEDLINE	23179078	UbiNet 2.0	RING	1	Training data	H.sapiens
219	ARI2_HUMAN	ABC3G_HUMAN	O95376	Q9HC16	ARIH2	APOBEC3G	MEDLINE	31253590	UbiNet 2.0	RING	1	Other	H.sapiens
220	ARI2_HUMAN	GFI1_HUMAN	O95376	Q99684	ARIH2	GFI1	MEDLINE	17646546	Because neither proteasome-ubiquitin nor <span class="match term0">Triad1</span> ubiquitin ligase activity was required for the inhibition of <span class="match term1">Gfi1</span> ubiquitination, these data suggest that <span class="match term0">Triad1</span> competes for <span class="match term1">Gfi1</span> binding with as yet to be identified E3 ubiquitin ligases that do mark <span class="match term1">Gfi1</span> for proteasomal degradation	RING	1	Training data	H.sapiens
221	ARI2_HUMAN	ARI2_HUMAN	O95376	O95376	ARIH2	ARIH2	MEDLINE	16118314	hUbiquitome	RING	1	Other	H.sapiens
222	ASAP1_HUMAN#TP53B_HUMAN	P53_HUMAN	Q9ULH1#Q12888	P04637	ASAP1#TP53BP1	TP53	MEDLINE	32296023	UbiNet 2.0	Other	1	Other	H.sapiens
223	ASB11_HUMAN	BIK_HUMAN	Q8WXH4	Q13323	ASB11	BIK	MEDLINE	31387940	ER stress leads to the activation of <span class="match term0">ASB11</span> by XBP1s during the adaptive phase of the unfolded protein response, which stimulates <span class="match term1">BIK</span> ubiquitination, interaction with p97/VCP, and proteolysis	SOCS_VHL_BC-box	1	Other	H.sapiens
224	ASB11_HUMAN	RPN1_HUMAN	Q8WXH4	P04843	ASB11	RPN1	MEDLINE	24337577	We also demonstrated that <span class="match term0">ASB11</span> is a novel endoplasmic reticulum-associated ubiquitin ligase with the ability to interact and promote the ubiquitination of Ribophorin 1, an integral protein of the oligosaccharyltransferase (OST) glycosylation complex	SOCS_VHL_BC-box	1	Other	H.sapiens
225	ASB2_HUMAN	FLNA_HUMAN	Q96Q27	P21333	ASB2	FLNA	MEDLINE	18799729	<span class="match term0">ASB2</span> targets filamins A and B to proteasomal degradation.	SOCS_VHL_BC-box	1	Other	H.sapiens
226	ASB2_HUMAN	FLNB_HUMAN	Q96Q27	O75369	ASB2	FLNB	MEDLINE	19300455	ASB2beta is part of an active E3 ubiquitin ligase complex and targets the actin-binding protein filamin B (<span class="match term1">FLNb</span>) for proteasomal degradation	SOCS_VHL_BC-box	1	Training data	H.sapiens
227	ASB3_HUMAN	TNR1B_HUMAN	Q9Y575	P20333	ASB3	TNFRSF1B	MEDLINE	15899873	<span class="match term0">ASB3</span> expression and activities are required for (i) TNF-R2 ubiquitination both in vivo and in vitro, (ii) TNF-R2 proteolysis via the proteasome pathway, and (iii) the inhibition of TNF-R2-mediated Jun N-terminal protein kinase (JNK) activation	SOCS_VHL_BC-box	1	Training data	H.sapiens
228	ASB4_HUMAN	ID2_HUMAN	Q9Y574	Q02363	ASB4	ID2	MEDLINE	24586788	The ubiquitin ligase <span class="match term0">ASB4</span> promotes trophoblast differentiation through the degradation of <span class="match term1">ID2</span>.	SOCS_VHL_BC-box	1	Other	H.sapiens
229	ASB8_HUMAN	RED_HUMAN	Q9H765	Q13123	ASB8	IK	MEDLINE	31009856	In turn, <span class="match term0">ASB8</span> facilitated K48-linked ubiquitination and degradation of IKKbeta via the ubiquitin-proteasome pathway, resulting in remarkable inhibition of I-kappa-B-alpha (IkappaBalpha) and of p65 phosphorylation, consequently suppressing NF-kappaB activity	SOCS_VHL_BC-box	1	Other	H.sapiens
230	ASB9_HUMAN	KCRB_HUMAN	Q96DX5	P12277	ASB9	CKB	MEDLINE	17148442	The targeting of <span class="match term1">CKB</span> for degradation by Asb-9 was primarily SOCS box-dependent and suggests that Asb-9 acts as a specific ubiquitin ligase regulating levels of this evolutionarily conserved enzyme	SOCS_VHL_BC-box	1	Training data	H.sapiens
231	ASB9_HUMAN	KCRU_HUMAN	Q96DX5	P12532	ASB9	CKMT1A	MEDLINE	20302626	<span class="match term0">ASB9</span> interacts with ubiquitous mitochondrial creatine kinase and inhibits mitochondrial function.	SOCS_VHL_BC-box	1	Other	H.sapiens
232	AURKA_HUMAN	SODM_HUMAN	O14965	P04179	AURKA	SOD2	MEDLINE	30811038	Meanwhile, the IP results confirmed that <span class="match term0">AURKA</span> could bind to <span class="match term1">SOD2</span> and degrade it through K48 ubiquitination	SINGLE_OTHER	1	Other	H.sapiens
233	BARD1_HUMAN	H2AX_HUMAN	Q99728	P16104	BARD1	H2AX	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
234	BARD1_HUMAN	ESR1_HUMAN	Q99728	P03372	BARD1	ESR1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
235	BARD1_HUMAN	BRCA1_HUMAN	Q99728	P38398	BARD1	BRCA1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
236	BARD1_HUMAN	RPAB3_HUMAN	Q99728	P52434	BARD1	POLR2H	MEDLINE	17283126	UbiNet 2.0	RING	1	Other	H.sapiens
237	BARD1_HUMAN	RPB1_HUMAN	Q99728	P24928	BARD1	POLR2A	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
238	BFAR_HUMAN	BI1_HUMAN	Q9NZS9	P55061	BFAR	TMBIM6	MEDLINE	21068390	UbiNet 2.0	RING	1	Training data	H.sapiens
239	BFAR_HUMAN	TGFA_HUMAN	Q9NZS9	P01135	BFAR	TGFA	MEDLINE	33914044	Mechanistically, <span class="match term0">BFAR</span> mediates K63-linked ubiquitination of TGFbetaR1 at K268, which is critical to activate <span class="match term1">TGFbeta</span> signaling	RING	1	Other	H.sapiens
240	BIRC2_HUMAN	TANK_HUMAN	Q13490	Q92844	BIRC2	TANK	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
241	BIRC2_HUMAN	M3K14_HUMAN	Q13490	Q99558	BIRC2	MAP3K14	MEDLINE	18022362	Through their ubiquitin E3 ligase activities <span class="match term0">c-IAP1</span> and c-IAP2 promote proteasomal degradation of <span class="match term1">NIK</span>, the central ser/thr kinase in the noncanonical NF-kappaB pathway	RING	1	Training data	H.sapiens
242	BIRC2_HUMAN	RIPK4_HUMAN	Q13490	P57078	BIRC2	RIPK4	MEDLINE	21931591	<span class="match term0">cIAP1</span>/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).	RING	1	Other	H.sapiens
243	BIRC2_HUMAN	DBLOH_HUMAN	Q13490	Q9NR28	BIRC2	DIABLO	MEDLINE	14960576	Here we show that Smac/<span class="match term1">DIABLO</span>, a mammalian functional homolog of Reaper/Hid/Grim, selectively causes the rapid degradation of <span class="match term0">c-IAP1</span> and c-IAP2 but not XIAP and Livin in HeLa cells, although it efficiently promotes the auto-ubiquitination of them all	RING	1	Training data	H.sapiens
244	BIRC2_HUMAN	XPO2_HUMAN	Q13490	P55060	BIRC2	CSE1L	MEDLINE	26668314	UbiNet 2.0	RING	1	Other	H.sapiens
245	BIRC2_HUMAN	RAC1_HUMAN	Q13490	P63000	BIRC2	RAC1	MEDLINE	22117219	UbiNet 2.0	RING	1	Other	H.sapiens
246	BIRC2_HUMAN	CASP8_HUMAN	Q13490	Q14790	BIRC2	CASP8	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
247	BIRC2_HUMAN	RIPK1_HUMAN	Q13490	Q13546	BIRC2	RIPK1	MEDLINE	18570872	UbiNet 2.0	RING	1	Training data	H.sapiens
248	BIRC2_HUMAN	TRAF1_HUMAN	Q13490	Q13077	BIRC2	TRAF1	UniProt	BIRC2_HUMAN	Polyubiquitinated by <span class="match term0">BIRC2</span> and/or BIRC3, leading to its subsequent proteasomal degradation	RING	1	Training data	H.sapiens
249	BIRC2_HUMAN	TRAF2_HUMAN	Q13490	Q12933	BIRC2	TRAF2	MEDLINE	16282325	Here, we compared the structural features of <span class="match term0">cIAP1</span> responsible for its interactions with two known target proteins, <span class="match term1">TRAF2</span> and SMAC	RING	1	Training data	H.sapiens
250	BIRC2_HUMAN	TRAF6_HUMAN	Q13490	Q9Y4K3	BIRC2	TRAF6	MEDLINE	20097753	UbiNet 2.0	RING	1	Training data	H.sapiens
251	BIRC2_HUMAN	CASP7_HUMAN	Q13490	P55210	BIRC2	CASP7	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
252	BIRC2_HUMAN	BIRC2_HUMAN	Q13490	Q13490	BIRC2	BIRC2	MEDLINE	18939944	UbiNet 2.0	RING	1	Training data	H.sapiens
253	BIRC2_HUMAN	NEMO_HUMAN	Q13490	Q9Y6K9	BIRC2	IKBKG	UniProt	BIRC2_HUMAN	LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by <span class="match term0">BIRC2</span> and/or BIRC3 and to conjugate linear polyubiquitin to <span class="match term1">IKBKG</span> and possibly other components contributing to the stability of the complex	RING	1	Training data	H.sapiens
254	BIRC2_HUMAN	MAD1_HUMAN	Q13490	Q05195	BIRC2	MXD1	MEDLINE	18082613	Here we show that <span class="match term0">c-IAP1</span> catalyzes ubiquitination of Max-dimerization protein-1 (<span class="match term1">Mad1</span>), a cellular antagonist of Myc	RING	1	Training data	H.sapiens
255	BIRC2_HUMAN	RIPK3_HUMAN	Q13490	Q9Y572	BIRC2	RIPK3	MEDLINE	21931591	<span class="match term0">cIAP1</span>/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).	RING	1	Other	H.sapiens
256	BIRC2_HUMAN	CASP3_HUMAN	Q13490	P42574	BIRC2	CASP3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
257	BIRC2_HUMAN	PGAM5_HUMAN	Q13490	Q96HS1	BIRC2	PGAM5	MEDLINE	23201124	UbiNet 2.0	RING	1	Other	H.sapiens
258	BIRC2_HUMAN	M3K5_HUMAN	Q13490	Q99683	BIRC2	MAP3K5	MEDLINE	17220297	Tumor necrosis factor receptor 2 signaling induces selective <span class="match term0">c-IAP1</span>-dependent <span class="match term1">ASK1</span> ubiquitination and terminates mitogen-activated protein kinase signaling	RING	1	Training data	H.sapiens
259	BIRC2_HUMAN	IKKE_HUMAN	Q13490	Q14164	BIRC2	IKBKE	MEDLINE	23453969	UbiNet 2.0	RING	1	Other	H.sapiens
260	BIRC2_HUMAN	TRAF3_HUMAN	Q13490	Q13114	BIRC2	TRAF3	MEDLINE	20097753	UbiNet 2.0	RING	1	Training data	H.sapiens
261	BIRC2_HUMAN	MD1L1_HUMAN	Q13490	Q9Y6D9	BIRC2	MAD1L1	MEDLINE	18082613	Here we show that <span class="match term0">c-IAP1</span> catalyzes ubiquitination of Max-dimerization protein-1 (<span class="match term1">Mad1</span>), a cellular antagonist of Myc	RING	1	Training data	H.sapiens
262	BIRC2_HUMAN	PCSK9_HUMAN	Q13490	Q8NBP7	BIRC2	PCSK9	MEDLINE	23085658	UbiNet 2.0	RING	1	Training data	H.sapiens
263	BIRC2_HUMAN	PACS2_HUMAN	Q13490	Q86VP3	BIRC2	PACS2	MEDLINE	24633224	UbiNet 2.0	RING	1	Other	H.sapiens
264	BIRC2_HUMAN	RIPK2_HUMAN	Q13490	O43353	BIRC2	RIPK2	MEDLINE	21931591	<span class="match term0">cIAP1</span>/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).	RING	1	Other	H.sapiens
265	BIRC3_HUMAN	M3K14_HUMAN	Q13489	Q99558	BIRC3	MAP3K14	MEDLINE	18997792	Degradation of TRAF3 prevented association of <span class="match term1">NIK</span> with the cIAP1-<span class="match term0">cIAP2</span>-TRAF2 ubiquitin ligase complex, which resulted in <span class="match term1">NIK</span> stabilization and NF-kappaB2-p100 processing	RING	1	Training data	H.sapiens
266	BIRC3_HUMAN	KRR1_HUMAN	Q13489	Q13601	BIRC3	KRR1	MEDLINE	18570872	We demonstrate that AEG40730, a compound modeled on BIR-binding tetrapeptides, binds to cIAP1 and <span class="match term0">cIAP2</span>, facilitates their autoubiquitination and proteosomal degradation, and causes a dramatic reduction in RIP1 ubiquitination	RING	1	Training data	H.sapiens
267	BIRC3_HUMAN	IRF1_HUMAN	Q13489	P10914	BIRC3	IRF1	MEDLINE	24464131	UbiNet 2.0	RING	1	Other	H.sapiens
268	BIRC3_HUMAN	TRAF1_HUMAN	Q13489	Q13077	BIRC3	TRAF1	MEDLINE	15468071	In this report, we have shown that <span class="match term0">cIAP2</span> specifically mediated ubiquitination and proteasome-dependent degradation of <span class="match term1">TRAF1</span>	RING	1	Training data	H.sapiens
269	BIRC3_HUMAN	TRAF6_HUMAN	Q13489	Q9Y4K3	BIRC3	TRAF6	MEDLINE	20097753	UbiNet 2.0	RING	1	Training data	H.sapiens
270	BIRC3_HUMAN	RIPK3_HUMAN	Q13489	Q9Y572	BIRC3	RIPK3	MEDLINE	21931591	cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).	RING	1	Other	H.sapiens
271	BIRC3_HUMAN	RIPK4_HUMAN	Q13489	P57078	BIRC3	RIPK4	MEDLINE	21931591	cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).	RING	1	Other	H.sapiens
272	BIRC3_HUMAN	BCL10_HUMAN	Q13489	O95999	BIRC3	BCL10	MEDLINE	19279678	Auto-ubiquitination-induced degradation of MALT1-<span class="match term0">API2</span> prevents <span class="match term1">BCL10</span> destabilization in t(11;18)(q21;q21)-positive MALT lymphoma	RING	1	Training data	H.sapiens
273	BIRC3_HUMAN	CASP8_HUMAN	Q13489	Q14790	BIRC3	CASP8	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
274	BIRC3_HUMAN	TANK_HUMAN	Q13489	Q92844	BIRC3	TANK	MEDLINE	23007157	UbiNet 2.0	RING	1	Other	H.sapiens
275	BIRC3_HUMAN	PACS2_HUMAN	Q13489	Q86VP3	BIRC3	PACS2	MEDLINE	24633224	UbiNet 2.0	RING	1	Other	H.sapiens
276	BIRC3_HUMAN	MALT1_HUMAN	Q13489	Q9UDY8	BIRC3	MALT1	MEDLINE	19279678	Auto-ubiquitination-induced degradation of <span class="match term1">MALT1</span>-<span class="match term0">API2</span> prevents BCL10 destabilization in t(11;18)(q21;q21)-positive MALT lymphoma	RING	1	Training data	H.sapiens
277	BIRC3_HUMAN	IKKE_HUMAN	Q13489	Q14164	BIRC3	IKBKE	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
278	BIRC3_HUMAN	TRAF3_HUMAN	Q13489	Q13114	BIRC3	TRAF3	MEDLINE	20097753	UbiNet 2.0	RING	1	Training data	H.sapiens
279	BIRC3_HUMAN	RIPK1_HUMAN	Q13489	Q13546	BIRC3	RIPK1	MEDLINE	18570872	UbiNet 2.0	RING	1	Training data	H.sapiens
280	BIRC3_HUMAN	CASP3_HUMAN	Q13489	P42574	BIRC3	CASP3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
281	BIRC3_HUMAN	DBLOH_HUMAN	Q13489	Q9NR28	BIRC3	DIABLO	MEDLINE	12525502	UbiNet 2.0	RING	1	Training data	H.sapiens
282	BIRC3_HUMAN	BIRC3_HUMAN	Q13489	Q13489	BIRC3	BIRC3	MEDLINE	18939944	UbiNet 2.0	RING	1	Training data	H.sapiens
283	BIRC3_HUMAN	RIPK2_HUMAN	Q13489	O43353	BIRC3	RIPK2	MEDLINE	21931591	cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).	RING	1	Other	H.sapiens
284	BIRC3_HUMAN	CASP7_HUMAN	Q13489	P55210	BIRC3	CASP7	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
285	BIRC3_HUMAN	TRAF2_HUMAN	Q13489	Q12933	BIRC3	TRAF2	MEDLINE	23007157	23007157	RING	1	Other	H.sapiens
286	BIRC6_HUMAN	DBLOH_HUMAN	Q9NR09	Q9NR28	BIRC6	DIABLO	MEDLINE	15300255	UbiNet 2.0	Other	1	Other	H.sapiens
287	BIRC7_HUMAN	DBLOH_HUMAN	Q96CA5	Q9NR28	BIRC7	DIABLO	MEDLINE	16729033	UbiNet 2.0	RING	1	Training data	H.sapiens
288	BMI1_HUMAN	GEMI_HUMAN	P35226	O75496	BMI1	GMNN	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
289	BMI1_HUMAN	H2A2B_HUMAN	P35226	Q8IUE6	BMI1	HIST2H2AB	UniProt	BMI1_HUMAN	Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals	RING	1	Training data	H.sapiens
290	BMI1_HUMAN	H2A2C_HUMAN	P35226	Q16777	BMI1	H2AC20	MEDLINE	16714294	UbiNet 2.0	RING	1	Training data	H.sapiens
291	BMI1_HUMAN	RING2_HUMAN	P35226	Q99496	BMI1	RNF2	UniProt	BMI1_HUMAN	<span class="match term1">BAP1</span> mediated deubiquitination of 'Lys-48'-linked polyubiquitin chains; deubiquitination by <span class="match term1">BAP1</span> does not seem to stabilize the protein (By similarity)	RING	1	Training data	H.sapiens
292	BMI1_HUMAN	H2A1H_HUMAN	P35226	Q96KK5	BMI1	HIST1H2AH	UniProt	BMI1_HUMAN	Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals	RING	1	Training data	H.sapiens
293	BMI1_HUMAN	H2A1B_HUMAN	P35226	P04908	BMI1	H2AC4	MEDLINE	16359901	UbiNet 2.0	RING	1	Training data	H.sapiens
294	BMI1_HUMAN	H2A1A_HUMAN	P35226	Q96QV6	BMI1	HIST1H2AA	MEDLINE	16751658	In previous studies, we identified the histone H2A ubiquitin ligase as Ring2, together in a complex with Ring1, <span class="match term0">Bmi1</span>, and HPH2 (human polyhomeotic 2)	RING	1	Training data	H.sapiens
295	BMI1_HUMAN	H2A1D_HUMAN	P35226	P20671	BMI1	H2AC7	MEDLINE	16359901	UbiNet 2.0	RING	1	Training data	H.sapiens
296	BMI1_HUMAN	H2A1C_HUMAN	P35226	Q93077	BMI1	HIST1H2AC	UniProt	BMI1_HUMAN	Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals	RING	1	Training data	H.sapiens
297	BMI1_HUMAN	H2A1J_HUMAN	P35226	Q99878	BMI1	HIST1H2AJ	UniProt	BMI1_HUMAN	Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals	RING	1	Training data	H.sapiens
298	BMI1_HUMAN	H2A3_HUMAN	P35226	Q7L7L0	BMI1	HIST3H2A	UniProt	BMI1_HUMAN	Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals	RING	1	Training data	H.sapiens
299	BMI1_HUMAN	H2AX_HUMAN	P35226	P16104	BMI1	H2AFX	MEDLINE	20921134	We found that <span class="match term0">BMI1</span> and RING2 are recruited to sites of DNA double-strand breaks (DSBs) where they contribute to the ubiquitylation of gamma-H2AX.	RING	1	Training data	H.sapiens
300	BMI1_HUMAN	H2A1_HUMAN	P35226	P0C0S8	BMI1	HIST1H2AM	UniProt	BMI1_HUMAN	Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals	RING	1	Training data	H.sapiens
301	BMI1_HUMAN	H2A2A_HUMAN	P35226	Q6FI13	BMI1	H2AC18	MEDLINE	21772249	UbiNet 2.0	RING	1	Training data	H.sapiens
302	BMI1_HUMAN	RIR1_HUMAN	P35226	P23921	BMI1	RRM1	MEDLINE	24614341	Ubiquitination and degradation of ribonucleotide reductase M1 by the polycomb group proteins RNF2 and <span class="match term0">Bmi1</span> and cellular response to gemcitabine.	RING	1	Other	H.sapiens
303	BMI1_HUMAN	H2AZ_HUMAN	P35226	P0C0S5	BMI1	H2AFZ	MEDLINE	17636032	Finally, ubiquitylation of H2A.Z is mediated by the RING1b E3 ligase of the human polycomb complex, further supporting a silencing role of ubiquitylated H2A.Z	RING	1	Training data	H.sapiens
304	BMI1_HUMAN#RING2_HUMAN	H2AZ_HUMAN	P35226#Q99496	P0C0S5	BMI1#RNF2	H2AZ1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
305	BMI1_HUMAN#RING2_HUMAN	H2A2A_HUMAN	P35226#Q99496	Q6FI13	BMI1#RNF2	H2AC18	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
306	BMI1_HUMAN#RING2_HUMAN	H2A1H_HUMAN	P35226#Q99496	Q96KK5	BMI1#RNF2	H2AC12	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
307	BMI1_HUMAN#RING2_HUMAN	RING2_HUMAN	P35226#Q99496	Q99496	BMI1#RNF2	RNF2	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
308	BMI1_HUMAN#RING2_HUMAN	H2A1_HUMAN	P35226#Q99496	P0C0S8	BMI1#RNF2	H2AC11	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
309	BMI1_HUMAN#RING2_HUMAN	H2A3_HUMAN	P35226#Q99496	Q7L7L0	BMI1#RNF2	H2AW	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
310	BMI1_HUMAN#RING2_HUMAN	H2A2C_HUMAN	P35226#Q99496	Q16777	BMI1#RNF2	H2AC20	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
311	BMI1_HUMAN#RING2_HUMAN	H2A1B_HUMAN	P35226#Q99496	P04908	BMI1#RNF2	H2AC4	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
312	BMI1_HUMAN#RING2_HUMAN	H2A1C_HUMAN	P35226#Q99496	Q93077	BMI1#RNF2	H2AC6	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
313	BMI1_HUMAN#RING2_HUMAN	H2A1A_HUMAN	P35226#Q99496	Q96QV6	BMI1#RNF2	H2AC1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
314	BMI1_HUMAN#RING2_HUMAN	H2A1D_HUMAN	P35226#Q99496	P20671	BMI1#RNF2	H2AC7	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
315	BMI1_HUMAN#RING2_HUMAN	H2A1J_HUMAN	P35226#Q99496	Q99878	BMI1#RNF2	H2AC14	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
316	BMI1_HUMAN#RING2_HUMAN	H2AX_HUMAN	P35226#Q99496	P16104	BMI1#RNF2	H2AX	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
317	BMI1_HUMAN#RING2_HUMAN	H2A2B_HUMAN	P35226#Q99496	Q8IUE6	BMI1#RNF2	H2AC21	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
318	BRAP_HUMAN	CC14A_HUMAN	Q7Z569	Q9UNH5	BRAP	CDC14A	MEDLINE	19152073	Our findings imply that <span class="match term0">Brap2</span> plays a significant role in cell cycle regulation besides its facilitation of HsCdc14A ubiquitination	RING	1	Training data	H.sapiens
319	BRAP_HUMAN	BRAP_HUMAN	Q7Z569	Q7Z569	BRAP	BRAP	MEDLINE	23105109	UbiNet 2.0	RING	1	Training data	H.sapiens
320	BRAP_HUMAN	UBP15_HUMAN	Q7Z569	Q9Y4E8	BRAP	USP15	MEDLINE	23105109	UbiNet 2.0	RING	1	Training data	H.sapiens
321	BRCA1_HUMAN	ESR1_HUMAN	P38398	P03372	BRCA1	ESR1	MEDLINE	17392432	Cancer-predisposing mutations in <span class="match term0">BRCA1</span> are observed to abrogate <span class="match term1">ERalpha</span> ubiquitination	RING	1	Training data	H.sapiens
322	BRCA1_HUMAN	NPM_HUMAN	P38398	P06748	BRCA1	NPM1	MEDLINE	19117993	The perturbation resulted in inhibition of <span class="match term0">BRCA1</span> autoubiquitination and <span class="match term1">NPM1</span>/B23 ubiquitination by <span class="match term0">BRCA1</span>/BARD1	RING	1	Training data	H.sapiens
323	BRCA1_HUMAN	BRCA1_HUMAN	P38398	P38398	BRCA1	BRCA1	MEDLINE	19117993	The perturbation resulted in inhibition of <span class="match term0">BRCA1</span> autoubiquitination and NPM1/B23 ubiquitination by <span class="match term0">BRCA1</span>/BARD1	RING	1	Training data	H.sapiens
324	BRCA1_HUMAN	COM1_HUMAN	P38398	Q99708	BRCA1	RBBP8	MEDLINE	16818604	<span class="match term0">BRCA1</span> ubiquitinates its phosphorylation-dependent binding partner <span class="match term1">CtIP</span>	RING	1	Training data	H.sapiens
325	BRCA1_HUMAN	AKT1_HUMAN	P38398	P31749	BRCA1	AKT1	MEDLINE	19074868	The <span class="match term0">BRCA1</span>-BRCT domains bind to phosphorylated <span class="match term1">AKT</span> (pAKT) and lead to its ubiquitination toward protein degradation	RING	1	Other	H.sapiens
326	BRCA1_HUMAN	CLSPN_HUMAN	P38398	Q9HAW4	BRCA1	CLSPN	MEDLINE	22863316	UbiNet 2.0	RING	1	Other	H.sapiens
327	BRCA1_HUMAN	H2A1_HUMAN	P38398	P0C0S8	BRCA1	H2AC11	MEDLINE	12431996	UbiNet 2.0	RING	1	Training data	H.sapiens
328	BRCA1_HUMAN	PRGR_HUMAN	P38398	P06401	BRCA1	PGR	MEDLINE	21531767	UbiNet 2.0	RING	1	Training data	H.sapiens
329	BRCA1_HUMAN	RPAB3_HUMAN	P38398	P52434	BRCA1	POLR2H	MEDLINE	17283126	<span class="match term0">BRCA1</span> ubiquitinates <span class="match term1">RPB8</span> in response to DNA damage	RING	1	Training data	H.sapiens
330	BRCA1_HUMAN	CCNB1_HUMAN	P38398	P14635	BRCA1	CCNB1	MEDLINE	23246971	UbiNet 2.0	RING	1	Other	H.sapiens
331	BRCA1_HUMAN	H2A1B_HUMAN	P38398	P04908	BRCA1	H2AC4	MEDLINE	25131202	<span class="match term0">BRCA1</span> is a histone-H2A-specific ubiquitin ligase.	RING	1	Other	H.sapiens
332	BRCA1_HUMAN	TBG1_HUMAN	P38398	P23258	BRCA1	TUBG1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
333	BRCA1_HUMAN	H2A1A_HUMAN	P38398	Q96QV6	BRCA1	H2AC1	MEDLINE	11927591	UbiNet 2.0	RING	1	Training data	H.sapiens
334	BRCA1_HUMAN	MERL_HUMAN	P38398	P35240	BRCA1	NF2	MEDLINE	30918126	Here, we show that <span class="match term0">BRCA1</span> facilitates stabilization of YAP1 protein and turning off the Hippo pathway through ubiquitination of <span class="match term1">NF2</span>	RING	1	Other	H.sapiens
335	BRCA1_HUMAN	H2B1A_HUMAN	P38398	Q96A08	BRCA1	H2BC1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
336	BRCA1_HUMAN	RPB1_HUMAN	P38398	P24928	BRCA1	POLR2A	MEDLINE	15886201	In cells, however, efficient <span class="match term1">Rpb1</span> ubiquitination required the carboxyl terminus of <span class="match term0">BRCA1</span>, suggesting that interactions mediated by this region were essential in the complex milieu of the nucleus	RING	1	Training data	H.sapiens
337	BRCA1_HUMAN	PSA7_HUMAN	P38398	O14818	BRCA1	PSMA7	MEDLINE	25620702	UbiNet 2.0	RING	1	Other	H.sapiens
338	BRCA1_HUMAN	TOP2A_HUMAN	P38398	P11388	BRCA1	TOP2A	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
339	BRCA1_HUMAN	NR1H3_HUMAN	P38398	Q13133	BRCA1	NR1H3	MEDLINE	19164445	Liver X receptor ligands suppress ubiquitination and degradation of LXRalpha by displacing BARD1/<span class="match term0">BRCA1</span>	RING	1	Training data	H.sapiens
340	BRCA1_HUMAN	BARD1_HUMAN	P38398	Q99728	BRCA1	BARD1	MEDLINE	19117993	UbiNet 2.0	RING	1	Training data	H.sapiens
341	BRCA1_HUMAN	FACD2_HUMAN	P38398	Q9BXW9	BRCA1	FANCD2	MEDLINE	12887909	UbiNet 2.0	RING	1	Training data	H.sapiens
342	BRCA1_HUMAN	H2AX_HUMAN	P38398	P16104	BRCA1	H2AFX	MEDLINE	11927591	Purified <span class="match term0">BRCA1</span>-(1-639)*BARD1 stimulated the Ubc5c-mediated monoubiquitination of histone H2A/H2AX in vitro, suggesting a possible role for <span class="match term0">BRCA1</span>*BARD1 in modifying chromatin structure	RING	1	Training data	H.sapiens
343	BRCA1_HUMAN	H2A2C_HUMAN	P38398	Q16777	BRCA1	H2AC20	MEDLINE	11927591	UbiNet 2.0	RING	1	Other	H.sapiens
344	BRCA1_HUMAN	PTPA_HUMAN	P38398	Q86WV6	BRCA1	HIST1H2AB	MEDLINE	25131202	25131202	RING	1	Other	H.sapiens
345	BRCA1_HUMAN	MPIP3_HUMAN	P38398	P30307	BRCA1	CDC25C	MEDLINE	23246971	UbiNet 2.0	RING	1	Training data	H.sapiens
346	BRCA1_HUMAN	PO2F1_HUMAN	P38398	P14859	BRCA1	POU2F1	MEDLINE	29330289	<span class="match term0">BRCA1</span> E3 ubiquitin ligase mutation skews cells toward a glycolytic metabolic profile while elevating <span class="match term1">Oct1</span> protein	RING	1	Other	H.sapiens
347	BRCA1_HUMAN	ERPG3_HUMAN	P38398	P0DP91	BRCA1	ERCC6	MEDLINE	21756275	<span class="match term0">BRCA1</span> polyubiquitinates <span class="match term1">CSB</span> and this polyubiquitination and subsequent degradation of <span class="match term1">CSB</span> occur following UV irradiation, even in the absence of Cockayne syndrome A (CSA) protein.	RING	1	Other	H.sapiens
348	BRCA1_HUMAN	Q2PQ59_9TRYP	P38398	Q2PQ59	BRCA1	TOP2alpha	MEDLINE	18162055	hUbiquitome	RING	1	Other	H.sapiens
349	FBW1A_HUMAN	CD4_HUMAN	Q9Y297	P01730	BTRC	CD4	MEDLINE	14674748	Phosphorylation of Vpu at two sites, Ser52 and Ser56, on the motif DSGXXS is required for the interaction of Vpu with the ubiquitin ligase SCF-<span class="match term0">betaTrCP</span> which triggers <span class="match term1">CD4</span> degradation by the proteasome	F-box	1	Training data	H.sapiens
350	FBW1A_HUMAN	CTNB1_HUMAN	Q9Y297	P35222	BTRC	CTNNB1	MEDLINE	19795382	We found that BMP-2 stimulates Lrp5 expression and inhibits the expression of <span class="match term0">beta-TrCP</span>, the F-box E3 ligase responsible for <span class="match term1">beta-catenin</span> degradation and subsequently increases <span class="match term1">beta-catenin</span> protein levels in osteoblasts	F-box	1	Training data	H.sapiens
351	FBW1A_HUMAN	MPIP1_HUMAN	Q9Y297	P30304	BTRC	CDC25A	MEDLINE	15845771	When analyzed by using Xenopus eggs, the binding of <span class="match term0">beta-TrCP</span> to the DDG motif is essential for the Chk1-induced ubiquitination and degradation of Xenopus <span class="match term1">Cdc25A</span> and also plays a role in the degradation of human <span class="match term1">Cdc25A</span>	F-box	1	Training data	H.sapiens
352	FBW1A_HUMAN	IKBB_HUMAN	Q9Y297	Q15653	BTRC	NFKBIB	UniProt	FBW1A_HUMAN	SCF(<span class="match term0">BTRC</span>) mediates the ubiquitination of NFKBIA, <span class="match term1">NFKBIB</span> and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription	F-box	1	Training data	H.sapiens
353	FBW1A_HUMAN	PER2_HUMAN	Q9Y297	O15055	BTRC	PER2	MEDLINE	17876059	Mathematical modeling conceptualizes the authors' findings and suggests that loss of sustained rhythmicity in cells with eliminated <span class="match term0">beta-TrCP</span>-mediated <span class="match term1">PER2</span> degradation is due to excessive nuclear repression, a prediction they verified experimentally	F-box	1	Training data	H.sapiens
354	FBW1A_HUMAN	PER1_HUMAN	Q9Y297	O15534	BTRC	PER1	MEDLINE	15917222	Finally, RNA interference against <span class="match term0">beta-TRCP</span> greatly decreases Clock-dependent gene expression in tissue culture cells, indicating that <span class="match term0">beta-TRCP</span> controls endogenous <span class="match term1">Per1</span> activity and the circadian clock by directly targeting <span class="match term1">Per1</span> for degradation	F-box	1	Training data	H.sapiens
355	FBW1A_HUMAN	INGR1_HUMAN	Q9Y297	P15260	BTRC	IFNGR1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
356	FBW1A_HUMAN	ATF4_HUMAN	Q9Y297	P18848	BTRC	ATF4	UniProt	FBW1A_HUMAN	SCF(<span class="match term0">BTRC</span>) directs ubiquitination of NFKBIB, NFKBIE, <span class="match term1">ATF4</span>, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2	F-box	1	Training data	H.sapiens
357	FBW1A_HUMAN	IKBA_HUMAN	Q9Y297	P25963	BTRC	NFKBIA	MEDLINE	19180189	The data presented show that phosphorylated <span class="match term1">IkappaBalpha</span> is stable in rotavirus-infected cells because infection induces proteasome-dependent degradation of <span class="match term0">beta-TrCP</span>	F-box	1	Training data	H.sapiens
358	FBW1A_HUMAN	MS18A_HUMAN	Q9Y297	Q9NYP9	BTRC	MIS18A	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
359	FBW1A_HUMAN	UBP37_HUMAN	Q9Y297	Q86T82	BTRC	USP37	MEDLINE	23027877	Skp1-Cul1-F-box ubiquitin ligase (SCF(<span class="match term0">betaTrCP</span>))-mediated destruction of the ubiquitin-specific protease <span class="match term1">USP37</span> during G2-phase promotes mitotic entry	F-box	1	Other	H.sapiens
360	FBW1A_HUMAN	BORA_HUMAN	Q9Y297	Q6PGQ7	BTRC	BORA	MEDLINE	19390576	In mitosis, <span class="match term1">Bora</span> is degraded in a manner dependent on Plk1 kinase activity and the E3 ubiquitin ligase SCF-<span class="match term0">betaTrCP</span>	F-box	1	Training data	H.sapiens
361	FBW1A_HUMAN	GLI2_HUMAN	Q9Y297	P10070	BTRC	GLI2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
362	FBW1A_HUMAN	NF2L1_HUMAN	Q9Y297	Q14494	BTRC	NFE2L1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
363	FBW1A_HUMAN	ZNRF3_HUMAN	Q9Y297	Q9ULT6	BTRC	ZNRF3	MEDLINE	29497989	Furthermore, the Cullin 1-specific SCF complex containing <span class="match term0">beta-TRCP</span> has been identified to directly interact with and ubiquitinate <span class="match term1">ZNRF3</span> thereby regulating its protein stability	F-box	1	Other	H.sapiens
364	FBW1A_HUMAN	HSF1_HUMAN	Q9Y297	Q00613	BTRC	HSF1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
365	FBW1A_HUMAN	CLSPN_HUMAN	Q9Y297	Q9HAW4	BTRC	CLSPN	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
366	FBW1A_HUMAN	FBX5_HUMAN	Q9Y297	Q9UKT4	BTRC	FBXO5	MEDLINE	17676996	We further addressed this Vpu inhibitory function with respect to the degradation of <span class="match term1">Emi1</span> and Cdc25A, two <span class="match term0">betaTrCP</span> substrates involved in cell-cycle progression	F-box	1	Training data	H.sapiens
367	FBW1A_HUMAN	FOXN2_HUMAN	Q9Y297	P32314	BTRC	FOXN2	MEDLINE	29396548	we find that <span class="match term1">FOXN2</span> binds to and is ubiquitinated by <span class="match term0">beta-Trcp</span> ubiquitin ligase and RSK2 kinase for degradation.	F-box	1	Other	H.sapiens
368	FBW1A_HUMAN	MDM2_HUMAN	Q9Y297	Q00987	BTRC	MDM2	MEDLINE	20708156	Here, we report that <span class="match term1">Mdm2</span> is rapidly degraded after DNA damage and that phosphorylation of <span class="match term1">Mdm2</span> by casein kinase I (CKI) at multiple sites triggers its interaction with, and subsequent ubiquitination and destruction, by SCF(<span class="match term0">beta-TRCP</span>)	F-box	1	Training data	H.sapiens
369	FBW1A_HUMAN	TWST1_HUMAN	Q9Y297	Q15672	BTRC	TWIST1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
370	FBW1A_HUMAN	HNRPD_HUMAN	Q9Y297	Q14103	BTRC	HNRNPD	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
371	FBW1A_HUMAN	PRLR_HUMAN	Q9Y297	P16471	BTRC	PRLR	MEDLINE	15082796	Knockdown of <span class="match term0">beta-TrCP</span> expression inhibits the ubiquitination and degradation of <span class="match term1">PRLR</span> and promotes PRL-dependent phosphorylation of Stat5 as well as Stat5-dependent transcription in cells	F-box	1	Training data	H.sapiens
372	FBW1A_HUMAN	FANCM_HUMAN	Q9Y297	Q8IYD8	BTRC	FANCM	MEDLINE	19270156	<span class="match term0">beta-TRCP</span> and Plk1 are the key regulators of <span class="match term1">FANCM</span> degradation	F-box	1	Training data	H.sapiens
373	FBW1A_HUMAN	SP1_HUMAN	Q9Y297	P08047	BTRC	SP1	MEDLINE	19372209	UbiNet 2.0	F-box	1	Training data	H.sapiens
374	FBW1A_HUMAN	MPIP2_HUMAN	Q9Y297	P30305	BTRC	CDC25B	MEDLINE	21807946	UbiNet 2.0	F-box	1	Other	H.sapiens
375	FBW1A_HUMAN	DAND5_HUMAN	Q9Y297	Q8N907	BTRC	DAND5	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
376	FBW1A_HUMAN	F263_HUMAN	Q9Y297	Q16875	BTRC	PFKFB3	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
377	FBW1A_HUMAN	WEE1_HUMAN	Q9Y297	P30291	BTRC	WEE1	MEDLINE	18560763	At the onset of mitosis, <span class="match term1">Wee1</span> is ubiquitinated by the E3 ubiquitin ligase SCF(<span class="match term0">beta-TrCP</span>) and subsequently degraded by the proteasome machinery	F-box	1	Training data	H.sapiens
378	FBW1A_HUMAN	SMAD3_HUMAN	Q9Y297	P84022	BTRC	SMAD3	UniProt	FBW1A_HUMAN	SCF(<span class="match term0">BTRC</span>) mediates the ubiquitination of phosphorylated NFKB1/nuclear factor NF-kappa-B p105 subunit, ATF4, <span class="match term1">SMAD3</span>, SMAD4, CDC25A, DLG1, FBXO5 and probably NFKB2	F-box	1	Training data	H.sapiens
379	FBW1A_HUMAN	GLI3_HUMAN	Q9Y297	P10071	BTRC	GLI3	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
380	FBW1A_HUMAN	SPAR_HUMAN	Q9Y297	A0A1B0GVQ0	BTRC	SPAAR	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
381	FBW1A_HUMAN	YAP1_HUMAN	Q9Y297	P46937	BTRC	YAP1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
382	FBW1A_HUMAN	EPOR_HUMAN	Q9Y297	P19235	BTRC	EPOR	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
383	FBW1A_HUMAN	B2L11_HUMAN	Q9Y297	O43521	BTRC	BCL2L11	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
384	FBW1A_HUMAN	BTG1_HUMAN	Q9Y297	P62324	BTRC	BTG1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
385	FBW1A_HUMAN	CASP3_HUMAN	Q9Y297	P42574	BTRC	CASP3	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
386	FBW1A_HUMAN	RCAN1_HUMAN	Q9Y297	P53805	BTRC	RCAN1	MEDLINE	18575781	In vitro ubiquitination assay showed that SCFbeta-TrCP but not SCFFBW4 increased ubiquitination of <span class="match term1">RCAN1</span>, dependent on H2O2 stimulation	F-box	1	Training data	H.sapiens
387	FBW1A_HUMAN	UHRF1_HUMAN	Q9Y297	Q96T88	BTRC	UHRF1	MEDLINE	23297342	UbiNet 2.0	F-box	1	Training data	H.sapiens
388	FBW1A_HUMAN	GBF1_HUMAN	Q9Y297	Q92538	BTRC	GBF1	MEDLINE	29898406	<span class="match term1">GBF1</span> interaction with <span class="match term0">betaTrCP</span> recruits <span class="match term1">GBF1</span> to the SCFbetaTrCP ubiquitin ligase complex, triggering its degradation	F-box	1	Other	H.sapiens
389	FBW1A_HUMAN	STAT1_HUMAN	Q9Y297	P42224	BTRC	STAT1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
390	FBW1A_HUMAN	TBCD7_HUMAN	Q9Y297	Q9P0N9	BTRC	TBC1D7	MEDLINE	30143532	The sequence immediately upstream of Ser-124 aligned with a canonical <span class="match term0">beta-TrCP</span> degron, and we found that the E3 ubiquitin ligase beta-TrCP2 ubiquitinates <span class="match term1">TBC1D7</span> and decreases its stability	F-box	1	Other	H.sapiens
391	FBW1A_HUMAN	GSK3B_HUMAN	Q9Y297	P49841	BTRC	GSK3B	MEDLINE	24451375	Induction of Gsk3beta-<span class="match term0">beta-TrCP</span> interaction is required for late phase stabilization of beta-catenin in canonical Wnt signaling.	F-box	1	Other	H.sapiens
392	FBW1A_HUMAN	PDCD4_HUMAN	Q9Y297	Q53EL6	BTRC	PDCD4	MEDLINE	17053147	UbiNet 2.0	F-box	1	Training data	H.sapiens
393	FBW1A_HUMAN	NF2L2_HUMAN	Q9Y297	Q16236	BTRC	NFE2L2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
394	FBW1A_HUMAN	ELF3_HUMAN	Q9Y297	P78545	BTRC	ELF3	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
395	FBW1A_HUMAN	NFKB1_HUMAN	Q9Y297	P19838	BTRC	NFKB1	UniProt	FBW1A_HUMAN	SCF(<span class="match term0">BTRC</span>) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated <span class="match term1">NFKB1</span> to translocate into the nucleus and to activate transcription	F-box	1	Training data	H.sapiens
396	FBW1A_HUMAN	TFAP4_HUMAN	Q9Y297	Q01664	BTRC	TFAP4	MEDLINE	24500709	We have found that, during the G2 phase of the cell division cycle, <span class="match term1">TFAP4</span> is targeted for proteasome-dependent degradation by the SCF(<span class="match term0">betaTrCP</span>) ubiquitin ligase	F-box	1	Other	H.sapiens
397	FBW1A_HUMAN	VGFR2_HUMAN	Q9Y297	P35968	BTRC	KDR	MEDLINE	22711876	UbiNet 2.0	F-box	1	Training data	H.sapiens
398	FBW1A_HUMAN	COMD1_HUMAN	Q9Y297	Q8N668	BTRC	COMMD1	MEDLINE	20068069	UbiNet 2.0	F-box	1	Training data	H.sapiens
399	FBW1A_HUMAN	BCL10_HUMAN	Q9Y297	O95999	BTRC	BCL10	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
400	FBW1A_HUMAN	TIAM1_HUMAN	Q9Y297	Q13009	BTRC	TIAM1	MEDLINE	25124033	Degradation of <span class="match term1">Tiam1</span> by casein kinase 1 and the SCFbetaTrCP ubiquitin ligase controls the duration of mTOR-S6K signaling.	F-box	1	Other	H.sapiens
401	FBW1A_HUMAN	TP4A3_HUMAN	Q9Y297	O75365	BTRC	PTP4A3	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
402	FBW1A_HUMAN	CDK1_HUMAN	Q9Y297	P06493	BTRC	CDK1	MEDLINE	25149538	We show that <span class="match term1">CDK1</span> is ubiquitinated by the E3 ubiquitin ligase SCFbetaTrCP and degraded by the lysosome	F-box	1	Other	H.sapiens
403	FBW1A_HUMAN	SMAD4_HUMAN	Q9Y297	Q13485	BTRC	SMAD4	UniProt	FBW1A_HUMAN	SCF(<span class="match term0">BTRC</span>) mediates the ubiquitination of phosphorylated NFKB1/nuclear factor NF-kappa-B p105 subunit, ATF4, SMAD3, <span class="match term1">SMAD4</span>, CDC25A, DLG1, FBXO5 and probably NFKB2	F-box	1	Training data	H.sapiens
404	FBW1A_HUMAN	P53_HUMAN	Q9Y297	P04637	BTRC	TP53	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
405	FBW1A_HUMAN	MCL1_HUMAN	Q9Y297	Q07820	BTRC	MCL1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
406	FBW1A_HUMAN	DLG1_HUMAN	Q9Y297	Q12959	BTRC	DLG1	MEDLINE	12902344	Finally, we show that <span class="match term0">beta-TrCP</span> selectively induces the degradation of the membrane-cytoplasmic pool, without affecting the nuclear pool of <span class="match term1">hDlg</span>	F-box	1	Training data	H.sapiens
407	FBW1A_HUMAN	NFKB2_HUMAN	Q9Y297	Q00653	BTRC	NFKB2	UniProt	FBW1A_HUMAN	SCF(<span class="match term0">BTRC</span>) mediates the ubiquitination of phosphorylated NFKB1/nuclear factor NF-kappa-B p105 subunit, ATF4, SMAD3, SMAD4, CDC25A, DLG1, FBXO5 and probably <span class="match term1">NFKB2</span>	F-box	1	Training data	H.sapiens
408	FBW1A_HUMAN	IKBE_HUMAN	Q9Y297	O00221	BTRC	NFKBIE	UniProt	FBW1A_HUMAN	SCF(<span class="match term0">BTRC</span>) directs ubiquitination of NFKBIB, <span class="match term1">NFKBIE</span>, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2	F-box	1	Training data	H.sapiens
409	FBW1A_HUMAN	NRF1_HUMAN	Q9Y297	Q16656	BTRC	NRF1	MEDLINE	21911472	UbiNet 2.0	F-box	1	Training data	H.sapiens
410	FBW1A_HUMAN	FGD3_HUMAN	Q9Y297	Q5JSP0	BTRC	FGD3	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
411	FBW1A_HUMAN	MYC_HUMAN	Q9Y297	P01106	BTRC	MYC	MEDLINE	20852628	Whereas SCFFbw7 with the Cdc34 ubiquitin-conjugating enzyme specifically requires lysine 48 (K48) of ubiquitin, SCFbeta-TrCP uses the UbcH5 ubiquitin-conjugating enzyme to form heterotypic polyubiquitin chains on <span class="match term1">Myc</span>	F-box	1	Other	H.sapiens
412	FBW1A_HUMAN	DLG5_HUMAN	Q9Y297	Q8TDM6	BTRC	DLG5	MEDLINE	12902344	UbiNet 2.0	F-box	1	Training data	H.sapiens
413	FBW1A_HUMAN	BHE40_HUMAN	Q9Y297	O14503	BTRC	BHLHE40	MEDLINE	25202122	UbiNet 2.0	F-box	1	Other	H.sapiens
414	FBW1A_HUMAN	IKKA_HUMAN	Q9Y297	O15111	BTRC	CHUK	MEDLINE	19109186	UbiNet 2.0	F-box	1	Training data	H.sapiens
415	FBW1A_HUMAN	TFR1_HUMAN	Q9Y297	P02786	BTRC	TFRC	MEDLINE	34315867	We also found that beta-transducin repeat containing E3 ubiqutin protein ligase (<span class="match term0">betaTrCP</span>) was a genuine E3 for the ubiquitination of <span class="match term1">TFRC</span>, and TRIB2 was unable to decline labile iron level once upon <span class="match term0">betaTrCP</span> was knocked out	F-box	1	Other	H.sapiens
416	FBW1A_HUMAN	DDIT4_HUMAN	Q9Y297	Q9NX09	BTRC	DDIT4	MEDLINE	19557001	Here, we show that <span class="match term1">REDD1</span> is subject to ubiquitin-mediated degradation mediated by the CUL4A-DDB1-ROC1-<span class="match term0">beta-TRCP</span> E3 ligase complex and through the activity of glycogen synthase kinase 3beta	F-box	1	Training data	H.sapiens
417	FBW1A_HUMAN	XRCC1_HUMAN	Q9Y297	P18887	BTRC	XRCC1	MEDLINE	31043584	E3 ligase <span class="match term0">beta-TrCP</span> catalyzed the poly-ubiquitination of <span class="match term1">XRCC1</span> to promote its proteasome-dependent degradation	F-box	1	Other	H.sapiens
418	FBW1A_HUMAN	BST2_HUMAN	Q9Y297	Q10589	BTRC	BST2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
419	FBW1A_HUMAN	PSMD4_HUMAN	Q9Y297	P55036	BTRC	PSMD4	MEDLINE	19240029	UbiNet 2.0	F-box	1	Other	H.sapiens
420	FBW1A_HUMAN	CPEB1_HUMAN	Q9Y297	Q9BZB8	BTRC	CPEB1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
421	FBW1A_HUMAN	PCAT1_HUMAN	Q9Y297	Q8NF37	BTRC	LPCAT1	MEDLINE	21068446	UbiNet 2.0	F-box	1	Training data	H.sapiens
422	FBW1A_HUMAN	FINC_HUMAN	Q9Y297	P02751	BTRC	FN1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
423	FBW1A_HUMAN	BTG2_HUMAN	Q9Y297	P78543	BTRC	BTG2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
424	FBW1A_HUMAN	IRAK1_HUMAN	Q9Y297	P51617	BTRC	IRAK1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
425	FBW1A_HUMAN	SNAI1_HUMAN	Q9Y297	O95863	BTRC	SNAI1	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
426	FBW1A_HUMAN	FZR1_HUMAN	Q9Y297	Q9UM11	BTRC	FZR1	MEDLINE	23972993	UbiNet 2.0	F-box	1	Other	H.sapiens
427	FBW1A_HUMAN	DPTOR_HUMAN	Q9Y297	Q8TB45	BTRC	DEPTOR	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
428	FBW1A_HUMAN	TERF1_HUMAN	Q9Y297	P54274	BTRC	TERF1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
429	FBW1A_HUMAN	TRIB2_HUMAN	Q9Y297	Q92519	BTRC	TRIB2	MEDLINE	24211582	In the present study, we reveal that the stability and ubiquitination of <span class="match term1">TRIB2</span> can also be controlled by ubiquitin E3 ligase SCF(<span class="match term0">beta-TRCP</span>)	F-box	1	Other	H.sapiens
430	FBW1A_HUMAN	CCNE1_HUMAN	Q9Y297	P24864	BTRC	CCNE1	MEDLINE	18851830	UbiNet 2.0	F-box	1	Other	H.sapiens
431	FBW1A_HUMAN	PKD2_HUMAN	Q9Y297	Q13563	BTRC	PKD2	MEDLINE	17636028	Replacements of serines in a phosphodegron motif in TAZ prevent <span class="match term0">beta-Trcp</span> binding and <span class="match term1">PC2</span> degradation	F-box	1	Training data	H.sapiens
432	FBW1A_HUMAN	PLK4_HUMAN	Q9Y297	O00444	BTRC	PLK4	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
433	FBW1A_HUMAN	CEP68_HUMAN	Q9Y297	Q76N32	BTRC	CEP68	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
434	FBW1A_HUMAN	REST_HUMAN	Q9Y297	Q13127	BTRC	REST	MEDLINE	14523018	Our data suggest that LMP1-95-8 is a pseudo-substrate of SCFHOS/<span class="match term0">betaTrCP</span> E3 ubiquitin ligase and that interaction between LMP1 and HOS restricts the extent of LMP1-induced NF-kappaB signaling	F-box	1	Training data	H.sapiens
435	FBW1A_HUMAN	EF2K_HUMAN	Q9Y297	O00418	BTRC	EEF2K	MEDLINE	22669845	UbiNet 2.0	F-box	1	Training data	H.sapiens
436	FBW1A_HUMAN	PTTG1_HUMAN	Q9Y297	O95997	BTRC	PTTG1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
437	FBW1A_HUMAN	CADH1_HUMAN	Q9Y297	P12830	BTRC	CDH1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
438	FBW1A_HUMAN	CCND1_HUMAN	Q9Y297	P24385	BTRC	CCND1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
439	FBW1A_HUMAN	FOXO3_HUMAN	Q9Y297	O43524	BTRC	FOXO3	MEDLINE	20625400	UbiNet 2.0	F-box	1	Training data	H.sapiens
440	FBW1A_HUMAN	GHR_HUMAN	Q9Y297	P10912	BTRC	GHR	MEDLINE	23607312	In the present study, we show that <span class="match term0">betaTrCP</span> interacts directly via its WD40 domain with the UbE (ubiquitin-dependent endocytosis) motif in <span class="match term1">GHR</span>, promoting <span class="match term1">GHR</span> ubiquitination in vitro.	F-box	1	Other	H.sapiens
441	FBW1A_HUMAN	INAR1_HUMAN	Q9Y297	P17181	BTRC	IFNAR1	MEDLINE	16551269	UbiNet 2.0	F-box	1	Training data	H.sapiens
442	FBW1A_HUMAN	WWTR1_HUMAN	Q9Y297	Q9GZV5	BTRC	WWTR1	MEDLINE	20858893	The hippo tumor pathway promotes <span class="match term1">TAZ</span> degradation by phosphorylating a phosphodegron and recruiting the SCF{beta}-TrCP E3 ligase.	F-box	1	Other	H.sapiens
443	FBW1A_HUMAN	MAP2_HUMAN	Q9Y297	P50579	BTRC	METAP2	MEDLINE	11438690	UbiNet 2.0	F-box	1	Training data	H.sapiens
444	FBW1A_HUMAN	PHLP1_HUMAN	Q9Y297	O60346	BTRC	PHLPP1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
445	FBW1A_HUMAN	UBP47_HUMAN	Q9Y297	Q96K76	BTRC	USP47	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
446	FBW1A_HUMAN	MXI1_HUMAN	Q9Y297	P50539	BTRC	MXI1	MEDLINE	29507620	Furthermore, we demonstrated that <span class="match term1">Mxi1</span> is phosphorylated at S160 site by the protein kinase S6K1 and subsequently degraded via the ubiquitin ligase <span class="match term0">beta-Trcp</span>	F-box	1	Other	H.sapiens
447	FBW1A_HUMAN	CIKS_HUMAN	Q9Y297	O43734	BTRC	TRAF3IP2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
448	FBW1A_HUMAN	ELAV1_HUMAN	Q9Y297	Q15717	BTRC	ELAVL1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
449	FBW1A_HUMAN	LPIN2_HUMAN	Q9Y297	Q92539	BTRC	LPIN2	MEDLINE	32008742	UbiNet 2.0	F-box	1	Other	H.sapiens
450	FBW1A_HUMAN	RASF1_HUMAN	Q9Y297	Q9NS23	BTRC	RASSF1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
451	FBW1A_HUMAN	TAZ_HUMAN	Q9Y297	Q16635	BTRC	TAZ	MEDLINE	20858893	20858893	F-box	1	Other	H.sapiens
452	FBW1A_HUMAN	FGD1_HUMAN	Q9Y297	P98174	BTRC	FGD1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
453	FBW1A_HUMAN	ZHANG_HUMAN	Q9Y297	Q9NS37	BTRC	CREBZF	MEDLINE	11238952	ATF4 represents a novel substrate for the SCF(<span class="match term0">betaTrCP</span>) complex, which is the first mammalian E3 ubiquitin ligase identified so far for the control of the degradation of a bZIP transcription factor	F-box	1	Training data	H.sapiens
454	FBW1A_HUMAN	RASH_HUMAN	Q9Y297	P01112	BTRC	HRAS	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
455	FBW1A_HUMAN	FBW1B_HUMAN	Q9Y297	Q9UKB1	BTRC	FBXW11	MEDLINE	31406304	UbiNet 2.0	F-box	1	Other	H.sapiens
456	FBW1A_HUMAN	I10R1_HUMAN	Q9Y297	Q13651	BTRC	IL10RA	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
457	FBW1A_HUMAN	BMI1_HUMAN	Q9Y297	P35226	BTRC	BMI1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
458	FBW1A_HUMAN	SRC8_HUMAN	Q9Y297	Q14247	BTRC	CTTN	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
459	CJ090_HUMAN	P53_HUMAN	Q96M02	P04637	C10orf90	TP53	MEDLINE	24240685	Here, we show that <span class="match term0">FATS</span> acts as a <span class="match term1">p53</span> activator by inhibiting Mdm2 binding to <span class="match term1">p53</span> and stimulating non-proteolytic polyubiquitination of <span class="match term1">p53</span>	Other	1	Other	H.sapiens
460	CBL_HUMAN	SRC_HUMAN	P22681	P12931	CBL	SRC	MEDLINE	10734113	We tested the hypothesis that <span class="match term1">Src</span> family kinases (SFK) contribute to c-<span class="match term0">Cbl</span>-mediated degradation of the platelet-derived growth factor (PDGF) alpha receptor (alphaPDGFR)	RING	1	Training data	H.sapiens
461	CBL_HUMAN	EGFR_HUMAN	P22681	P00533	CBL	EGFR	MEDLINE	15194809	On overexpression of the <span class="match term0">Cbl</span>-binding protein Sprouty, ubiquitination of the <span class="match term1">EGFR</span> was inhibited, the <span class="match term1">EGFR</span> was recruited only to the rim of coated pits, and endocytosis of the <span class="match term1">EGFR</span> was inhibited	RING	1	Training data	H.sapiens
462	CBL_HUMAN	FGFR2_HUMAN	P22681	P21802	CBL	FGFR2	MEDLINE	17944804	Biochemical analysis showed that <span class="match term1">KGFR</span> is ubiquitinated and degraded after KGF treatment but not after FGF10 treatment, and that the alternative fate of <span class="match term1">KGFR</span> might depend on the different ability of the receptor to phosphorylate the fibroblast growth factor receptor substrate 2 (FRS2) substrate and to recruit the ubiquitin ligase c-<span class="match term0">Cbl</span>	RING	1	Training data	H.sapiens
463	CBL_HUMAN	BCR_HUMAN	P22681	P11274	CBL	BCR	MEDLINE	20675402	UbiNet 2.0	RING	1	Training data	H.sapiens
464	CBL_HUMAN	VGFR1_HUMAN	P22681	P17948	CBL	FLT1	MEDLINE	15001553	In <span class="match term1">Flt-1</span>-overexpressing NIH3T3 cells, expression of the wild-type CD2AP enhanced VEGF-stimulated internalization as well as ubiquitination of <span class="match term1">Flt-1</span> whereas that of a mutated form of either CD2AP or c-<span class="match term0">Cbl</span> failed to do so	RING	1	Training data	H.sapiens
465	CBL_HUMAN	LCK_HUMAN	P22681	P06239	CBL	LCK	MEDLINE	20150895	This steady state, tonic CD3 monoubiquitylation is mediated by the CD3varepsilon proline-rich sequence, <span class="match term1">Lck</span>, c-<span class="match term0">Cbl</span>, and SLAP, which collectively trigger the dynamin-dependent downmodulation, lysosomal sequestration and degradation of surface TCR:CD3 complexes	RING	1	Training data	H.sapiens
466	CBL_HUMAN	IL6RB_HUMAN	P22681	P40189	CBL	IL6ST	MEDLINE	18519587	Deficiency of either Hrs or c-<span class="match term0">Cbl</span> suppressed <span class="match term1">gp130</span> degradation, which leads to a prolonged and amplified IL-6 signal	RING	1	Training data	H.sapiens
467	CBL_HUMAN	FGFR3_HUMAN	P22681	P22607	CBL	FGFR3	MEDLINE	18485666	Our findings suggest that activated Spry2 may interfere with c-<span class="match term0">Cbl</span>-mediated ubiquitination of <span class="match term1">FGFR3</span> by sequestering c-<span class="match term0">Cbl</span>	RING	1	Training data	H.sapiens
468	CBL_HUMAN	FYN_HUMAN	P22681	P06241	CBL	FYN	MEDLINE	15208330	Mutational induction of an open conformation enhanced the susceptibility of kinase-active <span class="match term1">Fyn</span> to <span class="match term0">Cbl</span> but was insufficient to promote the ubiquitinylation and degradation of kinase-inactive <span class="match term1">Fyn</span>	RING	1	Training data	H.sapiens
469	CBL_HUMAN	P85A_HUMAN	P22681	P27986	CBL	PIK3R1	MEDLINE	24113870	<span class="match term0">Cbl</span> ubiquitination of <span class="match term1">p85</span> is essential for Epo-induced EpoR endocytosis.	RING	1	Other	H.sapiens
470	CBL_HUMAN	FRS2_HUMAN	P22681	Q8WU20	CBL	FRS2	MEDLINE	11997436	Here, we demonstrate that Grb2 bound to tyrosine-phosphorylated <span class="match term1">FRS2</span> alpha forms a ternary complex with <span class="match term0">Cbl</span> by means of its Src homology 3 domains resulting in the ubiquitination of fibroblast growth factor (FGF) receptor and <span class="match term1">FRS2</span> alpha in response to FGF stimulation	RING	1	Training data	H.sapiens
471	CBL_HUMAN	MTOR_HUMAN	P22681	P42345	CBL	MTOR	MEDLINE	32386556	In contrast, MPs activate translation in an <span class="match term1">mTOR</span>-independent manner due, at least in part, to proteasomal degradation of <span class="match term1">mTOR</span> by the E3 ubiquitin ligase c-<span class="match term0">Cbl</span>	RING	1	Other	H.sapiens
472	CBL_HUMAN	KSYK_HUMAN	P22681	P43405	CBL	SYK	MEDLINE	15701717	In c-<span class="match term0">Cbl</span>-deficient mice, <span class="match term1">Syk</span> is not ubiquitinated, implicating c-<span class="match term0">Cbl</span> as the E3 ligase involved in <span class="match term1">Syk</span> ubiquitination	RING	1	Training data	H.sapiens
473	CBL_HUMAN	ABL1_HUMAN	P22681	P00519	CBL	ABL1	MEDLINE	8770364	Parallel studies have demonstrated that p120cbl is a substrate of protein Tyrosine kinases activated by engagement of the T cell antigen receptor and that <span class="match term0">cbl</span> is phosphorylated by oncogenic forms of the <span class="match term1">Abl</span> tyrosine kinase	RING	1	Training data	H.sapiens
474	CBL_HUMAN	SH3K1_HUMAN	P22681	Q96B97	CBL	SH3KBP1	UniProt	CBL_HUMAN	<span class="match term0">CBL</span>_HUMAN	RING	1	Training data	H.sapiens
475	CBL_HUMAN	STA5B_HUMAN	P22681	P51692	CBL	STAT5B	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
476	CBL_HUMAN	TPOR_HUMAN	P22681	P40238	CBL	MPL	MEDLINE	19880496	Using siRNA and dominant negative overexpression, we also found that c-<span class="match term0">Cbl</span>, which is activated by Tpo, acts as an E3 ubiquitin ligase in the ubiquitination of c-<span class="match term1">Mpl</span>	RING	1	Training data	H.sapiens
477	CBL_HUMAN	EPHA2_HUMAN	P22681	P29317	CBL	EPHA2	MEDLINE	12496371	We also show that c-<span class="match term0">Cbl</span> promotes stimulation-dependent <span class="match term1">EphA2</span> degradation	RING	1	Training data	H.sapiens
478	CBL_HUMAN	LYN_HUMAN	P22681	P07948	CBL	LYN	MEDLINE	15190072	<span class="match term0">Cbl</span>-mediated degradation of <span class="match term1">Lyn</span> and Fyn induced by constitutive fibroblast growth factor receptor-2 activation supports osteoblast differentiation	RING	1	Training data	H.sapiens
479	CBL_HUMAN	FGR_HUMAN	P22681	P09769	CBL	FGR	MEDLINE	12435267	UbiNet 2.0	RING	1	Training data	H.sapiens
480	CBL_HUMAN	FCG2A_HUMAN	P22681	P12318	CBL	FCGR2A	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
481	CBL_HUMAN	RON_HUMAN	P22681	Q04912	CBL	MST1R	MEDLINE	12802274	Although <span class="match term1">Ron</span> and c-<span class="match term0">Cbl</span> are found also in physical complexes that include Grb2, these associations are insufficient for productive ubiquitylation of <span class="match term1">Ron</span>	RING	1	Training data	H.sapiens
482	CBL_HUMAN	CRKL_HUMAN	P22681	P46109	CBL	CRKL	MEDLINE	12671687	<span class="match term0">Cbl</span> was shown to promote the ubiquitylation of <span class="match term1">CrkL</span> without any apparent effect on its stability	RING	1	Training data	H.sapiens
483	CBL_HUMAN	MYBPP_HUMAN	P22681	Q8TBZ2	CBL	MYCBPAP	MEDLINE	17255943	We moreover found that <span class="match term1">AMAP1</span> is monoubiquitinated, rather than polyubiquitinated, by virtue of <span class="match term0">Cbl</span> and provide evidence that the ability of <span class="match term1">AMAP1</span> to be monoubiquitinated is important for its involvement in invasion	RING	1	Training data	H.sapiens
484	CBL_HUMAN	VAV_HUMAN	P22681	P15498	CBL	VAV1	MEDLINE	11857085	A major <span class="match term0">CBL</span>-B associated protein was identified as mono-ubiquitinated <span class="match term1">Vav</span>, a nucleotide exchange factor for Rac1	RING	1	Training data	H.sapiens
485	CBL_HUMAN	TIE2_HUMAN	P22681	Q02763	CBL	TEK	MEDLINE	23754070	UbiNet 2.0	RING	1	Training data	H.sapiens
486	CBL_HUMAN	PK3CG_HUMAN	P22681	P48736	CBL	PIK3CG	MEDLINE	18374639	Biochemical and molecular analyses revealed that the attenuated <span class="match term1">PI3K</span> signaling induced by FGFR2 activation is due to increased <span class="match term0">Cbl</span>-<span class="match term1">PI3K</span> molecular interaction mediated by the <span class="match term0">Cbl</span> Y731 residue, which results in increased <span class="match term1">PI3K</span> ubiquitination and proteasome degradation	RING	1	Training data	H.sapiens
487	CBL_HUMAN	FGFR4_HUMAN	P22681	P22455	CBL	FGFR4	MEDLINE	18480409	<span class="match term1">FGFR4</span> was found to be less ubiquitinated than FGFR1, and different levels of ubiquitination were proposed as a mechanism to regulate their sorting	RING	1	Training data	H.sapiens
488	CBL_HUMAN	ITA5_HUMAN	P22681	P08648	CBL	ITGA5	MEDLINE	15728256	<span class="match term0">Cbl</span>-mediated ubiquitination of alpha5 integrin subunit mediates fibronectin-dependent osteoblast detachment and apoptosis induced by FGFR2 activation	RING	1	Training data	H.sapiens
489	CBL_HUMAN	ARHG7_HUMAN	P22681	Q14155	CBL	ARHGEF7	MEDLINE	16407834	UbiNet 2.0	RING	1	Training data	H.sapiens
490	CBL_HUMAN	ERBB2_HUMAN	P22681	P04626	CBL	ERBB2	MEDLINE	19263517	Whereas retrovirally infected NIH3T3 cells containing the EGFR Y1045F mutation showed dramatically impaired <span class="match term0">Cbl</span> recruitment, EGFR ubiquitination and delayed EGFR degradation, replacement of the EGFR <span class="match term0">Cbl</span> binding site by that of <span class="match term1">ErbB2</span> or ErbB4 did not affect <span class="match term0">Cbl</span> recruitment, receptor-ubiquitination, -degradation, -downregulation or ligand degradation	RING	1	Training data	H.sapiens
491	CBL_HUMAN	SPY2_HUMAN	P22681	O43597	CBL	SPRY2	MEDLINE	16780213	Human Sprouty2 (<span class="match term1">hSpry2</span>) binds the catalytic RING Finger of Casitas B-lineage lymphoma (c-<span class="match term0">Cbl</span>), an E3 ubiquitin ligase that has been identified to target EGFR degradation	RING	1	Training data	H.sapiens
492	CBL_HUMAN	S100B_HUMAN	P22681	P04271	CBL	S100B	MEDLINE	33329486	Importantly, cellular c-<span class="match term0">Cbl</span> ubiquitinated and degraded <span class="match term1">Nef</span> proteins produced by HIV-1 NL4-3 virions, and ultimately attenuated HIV-1 virulence for infection of THP1 cells	RING	1	Other	H.sapiens
493	CBL_HUMAN	IRF8_HUMAN	P22681	Q02556	CBL	IRF8	MEDLINE	15837792	Furthermore, <span class="match term1">IRF-8</span> stability was increased by dominant negative <span class="match term0">Cbl</span>, and <span class="match term1">IRF-8</span> ubiquitination was significantly attenuated in <span class="match term0">Cbl</span>-/- cells	RING	1	Training data	H.sapiens
494	CBL_HUMAN	ALK_HUMAN	P22681	Q9UM73	CBL	ALK	MEDLINE	22479414	UbiNet 2.0	RING	1	Training data	H.sapiens
495	CBL_HUMAN	KIT_HUMAN	P22681	P10721	CBL	KIT	MEDLINE	16780420	Moreover, we demonstrate that <span class="match term0">Cbl</span> mediates monoubiquitination of c-<span class="match term1">Kit</span> and that the receptor is subsequently targeted for lysosomal degradation	RING	1	Training data	H.sapiens
496	CBL_HUMAN	PGFRB_HUMAN	P22681	P09619	CBL	PDGFRB	MEDLINE	15753096	Furthermore, the association of PDGFRbeta with c-<span class="match term0">Cbl</span>, a ubiquitin E3-ligase, as well as the ligand-induced ubiquitination of PDGFRbeta were increased in LRP1-deficient fibroblasts	RING	1	Training data	H.sapiens
497	CBL_HUMAN	NLRP3_HUMAN	P22681	Q96P20	CBL	NLRP3	MEDLINE	31553908	Once activated, P2Y2 enhances its interaction with <span class="match term1">NLRP3</span> and stimulates the recruitment of the E3 ubiquitin ligase <span class="match term0">CBL</span> to <span class="match term1">NLRP3</span>, ultimately leading to <span class="match term1">NLRP3</span> degradation	RING	1	Other	H.sapiens
498	CBL_HUMAN	FGFR1_HUMAN	P22681	P11362	CBL	FGFR1	MEDLINE	17944804	Biochemical analysis showed that KGFR is ubiquitinated and degraded after KGF treatment but not after FGF10 treatment, and that the alternative fate of KGFR might depend on the different ability of the receptor to phosphorylate the fibroblast growth factor receptor substrate 2 (FRS2) substrate and to recruit the ubiquitin ligase c-<span class="match term0">Cbl</span>	RING	1	Training data	H.sapiens
499	CBL_HUMAN	NFAC1_HUMAN	P22681	O95644	CBL	NFATC1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
500	CBL_HUMAN	MET_HUMAN	P22681	P08581	CBL	MET	MEDLINE	17449471	UbiNet 2.0	RING	1	Training data	H.sapiens
501	CBL_HUMAN	CD5_HUMAN	P22681	P06127	CBL	CD5	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
502	CBL_HUMAN	SRBS2_HUMAN	P22681	O94875	CBL	SORBS2	MEDLINE	12475393	<span class="match term0">Cbl</span>-<span class="match term1">ArgBP2</span> complex mediates ubiquitination and degradation of c-Abl	RING	1	Training data	H.sapiens
503	CBL_HUMAN	ZAP70_HUMAN	P22681	P43403	CBL	ZAP70	MEDLINE	29498112	Phosphorylation control of the ubiquitin ligase <span class="match term0">Cbl</span> is conserved in choanoflagellates.	RING	1	Other	H.sapiens
504	CBL_HUMAN	LRIG1_HUMAN	P22681	Q96JA1	CBL	LRIG1	MEDLINE	15282549	The underlying mechanism involves recruitment of c-<span class="match term0">Cbl</span>, an E3 ubiquitin ligase that simultaneously ubiquitylates EGFR and <span class="match term1">LRIG1</span> and sorts them for degradation	RING	1	Training data	H.sapiens
505	CBL_HUMAN	EPHB1_HUMAN	P22681	P54762	CBL	EPHB1	MEDLINE	18034775	Both <span class="match term0">Cbl</span> phosphorylation and <span class="match term1">EphB1</span> ubiquitination were blocked by the Src inhibitor PP2	RING	1	Training data	H.sapiens
506	CBL_HUMAN	PLCG1_HUMAN	P22681	P19174	CBL	PLCG1	MEDLINE	16467851	UbiNet 2.0	RING	1	Training data	H.sapiens
507	CBL_HUMAN	STA5A_HUMAN	P22681	P42229	CBL	STAT5A	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
508	CBL_HUMAN	B2L11_HUMAN	P22681	O43521	CBL	BCL2L11	MEDLINE	18198176	UbiNet 2.0	RING	1	Training data	H.sapiens
509	CBL_HUMAN	CSF1R_HUMAN	P22681	P07333	CBL	CSF1R	MEDLINE	11847211	In contrast, the expression of <span class="match term0">Cbl</span> drastically reduced the vc-<span class="match term1">Fms</span>-transformed phenotype and the activation of Erk and enhanced <span class="match term1">Fms</span> ubiquitination via phosphotyrosine residue 977	RING	1	Training data	H.sapiens
510	CBL_HUMAN	HGS_HUMAN	P22681	O14964	CBL	HGS	MEDLINE	20029031	UbiNet 2.0	RING	1	Training data	H.sapiens
511	CBL_HUMAN	STAP2_HUMAN	P22681	Q9UGK3	CBL	STAP2	MEDLINE	19401194	In contrast, over-expression of <span class="match term0">Cbl</span> induced STAP-2 degradation	RING	1	Training data	H.sapiens
512	CBL_HUMAN	CFTR_HUMAN	P22681	P13569	CBL	CFTR	MEDLINE	22467879	UbiNet 2.0	RING	1	Training data	H.sapiens
513	CBL_HUMAN	PDGFA_HUMAN	P22681	P04085	CBL	PDGFA	MEDLINE	17620338	UbiNet 2.0	RING	1	Training data	H.sapiens
514	CBL_HUMAN	VGFR2_HUMAN	P22681	P35968	CBL	KDR	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
515	CBL_HUMAN	IL2RG_HUMAN	P22681	P31785	CBL	IL2RG	MEDLINE	16004964	The common cytokine receptor gamma(c) is shared by the interleukin-2, -4, -7, -9, -15, and -21 receptors, and is essential for lymphocyte proliferation and survival. We report that the ubiquitin-ligase c-<span class="match term0">Cbl</span> induces gamma(c) down-regulation.	RING	1	Training data	H.sapiens
516	CBL_HUMAN	IGF1R_HUMAN	P22681	P08069	CBL	IGF1R	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
517	CBL_HUMAN	PAR2_HUMAN	P22681	P55085	CBL	F2RL1	UniProt	CBL_HUMAN	<span class="match term0">CBL</span>_HUMAN	RING	1	Training data	H.sapiens
518	CBL_HUMAN	PGFRA_HUMAN	P22681	P16234	CBL	PDGFRA	MEDLINE	10347229	Our previous observations that <span class="match term0">Cbl</span> overexpression in NIH3T3 cells enhanced the ubiquitination and degradation of the platelet-derived growth factor receptor-alpha (<span class="match term1">PDGFRalpha</span>) and that the expression of oncogenic <span class="match term0">Cbl</span> mutants up-regulated the <span class="match term1">PDGFRalpha</span> signaling machinery strongly suggested that <span class="match term0">Cbl</span> negatively regulates <span class="match term1">PDGFRalpha</span> signaling	RING	1	Training data	H.sapiens
519	CBL_HUMAN	EPHA8_HUMAN	P22681	P29322	CBL	EPHA8	MEDLINE	20100865	UbiNet 2.0	RING	1	Training data	H.sapiens
520	CBL_HUMAN	CTNB1_HUMAN	P22681	P35222	CBL	CTNNB1	MEDLINE	23744067	This study defines for the first time c-<span class="match term0">Cbl</span> as a ubiquitin E3 ligase that targets nuclearly active <span class="match term1">beta-catenin</span> in the Wnt-on phase and uncovers a novel layer of regulation of Wnt signaling	RING	1	Other	H.sapiens
521	CBL_HUMAN	TNR16_HUMAN	P22681	P08138	CBL	NGFR	MEDLINE	15337528	Our data suggest a c-<span class="match term0">Cbl</span>-dependent ubiquitination of <span class="match term1">p75NTR</span> involved in the regulation of <span class="match term1">p75NTR</span> signalling	RING	1	Training data	H.sapiens
522	CBL_HUMAN	SPRE2_HUMAN	P22681	Q7Z698	CBL	SPRED2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
523	CBL_HUMAN	YES_HUMAN	P22681	P07947	CBL	YES1	MEDLINE	21596750	UbiNet 2.0	RING	1	Training data	H.sapiens
524	CBLB_HUMAN	SH3K1_HUMAN	Q13191	Q96B97	CBLB	SH3KBP1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
525	CBLB_HUMAN	CBLB_HUMAN	Q13191	Q13191	CBLB	CBLB	MEDLINE	11375397	UbiNet 2.0	RING	1	Training data	H.sapiens
526	CBLB_HUMAN	CD3Z_HUMAN	Q13191	P20963	CBLB	CD247	MEDLINE	20637659	UbiNet 2.0	RING	1	Other	H.sapiens
527	CBLB_HUMAN	Q9I788_PSEAE	Q13191	Q9I788	CBLB	exoT	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
528	CBLB_HUMAN	NLRP3_HUMAN	Q13191	Q96P20	CBLB	NLRP3	MEDLINE	31999304	<span class="match term0">Cbl-b</span> binds to the K63-ubiquitin chains attached to the <span class="match term1">NLRP3</span> leucine-rich repeat domain (LRR) via its ubiquitin-associated region (UBA) and then targets <span class="match term1">NLRP3</span> at K496 for K48-linked ubiquitination and proteasome-mediated degradation	RING	1	Other	H.sapiens
529	CBLB_HUMAN	KSYK_HUMAN	Q13191	P43405	CBLB	SYK	MEDLINE	12771181	<span class="match term0">Cbl-b</span> negatively regulates B cell antigen receptor signaling in mature B cells through ubiquitination of the tyrosine kinase <span class="match term1">Syk</span>	RING	1	Training data	H.sapiens
530	CBLB_HUMAN	EGFR_HUMAN	Q13191	P00533	CBLB	EGFR	MEDLINE	16702950	The Cbl family of ubiquitin ligases (Cbl, <span class="match term0">Cbl-b</span>, and Cbl-c) targets the activated <span class="match term1">EGFR</span> for degradation	RING	1	Training data	H.sapiens
531	CBLB_HUMAN	IRS1_HUMAN	Q13191	P35568	CBLB	IRS1	MEDLINE	23187081	UbiNet 2.0	RING	1	Training data	H.sapiens
532	CBLB_HUMAN	PGFRA_HUMAN	Q13191	P16234	CBLB	PDGFRA	MEDLINE	29237719	Here, we provide evidence that intraflagellar transport protein 20 (IFT20) interacts with E3 ubiquitin ligases c-Cbl and <span class="match term0">Cbl-b</span> and is required for Cbl-mediated ubiquitination and internalization of <span class="match term1">PDGFRalpha</span> for feedback inhibition of receptor signaling	RING	1	Other	H.sapiens
533	CBLB_HUMAN	PLCG1_HUMAN	Q13191	P19174	CBLB	PLCG1	UniProt	CBLB_HUMAN	Ubiquitinated by <span class="match term0">CBLB</span> in activated T-cells (By similarity)	RING	1	Training data	H.sapiens
534	CBLB_HUMAN	SRC_HUMAN	Q13191	P12931	CBLB	SRC	MEDLINE	12907674	<span class="match term0">Cbl-b</span> also targets active <span class="match term1">Src</span> for degradation in cells, and Nedd4 similarly reverses Cbl-mediated <span class="match term1">Src</span> degradation	RING	1	Training data	H.sapiens
535	CBLB_HUMAN	P85A_HUMAN	Q13191	P27986	CBLB	PIK3R1	MEDLINE	11087752	UbiNet 2.0	RING	1	Training data	H.sapiens
536	CBLB_HUMAN	P85B_HUMAN	Q13191	O00459	CBLB	PIK3R2	MEDLINE	11087752	UbiNet 2.0	RING	1	Training data	H.sapiens
537	CBLC_HUMAN	EGFR_HUMAN	Q9ULV8	P00533	CBLC	EGFR	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
538	CBLC_HUMAN	SRC_HUMAN	Q9ULV8	P12931	CBLC	SRC	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
539	HAKAI_HUMAN	CADH1_HUMAN	Q75N03	P12830	CBLL1	CDH1	MEDLINE	19893985	<span class="match term1">CDH1</span> expression is repressed by transcription factors such as Snail (SNAI1) and its product is degraded after <span class="match term0">Hakai</span> ubiquitination	RING	1	Training data	H.sapiens
540	HAKAI_HUMAN	ANXA2_HUMAN	Q75N03	P07355	CBLL1	ANXA2	MEDLINE	31952268	UbiNet 2.0	RING	1	Other	H.sapiens
541	HAKAI_HUMAN	NAR4_HUMAN	Q75N03	Q93070	CBLL1	ART4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
542	HAKAI_HUMAN	SRC8_HUMAN	Q75N03	Q14247	CBLL1	CTTN	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
543	CCAR1_HUMAN	P53_HUMAN	Q8IX12	P04637	CCAR1	TP53	MEDLINE	32296023	UbiNet 2.0	Other	1	Other	H.sapiens
544	CIP1_HUMAN	CIP1_HUMAN	Q9NPC3	Q9NPC3	CCNB1IP1	CCNB1IP1	MEDLINE	12612082	Finally, <span class="match term0">HEI10</span> is itself ubiquitinated in egg extracts and is also autoubiquitinated in vitro	RING	1	Training data	H.sapiens
545	CIP1_HUMAN	CCNB1_HUMAN	Q9NPC3	P14635	CCNB1IP1	CCNB1	MEDLINE	12612082	UbiNet 2.0	RING	1	Training data	H.sapiens
546	CCNF_HUMAN	RIR2_HUMAN	P41002	P31350	CCNF	RRM2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
547	CCNF_HUMAN	CDC6_HUMAN	P41002	Q99741	CCNF	CDC6	MEDLINE	26818844	UbiNet 2.0	F-box	1	Other	H.sapiens
548	CCNF_HUMAN	CP110_HUMAN	P41002	O43303	CCNF	CCP110	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
549	CDC20_HUMAN	CDN1B_HUMAN	Q12834	P46527	CDC20	CDKN1B	MEDLINE	22199232	E3Net	CDC20	1	Other	H.sapiens
550	CDC20_HUMAN	CCNB1_HUMAN	Q12834	P14635	CDC20	CCNB1	MEDLINE	21336306	The spindle assembly checkpoint (SAC) acts on the APC/C co-activator, <span class="match term0">Cdc20</span> (cell division cycle 20), to block the degradation of metaphase substrates (for example, cyclin B1 and securin), but not others (for example, cyclin A)	CDC20	1	Training data	H.sapiens
551	CDC20_HUMAN	CENPF_HUMAN	Q12834	P49454	CDC20	CENPF	MEDLINE	20053638	<span class="match term0">Cdc20</span> is required for the post-anaphase, KEN-dependent degradation of centromere protein F.	CDC20	1	Other	H.sapiens
552	CDC20_HUMAN	PTTG1_HUMAN	Q12834	O95997	CDC20	PTTG1	MEDLINE	17891138	APC(cdh1) targeted <span class="match term0">cdc20</span> for degradation, but did not target securin or cyclin B1	CDC20	1	Training data	H.sapiens
553	CDC20_HUMAN	RUNX1_HUMAN	Q12834	Q01196	CDC20	RUNX1	MEDLINE	17015473	A phospho-mimic protein, <span class="match term1">AML1</span>-4D, can be targeted by <span class="match term0">Cdc20</span> or Cdh1	CDC20	1	Training data	H.sapiens
554	CDC20_HUMAN	MCL1_HUMAN	Q12834	Q07820	CDC20	MCL1	MEDLINE	20526282	<span class="match term1">Mcl-1</span> destruction during mitotic arrest requires proteasome activity and is dependent on <span class="match term0">Cdc20</span>/Fizzy, which mediates recognition of mitotic substrates by the anaphase-promoting complex/cyclosome (APC/C) E3 ubiquitin ligase	CDC20	1	Other	H.sapiens
555	CDC20_HUMAN	BUB1B_HUMAN	Q12834	O60566	CDC20	BUB1B	MEDLINE	16856867	To prevent chromosome missegregation due to early degradation of cyclin B and securin, mitotic checkpoint protein complexes consisting of <span class="match term1">BubR1</span>, Bub3 and Mad2 bind to and inhibit APC(<span class="match term0">Cdc20</span>) until all chromosomes are properly attached to the mitotic spindle and aligned in the metaphase plate	CDC20	1	Training data	H.sapiens
556	CDC20_HUMAN	NEK2_HUMAN	Q12834	P51955	CDC20	NEK2	MEDLINE	16648845	Early mitotic degradation of <span class="match term1">Nek2A</span> depends on <span class="match term0">Cdc20</span>-independent interaction with the APC/C	CDC20	1	Training data	H.sapiens
557	CDC20_HUMAN	CCNA2_HUMAN	Q12834	P20248	CDC20	CCNA2	MEDLINE	19826003	UbiNet 2.0	CDC20	1	Other	H.sapiens
558	CDC20_HUMAN	KMT2A_HUMAN	Q12834	Q03164	CDC20	KMT2A	MEDLINE	17908926	UbiNet 2.0	CDC20	1	Training data	H.sapiens
559	CDC20_HUMAN	NDF2_HUMAN	Q12834	Q15784	CDC20	NEUROD2	MEDLINE	22199232	E3Net	CDC20	1	Other	H.sapiens
560	CDC20_HUMAN	REV1_HUMAN	Q12834	Q9UBZ9	CDC20	REV1	MEDLINE	23287467	Overexpression of APC coactivator CDH1 or <span class="match term0">CDC20</span> promotes polyubiquitination and proteosomal degradation of <span class="match term1">REV1</span>	CDC20	1	Other	H.sapiens
561	CDC20_HUMAN	MLP3A_HUMAN	Q12834	Q9H492	CDC20	MAP1LC3A	MEDLINE	30613277	Furthermore, we found that <span class="match term0">CDC20</span> directly targeted <span class="match term1">LC3</span>, a key regulator of autophagy, and promoted <span class="match term1">LC3</span> ubiquitination and degradation by the proteasome, which inhibited autophagy leading to hypertrophy	CDC20	1	Other	H.sapiens
562	CDC20_HUMAN	PHF8_HUMAN	Q12834	Q9UPP1	CDC20	PHF8	MEDLINE	23979597	UbiNet 2.0	CDC20	1	Other	H.sapiens
563	CDC20_HUMAN	RASF1_HUMAN	Q12834	Q9NS23	CDC20	RASSF1	MEDLINE	21874044	Paradoxically, <span class="match term1">RASSF1A</span> was also demonstrated to be ubiquitinated by APC/C(<span class="match term0">Cdc20</span>) in vitro and degraded at prometaphase despite of active spindle checkpoint presence	CDC20	1	Other	H.sapiens
564	CDC20_HUMAN	DRB4_HUMAN	Q12834	P13762	CDC20	HLA-DRB4	MEDLINE	22545099	UbiNet 2.0	CDC20	1	Training data	H.sapiens
565	CDC20_HUMAN	CDN1A_HUMAN	Q12834	P38936	CDC20	CDKN1A	MEDLINE	17679094	APC/C(<span class="match term0">Cdc20</span>) controls the ubiquitin-mediated degradation of <span class="match term1">p21</span> in prometaphase	CDC20	1	Training data	H.sapiens
566	CDC20_HUMAN	SP100_HUMAN	Q12834	P23497	CDC20	SP100	MEDLINE	22086178	Our results suggested that <span class="match term1">sp100</span> is a novel substrate of <span class="match term0">Cdc20</span> and it is degraded by the ubiquitination pathway	CDC20	1	Other	H.sapiens
567	CDC20_HUMAN	TRRAP_HUMAN	Q12834	Q9Y4A5	CDC20	TRRAP	MEDLINE	23318449	UbiNet 2.0	CDC20	1	Training data	H.sapiens
568	CDC20_HUMAN	AXIN2_HUMAN	Q12834	Q9Y2T1	CDC20	AXIN2	MEDLINE	22322943	UbiNet 2.0	CDC20	1	Other	H.sapiens
569	UB2R1_HUMAN	IKBA_HUMAN	P49427	P25963	CDC34	NFKBIA	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
570	UB2R1_HUMAN	MYBB_HUMAN	P49427	P10244	CDC34	MYBL2	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
571	UB2R1_HUMAN	FBW1A_HUMAN	P49427	Q9Y297	CDC34	BTRC	MEDLINE	10531035	UbiNet 2.0	Other	1	Other	H.sapiens
572	UB2R1_HUMAN	CREM_HUMAN	P49427	Q03060	CDC34	CREM	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
573	UB2R1_HUMAN	CDN1B_HUMAN	P49427	P46527	CDC34	CDKN1B	MEDLINE	19123975	UbiNet 2.0	Other	1	Other	H.sapiens
574	UB2R1_HUMAN	CTNB1_HUMAN	P49427	P35222	CDC34	CTNNB1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
575	CDCA3_HUMAN	WEE1_HUMAN	Q99618	P30291	CDCA3	WEE1	MEDLINE	18032919	We demonstrate that this complex, and a second SCF complex containing the F-box protein <span class="match term0">Tome-1</span>, regulate <span class="match term1">wee1</span> degradation during the S and G2 phases of the cell cycle	F-box	1	Training data	H.sapiens
576	CDCA3_HUMAN	CDN1A_HUMAN	Q99618	P38936	CDCA3	CDKN1A	MEDLINE	14761977	Instead, MDM2 promotes <span class="match term1">p21</span> degradation by facilitating binding of <span class="match term1">p21</span> with the proteasomal C8 subunit	F-box	1	Training data	H.sapiens
577	CADH1_HUMAN	AURKA_HUMAN	P12830	O14965	CDH1	AURKA	MEDLINE	32705157	Further studies demonstrated that ID1 competitively binds with anaphase-promoting complex/cyclosome <span class="match term0">Cdh1</span> (APC/CCdh1), which is responsible for ubiquitination-mediated <span class="match term1">AURKA</span> protein degradation, resulting in upregulation of <span class="match term1">AURKA</span>	Other	1	Other	H.sapiens
578	CGRF1_HUMAN	WLS_HUMAN	Q99675	Q5T9L3	CGRRF1	WLS	MEDLINE	29378775	Ubiquitination of <span class="match term1">Evi</span> involves the E2-conjugating enzyme UBE2J2 and the E3-ligase <span class="match term0">CGRRF1</span>	Other	1	Other	H.sapiens
579	CGRF1_HUMAN	EGFR_HUMAN	Q99675	P00533	CGRRF1	EGFR	MEDLINE	31801577	<span class="match term0">CGRRF1</span> ubiquitinates <span class="match term1">EGFR</span> through K48-linked ubiquitination, which leads to proteasome degradation	Other	1	Other	H.sapiens
580	CHFR_HUMAN	HDAC1_HUMAN	Q96EP1	Q13547	CHFR	HDAC1	UniProt	CHFR_HUMAN	Ubiquitinated by <span class="match term0">CHFR</span>, leading to its degradation by the proteasome (By similarity)	RING	1	Training data	H.sapiens
581	CHFR_HUMAN	KIF22_HUMAN	Q96EP1	Q14807	CHFR	KIF22	MEDLINE	19321445	We demonstrated that <span class="match term1">Kif22</span> is a novel substrate of <span class="match term0">Chfr</span>	RING	1	Training data	H.sapiens
582	CHFR_HUMAN	CHFR_HUMAN	Q96EP1	Q96EP1	CHFR	CHFR	MEDLINE	17442268	In fact, USP7 can remove ubiquitin moiety from the autoubiquitinated <span class="match term0">Chfr</span> both in vivo and in vitro, which results in the accumulation of <span class="match term0">Chfr</span> in the cell	RING	1	Training data	H.sapiens
583	CHFR_HUMAN	PLK1_HUMAN	Q96EP1	P53350	CHFR	PLK1	MEDLINE	11807090	The checkpoint protein <span class="match term0">Chfr</span> is a ligase that ubiquitinates <span class="match term1">Plk1</span> and inhibits Cdc2 at the G2 to M transition	RING	1	Training data	H.sapiens
584	CHFR_HUMAN	TOPK_HUMAN	Q96EP1	Q96KB5	CHFR	PBK	MEDLINE	24012691	UbiNet 2.0	RING	1	Training data	H.sapiens
585	CHFR_HUMAN	CHD1L_HUMAN	Q96EP1	Q86WJ1	CHFR	CHD1L	MEDLINE	31322269	PARP1/2 inhibitors were added to identify the ubiquitination of <span class="match term1">ALC1</span> by <span class="match term0">CHFR</span>	RING	1	Other	H.sapiens
586	CHFR_HUMAN	PARP1_HUMAN	Q96EP1	P09874	CHFR	PARP1	MEDLINE	23268447	UbiNet 2.0	RING	1	Training data	H.sapiens
587	CHFR_HUMAN	SNF5_HUMAN	Q96EP1	Q12824	CHFR	SMARCB1	MEDLINE	22285184	UbiNet 2.0	RING	1	Other	H.sapiens
588	CHFR_HUMAN	HLTF_HUMAN	Q96EP1	Q14527	CHFR	HLTF	MEDLINE	20388495	<span class="match term0">CHFR</span> functions as a ubiquitin ligase for <span class="match term1">HLTF</span> to regulate its stability and functions.	RING	1	Other	H.sapiens
589	CHFR_HUMAN	SMCA4_HUMAN	Q96EP1	P51532	CHFR	SMARCA4	MEDLINE	22285184	UbiNet 2.0	RING	1	Other	H.sapiens
590	CHFR_HUMAN	SMRD1_HUMAN	Q96EP1	Q96GM5	CHFR	SMARCD1	MEDLINE	22285184	UbiNet 2.0	RING	1	Other	H.sapiens
591	CHFR_HUMAN	AURKA_HUMAN	Q96EP1	O14965	CHFR	AURKA	MEDLINE	18335050	UbiNet 2.0	RING	1	Training data	H.sapiens
592	CISH_HUMAN	B2L11_HUMAN	Q9NSE2	O43521	CISH	BCL2L11	MEDLINE	19622774	Further analyses revealed that Drg1 promotes degradation of <span class="match term1">Bim</span> through the Cullin2/ElonginB-<span class="match term0">CIS</span> ubiquitin-protein ligase complex	SOCS_VHL_BC-box	1	Training data	H.sapiens
593	CNOT4_HUMAN	YAP1_HUMAN	O95628	P46937	CNOT4	YAP1	MEDLINE	22707721	UbiNet 2.0	RING	1	Training data	H.sapiens
594	CNOT4_HUMAN	RBM15_HUMAN	O95628	Q96T37	CNOT4	RBM15	MEDLINE	26575292	UbiNet 2.0	RING	1	Other	H.sapiens
595	CNOT4_HUMAN	CNOT4_HUMAN	O95628	O95628	CNOT4	CNOT4	MEDLINE	11823428	UbiNet 2.0	RING	1	Training data	H.sapiens
596	CNOT4_HUMAN	KDM5C_HUMAN	O95628	P41229	CNOT4	KDM5C	MEDLINE	19346402	Finally, we show that human <span class="match term0">NOT4</span> can polyubiquitinate human JARID1C/<span class="match term1">SMCX</span>, a homolog of Jhd2, suggesting that this is likely a conserved mechanism	RING	1	Training data	H.sapiens
597	COP1_HUMAN	SOX2_HUMAN	Q8NHY2	P48431	COP1	SOX2	MEDLINE	30405104	Here we show that the RING-finger ubiquitin ligase complex CUL4ADET1-<span class="match term0">COP1</span> and the deubiquitylase OTUD7B govern <span class="match term1">Sox2</span> protein stability during neural progenitor cells (NPCs) differentiation	Other	1	Other	H.sapiens
598	COP1_HUMAN	JUN_HUMAN	Q8NHY2	P05412	COP1	JUN	MEDLINE	12615916	Characterization of human constitutive photomorphogenesis protein 1, a RING finger ubiquitin ligase that interacts with <span class="match term1">Jun</span> transcription factors and modulates their transcriptional activity.	Other	1	Other	H.sapiens
599	COP1_HUMAN	ETV5_HUMAN	Q8NHY2	P41161	COP1	ETV5	MEDLINE	20062082	UbiNet 2.0	Other	1	Other	H.sapiens
600	COP1_HUMAN	ETV4_HUMAN	Q8NHY2	P43268	COP1	ETV4	MEDLINE	20062082	In this study, we report that the <span class="match term1">PEA3</span> group members interact with the mammalian really interesting new gene (RING) E3 ubiquitin ligase constitutive photomorphogenetic 1 (<span class="match term0">COP1</span>), which mediates ubiquitylation and subsequent proteasome degradation of the p53 and c-Jun transcription factors	Other	1	Other	H.sapiens
601	COP1_HUMAN	MTA1_HUMAN	Q8NHY2	Q13330	COP1	MTA1	MEDLINE	19805145	E3 ubiquitin ligase <span class="match term0">COP1</span> regulates the stability and functions of <span class="match term1">MTA1</span>.	Other	1	Other	H.sapiens
602	COP1_HUMAN	CTNB1_HUMAN	Q8NHY2	P35222	COP1	CTNNB1	MEDLINE	25311538	UbiNet 2.0	Other	1	Other	H.sapiens
603	COP1_HUMAN	P53_HUMAN	Q8NHY2	P04637	COP1	TP53	MEDLINE	15103385	Moreover, <span class="match term0">COP1</span> serves as an E3 ubiquitin ligase for <span class="match term1">p53</span> in vitro and in vivo, and inhibits <span class="match term1">p53</span>-dependent transcription and apoptosis	Other	1	Other	H.sapiens
604	COP1_HUMAN	TCPD_HUMAN	Q8NHY2	P50991	COP1	CCT4	MEDLINE	24298020	UbiNet 2.0	Other	1	Other	H.sapiens
605	COP1_HUMAN	CDN1B_HUMAN	Q8NHY2	P46527	COP1	CDKN1B	MEDLINE	26254224	<span class="match term0">COP1</span> enhances ubiquitin-mediated degradation of <span class="match term1">p27Kip1</span> to promote cancer cell growth	Other	1	Other	H.sapiens
606	COP1_HUMAN	ACACA_HUMAN	Q8NHY2	Q13085	COP1	ACACA	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
607	COP1_HUMAN	DCTN6_HUMAN	Q8NHY2	O00399	COP1	DCTN6	MEDLINE	33968945	Further exploration unveiled that <span class="match term0">RFWD2</span> meditated <span class="match term1">P27</span> ubiquitination via interacting with RCHY1, which served as an E3 ubiquitin ligase of <span class="match term1">P27</span>	Other	1	Other	H.sapiens
608	COP1_HUMAN	STAT3_HUMAN	Q8NHY2	P40763	COP1	STAT3	MEDLINE	27820701	We found that miR-424 targets the E3 ubiquitin ligase <span class="match term0">COP1</span> and identified <span class="match term1">STAT3</span> as a key substrate of <span class="match term0">COP1</span> in promoting tumorigenic and cancer stem-like properties in prostate epithelial cells	Other	1	Other	H.sapiens
609	COP1_HUMAN	FOXO4_HUMAN	Q8NHY2	P98177	COP1	FOXO4	MEDLINE	33101846	Mechanistic studies show that CSN6 binds and regulates <span class="match term1">FOXO4</span> stability through enhancing the E3 ligase activity of <span class="match term0">COP1</span>, and that <span class="match term0">COP1</span> directly interacts with <span class="match term1">FOXO4</span> through a VP motif on <span class="match term1">FOXO4</span> and accelerates the ubiquitin-mediated degradation of <span class="match term1">FOXO4</span>	Other	1	Other	H.sapiens
610	COP1_HUMAN	1433S_HUMAN	Q8NHY2	P31947	COP1	SFN	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
611	COP1_HUMAN	SIR1_HUMAN	Q8NHY2	Q96EB6	COP1	SIRT1	MEDLINE	31125554	<span class="match term0">COP1</span> was a new E3 ubiquitin ligase for <span class="match term1">SIRT1</span>.	Other	1	Other	H.sapiens
612	COP1_HUMAN	CRTC1_HUMAN	Q8NHY2	Q6UUV9	COP1	CRTC1	MEDLINE	29408765	Finally, SIK1-induced ubiquitination of <span class="match term1">CRTC1</span> was mediated by <span class="match term0">RFWD2</span> ubiquitin ligase at a site not equivalent to K628 in CRTC2	Other	1	Other	H.sapiens
613	COP1_HUMAN	ETV1_HUMAN	Q8NHY2	P50549	COP1	ETV1	MEDLINE	20062082	UbiNet 2.0	Other	1	Other	H.sapiens
614	COP1_HUMAN	5NTD_HUMAN	Q8NHY2	P21589	COP1	NT5E	MEDLINE	33168024	CONCLUSIONS: MiR-340-5p promoted CD8+ T-TIL infiltration and antitumor function by regulating KMT5A and <span class="match term0">COP1</span> and further activating <span class="match term1">CD73</span> ubiquitination	Other	1	Other	H.sapiens
615	COP1_HUMAN	MMP1_HUMAN	Q8NHY2	P03956	COP1	MMP1	MEDLINE	12615916	UbiNet 2.0	Other	1	Training data	H.sapiens
616	COP1_HUMAN	COP1_HUMAN	Q8NHY2	Q8NHY2	COP1	COP1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
617	COP1_HUMAN	ACACB_HUMAN	Q8NHY2	O00763	COP1	ACACB	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
618	COP1_HUMAN	CRTC2_HUMAN	Q8NHY2	Q53ET0	COP1	CRTC2	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
619	CRBN_HUMAN	CRBN_HUMAN	Q96SW2	Q96SW2	CRBN	CRBN	MEDLINE	30836149:31157769	30836149:31157769	SINGLE_OTHER	1	Other	H.sapiens
620	CRBN_HUMAN	SALL4_HUMAN	Q96SW2	Q9UJQ4	CRBN	SALL4	MEDLINE	32071327	Thalidomide binding to <span class="match term0">CRBN</span> elicits subsequent ubiquitination and proteasomal degradation of <span class="match term0">CRBN</span> neosubstrates including <span class="match term1">SALL4</span>, a transcription factor of which polymorphisms phenocopy thalidomide-induced limb defects in humans	SINGLE_OTHER	1	Other	H.sapiens
621	CRBN_HUMAN	IKZF3_HUMAN	Q96SW2	Q9UKT9	CRBN	IKZF3	MEDLINE	29496670	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
622	CRBN_HUMAN	TAU_HUMAN	Q96SW2	P10636	CRBN	MAPT	MEDLINE	30907729	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
623	CRBN_HUMAN	IKZF1_HUMAN	Q96SW2	Q13422	CRBN	IKZF1	MEDLINE	24292625	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
624	CRBN_HUMAN	P63_HUMAN	Q96SW2	Q9H3D4	CRBN	TP63	MEDLINE	31591562	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
625	-	WIPI2_HUMAN	-	Q9Y4P8	CRL4A	WIPI2	MEDLINE	30898011	Suppression of autophagy during mitosis via CUL4-RING ubiquitin ligases-mediated <span class="match term1">WIPI2</span> polyubiquitination and proteasomal degradation.	Other	1	Other	H.sapiens
626	DCAF1_HUMAN	LATS2_HUMAN	Q9Y4B6	Q9NRM7	DCAF1	LATS2	MEDLINE	25026211	UbiNet 2.0	Other	1	Other	H.sapiens
627	DCAF1_HUMAN	KTNA1_HUMAN	Q9Y4B6	O75449	DCAF1	KATNA1	MEDLINE	19287380	UbiNet 2.0	Other	1	Other	H.sapiens
628	DCAF1_HUMAN	2AAA_HUMAN	Q9Y4B6	P30153	DCAF1	PPP2R1A	MEDLINE	25720411	UbiNet 2.0	Other	1	Other	H.sapiens
629	DCAF1_HUMAN	UNG_HUMAN	Q9Y4B6	P13051	DCAF1	UNG	MEDLINE	20870715	HIV-1 Vpr loads uracil DNA glycosylase-2 onto <span class="match term0">DCAF1</span>, a substrate recognition subunit of a cullin 4A-ring E3 ubiquitin ligase for proteasome-dependent degradation	Other	1	Other	H.sapiens
630	DCAF1_HUMAN	TERT_HUMAN	Q9Y4B6	O14746	DCAF1	TERT	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
631	DCAF1_HUMAN	MCM10_HUMAN	Q9Y4B6	Q7L590	DCAF1	MCM10	MEDLINE	22570418	CRL4-DDB1-<span class="match term0">VPRBP</span> ubiquitin ligase mediates the stress triggered proteolysis of <span class="match term1">Mcm10</span>	Other	1	Other	H.sapiens
632	DCAF1_HUMAN	SAMH1_HUMAN	Q9Y4B6	Q9Y3Z3	DCAF1	SAMHD1	MEDLINE	23677995	HIV-2 and simian immunodeficiency virus (SIV) counteract this restriction via a virion-associated virulence accessory factor, Vpx (Vpr in some SIVs), which loads <span class="match term1">SAMHD1</span> onto CRL4-<span class="match term0">DCAF1</span> E3 ubiquitin ligase for polyubiquitination, programming it for proteasome-dependent degradation	Other	1	Other	H.sapiens
633	DCAF1_HUMAN	LATS1_HUMAN	Q9Y4B6	O95835	DCAF1	LATS1	MEDLINE	25026211	UbiNet 2.0	Other	1	Other	H.sapiens
634	DCA11_HUMAN	TIF1B_HUMAN	Q8TEB1	Q13263	DCAF11	TRIM28	MEDLINE	29440432	<span class="match term0">Dcaf11</span> targets <span class="match term1">Kap1</span> for ubiquitination-mediated degradation	DWD	1	Other	H.sapiens
635	DCA11_HUMAN	PB2_I33A0	Q8TEB1	P03427	DCAF11	PB2	MEDLINE	32265326	UbiNet 2.0	DWD	1	Other	H.sapiens
636	DCA11_HUMAN	NF2L2_HUMAN	Q8TEB1	Q16236	DCAF11	NFE2L2	MEDLINE	31586112	TFEB activates <span class="match term1">Nrf2</span> by repressing its E3 ubiquitin ligase <span class="match term0">DCAF11</span> and promoting phosphorylation of p62	DWD	1	Other	H.sapiens
637	DCA11_HUMAN	GEN_HUMAN	Q8TEB1	Q17RS7	DCAF11	GEN1	MEDLINE	31409866	UbiNet 2.0	DWD	1	Other	H.sapiens
638	DCA12_HUMAN	MAGA3_HUMAN	Q5T6F0	P43357	DCAF12	MAGEA3	MEDLINE	31267705	Proteomic analysis reveals that degradation of MAGE-A3/6 is controlled by the CRL4-<span class="match term0">DCAF12</span> E3 ubiquitin ligase	DWD	1	Other	H.sapiens
639	DCA12_HUMAN	MAGA6_HUMAN	Q5T6F0	P43360	DCAF12	MAGEA6	MEDLINE	31267705	Regulation of MAGE-A3/6 by the CRL4-<span class="match term0">DCAF12</span> ubiquitin ligase and nutrient availability.	DWD	1	Other	H.sapiens
640	DC121_HUMAN	PB2_I33A0	Q5VU92	P03427	DCAF12L1	PB2	MEDLINE	32265326	UbiNet 2.0	Other	1	Other	H.sapiens
641	DCA15_HUMAN	RBM39_HUMAN	Q66K64	Q14498	DCAF15	RBM39	MEDLINE	31819272	Indisulam promotes an interaction between <span class="match term1">RBM39</span> and the <span class="match term0">DCAF15</span> E3 ligase substrate receptor, leading to <span class="match term1">RBM39</span> ubiquitination and proteasome-mediated degradation	Other	1	Other	H.sapiens
642	DCA16_HUMAN	SPIN4_HUMAN	Q9NXF7	Q56A73	DCAF16	SPIN4	MEDLINE	33636084	<span class="match term1">SPIN4</span> Is a Principal Endogenous Substrate of the E3 Ubiquitin Ligase <span class="match term0">DCAF16</span>	Other	1	Other	H.sapiens
643	DCAF4_HUMAN	OPTN_HUMAN	Q8WV16	Q96CV9	DCAF4	OPTN	MEDLINE	32014991	Of note, we found that <span class="match term0">DCAF4</span> mediates the ubiquitination of an ALS-associated protein and autophagy receptor, optineurin (<span class="match term1">OPTN</span>), and facilitates autophagic degradation of DBR-exposed SOD1	DWD	1	Other	H.sapiens
644	DCAF4_HUMAN	ST7_HUMAN	Q8WV16	Q9NRC1	DCAF4	ST7	MEDLINE	30945288	In vitro and in vivo ubiquitination analyses indicate that CRL4DCAF4 E3 ligase specifically directs degradation of <span class="match term1">ST7</span> (suppression of tumorigenicity 7)	DWD	1	Other	H.sapiens
645	DCAF8_HUMAN	MLF2_HUMAN	Q5TAQ9	Q15773	DCAF8	MLF2	MEDLINE	32703400	<span class="match term0">DCAF8</span> could promote <span class="match term1">MLF2</span> degradation through the ubiquitin-proteasome pathway	DWD	1	Other	H.sapiens
646	DDB1_HUMAN	NR5A2_HUMAN	Q16531	O00482	DDB1	NR5A2	MEDLINE	30923324	UbiNet 2.0	Other	1	Other	H.sapiens
647	DDB1_HUMAN	CSN5_HUMAN	Q16531	Q92905	DDB1	COPS5	MEDLINE	23357576	UbiNet 2.0	Other	1	Other	H.sapiens
648	DDB1_HUMAN	P73_HUMAN	Q16531	O15350	DDB1	TP73	MEDLINE	23085759	The Cul4A-<span class="match term0">DDB1</span> E3 ubiquitin ligase complex represses <span class="match term1">p73</span> transcriptional activity	Other	1	Other	H.sapiens
649	DDB1_HUMAN	CCNK_HUMAN	Q16531	O75909	DDB1	CCNK	MEDLINE	32494016	UbiNet 2.0	Other	1	Other	H.sapiens
650	DDB2_HUMAN	XPC_HUMAN	Q92466	Q01831	DDB2	XPC	MEDLINE	19481525	Here we demonstrate that the CUL4A ubiquitin ligase restricts the cellular repair capacity by orchestrating the concerted actions of nucleotide excision repair (NER) and the DNA damage-responsive G1/S checkpoint through selective degradation of the <span class="match term0">DDB2</span> and <span class="match term1">XPC</span> DNA damage sensors and the p21/CIP1/WAF1 checkpoint effector	DWD	1	Training data	H.sapiens
651	DDB2_HUMAN	DDB2_HUMAN	Q92466	Q92466	DDB2	DDB2	MEDLINE	18936169	UbiNet 2.0	DWD	1	Training data	H.sapiens
652	DDB2_HUMAN	H2A1A_HUMAN	Q92466	Q96QV6	DDB2	HIST1H2AA	MEDLINE	18593899	We previously showed that DDB1-CUL4ADDB2 ubiquitinates histone H2A at the sites of UV lesions in a <span class="match term0">DDB2</span>-dependent manner.	DWD	1	Training data	H.sapiens
653	DDB2_HUMAN	H2A1_HUMAN	Q92466	P0C0S8	DDB2	H2AC11	MEDLINE	18593899	UbiNet 2.0	DWD	1	Training data	H.sapiens
654	DDB2_HUMAN	DTL_HUMAN	Q92466	Q9NZJ0	DDB2	DTL	MEDLINE	33557942	In vivo ubiquitination assay was carried out to clarify the ubiquitination of <span class="match term1">CDT2</span> mediated by <span class="match term0">DDB2</span>	DWD	1	Other	H.sapiens
655	DDX58_HUMAN	MARH5_HUMAN	O95786	Q9NX47	DDX58	MARCHF5	MEDLINE	31881323	In an in vivo ubiquitination assay, <span class="match term1">MARCH5</span> transfers the Lys 48-linked polyubiquitin to Lys 193 and 203 residues of <span class="match term0">RIG-I</span>	Other	1	Other	H.sapiens
656	DET1_HUMAN	MTA1_HUMAN	Q7L5Y6	Q13330	DET1	MTA1	MEDLINE	19805145	UbiNet 2.0	Other	1	Training data	H.sapiens
657	DET1_HUMAN	ACACA_HUMAN	Q7L5Y6	Q13085	DET1	ACACA	MEDLINE	16794074	UbiNet 2.0	Other	1	Training data	H.sapiens
658	DET1_HUMAN	JUN_HUMAN	Q7L5Y6	P05412	DET1	JUN	MEDLINE	14739464	UbiNet 2.0	Other	1	Training data	H.sapiens
659	DET1_HUMAN	ACACB_HUMAN	Q7L5Y6	O00763	DET1	ACACB	MEDLINE	16794074	UbiNet 2.0	Other	1	Training data	H.sapiens
660	DET1_HUMAN	FOXO1_HUMAN	Q7L5Y6	Q12778	DET1	FOXO1	MEDLINE	18815134	UbiNet 2.0	Other	1	Training data	H.sapiens
661	DET1_HUMAN	P53_HUMAN	Q7L5Y6	P04637	DET1	TP53	MEDLINE	17968316	UbiNet 2.0	Other	1	Training data	H.sapiens
662	DET1_HUMAN	CRTC2_HUMAN	Q7L5Y6	Q53ET0	DET1	CRTC2	MEDLINE	17805301	UbiNet 2.0	Other	1	Training data	H.sapiens
663	DET1_HUMAN#COP1_HUMAN	ACACB_HUMAN	Q7L5Y6#Q8NHY2	O00763	DET1#COP1	ACACB	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
664	DET1_HUMAN#COP1_HUMAN	CRTC2_HUMAN	Q7L5Y6#Q8NHY2	Q53ET0	DET1#COP1	CRTC2	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
665	DET1_HUMAN#COP1_HUMAN	MTA1_HUMAN	Q7L5Y6#Q8NHY2	Q13330	DET1#COP1	MTA1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
666	DET1_HUMAN#COP1_HUMAN	ACACA_HUMAN	Q7L5Y6#Q8NHY2	Q13085	DET1#COP1	ACACA	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
667	DET1_HUMAN#COP1_HUMAN	FOXO1_HUMAN	Q7L5Y6#Q8NHY2	Q12778	DET1#COP1	FOXO1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
668	DET1_HUMAN#COP1_HUMAN	JUN_HUMAN	Q7L5Y6#Q8NHY2	P05412	DET1#COP1	JUN	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
669	DET1_HUMAN#COP1_HUMAN	P53_HUMAN	Q7L5Y6#Q8NHY2	P04637	DET1#COP1	TP53	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
670	DTL_HUMAN	CDN1A_HUMAN	Q9NZJ0	P38936	DTL	CDKN1A	UniProt	DTL_HUMAN	The DCX(<span class="match term0">DTL</span>) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of cdt1 and <span class="match term1">cdkn1a</span>/p21(cip1)	DWD	1	Training data	H.sapiens
671	DTL_HUMAN	FBH1_HUMAN	Q9NZJ0	Q8NFZ0	DTL	FBH1	MEDLINE	22199232	E3Net	DWD	1	Other	H.sapiens
672	DTL_HUMAN	PDCD4_HUMAN	Q9NZJ0	Q53EL6	DTL	PDCD4	MEDLINE	31409387	Through in vitro ubiquitination experiment, we proved that <span class="match term1">PDCD4</span> was degraded by <span class="match term0">DTL</span> through ubiquitination	DWD	1	Other	H.sapiens
673	DTL_HUMAN	PCNA_HUMAN	Q9NZJ0	P12004	DTL	PCNA	MEDLINE	20129063	UbiNet 2.0	DWD	1	Other	H.sapiens
674	DTL_HUMAN	CDT1_HUMAN	Q9NZJ0	Q9H211	DTL	CDT1	UniProt	DTL_HUMAN	DCX(<span class="match term0">DTL</span>) plays a role in PCNA-dependent polyubiquitination of <span class="match term1">CDT1</span> and MDM2-dependent ubiquitiantion of TP53 in response to radiation-induced DNA damage and during DNA replication	DWD	1	Training data	H.sapiens
675	DTL_HUMAN	A4F535_HBV	Q9NZJ0	A4F535	DTL	P	MEDLINE	30775435	UbiNet 2.0	DWD	1	Other	H.sapiens
676	DTL_HUMAN	DPOD4_HUMAN	Q9NZJ0	Q9HCU8	DTL	POLD4	MEDLINE	24022480	CRL4(<span class="match term0">Cdt2</span>) is an E3 ligase that ubiquitinates and degrades <span class="match term1">p12</span> after UV treatment	DWD	1	Other	H.sapiens
677	DTL_HUMAN	KMT5A_HUMAN	Q9NZJ0	Q9NQR1	DTL	KMT5A	MEDLINE	21035370	UbiNet 2.0	DWD	1	Training data	H.sapiens
678	DTL_HUMAN	P53_HUMAN	Q9NZJ0	P04637	DTL	TP53	UniProt	DTL_HUMAN	DCX(<span class="match term0">DTL</span>) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitiantion of <span class="match term1">TP53</span> in response to radiation-induced DNA damage and during DNA replication	DWD	1	Training data	H.sapiens
679	DTL_HUMAN	CDC6_HUMAN	Q9NZJ0	Q99741	DTL	CDC6	MEDLINE	24434580	UbiNet 2.0	DWD	1	Other	H.sapiens
680	DTL_HUMAN	ERCC5_HUMAN	Q9NZJ0	P28715	DTL	ERCC5	MEDLINE	25483071	UbiNet 2.0	DWD	1	Other	H.sapiens
681	DTL_HUMAN	CHK1_HUMAN	Q9NZJ0	O14757	DTL	CHEK1	MEDLINE	23533280	UbiNet 2.0	DWD	1	Other	H.sapiens
682	DTL_HUMAN	CRY1_HUMAN	Q9NZJ0	Q16526	DTL	CRY1	MEDLINE	26431207	UbiNet 2.0	DWD	1	Other	H.sapiens
683	DTL_HUMAN	SDE2_HUMAN	Q9NZJ0	Q6IQ49	DTL	SDE2	MEDLINE	27906959	UbiNet 2.0	DWD	1	Other	H.sapiens
684	DTL_HUMAN	TDG_HUMAN	Q9NZJ0	Q13569	DTL	TDG	MEDLINE	24962565	Thus physical interaction of <span class="match term1">TDG</span> with PCNA through the PIP degron is required for targeting <span class="match term1">TDG</span> to the CRL4(<span class="match term0">Cdt2</span>) E3 ubiquitin ligase complex	DWD	1	Other	H.sapiens
685	DTL_HUMAN	KAT2A_HUMAN	Q9NZJ0	Q92830	DTL	KAT2A	MEDLINE	21987584	UbiNet 2.0	DWD	1	Other	H.sapiens
686	DTL_HUMAN	POLH_HUMAN	Q9NZJ0	Q9Y253	DTL	POLH	MEDLINE	29208956	UbiNet 2.0	DWD	1	Other	H.sapiens
687	DTX1_HUMAN	M3K1_HUMAN	Q86Y01	Q13233	DTX1	MAP3K1	MEDLINE	9590294	UbiNet 2.0	RING	1	Training data	H.sapiens
688	DTX1_HUMAN	DTX1_HUMAN	Q86Y01	Q86Y01	DTX1	DTX1	MEDLINE	12670957	hUbiquitome	RING	1	Other	H.sapiens
689	DTX2_HUMAN	DTX2_HUMAN	Q86UW9	Q86UW9	DTX2	DTX2	MEDLINE	12670957	hUbiquitome	RING	1	Other	H.sapiens
690	DTX3_HUMAN	NOTC2_HUMAN	Q8N9I9	Q04721	DTX3	NOTCH2	MEDLINE	31854042	Ubiquitination of <span class="match term1">NOTCH2</span> by <span class="match term0">DTX3</span> suppresses the proliferation and migration of human esophageal carcinoma	RING	1	Other	H.sapiens
691	DTX3_HUMAN	XRCC5_HUMAN	Q8N9I9	P13010	DTX3	XRCC5	MEDLINE	33403043	Moreover, <span class="match term0">DTX3</span> was proved to be co-localized with <span class="match term1">XRCC5</span> in nucleus and promote ubiquitination of <span class="match term1">XRCC5</span>	RING	1	Other	H.sapiens
692	DTX3_HUMAN	DTX3_HUMAN	Q8N9I9	Q8N9I9	DTX3	DTX3	MEDLINE	12670957	hUbiquitome	RING	1	Other	H.sapiens
693	DTX3L_HUMAN	H2B1J_HUMAN	Q8TDB6	P06899	DTX3L	H2BC11	MEDLINE	26479788	UbiNet 2.0	RING	1	Other	H.sapiens
694	DTX3L_HUMAN	H4_HUMAN	Q8TDB6	P62805	DTX3L	H4C1	MEDLINE	19818714	UbiNet 2.0	RING	1	Training data	H.sapiens
695	DTX3L_HUMAN	DUS14_HUMAN	Q8TDB6	Q13501	DTX3L	HIST1H2BJ	MEDLINE	26479788	26479788	RING	1	Other	H.sapiens
696	DTX3L_HUMAN	DTX3L_HUMAN	Q8TDB6	Q8TDB6	DTX3L	DTX3L	MEDLINE	12670957	hUbiquitome	RING	1	Other	H.sapiens
697	DTX4_HUMAN	TBK1_HUMAN	Q9Y2E6	Q9UHD2	DTX4	TBK1	MEDLINE	22388039	UbiNet 2.0	RING	1	Training data	H.sapiens
698	DYRK2_HUMAN	TERT_HUMAN	Q92630	O14746	DYRK2	TERT	MEDLINE	23362280	<span class="match term0">Dyrk2</span>-associated EDD-DDB1-VprBP E3 ligase inhibits telomerase by <span class="match term1">TERT</span> degradation.	Other	1	Other	H.sapiens
699	DZIP3_HUMAN	ATX1_HUMAN	Q86Y13	P54253	DZIP3	ATXN1	MEDLINE	24326307	HOTAIR associates with E3 ubiquitin ligases bearing RNA-binding domains, <span class="match term0">Dzip3</span> and Mex3b, as well as with their respective ubiquitination substrates, Ataxin-1 and Snurportin-1	RING	1	Other	H.sapiens
700	DZIP3_HUMAN	H2A1B_HUMAN	Q86Y13	P04908	DZIP3	H2AC4	MEDLINE	18206970	UbiNet 2.0	RING	1	Other	H.sapiens
701	DZIP3_HUMAN	Q08AJ9_HUMAN	Q86Y13	Q08AJ9	DZIP3	HIST1H2AB	MEDLINE	18206970	18206970	RING	1	Other	H.sapiens
702	E4F1_HUMAN	P53_HUMAN	Q66K89	P04637	E4F1	TP53	MEDLINE	17110336	<span class="match term0">E4F1</span> stimulates oligo-ubiquitylation in the hinge region of <span class="match term1">p53</span> on lysine residues distinct from those targeted by Hdm2 and previously described to be acetylated by the acetyltransferase PCAF	HECT	1	Training data	H.sapiens
703	EP300_HUMAN	P53_HUMAN	Q09472	P04637	EP300	TP53	MEDLINE	12690203	Polyubiquitination of <span class="match term1">p53</span> by a ubiquitin ligase activity of <span class="match term0">p300</span>	HECT	1	Training data	H.sapiens
704	EP300_HUMAN	E2F1_HUMAN	Q09472	Q01094	EP300	E2F1	MEDLINE	15917652	Finally, <span class="match term0">p300</span>-induced <span class="match term1">E2F-1</span> ubiquitination is not influenced by RB	HECT	1	Training data	H.sapiens
705	ES8L3_HUMAN	SNAI2_HUMAN	Q8TE67	O43623	EPS8L3	SNAI2	MEDLINE	32943576	We performed a dual-luciferase-based, genome-wide E3 ligase siRNA library screen and identified ASB13 as an E3 ubiquitin ligase that targets <span class="match term1">SNAI2</span> for ubiquitination and degradation	Other	1	Other	H.sapiens
706	ERCC8_HUMAN	ERPG3_HUMAN	Q13216	P0DP91	ERCC8	ERCC6	MEDLINE	22199232	E3Net	DWD	1	Other	H.sapiens
707	ERCC8_HUMAN	ERCC6_HUMAN	Q13216	Q03468	ERCC8	ERCC6	MEDLINE	16751180	<span class="match term0">CSA</span>-dependent degradation of <span class="match term1">CSB</span> by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome	DWD	1	Training data	H.sapiens
708	FA12_HUMAN	HIF1A_HUMAN	P00748	Q16665	F12	HIF1A	MEDLINE	18838541	UbiNet 2.0	Other	1	Other	H.sapiens
709	FAF2_HUMAN	NF1_HUMAN	Q96CS3	P21359	FAF2	NF1	MEDLINE	20160012	UbiNet 2.0	Other	1	Other	H.sapiens
710	FANCL_HUMAN	FACD2_HUMAN	Q9NW38	Q9BXW9	FANCL	FANCD2	MEDLINE	16201245	A novel protein <span class="match term0">FANCL</span> is a component of the nuclear FA complex, functioned as an ubiquitin E3 ligase and monoubiquitinylated <span class="match term1">FANCD2</span>	RING	1	Training data	H.sapiens
711	FANCL_HUMAN	FANCI_HUMAN	Q9NW38	Q9NVI1	FANCL	FANCI	MEDLINE	20937699	A key event in FA pathway activation is the monoubiquitylation of the FA complementation group I (<span class="match term1">FANCI</span>)-FANCD2 (ID) complex by FA complementation group L (<span class="match term0">FANCL</span>), an E3 ubiquitin ligase	RING	1	Training data	H.sapiens
712	FANCL_HUMAN	CTNB1_HUMAN	Q9NW38	P35222	FANCL	CTNNB1	MEDLINE	22653977	UbiNet 2.0	RING	1	Training data	H.sapiens
713	FBH1_HUMAN	RAD51_HUMAN	Q8NFZ0	Q06609	FBH1	RAD51	MEDLINE	25585578	<span class="match term0">FBH1</span>?influences DNA replication fork stability and homologous recombination through ubiquitylation of?<span class="match term1">RAD51</span>.	Other	1	Other	H.sapiens
714	FBH1_HUMAN	ARF1_HUMAN	Q8NFZ0	P84077	FBH1	ARF1	MEDLINE	24658274	UbiNet 2.0	Other	1	Other	H.sapiens
715	FXL12_HUMAN	CDN1C_HUMAN	Q9NXK8	P49918	FBXL12	CDKN1C	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
716	FXL12_HUMAN	XRCC5_HUMAN	Q9NXK8	P13010	FBXL12	XRCC5	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
717	FXL12_HUMAN	KKCC2_HUMAN	Q9NXK8	Q96RR4	FBXL12	CAMKK2	MEDLINE	23707388	UbiNet 2.0	F-box	1	Other	H.sapiens
718	FXL12_HUMAN	KCC1A_HUMAN	Q9NXK8	Q14012	FBXL12	CAMK1	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
719	FXL12_HUMAN	AL3A1_HUMAN	Q9NXK8	P30838	FBXL12	ALDH3A1	MEDLINE	26124079	<span class="match term0">FBXL12</span>-Mediated Degradation of <span class="match term1">ALDH3</span> is Essential for Trophoblast Differentiation During Placental Development.	F-box	1	Other	H.sapiens
720	FXL14_HUMAN	TWST1_HUMAN	Q8N1E6	Q15672	FBXL14	TWIST1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
721	FXL14_HUMAN	CDCP1_HUMAN	Q8N1E6	Q9H5V8	FBXL14	CDCP1	MEDLINE	29973690	<span class="match term0">FBXL14</span> acts as an novel interaction partner of <span class="match term1">CDCP1</span>, and facilitates its ubiquitination and proteasomal degradation with an enhanced capacity to suppress <span class="match term1">CDCP1</span> protein stability that eventually prevents <span class="match term1">CDCP1</span> target genes involved in breast cancer metastasis	F-box	1	Other	H.sapiens
722	FXL14_HUMAN	SNAI2_HUMAN	Q8N1E6	O43623	FBXL14	SNAI2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
723	FXL14_HUMAN	SNAI1_HUMAN	Q8N1E6	O95863	FBXL14	SNAI1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
724	FXL14_HUMAN	DUS6_HUMAN	Q8N1E6	Q16828	FBXL14	DUSP6	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
725	FXL15_HUMAN	SMUF2_HUMAN	Q9H469	Q9HAU4	FBXL15	SMURF2	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
726	FXL15_HUMAN	SMUF1_HUMAN	Q9H469	Q9HCE7	FBXL15	SMURF1	MEDLINE	21572392	UbiNet 2.0	F-box	1	Training data	H.sapiens
727	FXL15_HUMAN	WWP2_HUMAN	Q9H469	O00308	FBXL15	WWP2	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
728	FXL17_HUMAN	FANCJ_HUMAN	Q9UF56	Q9BX63	FBXL17	BRIP1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
729	FXL17_HUMAN	BACH1_HUMAN	Q9UF56	O14867	FBXL17	BACH1	MEDLINE	PMC4306233	PMC4306233	F-box	1	Other	H.sapiens
730	FXL17_HUMAN	SUFU_HUMAN	Q9UF56	Q9UMX1	FBXL17	SUFU	MEDLINE	27234298	SCF (<span class="match term0">Fbxl17</span>) ubiquitylation of <span class="match term1">Sufu</span> regulates Hedgehog signaling and medulloblastoma development.	F-box	1	Other	H.sapiens
731	FXL18_HUMAN	FBXL7_HUMAN	Q96ME1	Q9UJT9	FBXL18	FBXL7	MEDLINE	25654763	F-box protein <span class="match term0">Fbxl18</span> mediates polyubiquitylation and proteasomal degradation of the pro-apoptotic SCF subunit <span class="match term1">Fbxl7</span>.	F-box	1	Other	H.sapiens
732	FXL19_HUMAN	CDC42_HUMAN	Q6PCT2	P60953	FBXL19	CDC42	MEDLINE	29522376	Further, we demonstrate that <span class="match term0">FBXL19</span> targets small GTPase <span class="match term1">Cdc42</span> for its ubiquitination and degradation, whereas this effect is reversed by inhibition of CBP, suggesting that CBP increases the effect of SCF <span class="match term0">FBXL19</span> E3 ligase through acetylation and stabilization of <span class="match term0">FBXL19</span>	F-box	1	Other	H.sapiens
733	FXL19_HUMAN	RAC1_HUMAN	Q6PCT2	P63000	FBXL19	RAC1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
734	FXL19_HUMAN	ILRL1_HUMAN	Q6PCT2	Q01638	FBXL19	IL1RL1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
735	FXL19_HUMAN	NKX21_HUMAN	Q6PCT2	P43699	FBXL19	NKX2-1	MEDLINE	31238008	Overexpression of ubiquitin E3 ligase subunit <span class="match term0">FBXL19</span> increased <span class="match term1">TTF1</span> ubiquitination and degradation in FTC133 cells, but it had no effect on <span class="match term1">TTF1</span> levels in Htori3 cells	F-box	1	Other	H.sapiens
736	FXL19_HUMAN	RHOA_HUMAN	Q6PCT2	P61586	FBXL19	RHOA	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
737	FBXL2_HUMAN	P85B_HUMAN	Q9UKC9	O00459	FBXL2	PIK3R2	MEDLINE	23604317	UbiNet 2.0	F-box	1	Other	H.sapiens
738	FBXL2_HUMAN	NLRP3_HUMAN	Q9UKC9	Q96P20	FBXL2	NLRP3	MEDLINE	26037928	<span class="match term0">FBXL2</span> recognizes Trp-73 within <span class="match term1">NALP3</span> for interaction and targets Lys-689 within <span class="match term1">NALP3</span> for ubiquitin ligation and degradation	F-box	1	Other	H.sapiens
739	FBXL2_HUMAN	ITPR3_HUMAN	Q9UKC9	Q14573	FBXL2	ITPR3	MEDLINE	30355490	<span class="match term0">FBXL2</span> targets <span class="match term1">IP3R3</span> for ubiquitin-mediated degradation to limit Ca2+ flux to mitochondria and, consequently, apoptosis	F-box	1	Other	H.sapiens
740	FBXL2_HUMAN	AURKB_HUMAN	Q9UKC9	Q96GD4	FBXL2	AURKB	MEDLINE	23370391	UbiNet 2.0	F-box	1	Other	H.sapiens
741	FBXL2_HUMAN	CCND3_HUMAN	Q9UKC9	P30281	FBXL2	CCND3	MEDLINE	22024926	UbiNet 2.0	F-box	1	Training data	H.sapiens
742	FBXL2_HUMAN	CCND2_HUMAN	Q9UKC9	P30279	FBXL2	CCND2	MEDLINE	22323446	F-box protein <span class="match term0">FBXL2</span> targets cyclin D2 for ubiquitination and degradation to inhibit leukemic cell proliferation.	F-box	1	Other	H.sapiens
743	FBXL2_HUMAN	FOXM1_HUMAN	Q9UKC9	Q08050	FBXL2	FOXM1	MEDLINE	31679690	We found that <span class="match term0">FBXL2</span> ubiquitinated <span class="match term1">FOXM1</span>, and the interaction with <span class="match term0">FBXL2</span> and ubiquitination of <span class="match term1">FOXM1</span> were reduced by TMG in NUGC-3 cells	F-box	1	Other	H.sapiens
744	FBXL2_HUMAN	PCY1A_HUMAN	Q9UKC9	P49585	FBXL2	PCYT1A	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
745	FBXL2_HUMAN	A4_HUMAN	Q9UKC9	P05067	FBXL2	APP	MEDLINE	22399757	<span class="match term0">FBL2</span> regulates amyloid precursor protein (<span class="match term1">APP</span>) metabolism by promoting ubiquitination-dependent <span class="match term1">APP</span> degradation and inhibition of <span class="match term1">APP</span> endocytosis.	F-box	1	Other	H.sapiens
746	FXL21_HUMAN	CRY2_HUMAN	Q9UKT6	Q49AN0	FBXL21P	CRY2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
747	FXL21_HUMAN	CRY1_HUMAN	Q9UKT6	Q16526	FBXL21P	CRY1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
748	FXL22_HUMAN	FLNC_HUMAN	Q6P050	Q14315	FBXL22	FLNC	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
749	FXL22_HUMAN	ACTN2_HUMAN	Q6P050	P35609	FBXL22	ACTN2	MEDLINE	22972877	UbiNet 2.0	F-box	1	Other	H.sapiens
750	FBXL3_HUMAN	CRY2_HUMAN	Q9UKT7	Q49AN0	FBXL3	CRY2	MEDLINE	17463251	UbiNet 2.0	F-box	1	Training data	H.sapiens
751	FBXL3_HUMAN	CRY1_HUMAN	Q9UKT7	Q16526	FBXL3	CRY1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
752	FBXL3_HUMAN	CYAA_YEAST	Q9UKT7	P08678	FBXL3	CYR1	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
753	FBXL4_HUMAN	KDM4A_HUMAN	Q9UKA2	O75164	FBXL4	KDM4A	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
754	FBXL5_HUMAN	IREB2_HUMAN	Q9UKA1	P48200	FBXL5	IREB2	MEDLINE	19762597	We found that an E3 ubiquitin ligase complex containing the <span class="match term0">FBXL5</span> protein targets <span class="match term1">IRP2</span> for proteasomal degradation	F-box	1	Training data	H.sapiens
755	FBXL5_HUMAN	DCTN1_HUMAN	Q9UKA1	Q14203	FBXL5	DCTN1	UniProt	FBXL5_HUMAN	Promotes ubiquitination and subsequent degradation of <span class="match term1">DCTN1</span>/p150-glued	F-box	1	Training data	H.sapiens
756	FBXL5_HUMAN	SYUA_HUMAN	Q9UKA1	P37840	FBXL5	SNCA	MEDLINE	31167929	Moreover, the SCF containing the F-box protein <span class="match term0">FBXL5</span> (SCFFBXL5) catalyzed <span class="match term1">alphaSyn</span> ubiquitination in reconstitution experiments in vitro using recombinant proteins and in cultured cells	F-box	1	Other	H.sapiens
757	FBXL5_HUMAN	ABL1_HUMAN	Q9UKA1	P00519	FBXL5	ABL1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
758	FBXL5_HUMAN	SOSB1_HUMAN	Q9UKA1	Q9BQ15	FBXL5	NABP2	MEDLINE	25249620	<span class="match term0">Fbxl5</span> interacts with and targets <span class="match term1">hSSB1</span> for ubiquitination and degradation, which could be prevented by ATM-mediated <span class="match term1">hSSB1</span> T117 phosphorylation	F-box	1	Other	H.sapiens
759	FBXL5_HUMAN	SNAI1_HUMAN	Q9UKA1	O95863	FBXL5	SNAI1	MEDLINE	24157836	Using a short hairpin RNA screening, we have identified <span class="match term0">FBXL5</span> as a novel <span class="match term1">Snail1</span> ubiquitin ligase	F-box	1	Other	H.sapiens
760	FBXL6_HUMAN	P53_HUMAN	Q8N531	P04637	FBXL6	TP53	MEDLINE	33568778	Mechanistically, <span class="match term0">FBXL6</span> targets phospho-<span class="match term1">p53</span> (S315) to mediate its polyubiquitination and proteasomal degradation, thereby inhibiting <span class="match term1">p53</span> signaling	F-box	1	Other	H.sapiens
761	FBXL7_HUMAN	SNAI1_HUMAN	Q9UJT9	O95863	FBXL7	SNAI1	MEDLINE	34249081	Mechanistically, <span class="match term0">FBXL7</span> bound to <span class="match term1">Snail1</span> and promoted its ubiquitination and proteasomal degradation	F-box	1	Other	H.sapiens
762	FBXL7_HUMAN	BIRC5_HUMAN	Q9UJT9	O15392	FBXL7	BIRC5	MEDLINE	25778398	UbiNet 2.0	F-box	1	Other	H.sapiens
763	FBXL7_HUMAN	AURKA_HUMAN	Q9UJT9	O14965	FBXL7	AURKA	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
764	FBXL7_HUMAN	SRC_HUMAN	Q9UJT9	P12931	FBXL7	SRC	MEDLINE	32839549	<span class="match term0">FBXL7</span> mediates the ubiquitylation and proteasomal degradation of active c-<span class="match term1">SRC</span> after its phosphorylation at Ser 104.	F-box	1	Other	H.sapiens
765	FBX10_HUMAN	BCL2_HUMAN	Q9UK96	P10415	FBXO10	BCL2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
766	FBX11_HUMAN	SNAI1_HUMAN	Q86XK2	O95863	FBXO11	SNAI1	MEDLINE	32657545	The F-box protein <span class="match term0">FBXO11</span> restrains hepatocellular carcinoma stemness via promotion of ubiquitin-mediated degradation of <span class="match term1">Snail</span>	F-box	1	Other	H.sapiens
767	FBX11_HUMAN	DTL_HUMAN	Q86XK2	Q9NZJ0	FBXO11	DTL	MEDLINE	23478441	UbiNet 2.0	F-box	1	Other	H.sapiens
768	FBX11_HUMAN	P53_HUMAN	Q86XK2	P04637	FBXO11	TP53	UniProt	FBX11_HUMAN	SCF(<span class="match term0">FBXO11</span>) does not seem to direct ubiquitination of <span class="match term1">TP53</span>	F-box	1	Training data	H.sapiens
769	FBX11_HUMAN	PRDM1_HUMAN	Q86XK2	O75626	FBXO11	PRDM1	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
770	FBX11_HUMAN	BCL6_HUMAN	Q86XK2	P41182	FBXO11	BCL6	MEDLINE	22113614	Here we show that <span class="match term1">BCL6</span> is targeted for ubiquitylation and proteasomal degradation by a SKP1-CUL1-F-box protein (SCF) ubiquitin ligase complex that contains the orphan F-box protein <span class="match term0">FBXO11</span> (refs 5, 6)	F-box	1	Other	H.sapiens
771	FBX15_HUMAN	MDR1_HUMAN	Q8NCQ5	P08183	FBXO15	ABCB1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
772	FBX15_HUMAN	CRLS1_HUMAN	Q8NCQ5	Q9UJA2	FBXO15	CRLS1	MEDLINE	24703837	E3 ligase subunit <span class="match term0">Fbxo15</span> and PINK1 kinase regulate cardiolipin synthase 1 stability and mitochondrial function in pneumonia.	F-box	1	Other	H.sapiens
773	FBX18_HUMAN	FBX18_HUMAN	Q8NFZ0	Q8NFZ0	FBXO18	FBXO18	UniProt	FBX18_HUMAN	Part of a SCF E3 ubiquitin ligase complex consisting of SKP1, CUL1, RBX1 and <span class="match term0">FBXO18</span>	F-box	1	Training data	H.sapiens
774	FBH1_HUMAN	HCD2_HUMAN	Q8NFZ0	P30153	FBXO18	RAD51	MEDLINE	25585578	25585578	F-box	1	Other	H.sapiens
775	FBX2_HUMAN	NMDZ1_HUMAN	Q9UK22	Q05586	FBXO2	GRIN1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
776	FBX2_HUMAN	SHPS1_HUMAN	Q9UK22	P78324	FBXO2	SIRPA	MEDLINE	24658274	UbiNet 2.0	Other	1	Other	H.sapiens
777	FBX2_HUMAN	OBP_HHV11	Q9UK22	P10193	FBXO2	UL9	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
778	FBX2_HUMAN	CXB2_HUMAN	Q9UK22	P29033	FBXO2	GJB2	MEDLINE	24658274	UbiNet 2.0	Other	1	Other	H.sapiens
779	FBX2_HUMAN	FETUA_HUMAN	Q9UK22	P02765	FBXO2	AHSG	MEDLINE	12140560	UbiNet 2.0	Other	1	Other	H.sapiens
780	FBX2_HUMAN	NDOR1_HUMAN	Q9UK22	Q9UHB4	FBXO2	NDOR1	MEDLINE	24658274	UbiNet 2.0	Other	1	Other	H.sapiens
781	FBX2_HUMAN	ITB1_HUMAN	Q9UK22	P05556	FBXO2	ITGB1	MEDLINE	16275327	UbiNet 2.0	Other	1	Other	H.sapiens
782	FBX2_HUMAN	FBN1_HUMAN	Q9UK22	P35555	FBXO2	FBN1	MEDLINE	32984335	We concluded that <span class="match term0">FBXO2</span> acts as an E3 ligase that targets <span class="match term1">FBN1</span> for ubiquitin-dependent degradation, so as to promote EC proliferation by regulating the cell cycle and the autophagy signaling pathway	Other	1	Other	H.sapiens
783	FBX2_HUMAN	CHIP_HUMAN	Q9UK22	Q9UNE7	FBXO2	STUB1	MEDLINE	16682404	A novel route for F-box protein-mediated ubiquitination links <span class="match term1">CHIP</span> to glycoprotein quality control.	Other	1	Other	H.sapiens
784	FBX2_HUMAN	BACE1_HUMAN	Q9UK22	P56817	FBXO2	BACE1	MEDLINE	20854419	SCFFbx2-E3-ligase-mediated degradation of <span class="match term1">BACE1</span> attenuates Alzheimer's disease amyloidosis and improves synaptic function.	Other	1	Other	H.sapiens
785	FBX21_HUMAN	COT2_HUMAN	O94952	P24468	FBXO21	NR2F2	MEDLINE	33531987	And the <span class="match term1">Nr2f2</span> protein abundance was regulated by <span class="match term0">Fbxo21</span> via ubiquitination and proteasomal degradation	F-box	1	Other	H.sapiens
786	FBX21_HUMAN	EID1_HUMAN	O94952	Q9Y6B2	FBXO21	EID1	MEDLINE	26085330	<span class="match term0">FBXO21</span> mediates the ubiquitylation and proteasomal degradation of <span class="match term1">EID1</span>.	F-box	1	Other	H.sapiens
787	FBX21_HUMAN	MDR1_HUMAN	O94952	P08183	FBXO21	ABCB1	MEDLINE	26299618	Here we demonstrate that a ubiquitin E3-ligase, <span class="match term0">FBXO21</span>, targets the multidrug resistance transporter, <span class="match term1">ABCB1</span>, also known as P-glycoprotein (P-gp), for proteasomal degradation	F-box	1	Other	H.sapiens
788	FBX22_HUMAN	BAG3_HUMAN	Q8NEZ5	O95817	FBXO22	BAG3	MEDLINE	34215846	<span class="match term0">FBXO22</span> mediates <span class="match term1">BAG3</span> ubiquitination and degradation that requires ERK-dependent <span class="match term1">BAG3</span> phosphorylation at S377	F-box	1	Other	H.sapiens
789	FBX22_HUMAN	MDM2_HUMAN	Q8NEZ5	Q00987	FBXO22	MDM2	MEDLINE	31138683	The results of protein decay rate analysis, ubiquitination, siRNA-mediated silencing, and coimmunoprecipitation experiments support a hypothesis that <span class="match term0">FBXO22</span> targets cellular <span class="match term1">HDM2</span> for ubiquitin-dependent degradation	F-box	1	Other	H.sapiens
790	FBX22_HUMAN	STK11_HUMAN	Q8NEZ5	Q15831	FBXO22	STK11	MEDLINE	31217475	<span class="match term0">FBXO22</span> mediates polyubiquitination and inactivation of <span class="match term1">LKB1</span> to promote lung cancer cell growth	F-box	1	Other	H.sapiens
791	FBX22_HUMAN	KDM4A_HUMAN	Q8NEZ5	O75164	FBXO22	KDM4A	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
792	FBX22_HUMAN	CDN1A_HUMAN	Q8NEZ5	P38936	FBXO22	CDKN1A	MEDLINE	30808376	CONCLUSIONS: This study uncovered a new mechanism by which <span class="match term0">FBXO22</span> functions as an oncogene in HCC pathogenesis and progression by mediating the ubiquitination and degradation of <span class="match term1">p21</span>	F-box	1	Other	H.sapiens
793	FBX22_HUMAN	KLF4_HUMAN	Q8NEZ5	O43474	FBXO22	KLF4	MEDLINE	26087183	We demonstrate that F-box only protein 22 (<span class="match term0">FBXO22</span>) interacts with and thereby destabilizes <span class="match term1">KLF4</span> via polyubiquitination	F-box	1	Other	H.sapiens
794	FBX22_HUMAN	PTEN_HUMAN	Q8NEZ5	P60484	FBXO22	PTEN	MEDLINE	32793396	<span class="match term0">FBXO22</span> exerts oncogenetic functions via promoting the ubiquitination and degradation of its substrates, including KDM4A, KDM4B, methylated p53, p21, KLF4, LKB1, Snail, CD147, Bach1, <span class="match term1">PTEN</span>, and HDM2	F-box	1	Other	H.sapiens
795	FBX22_HUMAN	BACH1_HUMAN	Q8NEZ5	O14867	FBXO22	BACH1	MEDLINE	32793396	<span class="match term0">FBXO22</span> exerts oncogenetic functions via promoting the ubiquitination and degradation of its substrates, including KDM4A, KDM4B, methylated p53, p21, KLF4, LKB1, Snail, CD147, <span class="match term1">Bach1</span>, PTEN, and HDM2	F-box	1	Other	H.sapiens
796	FBX22_HUMAN	SNAI1_HUMAN	Q8NEZ5	O95863	FBXO22	SNAI1	MEDLINE	32793396	<span class="match term0">FBXO22</span> exerts oncogenetic functions via promoting the ubiquitination and degradation of its substrates, including KDM4A, KDM4B, methylated p53, p21, KLF4, LKB1, <span class="match term1">Snail</span>, CD147, Bach1, PTEN, and HDM2	F-box	1	Other	H.sapiens
797	FBX22_HUMAN	KDM4B_HUMAN	Q8NEZ5	O94953	FBXO22	KDM4B	MEDLINE	32793396	<span class="match term0">FBXO22</span> exerts oncogenetic functions via promoting the ubiquitination and degradation of its substrates, including KDM4A, <span class="match term1">KDM4B</span>, methylated p53, p21, KLF4, LKB1, Snail, CD147, Bach1, PTEN, and HDM2	F-box	1	Other	H.sapiens
798	FBX22_HUMAN	PHLP1_HUMAN	Q8NEZ5	O60346	FBXO22	PHLPP1	MEDLINE	34182063	In conclusion, findings from our work proved that <span class="match term0">FBXO22</span> degraded <span class="match term1">PHLPP1</span> by ubiquitination to ameliorate rotenone induced neurotoxicity, which attributed to activate AKT pathway	F-box	1	Other	H.sapiens
799	FBX22_HUMAN	P53_HUMAN	Q8NEZ5	P04637	FBXO22	TP53	MEDLINE	26868148	SCF(<span class="match term0">Fbxo22</span>)-KDM4A targets methylated <span class="match term1">p53</span> for degradation and regulates senescence.	F-box	1	Other	H.sapiens
800	FBX22_HUMAN	BASI_HUMAN	Q8NEZ5	P35613	FBXO22	BSG	MEDLINE	28117675	UbiNet 2.0	F-box	1	Other	H.sapiens
801	FBX25_HUMAN	NKX25_HUMAN	Q8TCJ0	P52952	FBXO25	NKX2-5	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
802	FBX25_HUMAN	HAND1_HUMAN	Q8TCJ0	O96004	FBXO25	HAND1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
803	FBX25_HUMAN	ISL1_HUMAN	Q8TCJ0	P61371	FBXO25	ISL1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
804	FBX25_HUMAN	ELK1_HUMAN	Q8TCJ0	P19419	FBXO25	ELK1	MEDLINE	23940030	UbiNet 2.0	F-box	1	Training data	H.sapiens
805	FBX27_HUMAN	LAMP2_HUMAN	Q8NI29	P13473	FBXO27	LAMP2	MEDLINE	28743755	UbiNet 2.0	F-box	1	Other	H.sapiens
806	FBX28_HUMAN	FBX28_HUMAN	Q9NVF7	Q9NVF7	FBXO28	FBXO28	MEDLINE	31678254	UbiNet 2.0	F-box	1	Other	H.sapiens
807	FBX3_HUMAN	SMUF1_HUMAN	Q9UK99	Q9HCE7	FBXO3	SMURF1	MEDLINE	25721664	F-box protein <span class="match term0">Fbxo3</span> targets <span class="match term1">Smurf1</span> ubiquitin ligase for ubiquitination and degradation	F-box	1	Other	H.sapiens
808	FBX3_HUMAN	EP300_HUMAN	Q9UK99	Q09472	FBXO3	EP300	MEDLINE	18809579	<span class="match term0">Fbx3</span> formed SCF(<span class="match term0">Fbx3</span>) ubiquitin ligase and promoted the degradation of HIPK2 and <span class="match term1">p300</span> by the ubiquitin-proteasome pathway	F-box	1	Training data	H.sapiens
809	FBX3_HUMAN	FXL12_HUMAN	Q9UK99	Q9NXK8	FBXO3	FBXL12	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
810	FBX3_HUMAN	HIPK2_HUMAN	Q9UK99	Q9H2X6	FBXO3	HIPK2	MEDLINE	18809579	<span class="match term0">Fbx3</span> formed SCF(<span class="match term0">Fbx3</span>) ubiquitin ligase and promoted the degradation of <span class="match term1">HIPK2</span> and p300 by the ubiquitin-proteasome pathway	F-box	1	Training data	H.sapiens
811	FBX30_HUMAN	RARG_HUMAN	Q8TB52	P13631	FBXO30	RARG	MEDLINE	31320612	Collectively, our results demonstrate that <span class="match term1">RARgamma</span> levels are controlled by <span class="match term0">FBXO30</span>-mediated ubiquitination and that <span class="match term0">FBXO30</span> is a key regulator of BMP signaling	F-box	1	Other	H.sapiens
812	FBX31_HUMAN	CCND1_HUMAN	Q5XUX0	P24385	FBXO31	CCND1	UniProt	FBX31_HUMAN	Following DNA damage it is ubiquitinated by some SCF (SKP1-cullin-F-box) protein ligase complex containing <span class="match term0">FBXO31</span>	F-box	1	Training data	H.sapiens
813	FBX31_HUMAN	PAR6A_HUMAN	Q5XUX0	Q9NPB6	FBXO31	PARD6A	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
814	FBX31_HUMAN	CDT1_HUMAN	Q5XUX0	Q9H211	FBXO31	CDT1	MEDLINE	24828503	SCF-<span class="match term0">FBXO31</span> E3 ligase targets DNA replication factor <span class="match term1">Cdt1</span> for proteolysis in the G2 phase of cell cycle to prevent re-replication.	F-box	1	Other	H.sapiens
815	FBX31_HUMAN	CCND2_HUMAN	Q5XUX0	P30279	FBXO31	CCND2	MEDLINE	21537837	UbiNet 2.0	F-box	1	Training data	H.sapiens
816	FBX31_HUMAN	MP2K6_HUMAN	Q5XUX0	P52564	FBXO31	MAP2K6	MEDLINE	24936062	F-box only protein 31 (<span class="match term0">FBXO31</span>) negatively regulates p38 mitogen-activated protein kinase (MAPK) signaling by mediating lysine 48-linked ubiquitination and degradation of mitogen-activated protein kinase kinase 6 (<span class="match term1">MKK6</span>)	F-box	1	Other	H.sapiens
817	FBX31_HUMAN	MDM2_HUMAN	Q5XUX0	Q00987	FBXO31	MDM2	MEDLINE	26124108	F-box protein <span class="match term0">FBXO31</span> directs degradation of <span class="match term1">MDM2</span> to facilitate p53-mediated growth arrest following genotoxic stress.	F-box	1	Other	H.sapiens
818	FBX31_HUMAN	SNAI1_HUMAN	Q5XUX0	O95863	FBXO31	SNAI1	MEDLINE	29117943	Further evidence demonstrates that <span class="match term0">FBXO31</span> interacts with <span class="match term1">Snail1</span> and mediates the ubiquitin- and proteasome-dependent degradation of <span class="match term1">Snail1</span> in gastric cancer	F-box	1	Other	H.sapiens
819	FBX32_HUMAN	MYOD1_HUMAN	Q969P5	P15172	FBXO32	MYOD1	MEDLINE	19319192	Here we present evidence that <span class="match term0">MAFbx</span> targets <span class="match term1">MyoD</span> for degradation in several models of skeletal muscle atrophy	F-box	1	Training data	H.sapiens
820	FBX32_HUMAN	CABIN_HUMAN	Q969P5	Q9Y6J0	FBXO32	CABIN1	MEDLINE	18235241	UbiNet 2.0	F-box	1	Training data	H.sapiens
821	FBX32_HUMAN	TNNI3_HUMAN	Q969P5	P19429	FBXO32	TNNI3	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
822	FBX32_HUMAN	DUS1_HUMAN	Q969P5	P28562	FBXO32	DUSP1	MEDLINE	19117950	UbiNet 2.0	F-box	1	Training data	H.sapiens
823	FBX32_HUMAN	MYOTI_HUMAN	Q969P5	Q9UBF9	FBXO32	MYOT	MEDLINE	15100091	UbiNet 2.0	F-box	1	Training data	H.sapiens
824	FBX32_HUMAN	KLF4_HUMAN	Q969P5	O43474	FBXO32	KLF4	MEDLINE	28068319	Furthermore, we demonstrated that <span class="match term0">FBXO32</span> physically interacts with the N-terminus (1-60 aa) of <span class="match term1">KLF4</span> via its C-terminus (228-355 aa) and directly targets <span class="match term1">KLF4</span> for ubiquitination and degradation	F-box	1	Other	H.sapiens
825	FBX32_HUMAN	MYOG_HUMAN	Q969P5	P15173	FBXO32	MYOG	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
826	FBX32_HUMAN	FOXO1_HUMAN	Q969P5	Q12778	FBXO32	FOXO1	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
827	FBX32_HUMAN	EIF3F_HUMAN	Q969P5	O00303	FBXO32	EIF3F	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
828	FBX32_HUMAN	ATR_HUMAN	Q969P5	Q13535	FBXO32	ATR	MEDLINE	29805624	Additionally, <span class="match term0">FBXO32</span> interacts with <span class="match term1">ATR</span> in PANC-1 cells and <span class="match term1">ATR</span> is a degradation substrate of E3 ubiquitin ligase <span class="match term0">FBXO32</span>	F-box	1	Other	H.sapiens
829	FBX32_HUMAN	KCMB1_HUMAN	Q969P5	Q16558	FBXO32	KCNMB1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
830	FBX32_HUMAN	MYC_HUMAN	Q969P5	P01106	FBXO32	MYC	MEDLINE	25944903	UbiNet 2.0	F-box	1	Other	H.sapiens
831	FBX32_HUMAN	MYPC3_HUMAN	Q969P5	Q14896	FBXO32	MYBPC3	MEDLINE	19850579	UbiNet 2.0	F-box	1	Training data	H.sapiens
832	FBX33_HUMAN	EIF3F_HUMAN	Q7Z6M2	O00303	FBXO33	EIF3F	MEDLINE	18354498	UbiNet 2.0	F-box	1	Training data	H.sapiens
833	FBX33_HUMAN	YBOX1_HUMAN	Q7Z6M2	P67809	FBXO33	YBX1	UniProt	FBX33_HUMAN	SCF(<span class="match term0">FBXO33</span>) directs ubiquitination of <span class="match term1">YBX1</span>	F-box	1	Training data	H.sapiens
834	FBX34_HUMAN	MYOD1_HUMAN	Q9NWN3	P15172	FBXO34	MYOD1	MEDLINE	19319192	UbiNet 2.0	F-box	1	Training data	H.sapiens
835	FBX4_HUMAN	CCND1_HUMAN	Q9UKT5	P24385	FBXO4	CCND1	MEDLINE	19767775	Lysine 269 is essential for cyclin D1 ubiquitylation by the SCF(<span class="match term0">Fbx4</span>/alphaB-crystallin) ligase and subsequent proteasome-dependent degradation	F-box	1	Training data	H.sapiens
836	FBX4_HUMAN	MCL1_HUMAN	Q9UKT5	Q07820	FBXO4	MCL1	MEDLINE	28776569	Mechanically, <span class="match term0">FBXO4</span> is the E3 ubiquitin ligase to interact with and promote <span class="match term1">Mcl-1</span> ubiquitination and degradation	F-box	1	Other	H.sapiens
837	FBX4_HUMAN	FXR1_HUMAN	Q9UKT5	P51114	FBXO4	FXR1	MEDLINE	29142209	UbiNet 2.0	F-box	1	Other	H.sapiens
838	FBX4_HUMAN	TERF1_HUMAN	Q9UKT5	P54274	FBXO4	TERF1	MEDLINE	20181953	UbiNet 2.0	F-box	1	Training data	H.sapiens
839	FBX4_HUMAN	ICAM1_HUMAN	Q9UKT5	P05362	FBXO4	ICAM1	MEDLINE	29137327	UbiNet 2.0	F-box	1	Other	H.sapiens
840	FBX40_HUMAN	IRS1_HUMAN	Q9UH90	P35568	FBXO40	IRS1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
841	FBX42_HUMAN	P53_HUMAN	Q6P3S6	P04637	FBXO42	TP53	MEDLINE	19509332	We showed that <span class="match term0">JFK</span> promotes ubiquitination and degradation of <span class="match term1">p53</span>	F-box	1	Other	H.sapiens
842	FBX44_HUMAN	BRCA1_HUMAN	Q9H4M3	P38398	FBXO44	BRCA1	MEDLINE	23086937	UbiNet 2.0	F-box	1	Training data	H.sapiens
843	FBX44_HUMAN	UN13A_HUMAN	Q9H4M3	Q9UPW8	FBXO44	UNC13A	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
844	FBSP1_HUMAN	ZEB1_HUMAN	P0C2W1	P37275	FBXO45	ZEB1	MEDLINE	25460509	Atypical ubiquitin E3 ligase complex Skp1-Pam-<span class="match term0">Fbxo45</span> controls the core epithelial-to-mesenchymal transition-inducing transcription factors.	F-box	1	Other	H.sapiens
845	FBSP1_HUMAN	SNAI2_HUMAN	P0C2W1	O43623	FBXO45	SNAI2	MEDLINE	25460509	UbiNet 2.0	F-box	1	Other	H.sapiens
846	FBSP1_HUMAN	ZEB2_HUMAN	P0C2W1	O60315	FBXO45	ZEB2	MEDLINE	25460509	Atypical ubiquitin E3 ligase complex Skp1-Pam-<span class="match term0">Fbxo45</span> controls the core epithelial-to-mesenchymal transition-inducing transcription factors.	F-box	1	Other	H.sapiens
847	FBSP1_HUMAN	FBXW7_HUMAN	P0C2W1	Q969H0	FBXO45	FBXW7	MEDLINE	31285543	<span class="match term0">FBXO45</span> binds to a conserved acidic N-terminal motif of <span class="match term1">FBXW7</span> specifically under a prolonged delay in mitosis, leading to ubiquitylation and subsequent proteasomal degradation of <span class="match term1">FBXW7</span> by the <span class="match term0">FBXO45</span>-MYCBP2 E3 ubiquitin ligase	F-box	1	Other	H.sapiens
848	FBSP1_HUMAN	TWST1_HUMAN	P0C2W1	Q15672	FBXO45	TWIST1	MEDLINE	25460509	UbiNet 2.0	F-box	1	Other	H.sapiens
849	FBSP1_HUMAN	PAWR_HUMAN	P0C2W1	Q96IZ0	FBXO45	PAWR	MEDLINE	24992930	UbiNet 2.0	F-box	1	Other	H.sapiens
850	FBSP1_HUMAN	SNAI1_HUMAN	P0C2W1	O95863	FBXO45	SNAI1	MEDLINE	25460509	UbiNet 2.0	F-box	1	Other	H.sapiens
851	FBSP1_HUMAN	P73_HUMAN	P0C2W1	O15350	FBXO45	TP73	MEDLINE	19581926	Importantly, SCF(<span class="match term0">FBXO45</span>) ubiquitylates <span class="match term1">p73</span> both in vivo and in vitro	F-box	1	Training data	H.sapiens
852	FBX6_HUMAN	RNT2_HUMAN	Q9NRD1	O00584	FBXO6	RNASET2	MEDLINE	33767133	We found that the interaction between <span class="match term0">FBXO6</span> and <span class="match term1">RNASET2</span> induced <span class="match term1">RNASET2</span> instability through the ubiquitin-mediated proteasome degradation pathway	F-box	1	Other	H.sapiens
853	FBX6_HUMAN	CHK1_HUMAN	Q9NRD1	O14757	FBXO6	CHEK1	MEDLINE	19716789	Further, we show that low levels of <span class="match term0">Fbx6</span> and consequent impairment of replication stress-induced <span class="match term1">Chk1</span> degradation are associated with cancer cell resistance to the chemotherapeutic agent, camptothecin	F-box	1	Training data	H.sapiens
854	FBX6_HUMAN	RIOK1_HUMAN	Q9NRD1	Q9BRS2	FBXO6	RIOK1	MEDLINE	29384474	<span class="match term0">FBXO6</span> specifically interacts with K411-methylated <span class="match term1">RIOK1</span> through its FBA domain to induce <span class="match term1">RIOK1</span> ubiquitination	F-box	1	Other	H.sapiens
855	FBX6_HUMAN	TFR1_HUMAN	Q9NRD1	P02786	FBXO6	TFRC	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
856	FBX6_HUMAN	ERO1A_HUMAN	Q9NRD1	Q96HE7	FBXO6	ERO1A	MEDLINE	27855403	RESULTS: <span class="match term1">Ero1L</span> is a ubiquitination substrate of <span class="match term0">FBXO6</span>	F-box	1	Other	H.sapiens
857	FBX6_HUMAN	IRF3_HUMAN	Q9NRD1	Q14653	FBXO6	IRF3	MEDLINE	31308089	Structure and function delineation has further revealed that <span class="match term0">FBXO6</span> interacts with IAD domain of <span class="match term1">IRF3</span> through its FBA region to induce ubiquitination and degradation of <span class="match term1">IRF3</span> without the involvement of SCF	F-box	1	Other	H.sapiens
858	FBX6_HUMAN	ATRN_HUMAN	Q9NRD1	O75882	FBXO6	ATRN	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
859	FBX7_HUMAN	BIRC2_HUMAN	Q9Y3I1	Q13490	FBXO7	BIRC2	MEDLINE	16510124	Furthermore, we showed that overexpression of <span class="match term0">Fbxo7</span> promotes the ubiquitination of <span class="match term1">cIAP1</span>	F-box	1	Training data	H.sapiens
860	FBX7_HUMAN	CRBN_HUMAN	Q9Y3I1	Q96SW2	FBXO7	CRBN	MEDLINE	30026574	UbiNet 2.0	F-box	1	Other	H.sapiens
861	FBX7_HUMAN	LEUK_HUMAN	Q9Y3I1	P16150	FBXO7	SPN	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
862	FBX7_HUMAN	TRAF2_HUMAN	Q9Y3I1	Q12933	FBXO7	TRAF2	MEDLINE	33010352	<span class="match term0">Fbxo7</span> negatively regulates NF-kappaB signaling through <span class="match term1">TRAF2</span> and cIAP1 ubiquitination	F-box	1	Other	H.sapiens
863	FBX7_HUMAN	DLGP5_HUMAN	Q9Y3I1	Q15398	FBXO7	DLGAP5	MEDLINE	18495667	SCF(<span class="match term0">Fbxo7</span>) is known to catalyze the ubiquitination of hepatoma-up-regulated protein (<span class="match term1">HURP</span>) and the inhibitor of apoptosis (IAP) protein but also functions as an activator of cyclin D-Cdk6 complexes	F-box	1	Training data	H.sapiens
864	FBX8_HUMAN	MYC_HUMAN	Q9NRD0	P01106	FBXO8	MYC	MEDLINE	32796813	Mechanistically, <span class="match term0">FBX8</span> directly bound to HIF-1alpha, CDK4 and C-<span class="match term1">myc</span> through its Sec7 domain and led to the ubiquitin degradation of these proteins, thereby inhibiting cell cycle progression, proliferation, angiogenesis, and metastasis	F-box	1	Other	H.sapiens
865	FBX8_HUMAN	GSTP1_HUMAN	Q9NRD0	P09211	FBXO8	GSTP1	MEDLINE	31024008	<span class="match term0">FBX8</span> degrades <span class="match term1">GSTP1</span> through ubiquitination to suppress colorectal cancer progression	F-box	1	Other	H.sapiens
866	FBX8_HUMAN	ARF6_HUMAN	Q9NRD0	P62330	FBXO8	ARF6	MEDLINE	18094045	Here we show that <span class="match term0">Fbx8</span>, an F-box protein bearing the Sec7 domain, mediates ubiquitination of <span class="match term1">Arf6</span>	F-box	1	Other	H.sapiens
867	FBX9_HUMAN	NGN2_HUMAN	Q9UK97	Q9H2A3	FBXO9	NEUROG2	MEDLINE	32029586	Consistently, overexpression of <span class="match term0">Fbxo9</span> in NC progenitors down-regulated <span class="match term1">Neurog2</span> protein expression through ubiquitination and promoted the glial lineage at the expense of neuronal differentiation, whereas <span class="match term0">Fbxo9</span> knockdown resulted in the opposite phenomenon	F-box	1	Other	H.sapiens
868	FBX9_HUMAN	TTI1_HUMAN	Q9UK97	O43156	FBXO9	TTI1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
869	FBX9_HUMAN	TELO2_HUMAN	Q9UK97	Q9Y4R8	FBXO9	TELO2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
870	FBW10_HUMAN	CBX5_HUMAN	Q5XX13	P45973	FBXW10	CBX5	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
871	FBW1B_HUMAN	BHE40_HUMAN	Q9UKB1	O14503	FBXW11	BHLHE40	MEDLINE	25202122	UbiNet 2.0	F-box	1	Other	H.sapiens
872	FBW1B_HUMAN	FBW1B_HUMAN	Q9UKB1	Q9UKB1	FBXW11	FBXW11	UniProt	FBW1B_HUMAN	Association with the F-box proteins BTRC and <span class="match term0">FBXW11</span> targets the protein for ubiquitination by CUL1 and proteolysis by the ubiquitin-dependent proteasome pathway (By similarity)	F-box	1	Training data	H.sapiens
873	FBW1B_HUMAN	MPIP2_HUMAN	Q9UKB1	P30305	FBXW11	CDC25B	MEDLINE	21807946	UbiNet 2.0	F-box	1	Other	H.sapiens
874	FBW1B_HUMAN	PLK4_HUMAN	Q9UKB1	O00444	FBXW11	PLK4	MEDLINE	19084407	Here we show that centrosome amplification is normally inhibited by degradation of <span class="match term1">SAK</span>/PK4 degradation, mediated by the SCF/Slimb ubiquitin ligase	F-box	1	Training data	H.sapiens
875	FBW1B_HUMAN	IKBA_HUMAN	Q9UKB1	P25963	FBXW11	NFKBIA	MEDLINE	14707120	Increasing cellular levels of <span class="match term0">HOS</span> substrate (phosphorylated <span class="match term1">IkappaBalpha</span>) by activating IkappaB kinase inhibited <span class="match term0">HOS</span> ubiquitination and led to stabilization of <span class="match term0">HOS</span>, indicating that interaction between <span class="match term0">HOS</span> and its substrate might protect <span class="match term0">HOS</span> from proteolysis	F-box	1	Training data	H.sapiens
876	FBW1B_HUMAN	IKKA_HUMAN	Q9UKB1	O15111	FBXW11	CHUK	MEDLINE	10321728	UbiNet 2.0	F-box	1	Other	H.sapiens
877	FBW1B_HUMAN	MPIP1_HUMAN	Q9UKB1	P30304	FBXW11	CDC25A	MEDLINE	14681206	UbiNet 2.0	F-box	1	Other	H.sapiens
878	FBW1B_HUMAN	CTNB1_HUMAN	Q9UKB1	P35222	FBXW11	CTNNB1	UniProt	FBW1B_HUMAN	SCF(<span class="match term0">FBXW11</span>) mediates the ubiquitination of <span class="match term1">CTNNB1</span> and participates in Wnt signaling	F-box	1	Training data	H.sapiens
879	FBW1B_HUMAN	YAP1_HUMAN	Q9UKB1	P46937	FBXW11	YAP1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
880	FBW1B_HUMAN	SI1L2_HUMAN	Q9UKB1	Q9P2F8	FBXW11	SIPA1L2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
881	FBW1B_HUMAN	NFKB1_HUMAN	Q9UKB1	P19838	FBXW11	NFKB1	UniProt	FBW1B_HUMAN	SCF(<span class="match term0">FBXW11</span>) mediates the ubiquitination of NFKBIA, the degradation frees the associated <span class="match term1">NFKB1</span> to translocate into the nucleus and to activate transcription	F-box	1	Training data	H.sapiens
882	FBW1B_HUMAN	PRLR_HUMAN	Q9UKB1	P16471	FBXW11	PRLR	MEDLINE	15082796	UbiNet 2.0	F-box	1	Other	H.sapiens
883	FBW1B_HUMAN	IKKB_HUMAN	Q9UKB1	O14920	FBXW11	IKBKB	MEDLINE	10321728	UbiNet 2.0	F-box	1	Other	H.sapiens
884	FBW1B_HUMAN	INAR1_HUMAN	Q9UKB1	P17181	FBXW11	IFNAR1	UniProt	FBW1B_HUMAN	SCF(<span class="match term0">FBXW11</span>) mediates the ubiquitination of <span class="match term1">IFNAR1</span>	F-box	1	Training data	H.sapiens
885	FBW1B_HUMAN	WEE1_HUMAN	Q9UKB1	P30291	FBXW11	WEE1	MEDLINE	15070733	In the present study, we have identified the beta-transducin repeat-containing protein 1/2 (beta-TrCP1/2) F-box protein-containing SKP1/Cul1/F-box protein (SCF) complex (SCF(beta-TrCP1/2)) as an E3 ubiquitin ligase for <span class="match term1">Wee1A</span> ubiquitination	F-box	1	Training data	H.sapiens
886	FBW1B_HUMAN	PDCD4_HUMAN	Q9UKB1	Q53EL6	FBXW11	PDCD4	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
887	FBW1B_HUMAN	PER1_HUMAN	Q9UKB1	O15534	FBXW11	PER1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
888	FBW1B_HUMAN	RCAN1_HUMAN	Q9UKB1	P53805	FBXW11	RCAN1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
889	FBW1B_HUMAN	FBW1A_HUMAN	Q9UKB1	Q9Y297	FBXW11	BTRC	MEDLINE	31406304	UbiNet 2.0	F-box	1	Other	H.sapiens
890	FBW1B_HUMAN	CLSPN_HUMAN	Q9UKB1	Q9HAW4	FBXW11	CLSPN	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
891	FBW1B_HUMAN	TBCD4_HUMAN	Q9UKB1	O60343	FBXW11	TBC1D4	MEDLINE	25515538	UbiNet 2.0	F-box	1	Other	H.sapiens
892	FBW1B_HUMAN	DDIT4_HUMAN	Q9UKB1	Q9NX09	FBXW11	DDIT4	MEDLINE	31406304	UbiNet 2.0	F-box	1	Other	H.sapiens
893	FBW1B_HUMAN	REST_HUMAN	Q9UKB1	Q13127	FBXW11	REST	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
894	FBW1B_HUMAN	DLG1_HUMAN	Q9UKB1	Q12959	FBXW11	DLG1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
895	FBW1B_HUMAN	FBX5_HUMAN	Q9UKB1	Q9UKT4	FBXW11	FBXO5	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
896	FBW1B_HUMAN	DPTOR_HUMAN	Q9UKB1	Q8TB45	FBXW11	DEPTOR	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
897	FBW1B_HUMAN	CEP68_HUMAN	Q9UKB1	Q76N32	FBXW11	CEP68	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
898	FBW1B_HUMAN	PER2_HUMAN	Q9UKB1	O15055	FBXW11	PER2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
899	FBW1B_HUMAN	FANCM_HUMAN	Q9UKB1	Q8IYD8	FBXW11	FANCM	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
900	FBW12_HUMAN	I22R1_HUMAN	Q6X9E4	Q8N6P7	FBXW12	IL22RA1	MEDLINE	26171402	UbiNet 2.0	F-box	1	Other	H.sapiens
901	FBXW2_HUMAN	CCNE2_HUMAN	Q9UKT8	O96020	FBXW2	CCNE2	MEDLINE	17298674	UbiNet 2.0	F-box	1	Training data	H.sapiens
902	FBXW2_HUMAN	GCM1_HUMAN	Q9UKT8	Q9NP62	FBXW2	GCM1	UniProt	FBXW2_HUMAN	SCF(<span class="match term0">FBXW2</span>) directs ubiquitination of <span class="match term1">GCM1</span>	F-box	1	Training data	H.sapiens
903	FBXW2_HUMAN	CCNE1_HUMAN	Q9UKT8	P24864	FBXW2	CCNE1	MEDLINE	17298674	UbiNet 2.0	F-box	1	Training data	H.sapiens
904	FBXW2_HUMAN	MSX2_HUMAN	Q9UKT8	P35548	FBXW2	MSX2	MEDLINE	31548378	UbiNet 2.0	F-box	1	Other	H.sapiens
905	FBXW5_HUMAN	EPS8_HUMAN	Q969U6	Q12929	FBXW5	EPS8	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
906	FBXW5_HUMAN	SAS6_HUMAN	Q969U6	Q6UVJ0	FBXW5	SASS6	MEDLINE	21725316	The SCF-<span class="match term0">FBXW5</span> E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6 to control centrosome duplication.	F-box	1	Other	H.sapiens
907	FBXW5_HUMAN	DLEC1_HUMAN	Q969U6	Q9Y238	FBXW5	DLEC1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
908	FBXW5_HUMAN	TSC2_HUMAN	Q969U6	P49815	FBXW5	TSC2	MEDLINE	18381890	Overexpression of <span class="match term0">FBW5</span> or CUL4A promotes <span class="match term1">TSC2</span> protein degradation, and this is abrogated by the coexpression of TSC1	F-box	1	Training data	H.sapiens
909	FBXW5_HUMAN	RHG07_HUMAN	Q969U6	Q96QB1	FBXW5	DLC1	MEDLINE	PMC4306233	PMC4306233	F-box	1	Other	H.sapiens
910	FBXW7_HUMAN	MCL1_HUMAN	Q969H0	Q07820	FBXW7	MCL1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
911	FBXW7_HUMAN	CCNE1_HUMAN	Q969H0	P24864	FBXW7	CCNE1	MEDLINE	14648662	The present study has analysed amplification of the cyclin E gene (<span class="match term1">CCNE</span>) and mutation in <span class="match term0">hCDC4</span>, the gene coding for the F-box protein, which tags phosphorylated cyclin E for proteosomal degradation, to ascertain whether these alterations might be responsible for cyclin E overexpression in ECs	F-box	1	Training data	H.sapiens
912	FBXW7_HUMAN	JUNB_HUMAN	Q969H0	P17275	FBXW7	JUNB	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
913	FBXW7_HUMAN	MYC_HUMAN	Q969H0	P01106	FBXW7	MYC	MEDLINE	16131838	The Fbw7/<span class="match term0">hCdc4</span> F-box protein was first recognized by its ability to bind cyclin E, and the SCF (Fbw7) is now known to target c-<span class="match term1">Myc</span>, c-Jun and Notch for degradation in addition to its role in cyclin E proteolysis	F-box	1	Training data	H.sapiens
914	FBXW7_HUMAN	PRGC1_HUMAN	Q969H0	Q9UBK2	FBXW7	PPARGC1A	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
915	FBXW7_HUMAN	JUN_HUMAN	Q969H0	P05412	FBXW7	JUN	MEDLINE	18094723	SCF(<span class="match term0">FBW7</span>) degrades several proto-oncogenes that function in cellular growth and division pathways, including MYC, cyclin E, Notch and <span class="match term1">JUN</span>	F-box	1	Training data	H.sapiens
916	FBXW7_HUMAN	CSF3R_HUMAN	Q969H0	Q99062	FBXW7	CSF3R	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
917	FBXW7_HUMAN	NOTC1_HUMAN	Q969H0	P46531	FBXW7	NOTCH1	MEDLINE	18185524	In addition, 19 other genetic lesions were detected once in TLX3 rearranged T-ALL cases, including a cryptic WT1 deletion and a deletion covering the <span class="match term0">FBXW7</span> gene, an U3-ubiquitin ligase that mediates the degradation of <span class="match term1">NOTCH1</span>, MYC, JUN and CyclinE	F-box	1	Training data	H.sapiens
918	FBXW7_HUMAN	AURKA_HUMAN	Q969H0	O14965	FBXW7	AURKA	MEDLINE	16863506	UbiNet 2.0	F-box	1	Training data	H.sapiens
919	FBXW7_HUMAN	STAT2_HUMAN	Q969H0	P52630	FBXW7	STAT2	MEDLINE	31843895	We found that the interaction of <span class="match term0">FBXW7</span> and <span class="match term1">STAT2</span> induced <span class="match term1">STAT2</span> destabilization via a ubiquitination-mediated proteasomal degradation pathway	F-box	1	Other	H.sapiens
920	FBXW7_HUMAN	P53_HUMAN	Q969H0	P04637	FBXW7	TP53	MEDLINE	31346036	Abrogation of FBW7alpha-dependent <span class="match term1">p53</span> degradation enhances <span class="match term1">p53</span>'s function as a tumor suppressor.	F-box	1	Other	H.sapiens
921	FBXW7_HUMAN	ASCC2_HUMAN	Q969H0	Q9H1I8	FBXW7	ASCC2	MEDLINE	22388891	UbiNet 2.0	F-box	1	Training data	H.sapiens
922	FBXW7_HUMAN	KLF10_HUMAN	Q969H0	Q13118	FBXW7	KLF10	MEDLINE	29198712	<span class="match term0">FBW7</span> targets <span class="match term1">KLF10</span> for ubiquitin-dependent degradation	F-box	1	Other	H.sapiens
923	FBXW7_HUMAN	KLF13_HUMAN	Q969H0	Q9Y2Y9	FBXW7	KLF13	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
924	FBXW7_HUMAN	SRBP1_HUMAN	Q969H0	P36956	FBXW7	SREBF1	MEDLINE	16054087	<span class="match term0">Fbw7</span> also degrades nuclear SREBP1c and SREBP2, and inactivation of endogenous <span class="match term0">Fbw7</span> results in stabilization of nuclear <span class="match term1">SREBP1</span> and -2, enhanced expression of SREBP target genes, enhanced synthesis of cholesterol and fatty acids, and enhanced receptor-mediated uptake of LDL	F-box	1	Training data	H.sapiens
925	FBXW7_HUMAN	MYB_HUMAN	Q969H0	P10242	FBXW7	MYB	MEDLINE	19421138	<span class="match term0">Fbw7</span> facilitated ubiquitylation and degradation of c-<span class="match term1">Myb</span> in intact cells	F-box	1	Training data	H.sapiens
926	FBXW7_HUMAN	CR3L1_HUMAN	Q969H0	Q96BA8	FBXW7	CREB3L1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
927	FBXW7_HUMAN	BIRC2_HUMAN	Q969H0	Q13490	FBXW7	BIRC2	MEDLINE	16510124	UbiNet 2.0	F-box	1	Training data	H.sapiens
928	FBXW7_HUMAN	NF1_HUMAN	Q969H0	P21359	FBXW7	NF1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
929	FBXW7_HUMAN	NONO_HUMAN	Q969H0	Q15233	FBXW7	NONO	MEDLINE	29150959	<span class="match term1">NONO</span> ubiquitination is mediated by <span class="match term0">FBW7</span> and GSK3 beta via a degron lost upon chromosomal rearrangement in cancer	F-box	1	Other	H.sapiens
930	FBXW7_HUMAN	NCOA3_HUMAN	Q969H0	Q9Y6Q9	FBXW7	NCOA3	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
931	FBXW7_HUMAN	CCDC6_HUMAN	Q969H0	Q16204	FBXW7	CCDC6	MEDLINE	25885523	<span class="match term0">FBXW7</span> and USP7 regulate <span class="match term1">CCDC6</span> turnover during the cell cycle and affect cancer drugs susceptibility in NSCLC.	F-box	1	Other	H.sapiens
932	FBXW7_HUMAN	CEBPA_HUMAN	Q969H0	P49715	FBXW7	CEBPA	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
933	FBXW7_HUMAN	GCR_HUMAN	Q969H0	P04150	FBXW7	NR3C1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
934	FBXW7_HUMAN	TOP2A_HUMAN	Q969H0	P11388	FBXW7	TOP2A	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
935	FBXW7_HUMAN	SNAI1_HUMAN	Q969H0	O95863	FBXW7	SNAI1	MEDLINE	30094882	<span class="match term0">FBXW7</span> suppresses epithelial-mesenchymal transition and chemo-resistance of non-small-cell lung cancer cells by targeting <span class="match term1">snai1</span> for ubiquitin-dependent degradation	F-box	1	Other	H.sapiens
936	FBXW7_HUMAN	P63_HUMAN	Q969H0	Q9H3D4	FBXW7	TP63	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
937	FBXW7_HUMAN	KLF2_HUMAN	Q969H0	Q9Y5W3	FBXW7	KLF2	MEDLINE	23507969	<span class="match term0">FBW7</span> regulates endothelial functions by targeting <span class="match term1">KLF2</span> for ubiquitination and degradation.	F-box	1	Other	H.sapiens
938	FBXW7_HUMAN	SOX9_HUMAN	Q969H0	P48436	FBXW7	SOX9	MEDLINE	27566146	The binding of FBW7alpha to the <span class="match term1">SOX9</span> K2 domain at T236-T240 targets <span class="match term1">SOX9</span> for subsequent ubiquitination and proteasomal destruction	F-box	1	Other	H.sapiens
939	FBXW7_HUMAN	ZEB2_HUMAN	Q969H0	O60315	FBXW7	ZEB2	MEDLINE	30783098	Using a modified yeast-2-hybrid system and 2D gel-based proteomics methods, we show that the E3-ubiquitin ligase <span class="match term0">FBXW7</span> directly binds and degrades the EMT-inducing transcription factor <span class="match term1">ZEB2</span> in a phosphorylation-dependent manner	F-box	1	Other	H.sapiens
940	FBXW7_HUMAN	SPI1_HUMAN	Q969H0	P17947	FBXW7	SPI1	MEDLINE	33188146	We demonstrate that GSK3beta phosphorylates <span class="match term1">PU.1</span> at Ser41 and Ser140 leading to its recognition and subsequent ubiquitin-mediated degradation by E3 ubiquitin ligase <span class="match term0">FBW7</span>	F-box	1	Other	H.sapiens
941	FBXW7_HUMAN	SIK2_HUMAN	Q969H0	Q9H0K1	FBXW7	SIK2	MEDLINE	32437091	Tumor-suppressor <span class="match term0">Fbxw7</span> targets <span class="match term1">SIK2</span> for degradation to interfere with TORC2-AKT signaling in pancreatic cancer.	F-box	1	Other	H.sapiens
942	FBXW7_HUMAN	ENOA_HUMAN	Q969H0	P06733	FBXW7	ENO1	MEDLINE	34335983	130-484) and further promoted ubiquitylation and degradation of <span class="match term1">ENO1</span> by recruiting E3 ubiquitin ligase <span class="match term0">FBXW7</span>	F-box	1	Other	H.sapiens
943	FBXW7_HUMAN	SHOC2_HUMAN	Q969H0	Q9UQ13	FBXW7	SHOC2	MEDLINE	30865892	UbiNet 2.0	F-box	1	Other	H.sapiens
944	FBXW7_HUMAN	CRY2_HUMAN	Q969H0	Q49AN0	FBXW7	CRY2	MEDLINE	25855785	We also identify <span class="match term0">FBXW7</span> as a novel E3 ubiquitin ligase for targeting <span class="match term1">CRY2</span> through proteasomal degradation	F-box	1	Other	H.sapiens
945	FBXW7_HUMAN	RCAN1_HUMAN	Q969H0	P53805	FBXW7	RCAN1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
946	FBXW7_HUMAN	TGIF1_HUMAN	Q969H0	Q15583	FBXW7	TGIF1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
947	FBXW7_HUMAN	HDAC7_HUMAN	Q969H0	Q8WUI4	FBXW7	HDAC7	MEDLINE	34288252	Mechanistically, <span class="match term0">FBXW7</span> interacted with <span class="match term1">HDAC7</span> to promote <span class="match term1">HDAC7</span> ubiquitination, however, the overexpression of <span class="match term1">HDAC7</span> in glioblastoma cells blocked <span class="match term0">FBXW7</span>-induced apoptosis	F-box	1	Other	H.sapiens
948	FBXW7_HUMAN	CEBPD_HUMAN	Q969H0	P49716	FBXW7	CEBPD	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
949	FBXW7_HUMAN	SRBP2_HUMAN	Q969H0	Q12772	FBXW7	SREBF2	MEDLINE	16054087	<span class="match term0">Fbw7</span> also degrades nuclear SREBP1c and <span class="match term1">SREBP2</span>, and inactivation of endogenous <span class="match term0">Fbw7</span> results in stabilization of nuclear SREBP1 and -2, enhanced expression of SREBP target genes, enhanced synthesis of cholesterol and fatty acids, and enhanced receptor-mediated uptake of LDL	F-box	1	Training data	H.sapiens
950	FBXW7_HUMAN	CR3L2_HUMAN	Q969H0	Q70SY1	FBXW7	CREB3L2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
951	FBXW7_HUMAN	MD13L_HUMAN	Q969H0	Q71F56	FBXW7	MED13L	MEDLINE	23322298	The SCF-<span class="match term0">Fbw7</span> ubiquitin ligase degrades MED13 and <span class="match term1">MED13L</span> and regulates CDK8 module association with Mediator.	F-box	1	Other	H.sapiens
952	FBXW7_HUMAN	CCNE2_HUMAN	Q969H0	O96020	FBXW7	CCNE2	MEDLINE	19084516	Here we report that cyclin E2 is targeted for ubiquitin-dependent proteolysis by the ubiquitin ligase SCF(<span class="match term0">Fbxw7</span>/hCdc4)	F-box	1	Training data	H.sapiens
953	FBXW7_HUMAN	PTN11_HUMAN	Q969H0	Q06124	FBXW7	PTPN11	MEDLINE	34046815	Further studies showed that PML increased the expression of <span class="match term0">FBXW7</span> by inhibiting its K48-linked ubiquitination and enhanced the interaction between <span class="match term0">FBXW7</span> and <span class="match term1">SHP2</span>, which negatively regulated IAV replication during infection	F-box	1	Other	H.sapiens
954	FBXW7_HUMAN	BRAF_HUMAN	Q969H0	P15056	FBXW7	BRAF	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
955	FBXW7_HUMAN	FETUA_HUMAN	Q969H0	P02765	FBXW7	AHSG	MEDLINE	29475832	Mechanistically, <span class="match term0">FBXW7</span> directly binds to hepatokine <span class="match term1">fetuin-A</span> to induce its ubiquitination and subsequent proteasomal degradation, comprising an important mechanism maintaining glucose homeostasis	F-box	1	Other	H.sapiens
956	FBXW7_HUMAN	RUNX2_HUMAN	Q969H0	Q13950	FBXW7	RUNX2	MEDLINE	30610124	Withdrawal: E3 ubiquitin ligase <span class="match term0">Fbw7</span> negatively regulates osteoblast differentiation by targeting <span class="match term1">Runx2</span> for degradation.	F-box	1	Other	H.sapiens
957	FBXW7_HUMAN	NRF1_HUMAN	Q969H0	Q16656	FBXW7	NRF1	MEDLINE	PMC4306233	PMC4306233	F-box	1	Other	H.sapiens
958	FBXW7_HUMAN	PSN1_HUMAN	Q969H0	P49768	FBXW7	PSEN1	MEDLINE	12354302	In this study, we show that human <span class="match term0">SEL-10</span> interacts with <span class="match term1">PS1</span> and enhances <span class="match term1">PS1</span> ubiquitination, thus altering cellular levels of unprocessed <span class="match term1">PS1</span> and its N- and C-terminal fragments	F-box	1	Training data	H.sapiens
959	FBXW7_HUMAN	HIF1A_HUMAN	Q969H0	Q16665	FBXW7	HIF1A	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
960	FBXW7_HUMAN	MYCN_HUMAN	Q969H0	P04198	FBXW7	MYCN	MEDLINE	19111882	Aurora A interacts with both <span class="match term1">N-Myc</span> and the SCF(<span class="match term0">Fbxw7</span>) ubiquitin ligase that ubiquitinates <span class="match term1">N-Myc</span> and counteracts degradation of <span class="match term1">N-Myc</span>, thereby uncoupling <span class="match term1">N-Myc</span> stability from growth factor-dependent signals	F-box	1	Training data	H.sapiens
961	FBXW7_HUMAN	DISC1_HUMAN	Q969H0	Q9NRI5	FBXW7	DISC1	MEDLINE	28727686	<span class="match term0">FBXW7</span> regulates <span class="match term1">DISC1</span> stability via the ubiquitin-proteosome system	F-box	1	Other	H.sapiens
962	FBXW7_HUMAN	NFKB2_HUMAN	Q969H0	Q00653	FBXW7	NFKB2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
963	FBXW7_HUMAN	NF2L1_HUMAN	Q969H0	Q14494	FBXW7	NFE2L1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
964	FBXW7_HUMAN	XBP1_HUMAN	Q969H0	P17861	FBXW7	XBP1	MEDLINE	30783083	Here we show that <span class="match term0">Fbw7</span>, a substrate recognition component of the SKP1-Cullin-F-box-type E3 ligase, interacts with <span class="match term1">XBP1</span> in a phosphorylation-dependent manner, and facilitates <span class="match term1">XBP1</span> ubiquitination and protein degradation	F-box	1	Other	H.sapiens
965	FBXW7_HUMAN	MTOR_HUMAN	Q969H0	P42345	FBXW7	MTOR	MEDLINE	18787170	<span class="match term0">FBXW7</span> targets <span class="match term1">mTOR</span> for degradation and cooperates with PTEN in tumor suppression	F-box	1	Training data	H.sapiens
966	FBXW7_HUMAN	EBP2_HUMAN	Q969H0	Q99848	FBXW7	EBNA1BP2	MEDLINE	21220517	UbiNet 2.0	F-box	1	Other	H.sapiens
967	FBXW7_HUMAN	KLF5_HUMAN	Q969H0	Q13887	FBXW7	KLF5	MEDLINE	20484041	UbiNet 2.0	F-box	1	Training data	H.sapiens
968	FBXW7_HUMAN	DEK_HUMAN	Q969H0	P35659	FBXW7	DEK	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
969	FBXW7_HUMAN	AURKB_HUMAN	Q969H0	Q96GD4	FBXW7	AURKB	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
970	FBXW7_HUMAN	MED13_HUMAN	Q969H0	Q9UHV7	FBXW7	MED13	MEDLINE	23322298	The SCF-<span class="match term0">Fbw7</span> ubiquitin ligase degrades <span class="match term1">MED13</span> and MED13L and regulates CDK8 module association with Mediator.	F-box	1	Other	H.sapiens
971	FBXW7_HUMAN	HSF1_HUMAN	Q969H0	Q00613	FBXW7	HSF1	MEDLINE	30284149	Here, we show that the ubiquitin ligase <span class="match term0">FBXW7</span> targets <span class="match term1">HSF1</span> for ubiquitination and degradation in intestinal I/R. In this study, we found that <span class="match term0">FBXW7</span> expression was upregulated at the transcriptional level in intestinal mucosae subjected to I/R.	F-box	1	Other	H.sapiens
972	FBXW8_HUMAN	IRS1_HUMAN	Q8N3Y1	P35568	FBXW8	IRS1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
973	FBXW8_HUMAN	TBC3A_HUMAN	Q8N3Y1	Q8IZP1	FBXW8	TBC1D3	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
974	FBXW8_HUMAN	M4K1_HUMAN	Q8N3Y1	Q92918	FBXW8	MAP4K1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
975	FBXW8_HUMAN	IBP2_HUMAN	Q8N3Y1	P18065	FBXW8	IGFBP2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
976	FBXW8_HUMAN	GORS1_HUMAN	Q8N3Y1	Q9BQQ3	FBXW8	GORASP1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
977	FBXW8_HUMAN	CCND1_HUMAN	Q8N3Y1	P24385	FBXW8	CCND1	MEDLINE	17205132	A critical role for <span class="match term0">FBXW8</span> and MAPK in cyclin D1 degradation and cancer cell proliferation.	F-box	1	Other	H.sapiens
978	FZR_HUMAN	PLK1_HUMAN	Q9UM11	P53350	FZR1	PLK1	UniProt	FZR_HUMAN	Dephosphorylation of <span class="match term0">FZR1</span>/CDH1 activates the APC/C, leading to the ubiquitination of <span class="match term1">PLK1</span>, preventing entry into mitosis	CDC20	1	Training data	H.sapiens
979	FZR1_HUMAN	E2F3_HUMAN	Q9UM11	O00716	FZR1	E2F3	MEDLINE	22580460	UbiNet 2.0	CDC20	1	Other	H.sapiens
980	FZR1_HUMAN	LATS2_HUMAN	Q9UM11	Q9NRM7	FZR1	LATS2	MEDLINE	31000600	31000600	CDC20	1	Other	H.sapiens
981	FZR_HUMAN	CDC20_HUMAN	Q9UM11	Q12834	FZR1	CDC20	MEDLINE	15916961	Activation of the anaphase-promoting complex/cyclosome (APC/C) by <span class="match term1">Cdc20</span> and <span class="match term0">Cdh1</span> leads to ubiquitin-dependent degradation of securin and cyclin B and thereby promotes the initiation of anaphase and exit from mitosis	CDC20	1	Training data	H.sapiens
982	FZR_HUMAN	CCNA2_HUMAN	Q9UM11	P20248	FZR1	CCNA2	MEDLINE	11285280	Cyclin A was efficiently polyubiquitylated by Cdc20 or <span class="match term0">Cdh1</span>-activated APC/C in vitro, but in contrast to cyclin B1, the proteolysis of cyclin A was not delayed by the spindle assembly checkpoint	CDC20	1	Training data	H.sapiens
983	FZR_HUMAN	BUB1_HUMAN	Q9UM11	O43683	FZR1	BUB1	MEDLINE	17158872	A <span class="match term1">Bub1</span> mutant protein with both KEN-boxes mutated is stable in cells but fails to elicit a cell cycle phenotype, indicating that degradation of <span class="match term1">Bub1</span> by APC/C(<span class="match term0">Cdh1</span>) is not required for mitotic exit	CDC20	1	Training data	H.sapiens
984	FZR_HUMAN	SKP2_HUMAN	Q9UM11	Q13309	FZR1	SKP2	MEDLINE	20717963	Collectively, our results suggest that Bcr-Abl increases Emi1 phosphorylation and stability to prevent <span class="match term1">Skp2</span> protein degradation via APC/<span class="match term0">Cdh1</span>-induced ubiquitination and to enhance proliferation of CML cells	CDC20	1	Training data	H.sapiens
985	FZR1_HUMAN	MYF5_HUMAN	Q9UM11	P13349	FZR1	MYF5	MEDLINE	17601983	UbiNet 2.0	CDC20	1	Training data	H.sapiens
986	FZR_HUMAN	PTTG1_HUMAN	Q9UM11	O95997	FZR1	PTTG1	MEDLINE	16355229	Cdc20 and <span class="match term0">Cdh1</span> are the activating subunits of the anaphase-promoting complex (APC), an E3 ubiquitin ligase that drives cells into anaphase by inducing degradation of cyclin B and the anaphase inhibitor securin	CDC20	1	Training data	H.sapiens
987	FZR_HUMAN	KTHY_HUMAN	Q9UM11	P23919	FZR1	DTYMK	MEDLINE	16103219	We demonstrate that <span class="match term1">TMPK</span> is recognized and degraded by APC/C-Cdc20/<span class="match term0">Cdh1</span>-mediated pathways from mitosis to the early G1 phase, whereas TK1 is targeted for degradation by APC/C-<span class="match term0">Cdh1</span> after mitotic exit	CDC20	1	Training data	H.sapiens
988	FZR1_HUMAN	NIPA_HUMAN	Q9UM11	Q86WB0	FZR1	ZC3HC1	MEDLINE	22205987	APC/C(<span class="match term0">Cdh1</span>)-mediated degradation of the F-box protein <span class="match term1">NIPA</span> is regulated by its association with Skp1.	CDC20	1	Other	H.sapiens
989	FZR_HUMAN	KITH_HUMAN	Q9UM11	P04183	FZR1	TK1	MEDLINE	16103219	We demonstrate that TMPK is recognized and degraded by APC/C-Cdc20/<span class="match term0">Cdh1</span>-mediated pathways from mitosis to the early G1 phase, whereas <span class="match term1">TK1</span> is targeted for degradation by APC/C-<span class="match term0">Cdh1</span> after mitotic exit	CDC20	1	Training data	H.sapiens
990	FZR1_HUMAN	STIL_HUMAN	Q9UM11	Q15468	FZR1	STIL	MEDLINE	24485834	UbiNet 2.0	CDC20	1	Other	H.sapiens
991	FZR_HUMAN	CCNB1_HUMAN	Q9UM11	P14635	FZR1	CCNB1	MEDLINE	18753608	As CDC20 is a substrate of APC (<span class="match term0">FZR1</span>), CDC20 might have competed with cyclin B and inhibited the <span class="match term0">FZR1</span> function	CDC20	1	Training data	H.sapiens
992	FZR_HUMAN	ID1_HUMAN	Q9UM11	P41134	FZR1	ID1	MEDLINE	16810178	APC/C(<span class="match term0">Cdh1</span>) targets Id2 for degradation through a destruction box motif (D box) that is conserved in <span class="match term1">Id1</span> and Id4	CDC20	1	Training data	H.sapiens
993	FZR_HUMAN	CDC6_HUMAN	Q9UM11	Q99741	FZR1	CDC6	MEDLINE	17567951	Previous studies have demonstrated that, in response to ionizing radiation, <span class="match term1">Cdc6</span> is ubiquitinated by the anaphase promoting complex (APC(<span class="match term0">Cdh1</span>)) in a p53-dependent manner	CDC20	1	Training data	H.sapiens
994	FZR1_HUMAN	BUB1B_HUMAN	Q9UM11	O60566	FZR1	BUB1B	MEDLINE	23091007	UbiNet 2.0	CDC20	1	Other	H.sapiens
995	FZR_HUMAN	TPX2_HUMAN	Q9UM11	Q9ULW0	FZR1	TPX2	MEDLINE	16287863	In a reconstituted system, <span class="match term1">TPX2</span> is efficiently ubiquitinated by APC/C that has been activated by <span class="match term0">Cdh1</span>	CDC20	1	Training data	H.sapiens
996	FZR1_HUMAN	NEK2_HUMAN	Q9UM11	P51955	FZR1	NEK2	MEDLINE	26387737	UbiNet 2.0	CDC20	1	Other	H.sapiens
997	FZR1_HUMAN	FOXM1_HUMAN	Q9UM11	Q08050	FZR1	FOXM1	MEDLINE	18573889	UbiNet 2.0	CDC20	1	Training data	H.sapiens
998	FZR_HUMAN	GEMI_HUMAN	Q9UM11	O75496	FZR1	GMNN	MEDLINE	19101468	Geminin is a direct substrate of the APC(<span class="match term0">Cdh1</span>) complex, and accumulates during the S, G(2), and M phases	CDC20	1	Training data	H.sapiens
999	FZR1_HUMAN	SOX2_HUMAN	Q9UM11	P48431	FZR1	SOX2	MEDLINE	23972993	UbiNet 2.0	CDC20	1	Other	H.sapiens
1000	FZR1_HUMAN	PAF15_HUMAN	Q9UM11	Q15004	FZR1	PCLAF	MEDLINE	21700221	UbiNet 2.0	CDC20	1	Other	H.sapiens
1001	FZR1_HUMAN	OPA1_HUMAN	Q9UM11	O60313	FZR1	OPA1	MEDLINE	23045728	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1002	FZR_HUMAN	CLSPN_HUMAN	Q9UM11	Q9HAW4	FZR1	CLSPN	MEDLINE	19124652	Importantly, we demonstrate that USP7 specifically opposes the SCF(betaTrCP)- but not APC(<span class="match term0">Cdh1</span>)-mediated degradation of <span class="match term1">Claspin</span>	CDC20	1	Training data	H.sapiens
1003	FZR_HUMAN	NUSAP_HUMAN	Q9UM11	Q9BXS6	FZR1	NUSAP1	MEDLINE	17618083	Here we show that <span class="match term1">NuSAP</span> can be ubiquitinated and degraded by APC/C-<span class="match term0">hCdh1</span> E3 ligase	CDC20	1	Training data	H.sapiens
1004	FZR1_HUMAN	HECW2_HUMAN	Q9UM11	Q9P2P5	FZR1	HECW2	MEDLINE	24163370	UbiNet 2.0	CDC20	1	Other	H.sapiens
1005	FZR1_HUMAN	TFAM_HUMAN	Q9UM11	Q00059	FZR1	TFAM	MEDLINE	23045728	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1006	FZR1_HUMAN	SAS6_HUMAN	Q9UM11	Q6UVJ0	FZR1	SASS6	MEDLINE	17681132	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1007	FZR_HUMAN	SKIL_HUMAN	Q9UM11	P12757	FZR1	SKIL	MEDLINE	11741538	Furthermore, the APC activator <span class="match term0">CDH1</span> and Smad3 synergistically regulate <span class="match term1">SnoN</span> degradation	CDC20	1	Training data	H.sapiens
1008	FZR_HUMAN	CKAP2_HUMAN	Q9UM11	Q8WWK9	FZR1	CKAP2	MEDLINE	17339342	Functional importance of the anaphase-promoting complex-<span class="match term0">Cdh1</span>-mediated degradation of TMAP/<span class="match term1">CKAP2</span> in regulation of spindle function and cytokinesis	CDC20	1	Training data	H.sapiens
1009	FZR1_HUMAN	DCPS_HUMAN	Q9UM11	Q96C86	FZR1	DCPS	MEDLINE	25043029	UbiNet 2.0	CDC20	1	Other	H.sapiens
1010	FZR_HUMAN	RUNX1_HUMAN	Q9UM11	Q01196	FZR1	RUNX1	MEDLINE	17015473	A phospho-mimic protein, <span class="match term1">AML1</span>-4D, can be targeted by Cdc20 or <span class="match term0">Cdh1</span>	CDC20	1	Training data	H.sapiens
1011	FZR1_HUMAN	MK08_HUMAN	Q9UM11	P45983	FZR1	MAPK8	MEDLINE	20581839	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1012	FZR1_HUMAN	F263_HUMAN	Q9UM11	Q16875	FZR1	PFKFB3	MEDLINE	20080744	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1013	FZR1_HUMAN	PECA1_HUMAN	Q9UM11	P16284	FZR1	PECAM1	MEDLINE	31489637	APC/<span class="match term0">Cdh1</span> targets <span class="match term1">PECAM-1</span> for ubiquitination and degradation in endothelial cells.	CDC20	1	Other	H.sapiens
1014	FZR1_HUMAN	ANLN_HUMAN	Q9UM11	Q9NQW6	FZR1	ANLN	MEDLINE	16040610	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1015	FZR1_HUMAN	E2F1_HUMAN	Q9UM11	Q01094	FZR1	E2F1	MEDLINE	22580462	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1016	FZR_HUMAN	DNMT1_HUMAN	Q9UM11	P26358	FZR1	DNMT1	MEDLINE	15899874	Both <span class="match term1">Dnmt1</span> and <span class="match term0">Cdh1</span> were phosphorylated in vivo, but only <span class="match term0">Cdh1</span> was significantly dephosphorylated upon 5-aza-CdR treatment, suggesting its involvement in initiating the proteasomal degradation of <span class="match term1">DNMT1</span>	CDC20	1	Training data	H.sapiens
1017	FZR1_HUMAN	DNM1L_HUMAN	Q9UM11	O00429	FZR1	DNM1L	MEDLINE	21325626	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1018	FZR1_HUMAN	TRRAP_HUMAN	Q9UM11	Q9Y4A5	FZR1	TRRAP	MEDLINE	23318449	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1019	FZR_HUMAN	CASL_HUMAN	Q9UM11	Q14511	FZR1	NEDD9	MEDLINE	15144564	CONCLUSIONS: Our data suggests that Smad3 may recruit the APC complex via a direct interaction with the APC subunit APC10 to regulate the ubiquitination and degradation of its interactor <span class="match term1">HEF1</span>, which is recognized as an ubiquitination substrate by the <span class="match term0">CDH1</span> subunit of the APC complex	CDC20	1	Training data	H.sapiens
1020	FZR_HUMAN	CAD13_HUMAN	Q9UM11	P55290	FZR1	CDH13	MEDLINE	17631504	Ectopic expression of <span class="match term0">Cdh1</span> (CDC20 homolog 1), one of the substrate recognition components of anaphase promoting complex (E3 ligase), stimulated T-Cad degradation	CDC20	1	Training data	H.sapiens
1021	FZR_HUMAN	ID2_HUMAN	Q9UM11	Q02363	FZR1	ID2	MEDLINE	16810178	APC/C(<span class="match term0">Cdh1</span>) targets <span class="match term1">Id2</span> for degradation through a destruction box motif (D box) that is conserved in Id1 and Id4	CDC20	1	Training data	H.sapiens
1022	FZR1_HUMAN	AURKB_HUMAN	Q9UM11	Q96GD4	FZR1	AURKB	MEDLINE	16204042	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1023	FZR1_HUMAN	PAX3_HUMAN	Q9UM11	P23760	FZR1	PAX3	MEDLINE	26329581	The E3 ligase APC/C(<span class="match term0">Cdh1</span>) promotes ubiquitylation-mediated proteolysis of <span class="match term1">PAX3</span> to suppress melanocyte proliferation and melanoma growth.	CDC20	1	Other	H.sapiens
1024	FZR1_HUMAN	UBP1_HUMAN	Q9UM11	O94782	FZR1	USP1	MEDLINE	21768287	APC/CCdh1-dependent proteolysis of <span class="match term1">USP1</span> regulates the response to UV-mediated DNA damage.	CDC20	1	Other	H.sapiens
1025	FZR_HUMAN	SGOL1_HUMAN	Q9UM11	Q5FBB7	FZR1	SGOL1	MEDLINE	19015261	Sgo1 is ubiquitinated by APC/C bound to <span class="match term0">Cdh1</span> (APC/C(<span class="match term0">Cdh1</span>)) in vitro	CDC20	1	Training data	H.sapiens
1026	FZR1_HUMAN	MPIP1_HUMAN	Q9UM11	P30304	FZR1	CDC25A	MEDLINE	12234927	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1027	FZR1_HUMAN	CTIP_HUMAN	Q9UM11	Q99708	FZR1	RBBP8	MEDLINE	22199232	E3Net	CDC20	1	Other	H.sapiens
1028	FZR1_HUMAN	MK09_HUMAN	Q9UM11	P45984	FZR1	MAPK9	MEDLINE	20581839	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1029	FZR1_HUMAN	MK10_HUMAN	Q9UM11	P53779	FZR1	MAPK10	MEDLINE	20581839	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1030	FZR1_HUMAN	NDC80_HUMAN	Q9UM11	O14777	FZR1	NDC80	MEDLINE	21199005	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1031	FZR1_HUMAN	MFN1_HUMAN	Q9UM11	Q8IWA4	FZR1	MFN1	MEDLINE	23045728	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1032	FZR1_HUMAN	AURKA_HUMAN	Q9UM11	O14965	FZR1	AURKA	MEDLINE	12023018	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1033	FZR1_HUMAN	KLF4_HUMAN	Q9UM11	O43474	FZR1	KLF4	MEDLINE	21177849	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1034	FZR1_HUMAN	MOAP1_HUMAN	Q9UM11	Q96BY2	FZR1	MOAP1	MEDLINE	22529100	UbiNet 2.0	CDC20	1	Training data	H.sapiens
1035	GAN_HUMAN	-	Q9H2C0	-	GAN	IF	MEDLINE	23585478	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1036	GAN_HUMAN	TBCB_HUMAN	Q9H2C0	Q99426	GAN	TBCB	UniProt	GAN_HUMAN	Ubiquitinated in the presence of <span class="match term0">GAN</span> which targets it for degradation by the proteasome (By similarity)	BTB_3	1	Training data	H.sapiens
1037	GAN_HUMAN	MAP1S_HUMAN	Q9H2C0	Q66K74	GAN	MAP1S	MEDLINE	19168853	Gigaxonin has been proposed as a substrate adaptor for an E3 ubiquitin ligase, which affects proteasome-dependent degradation of microtubule-related proteins including MAP1B, <span class="match term1">MAP8</span> and the tubulin folding chaperone TBCB	BTB_3	1	Training data	H.sapiens
1038	GAN_HUMAN	A16L1_HUMAN	Q9H2C0	Q676U5	GAN	ATG16L1	MEDLINE	30770803	Gigaxonin interacts with the WD40 domain of <span class="match term1">ATG16L1</span> to drive its ubiquitination and subsequent degradation	BTB_3	1	Other	H.sapiens
1039	GAN_HUMAN	MAP1B_HUMAN	Q9H2C0	P46821	GAN	MAP1B	MEDLINE	19168853	Gigaxonin has been proposed as a substrate adaptor for an E3 ubiquitin ligase, which affects proteasome-dependent degradation of microtubule-related proteins including <span class="match term1">MAP1B</span>, MAP8 and the tubulin folding chaperone TBCB	BTB_3	1	Training data	H.sapiens
1040	GAN_HUMAN	SHH_HUMAN	Q9H2C0	Q15465	GAN	SHH	MEDLINE	31503551	31503551	BTB_3	1	Other	H.sapiens
1041	GAN_HUMAN	GFAP_HUMAN	Q9H2C0	P14136	GAN	GFAP	MEDLINE	27798231	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1042	HACE1_HUMAN	RAC1_HUMAN	Q8IYU2	P63000	HACE1	RAC1	MEDLINE	22036506	The E3 ubiquitin-ligase <span class="match term0">HACE1</span> catalyzes the ubiquitylation of active <span class="match term1">Rac1</span>.	HECT	1	Other	H.sapiens
1043	HACE1_HUMAN	GOLM1_HUMAN	Q8IYU2	Q8NBJ4	HACE1	GOLM1	MEDLINE	21988917	UbiNet 2.0	HECT	1	Training data	H.sapiens
1044	HACE1_HUMAN	CCND1_HUMAN	Q8IYU2	P24385	HACE1	CCND1	MEDLINE	17694067	Mechanistically, the tumor-suppressor function of <span class="match term0">HACE1</span> is dependent on its E3 ligase activity and <span class="match term0">HACE1</span> controls adhesion-dependent growth and cell cycle progression during cell stress through degradation of cyclin D1	HECT	1	Training data	H.sapiens
1045	HACE1_HUMAN	RARA_HUMAN	Q8IYU2	P10276	HACE1	RARA	MEDLINE	19350571	UbiNet 2.0	HECT	1	Training data	H.sapiens
1046	HACE1_HUMAN	RARB_HUMAN	Q8IYU2	P10826	HACE1	RARB	MEDLINE	19350571	UbiNet 2.0	HECT	1	Training data	H.sapiens
1047	HACE1_HUMAN	OPTN_HUMAN	Q8IYU2	Q96CV9	HACE1	OPTN	MEDLINE	25026213	UbiNet 2.0	HECT	1	Other	H.sapiens
1048	HDAC6_HUMAN	GLI1_HUMAN	Q9UBN7	P08151	HDAC6	GLI1	MEDLINE	33895473	RNF220-mediated ubiquitination promotes aggresomal accumulation and autophagic degradation of cytoplasmic <span class="match term1">Gli</span> via <span class="match term0">HDAC6</span>	Other	1	Other	H.sapiens
1049	HDAC6_HUMAN	CHK1_HUMAN	Q9UBN7	O14757	HDAC6	CHEK1	MEDLINE	33020410	We have found that <span class="match term0">HDAC6</span> and <span class="match term1">Chk1</span> directly interact, and that <span class="match term0">HDAC6</span> ubiquitinates <span class="match term1">Chk1</span> in vivo and in vitro	Other	1	Other	H.sapiens
1050	HECD1_HUMAN	PI51C_HUMAN	Q9ULT8	O60331	HECTD1	PIP5K1C	MEDLINE	23572508	UbiNet 2.0	HECT	1	Training data	H.sapiens
1051	HECD1_HUMAN	MACF1_HUMAN	Q9ULT8	Q9UPN3	HECTD1	MACF1	MEDLINE	29386124	The E3 Ubiquitin Ligase <span class="match term0">HectD1</span> Suppresses EMT and Metastasis by Targeting the +TIP <span class="match term1">ACF7</span> for Degradation	HECT	1	Other	H.sapiens
1052	HECD1_HUMAN	SNAI1_HUMAN	Q9ULT8	O95863	HECTD1	SNAI1	MEDLINE	32319576	On the whole, the data of the present study indicated that <span class="match term0">HECTD1</span> serves as an E3 ubiquitin ligase to mediate the stability of <span class="match term1">SNAIL</span> proteins.	HECT	1	Other	H.sapiens
1053	HECD2_HUMAN	PIAS1_HUMAN	Q5U5R9	O75925	HECTD2	PIAS1	MEDLINE	26157031	UbiNet 2.0	HECT	1	Other	H.sapiens
1054	HECD3_HUMAN	STX8_HUMAN	Q5T447	Q9UNK0	HECTD3	STX8	UniProt	HECD3_HUMAN	Ubiquitinated by <span class="match term0">HECTD3</span> (By similarity)	HECT	1	Training data	H.sapiens
1055	HECD3_HUMAN	CASP9_HUMAN	Q5T447	P55211	HECTD3	CASP9	MEDLINE	28716524	<span class="match term0">HECTD3</span> can bind and ubiquitinate caspase-9, which leads to inhibiting caspase-9 oligomerization and association with Apaf-1, and results in suppressing caspase-9 activation and inhibiting apoptosis	HECT	1	Other	H.sapiens
1056	HECD3_HUMAN	TARA_HUMAN	Q5T447	Q9H2D6	HECTD3	TRIOBP	MEDLINE	18194665	All these findings suggest that <span class="match term0">HECTD3</span> may facilitate cell cycle progression via regulating ubiquitination and degradation of <span class="match term1">Tara</span>	HECT	1	Training data	H.sapiens
1057	HECD3_HUMAN	MALT1_HUMAN	Q5T447	Q9UDY8	HECTD3	MALT1	MEDLINE	23358872	UbiNet 2.0	HECT	1	Training data	H.sapiens
1058	HECD3_HUMAN	CASP8_HUMAN	Q5T447	Q14790	HECTD3	CASP8	MEDLINE	24287696	These findings suggest that caspase-8 ubiquitination by <span class="match term0">HECTD3</span> confers cancer cell survival	HECT	1	Other	H.sapiens
1059	HECD3_HUMAN	RAF1_HUMAN	Q5T447	P04049	HECTD3	RAF1	MEDLINE	28636940	UbiNet 2.0	HECT	1	Other	H.sapiens
1060	HECW1_HUMAN	DVL1_HUMAN	Q76N89	O14640	HECW1	DVL1	UniProt	HECW1_HUMAN	E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent degradation of <span class="match term1">DVL1</span>	HECT	1	Training data	H.sapiens
1061	HECW1_HUMAN	TTF1_HUMAN	Q76N89	Q15361	HECW1	TTF1	MEDLINE	30849519	Furthermore, we demonstrate that an E3 ubiquitin ligase, named HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1 (<span class="match term0">HECW1</span>), targets <span class="match term1">TTF1</span> for its ubiquitination and degradation, while downregulation of <span class="match term0">HECW1</span> attenuates PMA-induced <span class="match term1">TTF1</span> ubiquitination and degradation	HECT	1	Other	H.sapiens
1062	HECW1_HUMAN	SMAD4_HUMAN	Q76N89	Q13485	HECW1	SMAD4	MEDLINE	33529121	E3 ubiquitin ligase <span class="match term0">HECW1</span> promotes the metastasis of non-small cell lung cancer cells through mediating the ubiquitination of <span class="match term1">Smad4</span>	HECT	1	Other	H.sapiens
1063	HECW2_HUMAN	PCNA_HUMAN	Q9P2P5	P12004	HECW2	PCNA	MEDLINE	29753763	E3 ubiquitin ligase <span class="match term0">HECW2</span> targets <span class="match term1">PCNA</span> and lamin B1	HECT	1	Other	H.sapiens
1064	HECW2_HUMAN	LMNB1_HUMAN	Q9P2P5	P20700	HECW2	LMNB1	MEDLINE	29753763	E3 ubiquitin ligase <span class="match term0">HECW2</span> targets PCNA and <span class="match term1">lamin B1</span>	HECT	1	Other	H.sapiens
1065	HECW2_HUMAN	P73_HUMAN	Q9P2P5	O15350	HECW2	TP73	MEDLINE	12890487	UbiNet 2.0	HECT	1	Training data	H.sapiens
1066	HERC1_HUMAN	SOX9_HUMAN	Q15751	P48436	HERC1	SOX9	MEDLINE	24155239	UbiNet 2.0	HECT	1	Other	H.sapiens
1067	HERC1_HUMAN	TSC2_HUMAN	Q15751	P49815	HERC1	TSC2	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1068	HERC1_HUMAN	RAF1_HUMAN	Q15751	P04049	HERC1	RAF1	MEDLINE	30140388	In vitro ubiquitylation assays indicate that <span class="match term1">C-RAF</span> is a substrate of the E3 ubiquitin ligase <span class="match term0">HERC1</span>	HECT	1	Other	H.sapiens
1069	HERC2_HUMAN	XPA_HUMAN	O95714	P23025	HERC2	XPA	MEDLINE	21193487	Ubiquitination and proteolysis of <span class="match term1">XPA</span> are inhibited by DNA damage that promotes tight association of the protein with chromatin and its dissociation from the <span class="match term0">HERC2</span> E3 ligase	HECT	1	Training data	H.sapiens
1070	HERC2_HUMAN	NEUL4_HUMAN	O95714	Q96JN8	HERC2	NEURL4	MEDLINE	22261722	UbiNet 2.0	HECT	1	Training data	H.sapiens
1071	HERC2_HUMAN	SUMO1_HUMAN	O95714	P63165	HERC2	SUMO1	MEDLINE	33377049	Here, we describe a protocol for biochemical and structural analysis of the ZZ domain of human E3 ubiquitin ligase <span class="match term0">HERC2</span> (HERC2ZZ) and its interaction with its ligands: the N-terminal tails of histone H3 and <span class="match term1">SUMO1</span>	HECT	1	Other	H.sapiens
1072	HERC2_HUMAN	BRCA1_HUMAN	O95714	P38398	HERC2	BRCA1	MEDLINE	20631078	<span class="match term0">HERC2</span> is an E3 ligase that targets <span class="match term1">BRCA1</span> for degradation.Conversely, BARD1 protects <span class="match term1">BRCA1</span> from <span class="match term0">HERC2</span>-mediated ubiquitination	HECT	1	Other	H.sapiens
1073	HERC2_HUMAN	UBP20_HUMAN	O95714	Q9Y2K6	HERC2	USP20	MEDLINE	25355518	UbiNet 2.0	HECT	1	Other	H.sapiens
1074	HERC4_HUMAN	LATS1_HUMAN	Q5GLZ8	O95835	HERC4	LATS1	MEDLINE	30710319	<span class="match term0">HERC4</span> is a new E3 ligase for the tumor suppressor <span class="match term1">LATS1</span> and destabilizes <span class="match term1">LATS1</span> by promoting the ubiquitination of <span class="match term1">LATS1</span>	HECT	1	Other	H.sapiens
1075	HERC5_HUMAN	CTBP1_HUMAN	Q9UII4	Q13363	HERC5	CTBP1	MEDLINE	34147029	Collectively, our results reveal that downregulation of <span class="match term0">HERC5</span> E3 ligase attenuates the ubiquitination of <span class="match term1">CtBP1</span> to inhibit apoptosis	HECT	1	Other	H.sapiens
1076	HERC5_HUMAN	NDKB_HUMAN	Q9UII4	P22392	HERC5	NME2	MEDLINE	18535780	While hPLIC proteins are not ubiquitinated by HERC3, <span class="match term0">HERC5</span> plays an important role in ubiquitination of <span class="match term1">Nm23B</span>	HECT	1	Training data	H.sapiens
1077	HLTF_HUMAN	PCNA_HUMAN	Q14527	P12004	HLTF	PCNA	MEDLINE	21269891	<span class="match term0">HLTF</span> and SHPRH are not essential for <span class="match term1">PCNA</span> polyubiquitination, survival and somatic hypermutation: Existence of an alternative E3 ligase	RING	1	Training data	H.sapiens
1078	HUWE1_HUMAN	MUTYH_HUMAN	Q7Z6Z7	Q9UIF7	HUWE1	MUTYH	MEDLINE	24443563	Regulation of human <span class="match term1">MutYH</span> DNA glycosylase by the E3 ubiquitin ligase <span class="match term0">mule</span>.	HECT	1	Other	H.sapiens
1079	HUWE1_HUMAN	H2A2B_HUMAN	Q7Z6Z7	Q8IUE6	HUWE1	H2AC21	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1080	HUWE1_HUMAN	KDM3A_HUMAN	Q7Z6Z7	Q9Y4C1	HUWE1	KDM3A	MEDLINE	32238799	Further, we found that ubiquitin ligase <span class="match term0">HUWE1</span> induced the K27-/K29-linked noncanonical ubiquitination of <span class="match term1">JMJD1A</span> at lysine-918	HECT	1	Other	H.sapiens
1081	HUWE1_HUMAN	P53_HUMAN	Q7Z6Z7	P04637	HUWE1	TP53	MEDLINE	21233842	Intriguingly, the human homologue of EEL-1, <span class="match term0">Huwe1</span>/ARF-BP1/Mule/HectH9, has been reported to possess both pro- and anti-apoptotic functions through its ability to stimulate Mcl-1 and <span class="match term1">p53</span> degradation, respectively	HECT	1	Training data	H.sapiens
1082	HUWE1_HUMAN	TGFR2_HUMAN	Q7Z6Z7	P37173	HUWE1	TGFBR2	MEDLINE	33405091	The E3 ligase <span class="match term0">HUWE1</span> mediates <span class="match term1">TGFBR2</span> ubiquitination and promotes gastric cancer cell proliferation, migration, and invasion	HECT	1	Other	H.sapiens
1083	HUWE1_HUMAN	MYC_HUMAN	Q7Z6Z7	P01106	HUWE1	MYC	MEDLINE	16269333	UbiNet 2.0	HECT	1	Training data	H.sapiens
1084	HUWE1_HUMAN	WIPI2_HUMAN	Q7Z6Z7	Q9Y4P8	HUWE1	WIPI2	MEDLINE	30646805	With this clue, we uncovered that <span class="match term1">WIPI2</span> is a phosphorylation substrate of MTORC1 and a ubiquitination target of <span class="match term0">HUWE1</span>	HECT	1	Other	H.sapiens
1085	HUWE1_HUMAN	H2B1B_HUMAN	Q7Z6Z7	P33778	HUWE1	H2BC3	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1086	HUWE1_HUMAN	HXK2_HUMAN	Q7Z6Z7	P52789	HUWE1	HK2	MEDLINE	31201299	Here we identify that K63-linked ubiquitination by <span class="match term0">HectH9</span> regulates the mitochondrial localization and function of <span class="match term1">HK2</span>	HECT	1	Other	H.sapiens
1087	HUWE1_HUMAN	H15_HUMAN	Q7Z6Z7	P16401	HUWE1	H1-5	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1088	HUWE1_HUMAN	NR1D1_HUMAN	Q7Z6Z7	P20393	HUWE1	NR1D1	MEDLINE	20534529	UbiNet 2.0	HECT	1	Training data	H.sapiens
1089	HUWE1_HUMAN	MCL1_HUMAN	Q7Z6Z7	Q07820	HUWE1	MCL1	MEDLINE	16213503	UbiNet 2.0	HECT	1	Training data	H.sapiens
1090	HUWE1_HUMAN	H32_HUMAN	Q7Z6Z7	Q71DI3	HUWE1	H3C15	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1091	HUWE1_HUMAN	CHK1_HUMAN	Q7Z6Z7	O14757	HUWE1	CHEK1	MEDLINE	31713291	We also identified multiple lysine residues on <span class="match term1">Chk1</span> that are poly-ubiquitinated by <span class="match term0">HUWE1</span> in vitro, many of which are within the kinase domain	HECT	1	Other	H.sapiens
1092	HUWE1_HUMAN	H2B1A_HUMAN	Q7Z6Z7	Q96A08	HUWE1	H2BC1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1093	HUWE1_HUMAN	PIAS2_HUMAN	Q7Z6Z7	O75928	HUWE1	PIAS2	MEDLINE	20624960	UbiNet 2.0	HECT	1	Other	H.sapiens
1094	HUWE1_HUMAN	PA2G4_HUMAN	Q7Z6Z7	Q9UQ80	HUWE1	PA2G4	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1095	HUWE1_HUMAN	PPARA_HUMAN	Q7Z6Z7	Q07869	HUWE1	PPARA	MEDLINE	29331071	Furthermore, the E3 ubiquitin ligase <span class="match term0">HUWE1</span> was identified to mediate <span class="match term1">PPARalpha</span> polyubiquitination.	HECT	1	Other	H.sapiens
1096	HUWE1_HUMAN	PCNA_HUMAN	Q7Z6Z7	P12004	HUWE1	PCNA	MEDLINE	22203964	UbiNet 2.0	HECT	1	Other	H.sapiens
1097	HUWE1_HUMAN	MYCN_HUMAN	Q7Z6Z7	P04198	HUWE1	MYCN	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1098	HUWE1_HUMAN	MYOD1_HUMAN	Q7Z6Z7	P15172	HUWE1	MYOD1	MEDLINE	22277673	<span class="match term0">HUWE1</span> ubiquitinates <span class="match term1">MyoD</span> and targets it for proteasomal degradation	HECT	1	Other	H.sapiens
1099	HUWE1_HUMAN	DUS4_HUMAN	Q7Z6Z7	Q13115	HUWE1	DUSP4	MEDLINE	34320342	Mechanistically, PRMT1-mediated methylation of <span class="match term1">DUSP4</span> triggers its ubiquitinylation by an E3 ligase <span class="match term0">HUWE1</span>	HECT	1	Other	H.sapiens
1100	HUWE1_HUMAN	OGT1_HUMAN	Q7Z6Z7	O15294	HUWE1	OGT	MEDLINE	30858176	30858176	HECT	1	Other	H.sapiens
1101	HUWE1_HUMAN	H4_HUMAN	Q7Z6Z7	P62805	HUWE1	H4C1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1102	HUWE1_HUMAN	DPOLL_HUMAN	Q7Z6Z7	Q9UGP5	HUWE1	POLL	MEDLINE	22203964	UbiNet 2.0	HECT	1	Other	H.sapiens
1103	HUWE1_HUMAN	H2A2C_HUMAN	Q7Z6Z7	Q16777	HUWE1	H2AC20	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1104	HUWE1_HUMAN	ZBT17_HUMAN	Q7Z6Z7	Q13105	HUWE1	ZBTB17	MEDLINE	26212014	Syk-mediated tyrosine phosphorylation of <span class="match term0">mule</span> promotes TNF-induced JNK activation and cell death.	HECT	1	Other	H.sapiens
1105	HUWE1_HUMAN	HUWE1_HUMAN	Q7Z6Z7	Q7Z6Z7	HUWE1	HUWE1	MEDLINE	17580310	Ubiquitin activated by UBE1L2 could be used for ubiquitylation of p53 by MDM2 and supported the autoubiquitylation of the E3 ubiquitin ligases <span class="match term0">HectH9</span> and E6-AP	HECT	1	Training data	H.sapiens
1106	HUWE1_HUMAN	H11_HUMAN	Q7Z6Z7	Q02539	HUWE1	H1-1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1107	HUWE1_HUMAN	Q8IZG5_HUMAN	Q7Z6Z7	Q8IZG5	HUWE1	SS18	MEDLINE	30818224	UbiNet 2.0	HECT	1	Other	H.sapiens
1108	HUWE1_HUMAN	CDC6_HUMAN	Q7Z6Z7	Q99741	HUWE1	CDC6	MEDLINE	18617514	UbiNet 2.0	HECT	1	Training data	H.sapiens
1109	HUWE1_HUMAN	BRCA1_HUMAN	Q7Z6Z7	P38398	HUWE1	BRCA1	MEDLINE	24472556	<span class="match term0">HUWE1</span> interacts with <span class="match term1">BRCA1</span> and promotes its degradation in the ubiquitin-proteasome pathway	HECT	1	Other	H.sapiens
1110	HUWE1_HUMAN	DPOLB_HUMAN	Q7Z6Z7	P06746	HUWE1	POLB	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1111	HUWE1_HUMAN	ASCL1_HUMAN	Q7Z6Z7	P50553	HUWE1	ASCL1	MEDLINE	29545540	Only cytoplasmic ubiquitylation targets <span class="match term1">Ascl1</span> for destruction, which occurs by conjugation of ubiquitin to lysines in the basic helix-loop-helix domain of <span class="match term1">Ascl1</span> and requires the E3 ligase <span class="match term0">Huwe1</span>	HECT	1	Other	H.sapiens
1112	HUWE1_HUMAN	ATOH1_HUMAN	Q7Z6Z7	Q92858	HUWE1	ATOH1	MEDLINE	27542412	Destabilization of <span class="match term1">Atoh1</span> by E3 Ubiquitin Ligase <span class="match term0">Huwe1</span> and Casein Kinase 1 Is Essential for Normal Sensory Hair Cell Development.	HECT	1	Other	H.sapiens
1113	HUWE1_HUMAN	HDAC2_HUMAN	Q7Z6Z7	Q92769	HUWE1	HDAC2	MEDLINE	22016339	UbiNet 2.0	HECT	1	Training data	H.sapiens
1114	I17RB_HUMAN	PEX7_HUMAN	Q9NRM6	O00628	IL17RB	PEX7	MEDLINE	30378028	Identification of DDB1 (damage-specific DNA-binding protein 1), a component of <span class="match term0">CRL4</span> (Cullin4A-RING ubiquitin ligase) E3 complex, as a <span class="match term1">Pex7</span>-interacting protein revealed that quality control of <span class="match term1">Pex7</span> by CRL4A is important for PTS2 protein import by preventing the accumulation of dysfunctional <span class="match term1">Pex7</span>	Other	1	Other	H.sapiens
1115	ING4_HUMAN	TF65_HUMAN	Q9UNL4	Q04206	ING4	RELA	MEDLINE	23624912	<span class="match term0">ING4</span> bound to <span class="match term1">p65</span> and delivered the Lys-48-linked polyubiquitin to Lys-62 residue of <span class="match term1">p65</span>, leading to ubiquitination of <span class="match term1">p65</span> and degradation	Other	1	Other	H.sapiens
1116	IRAK1_HUMAN	PELI1_HUMAN	P51617	Q96FA3	IRAK1	PELI1	MEDLINE	17675297	Whereas the Pellino proteins cause polyubiquitination of <span class="match term0">IRAK</span>-1, we also show that kinase-active members of the <span class="match term0">IRAK</span> family (<span class="match term0">IRAK</span>-1 and <span class="match term0">IRAK</span>-4) promote reciprocal polyubiquitination of the Pellino proteins and that this is associated with <span class="match term0">IRAK</span>-induced degradation of the Pellino family	SINGLE_OTHER	1	Training data	H.sapiens
1117	IRAK4_HUMAN	PELI1_HUMAN	Q9NWZ3	Q96FA3	IRAK4	PELI1	MEDLINE	17675297	Whereas the Pellino proteins cause polyubiquitination of IRAK-1, we also show that kinase-active members of the IRAK family (IRAK-1 and <span class="match term0">IRAK-4</span>) promote reciprocal polyubiquitination of the Pellino proteins and that this is associated with IRAK-induced degradation of the Pellino family	SINGLE_OTHER	1	Training data	H.sapiens
1118	ITCH_HUMAN	KLF10_HUMAN	Q96J02	Q13118	ITCH	KLF10	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1119	ITCH_HUMAN	SMAD7_HUMAN	Q96J02	O15105	ITCH	SMAD7	MEDLINE	15946939	UbiNet 2.0	HECT	1	Other	H.sapiens
1120	ITCH_HUMAN	FOXO1_HUMAN	Q96J02	Q12778	ITCH	FOXO1	MEDLINE	24859451	<span class="match term0">Itch</span> associated with the transcription factor <span class="match term1">Foxo1</span> and promoted its ubiquitination and degradation	HECT	1	Other	H.sapiens
1121	ITCH_HUMAN	CXCR4_HUMAN	Q96J02	P61073	ITCH	CXCR4	MEDLINE	19116316	The E3 ubiquitin ligase atrophin interacting protein 4 (<span class="match term0">AIP4</span>) mediates ubiquitination and down-regulation of the chemokine receptor <span class="match term1">CXCR4</span>	HECT	1	Training data	H.sapiens
1122	ITCH_HUMAN	BID_HUMAN	Q96J02	P55957	ITCH	BID	UniProt	ITCH_HUMAN	p15 <span class="match term1">BID</span> is ubiquitinated by <span class="match term0">ITCH</span>; ubiquitination results in proteasome-dependent degradation	HECT	1	Training data	H.sapiens
1123	ITCH_HUMAN	LRP6_HUMAN	Q96J02	O75581	ITCH	LRP6	MEDLINE	28966723	UbiNet 2.0	HECT	1	Other	H.sapiens
1124	ITCH_HUMAN	NOTC3_HUMAN	Q96J02	Q9UM47	ITCH	NOTCH3	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1125	ITCH_HUMAN	ITSN1_HUMAN	Q96J02	Q15811	ITCH	ITSN1	MEDLINE	29851086	Thus, different modes of ubiquitination regulated by <span class="match term0">AIP4</span> have opposite effects on <span class="match term1">ITSN1</span> isoform stability.	HECT	1	Other	H.sapiens
1126	ITCH_HUMAN	JUN_HUMAN	Q96J02	P05412	ITCH	JUN	MEDLINE	15469925	Inhibition of lysosomal protein degradation by bafilomycin or chloroquine stabilized <span class="match term1">Jun</span> but had no effect on the stability of mutated <span class="match term1">Jun</span> that was not ubiquitinated by <span class="match term0">Itch</span>/AIP4	HECT	1	Training data	H.sapiens
1127	ITCH_HUMAN	M1_I33A0	Q96J02	P05777	ITCH	M	MEDLINE	30328013	UbiNet 2.0	HECT	1	Other	H.sapiens
1128	ITCH_HUMAN	EGFR_HUMAN	Q96J02	P00533	ITCH	EGFR	MEDLINE	12226085	In addition, we observed that CBLC increases the ubiquitination of <span class="match term1">EGFR</span>, and that coexpressing the WW domains of <span class="match term0">AIP4</span> exerts a dominant negative effect on <span class="match term1">EGFR</span> ubiquitination	HECT	1	Training data	H.sapiens
1129	ITCH_HUMAN	P63_HUMAN	Q96J02	Q9H3D4	ITCH	TP63	MEDLINE	17592138	Similarly, both c-Jun and <span class="match term1">p63</span> polyubiquitylation by <span class="match term0">Itch</span> are inhibited by N4BP1	HECT	1	Training data	H.sapiens
1130	ITCH_HUMAN	SNX9_HUMAN	Q96J02	Q9Y5X1	ITCH	SNX9	MEDLINE	20491914	Interaction with the PRD of <span class="match term0">Itch</span> is essential for <span class="match term1">SNX9</span> ubiquitylation and degradation	HECT	1	Training data	H.sapiens
1131	ITCH_HUMAN	CPSF6_HUMAN	Q96J02	Q16630	ITCH	CPSF6	MEDLINE	16055720	We validated one complex in detail, showing that WW domains of the <span class="match term0">AIP4</span> E3 protein-ubiquitin ligase bind directly to a PPXY motif in the p68 subunit of pre-mRNA cleavage and polyadenylation factor Im in a manner that promotes p68 ubiquitylation	HECT	1	Training data	H.sapiens
1132	ITCH_HUMAN	LATS1_HUMAN	Q96J02	O95835	ITCH	LATS1	MEDLINE	21383157	UbiNet 2.0	HECT	1	Training data	H.sapiens
1133	ITCH_HUMAN	P73_HUMAN	Q96J02	O15350	ITCH	TP73	MEDLINE	18701449	A regulatory circuit controlling <span class="match term0">Itch</span>-mediated <span class="match term1">p73</span> degradation by Runx	HECT	1	Training data	H.sapiens
1134	ITCH_HUMAN	FYN_HUMAN	Q96J02	P06241	ITCH	FYN	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1135	ITCH_HUMAN	OCLN_HUMAN	Q96J02	Q16625	ITCH	OCLN	MEDLINE	15605377	UbiNet 2.0	HECT	1	Training data	H.sapiens
1136	ITCH_HUMAN	RASF5_HUMAN	Q96J02	Q8WWW0	ITCH	RASSF5	MEDLINE	23538446	Importantly, the overexpression of <span class="match term0">Itch</span> induces <span class="match term1">RASSF5</span> degradation by poly-ubiquitination via 26S proteasome pathway	HECT	1	Other	H.sapiens
1137	ITCH_HUMAN	JUNB_HUMAN	Q96J02	P17275	ITCH	JUNB	MEDLINE	15358865	Activation of the Jun amino-terminal kinase (JNK) mitogen-activated protein kinase cascade after T cell stimulation accelerated degradation of c-Jun and <span class="match term1">JunB</span> through phosphorylation-dependent activation of the E3 ligase <span class="match term0">Itch</span>	HECT	1	Training data	H.sapiens
1138	ITCH_HUMAN	SUFU_HUMAN	Q96J02	Q9UMX1	ITCH	SUFU	MEDLINE	29515120	<span class="match term0">Itch</span>/beta-arrestin2-dependent non-proteolytic ubiquitylation of <span class="match term1">SuFu</span> controls Hedgehog signalling and medulloblastoma tumorigenesis.	HECT	1	Other	H.sapiens
1139	ITCH_HUMAN	ITCH_HUMAN	Q96J02	Q96J02	ITCH	ITCH	MEDLINE	17592138	By competing with p73 alpha for binding to the WW2 domain, N4BP1 reduces the ability of <span class="match term0">Itch</span> to recruit and ubiquitylate p73 alpha and inhibits <span class="match term0">Itch</span> autoubiquitylation activity both in in vitro and in vivo ubiquitylation assays	HECT	1	Training data	H.sapiens
1140	ITCH_HUMAN	CBL_HUMAN	Q96J02	P22681	ITCH	CBL	MEDLINE	19341794	These effects combine to cause increased ubiquitylation of <span class="match term0">Itch</span> substrates including Endophilin and <span class="match term1">Cbl</span>, resulting in the proteasome-dependent down regulation of these key trafficking proteins	HECT	1	Training data	H.sapiens
1141	ITCH_HUMAN	CASL_HUMAN	Q96J02	Q14511	ITCH	NEDD9	MEDLINE	15051726	<span class="match term0">AIP4</span> forms a complex with both Smad3 and <span class="match term1">HEF1</span> through its WW domains in a TGF-beta-independent manner and regulates <span class="match term1">HEF1</span> ubiquitination and degradation, which can be enhanced by TGF-beta stimulation	HECT	1	Training data	H.sapiens
1142	ITCH_HUMAN	PLCG1_HUMAN	Q96J02	P19174	ITCH	PLCG1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1143	ITCH_HUMAN	PTC1_HUMAN	Q96J02	Q13635	ITCH	PTCH1	MEDLINE	25092867	Here, we report that the C-terminal domain (CTD) of <span class="match term1">PTCH1</span> interacts with and is ubiquitylated on K1413 by the E3 ubiquitin-protein ligase Itchy homolog (<span class="match term0">Itch</span>), a Nedd4 family member	HECT	1	Other	H.sapiens
1144	ITCH_HUMAN	GLI1_HUMAN	Q96J02	P08151	ITCH	GLI1	MEDLINE	20818436	Numb activates the E3 ligase <span class="match term0">Itch</span> to control <span class="match term1">Gli1</span> function through a novel degradation signal.	HECT	1	Other	H.sapiens
1145	ITCH_HUMAN	BRAT1_HUMAN	Q96J02	Q6PJG6	ITCH	BRAT1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1146	ITCH_HUMAN	NOTC1_HUMAN	Q96J02	P46531	ITCH	NOTCH1	MEDLINE	19567869	Numb mutants that do not interact with the ubiquitin-protein isopeptide ligase, <span class="match term0">Itch</span>, or that lack motifs important for interaction with endocytic proteins fail to promote <span class="match term1">Notch1</span> degradation	HECT	1	Training data	H.sapiens
1147	ITCH_HUMAN	ERBB3_HUMAN	Q96J02	P21860	ITCH	ERBB3	MEDLINE	27203743	The anti-HER3 (<span class="match term1">ErbB3</span>) therapeutic antibody 9F7-F11 induces HER3 ubiquitination and degradation in tumors through JNK1/2- dependent <span class="match term0">ITCH</span>/AIP4 activation.	HECT	1	Other	H.sapiens
1148	ITCH_HUMAN	PLIN1_HUMAN	Q96J02	O60240	ITCH	PLIN1	MEDLINE	20504295	UbiNet 2.0	HECT	1	Training data	H.sapiens
1149	ITCH_HUMAN	PO5F1_HUMAN	Q96J02	Q01860	ITCH	POU5F1	MEDLINE	23255053	UbiNet 2.0	HECT	1	Training data	H.sapiens
1150	ITCH_HUMAN	TGFI1_HUMAN	Q96J02	O43294	ITCH	TGFB1I1	MEDLINE	28612841	Mechanistically, we demonstrate that <span class="match term0">Itch</span> directly binds to <span class="match term1">HIC-5</span> and targets it for K63-linked ubiquitination to inhibit IL-17-driven intestinal fibrosis	HECT	1	Other	H.sapiens
1151	ITCH_HUMAN	BRAF_HUMAN	Q96J02	P15056	ITCH	BRAF	MEDLINE	31015455	K27-linked ubiquitination of <span class="match term1">BRAF</span> by <span class="match term0">ITCH</span> engages cytokine response to maintain MEK-ERK signaling	HECT	1	Other	H.sapiens
1152	ITCH_HUMAN	DDX5_HUMAN	Q96J02	P17844	ITCH	DDX5	MEDLINE	16055720	UbiNet 2.0	HECT	1	Training data	H.sapiens
1153	ITCH_HUMAN	GLIS3_HUMAN	Q96J02	Q8NEA6	ITCH	GLIS3	MEDLINE	26147758	HECT E3 Ubiquitin Ligase <span class="match term0">Itch</span> Functions as a Novel Negative Regulator of Gli-Similar 3 (<span class="match term1">Glis3</span>) Transcriptional Activity.	HECT	1	Other	H.sapiens
1154	ITCH_HUMAN	TRPV4_HUMAN	Q96J02	Q9HBA0	ITCH	TRPV4	MEDLINE	20650893	Surprisingly, angiotensin stimulation results in ubiquitination of <span class="match term1">TRPV4</span>, a process that requires beta-arrestin 1, and subsequently to internalization and functional down-regulation of <span class="match term1">TRPV4</span>. beta-Arrestin 1 interacts with, and acts as an adaptor for <span class="match term0">AIP4</span>, an E3 ubiquitin ligase responsible for <span class="match term1">TRPV4</span> ubiquitination.	HECT	1	Training data	H.sapiens
1155	ITCH_HUMAN	TAB1_HUMAN	Q96J02	Q15750	ITCH	TAB1	MEDLINE	25714464	The E3 ubiquitin ligase <span class="match term0">Itch</span> inhibits p38alpha signaling and skin inflammation through the ubiquitylation of <span class="match term1">Tab1</span>.	HECT	1	Other	H.sapiens
1156	ITCH_HUMAN	BIRC2_HUMAN	Q96J02	Q13490	ITCH	BIRC2	MEDLINE	23109427	UbiNet 2.0	HECT	1	Training data	H.sapiens
1157	ITCH_HUMAN	BCL10_HUMAN	Q96J02	O95999	ITCH	BCL10	MEDLINE	15082780	The HECT domain ubiquitin ligases NEDD4 and <span class="match term0">Itch</span> promote ubiquitination and degradation of <span class="match term1">Bcl10</span>, thus downmodulating NF-kappa B activation	HECT	1	Training data	H.sapiens
1158	ITCH_HUMAN	LAPM5_HUMAN	Q96J02	Q13571	ITCH	LAPTM5	MEDLINE	22009753	UbiNet 2.0	HECT	1	Training data	H.sapiens
1159	ITCH_HUMAN	SHLB1_HUMAN	Q96J02	Q9Y371	ITCH	SH3GLB1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1160	ITCH_HUMAN	SH3G2_HUMAN	Q96J02	Q99962	ITCH	SH3GL2	MEDLINE	14684745	UbiNet 2.0	HECT	1	Training data	H.sapiens
1161	ITCH_HUMAN	CD3Z_HUMAN	Q96J02	P20963	ITCH	CD247	MEDLINE	20637659	UbiNet 2.0	HECT	1	Other	H.sapiens
1162	ITCH_HUMAN	DVL2_HUMAN	Q96J02	O14641	ITCH	DVL2	MEDLINE	22826439	UbiNet 2.0	HECT	1	Other	H.sapiens
1163	ITCH_HUMAN	MAVS_HUMAN	Q96J02	Q7Z434	ITCH	MAVS	MEDLINE	19881509	UbiNet 2.0	HECT	1	Training data	H.sapiens
1164	ITCH_HUMAN	VFLIP_HHV8P	Q96J02	F5HEZ4	ITCH	ORF71	MEDLINE	27912080	UbiNet 2.0	HECT	1	Other	H.sapiens
1165	ITCH_HUMAN	CFLAR_HUMAN	Q96J02	O15519	ITCH	CFLAR	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1166	ITCH_HUMAN	ERBB4_HUMAN	Q96J02	Q15303	ITCH	ERBB4	MEDLINE	18334649	<span class="match term0">Itch</span> catalyzed ubiquitination of <span class="match term1">ErbB4</span> CYT-1, promoted its localization into intracellular vesicles, and stimulated degradation of <span class="match term1">ErbB4</span> CYT-1	HECT	1	Training data	H.sapiens
1167	ITCH_HUMAN	TXNIP_HUMAN	Q96J02	Q9H3M7	ITCH	TXNIP	MEDLINE	20068034	UbiNet 2.0	HECT	1	Training data	H.sapiens
1168	ITCH_HUMAN	SHIP2_HUMAN	Q96J02	O15357	ITCH	INPPL1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1169	ITCH_HUMAN	H12_HUMAN	Q96J02	P16403	ITCH	H1-2	MEDLINE	30517763	Phosphorylation of <span class="match term0">ITCH</span> at Ser257 by AKT led to the nuclear localization of <span class="match term0">ITCH</span> and ubiquitination of <span class="match term1">H1.2</span>	HECT	1	Other	H.sapiens
1170	ITCH_HUMAN	PLIN2_HUMAN	Q96J02	Q99541	ITCH	PLIN2	MEDLINE	20504295	UbiNet 2.0	HECT	1	Training data	H.sapiens
1171	ITCH_HUMAN	TGIF1_HUMAN	Q96J02	Q15583	ITCH	TGIF1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1172	ITCH_HUMAN	RIPK2_HUMAN	Q96J02	O43353	ITCH	RIPK2	MEDLINE	19592251	UbiNet 2.0	HECT	1	Training data	H.sapiens
1173	ITCH_HUMAN	TRPC4_HUMAN	Q96J02	Q9UBN4	ITCH	TRPC4	MEDLINE	17110928	UbiNet 2.0	HECT	1	Training data	H.sapiens
1174	ITCH_HUMAN	YAP1_HUMAN	Q96J02	P46937	ITCH	YAP1	MEDLINE	23564455	Consequently, Amot130 promotes the ubiquitination of <span class="match term1">YAP</span> by <span class="match term0">AIP4</span> and prevents <span class="match term0">AIP4</span> from binding to large tumor suppressor 1	HECT	1	Other	H.sapiens
1175	ITCH_HUMAN	MAR1_HUMAN	Q96J02	Q16655	ITCH	MLANA	MEDLINE	15703212	Both NEDD4 and <span class="match term0">Itch</span> participate in the degradation of Melan-A	HECT	1	Training data	H.sapiens
1176	ITCH_HUMAN	RIPK1_HUMAN	Q96J02	Q13546	ITCH	RIPK1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1177	ITCH_HUMAN	M3K7_HUMAN	Q96J02	O43318	ITCH	MAP3K7	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1178	ITCH_HUMAN	GNPTA_HUMAN	Q96J02	Q3T906	ITCH	GNPTAB	MEDLINE	33789105	Decreased O-GlcNAc modification of <span class="match term1">TM/ICD</span> increases the binding of E3 ubiquitin ligase <span class="match term0">Itch</span> to <span class="match term1">TM/ICD</span> and promotes its degradation	HECT	1	Other	H.sapiens
1179	ITCH_HUMAN	NFE2_HUMAN	Q96J02	Q16621	ITCH	NFE2	MEDLINE	18718448	Confocal microscopy revealed that ubiquitinated <span class="match term1">p45</span>/NF-E2 became localized in the cytoplasm when <span class="match term0">Itch</span> was over-expressed	HECT	1	Training data	H.sapiens
1180	ITCH_HUMAN	HGS_HUMAN	Q96J02	O14964	ITCH	HGS	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1181	ITCH_HUMAN	AMOT_HUMAN	Q96J02	Q4VCS5	ITCH	AMOT	MEDLINE	23564455	UbiNet 2.0	HECT	1	Other	H.sapiens
1182	ITCH_HUMAN	MP2K4_HUMAN	Q96J02	P45985	ITCH	MAP2K4	MEDLINE	19737936	The JNK substrate <span class="match term0">Itch</span> (a HECT domain-containing Nedd4-like ubiquitin protein ligase) bound to <span class="match term1">MKK4</span>, ubiquitinated lysines 140 and 143, and promoted <span class="match term1">MKK4</span> degradation	HECT	1	Training data	H.sapiens
1183	ITCH_HUMAN	P4K2A_HUMAN	Q96J02	Q9BTU6	ITCH	PI4K2A	MEDLINE	23146885	Phosphatidylinositol 4-kinase IIalpha function at endosomes is regulated by the ubiquitin ligase <span class="match term0">Itch</span>.	HECT	1	Other	H.sapiens
1184	ITCH_HUMAN	DTX1_HUMAN	Q96J02	Q86Y01	ITCH	DTX1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1185	ITCH_HUMAN	SMAD2_HUMAN	Q96J02	Q15796	ITCH	SMAD2	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1186	BACD3_HUMAN	CEP97_HUMAN	Q9H3F6	Q8IW35	KCTD10	CEP97	MEDLINE	30404837	Cullin-3-<span class="match term0">KCTD10</span>-mediated <span class="match term1">CEP97</span> degradation promotes primary cilium formation.	SINGLE_OTHER	1	Other	H.sapiens
1187	BACD3_HUMAN	RHOB_HUMAN	Q9H3F6	P62745	KCTD10	RHOB	MEDLINE	29358211	The Cullin-3-Rbx1-<span class="match term0">KCTD10</span> complex controls endothelial barrier function via K63 ubiquitination of <span class="match term1">RhoB</span>	SINGLE_OTHER	1	Other	H.sapiens
1188	BACD3_HUMAN	TCAM1_HUMAN	Q9H3F6	Q8IUC6	KCTD10	TICAM1	MEDLINE	32484264	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
1189	KCD11_HUMAN	HDAC1_HUMAN	Q693B1	Q13547	KCTD11	HDAC1	MEDLINE	20081843	Histone deacetylase and Cullin3-REN(<span class="match term0">KCTD11</span>) ubiquitin ligase interplay regulates Hedgehog signalling through Gli acetylation.	BTB_OTHER	1	Other	H.sapiens
1190	BACD1_HUMAN	RHOA_HUMAN	Q8WZ19	P61586	KCTD13	RHOA	UniProt	BACD1_HUMAN	The BCR(<span class="match term0">BACURD1</span>) E3 ubiquitin ligase complex mediates the ubiquitination of <span class="match term1">RHOA</span>, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration	BTB_OTHER	1	Training data	H.sapiens
1191	KCD17_HUMAN	TCHP_HUMAN	Q8N5Z5	Q9BT92	KCTD17	TCHP	MEDLINE	25270598	UbiNet 2.0	Other	1	Other	H.sapiens
1192	KDM2A_HUMAN	F263_HUMAN	Q9Y2K7	Q16875	KDM2A	PFKFB3	MEDLINE	34079757	Specifically, we defined that one of the key enzymes of glycolysis <span class="match term1">PFKFB3</span> (6-phosphofructo-2-kinase) is ubiquitylated by <span class="match term0">KDM2A</span> which suppresses MM cell proliferation.	F-box	1	Other	H.sapiens
1193	KDM2B_HUMAN	H2A2C_HUMAN	Q8NHM5	Q16777	KDM2B	H2AC20	MEDLINE	24658274	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
1194	KDM2B_HUMAN	FOS_HUMAN	Q8NHM5	P01100	KDM2B	FOS	MEDLINE	26725323	<span class="match term0">KDM2B</span>/FBXL10 targets c-<span class="match term1">Fos</span> for ubiquitylation and degradation in response to mitogenic stimulation.	SINGLE_OTHER	1	Other	H.sapiens
1195	KEAP1_HUMAN	NF2L2_HUMAN	Q14145	Q16236	KEAP1	NFE2L2	MEDLINE	15985429	<span class="match term0">Keap1</span> polyubiquitination coincided with <span class="match term1">Nrf2</span> stabilization and nuclear accumulation	BTB_3	1	Training data	H.sapiens
1196	KEAP1_HUMAN	MCM3_HUMAN	Q14145	P25205	KEAP1	MCM3	MEDLINE	22199232	E3Net	BTB_3	1	Other	H.sapiens
1197	KEAP1_HUMAN	PGAM5_HUMAN	Q14145	Q96HS1	KEAP1	PGAM5	MEDLINE	17046835	<span class="match term0">Keap1</span>-dependent ubiquitination of <span class="match term1">PGAM5</span> results in proteasome-dependent degradation of <span class="match term1">PGAM5</span>	BTB_3	1	Training data	H.sapiens
1198	KEAP1_HUMAN	SOX9_HUMAN	Q14145	P48436	KEAP1	SOX9	MEDLINE	33173725	This work reports that <span class="match term1">SOX9</span> protein abundance is regulated by the Cullin 3-based ubiquitin ligase <span class="match term0">KEAP1</span> via proteasome-mediated degradation	BTB_3	1	Other	H.sapiens
1199	KEAP1_HUMAN	PALB2_HUMAN	Q14145	Q86YC2	KEAP1	PALB2	MEDLINE	26649820	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1200	KEAP1_HUMAN	IKKB_HUMAN	Q14145	O14920	KEAP1	IKBKB	MEDLINE	19818716	<span class="match term0">KEAP1</span> E3 ligase-mediated downregulation of NF-kappaB signaling by targeting <span class="match term1">IKKbeta</span>.	BTB_3	1	Other	H.sapiens
1201	KEAP1_HUMAN	EGLN1_HUMAN	Q14145	Q9GZT9	KEAP1	EGLN1	MEDLINE	31763849	Overexpression of either CUL3, <span class="match term0">KEAP1</span> or both significantly increases <span class="match term1">PHD2</span> ubiquitination and reduces <span class="match term1">PHD2</span> protein abundance	BTB_3	1	Other	H.sapiens
1202	KEAP1_HUMAN	SQSTM_HUMAN	Q14145	Q13501	KEAP1	SQSTM1	MEDLINE	28380357	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1203	SCF_HUMAN	FBX28_HUMAN	P21583	Q9NVF7	KITLG	FBXO28	MEDLINE	31678254	Here we report that <span class="match term1">FBXO28</span>, a poorly characterized F-box protein, is a novel substrate of <span class="match term0">SCF</span> E3 ligase.	Other	1	Other	H.sapiens
1204	KLH10_HUMAN	CCNB1_HUMAN	Q6JEL2	P14635	KLHL10	CCNB1	MEDLINE	22199232	E3Net	BTB_3	1	Other	H.sapiens
1205	KLH11_HUMAN	CCNB1_HUMAN	Q9NVR0	P14635	KLHL11	CCNB1	MEDLINE	22199232	E3Net	BTB_3	1	Other	H.sapiens
1206	KLH12_HUMAN	-	Q53G59	-	KLHL12	DSH	MEDLINE	16547521	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1207	KLH12_HUMAN	DVL3_HUMAN	Q53G59	Q92997	KLHL12	DVL3	MEDLINE	22199232	E3Net	BTB_3	1	Other	H.sapiens
1208	KLH12_HUMAN	SC31B_HUMAN	Q53G59	Q9NQW1	KLHL12	SEC31B	MEDLINE	22358839	UbiNet 2.0	BTB_3	1	Training data	H.sapiens
1209	KLH12_HUMAN	LNP_HUMAN	Q53G59	Q9C0E8	KLHL12	LNPK	MEDLINE	32433973	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1210	KLH12_HUMAN	FUBP2_HUMAN	Q53G59	Q92945	KLHL12	KHSRP	MEDLINE	27899653;32032490	27899653;32032490	BTB_3	1	Other	H.sapiens
1211	KLH12_HUMAN	CCNB1_HUMAN	Q53G59	P14635	KLHL12	CCNB1	MEDLINE	22199232	E3Net	BTB_3	1	Other	H.sapiens
1212	KLH12_HUMAN	PEF1_HUMAN	Q53G59	Q9UBV8	KLHL12	PEF1	MEDLINE	22199232	E3Net	BTB_3	1	Other	H.sapiens
1213	KLH12_HUMAN	SC31A_HUMAN	Q53G59	O94979	KLHL12	SEC31A	MEDLINE	22358839	UbiNet 2.0	BTB_3	1	Training data	H.sapiens
1214	KLH12_HUMAN	DRD4_HUMAN	Q53G59	P21917	KLHL12	DRD4	MEDLINE	20100572	In previous studies, we identified <span class="match term0">KLHL12</span> as a novel interaction partner of the dopamine D4 receptor that functions as an adaptor in a Cullin3-based E3 ubiquitin ligase complex to target the receptor for ubiquitination	BTB_3	1	Other	H.sapiens
1215	KLH13_HUMAN	CCNB1_HUMAN	Q9P2N7	P14635	KLHL13	CCNB1	MEDLINE	18075312	Inactivation of the Cul3/KLHL9/<span class="match term0">KLHL13</span> ligase leads to premature degradation of Cyclin B and exit from the mitotic state in the presence of microtubule poisons	BTB_3	1	Training data	H.sapiens
1216	KLH13_HUMAN	BORA_HUMAN	Q9P2N7	Q6PGQ7	KLHL13	BORA	MEDLINE	17543862	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1217	KLH13_HUMAN	AURKB_HUMAN	Q9P2N7	Q96GD4	KLHL13	AURKB	MEDLINE	19995937	The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis.	BTB_3	1	Other	H.sapiens
1218	KLH15_HUMAN	2A5B_HUMAN	Q96M94	Q15173	KLHL15	PPP2R5B	MEDLINE	23135275	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
1219	KLH15_HUMAN	CTIP_HUMAN	Q96M94	Q99708	KLHL15	RBBP8	MEDLINE	27561354	Here, we identify the Cullin3 E3 ligase substrate adaptor Kelch-like protein 15 (<span class="match term0">KLHL15</span>) as a new interaction partner of <span class="match term1">CtIP</span> and show that <span class="match term0">KLHL15</span> promotes <span class="match term1">CtIP</span> protein turnover via the ubiquitin-proteasome pathway	SINGLE_OTHER	1	Other	H.sapiens
1220	KLH17_HUMAN	GRIK2_HUMAN	Q6TDP4	Q13002	KLHL17	GRIK2	UniProt	KLH17_HUMAN	The BCR(<span class="match term0">KLHL17</span>) mediates the ubiquitination and subsequenct degradation of <span class="match term1">GLUR6</span>	BTB_3	1	Training data	H.sapiens
1221	KLH18_HUMAN	AURKA_HUMAN	O94889	O14965	KLHL18	AURKA	MEDLINE	23213400	The CUL3-<span class="match term0">KLHL18</span> ligase regulates mitotic entry and ubiquitylates <span class="match term1">Aurora-A</span>.	BTB_3	1	Other	H.sapiens
1222	KLHL2_HUMAN	NPTXR_HUMAN	O95198	O95502	KLHL2	NPTXR	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
1223	KLHL2_HUMAN	WNK4_HUMAN	O95198	Q96J92	KLHL2	WNK4	MEDLINE	23838290	<span class="match term0">KLHL2</span> interacts with and ubiquitinates WNK kinases.	Other	1	Other	H.sapiens
1224	KLHL2_HUMAN	WNK1_HUMAN	O95198	Q9H4A3	KLHL2	WNK1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
1225	KLHL2_HUMAN	ARHG7_HUMAN	O95198	Q14155	KLHL2	ARHGEF7	MEDLINE	33163274	<span class="match term0">KLHL2</span> is capable of promoting <span class="match term1">ARHGEF7</span> degradation via the ubiquitin-proteasome pathway	Other	1	Other	H.sapiens
1226	KLHL2_HUMAN	WNK3_HUMAN	O95198	Q9BYP7	KLHL2	WNK3	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
1227	KLH20_HUMAN	ARHGB_HUMAN	Q9Y2M5	O15085	KLHL20	ARHGEF11	MEDLINE	22199232	E3Net	BTB_3	1	Other	H.sapiens
1228	KLH20_HUMAN	DAPK1_HUMAN	Q9Y2M5	P53355	KLHL20	DAPK1	MEDLINE	20389280	UbiNet 2.0	BTB_3	1	Training data	H.sapiens
1229	KLH20_HUMAN	PK3C3_HUMAN	Q9Y2M5	Q8NEB9	KLHL20	PIK3C3	MEDLINE	26687681	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1230	KLH20_HUMAN	BECN1_HUMAN	Q9Y2M5	Q14457	KLHL20	BECN1	MEDLINE	26687681	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1231	KLH20_HUMAN	PML_HUMAN	Q9Y2M5	P29590	KLHL20	PML	MEDLINE	31279627:21840486	31279627:21840486	BTB_3	1	Other	H.sapiens
1232	KLH20_HUMAN	ULK1_HUMAN	Q9Y2M5	O75385	KLHL20	ULK1	MEDLINE	26687681	Here, we show that <span class="match term1">ULK1</span>, a serine/threonine kinase critical for autophagy initiation, is a substrate of the Cul3-<span class="match term0">KLHL20</span> ubiquitin ligase	BTB_3	1	Other	H.sapiens
1233	KLH20_HUMAN	CORO7_HUMAN	Q9Y2M5	P57737	KLHL20	CORO7	MEDLINE	22199232	E3Net	BTB_3	1	Other	H.sapiens
1234	KLH21_HUMAN	AURKB_HUMAN	Q9UJP4	Q96GD4	KLHL21	AURKB	UniProt	KLH21_HUMAN	The BCR(<span class="match term0">KLHL21</span>) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of <span class="match term1">AURKB</span> (By similarity)	BTB_3	1	Training data	H.sapiens
1235	KLH21_HUMAN	Q5UEC6_HUMAN	Q9UJP4	Q5UEC6	KLHL21	EB1	MEDLINE	27641145	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1236	KLH22_HUMAN	DEPD5_HUMAN	Q53GT1	O75140	KLHL22	DEPDC5	MEDLINE	29769719;32296023	29769719;32296023	BTB_3	1	Other	H.sapiens
1237	KLH22_HUMAN	PLK1_HUMAN	Q53GT1	P53350	KLHL22	PLK1	MEDLINE	23455478	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1238	KLH25_HUMAN	4EBP1_HUMAN	Q9H0H3	Q13541	KLHL25	EIF4EBP1	MEDLINE	22578813	We identified the <span class="match term0">KLHL25</span>-CUL3 complex as the E3 ubiquitin ligase, which targets hypophosphorylated <span class="match term1">4E-BP1</span>	BTB_3	1	Other	H.sapiens
1239	KLHL3_HUMAN	WNK4_HUMAN	Q9UH77	Q96J92	KLHL3	WNK4	MEDLINE	23453970	UbiNet 2.0	BTB_3	1	Training data	H.sapiens
1240	KLHL3_HUMAN	WNK1_HUMAN	Q9UH77	Q9H4A3	KLHL3	WNK1	MEDLINE	23387299	The CUL3-<span class="match term0">KLHL3</span> E3 ligase complex mutated in Gordon's hypertension syndrome interacts with and ubiquitylates WNK isoforms: disease-causing mutations in <span class="match term0">KLHL3</span> and WNK4 disrupt interaction.	BTB_3	1	Other	H.sapiens
1241	KLH42_HUMAN	2A5E_HUMAN	Q9P2K6	Q16537	KLHL42	PPP2R5E	MEDLINE	32071084	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1242	KLHL6_HUMAN	RC3H2_HUMAN	Q8WZ60	Q9HBD1	KLHL6	RC3H2	MEDLINE	29695787	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1243	KLHL6_HUMAN	CDK2_HUMAN	Q8WZ60	P24941	KLHL6	CDK2	MEDLINE	29720484	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1244	KLHL7_HUMAN	STPAP_HUMAN	Q8IXQ5	Q9H6E5	KLHL7	TUT1	MEDLINE	29032201	In this study, we report that <span class="match term0">KLHL7</span> increases terminal uridylyl transferase 1 (<span class="match term1">TUT1</span>) ubiquitination involved in nucleolar integrity	BTB_3	1	Other	H.sapiens
1245	KLHL8_HUMAN	RAPSN_HUMAN	Q9P2G9	Q13702	KLHL8	RAPSN	MEDLINE	19158078	Mammalian <span class="match term1">rapsyn</span> was ubiquitinated by the CUL3/<span class="match term0">KLHL8</span>-containing E3 ligase in vitro, and the knockdown of KLHL-8, a mammalian KEL-8 homolog, inhibited <span class="match term1">rapsyn</span> ubiquitination in vivo, implying evolutionary conservation of the <span class="match term1">rapsyn</span> stability control machinery	BTB_3	1	Training data	H.sapiens
1246	KLHL9_HUMAN	BORA_HUMAN	Q9P2J3	Q6PGQ7	KLHL9	BORA	MEDLINE	17543862	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1247	KLHL9_HUMAN	CCNB1_HUMAN	Q9P2J3	P14635	KLHL9	CCNB1	MEDLINE	18075312	UbiNet 2.0	BTB_3	1	Training data	H.sapiens
1248	KLHL9_HUMAN	AURKB_HUMAN	Q9P2J3	Q96GD4	KLHL9	AURKB	MEDLINE	19995937	UbiNet 2.0	BTB_3	1	Training data	H.sapiens
1249	KLHL9_HUMAN	CEBPB_HUMAN	Q9P2J3	P17676	KLHL9	CEBPB	MEDLINE	25303533	UbiNet 2.0	BTB_3	1	Other	H.sapiens
1250	KLHL9_HUMAN#KLH13_HUMAN	CCNB1_HUMAN	Q9P2J3#Q9P2N7	P14635	KLHL9#KLHL13	CCNB1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
1251	LATS1_HUMAN	BECN1_HUMAN	O95835	Q14457	LATS1	BECN1	MEDLINE	31848340	Instead, <span class="match term0">LATS1</span> stabilizes the autophagy core-machinery component <span class="match term1">Beclin-1</span> by promoting K27-linked ubiquitination at lysine residues K32 and K263 on <span class="match term1">Beclin-1</span>	Other	1	Other	H.sapiens
1252	LHX1_HUMAN	LIMK1_HUMAN	P48742	P53667	LHX1	LIMK1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
1253	LNX1_HUMAN	TOPK_HUMAN	Q8TBB1	Q96KB5	LNX1	PBK	MEDLINE	22889411	We further revealed that the <span class="match term0">LNX1</span>-mediated ubiquitination and degradation of <span class="match term1">PBK</span> inhibited cell proliferation and enhanced sensitivity to doxorubicin-induced apoptosis	RING	1	Other	H.sapiens
1254	LNX1_HUMAN	RL1D1_HUMAN	Q8TBB1	O76021	LNX1	RSL1D1	MEDLINE	22889411	UbiNet 2.0	RING	1	Training data	H.sapiens
1255	LNX1_HUMAN	GIPR_HUMAN	Q8TBB1	P48546	LNX1	GIPR	MEDLINE	22889411	UbiNet 2.0	RING	1	Other	H.sapiens
1256	LNX1_HUMAN	NUMB_HUMAN	Q8TBB1	P49757	LNX1	NUMB	MEDLINE	14990566	Deletion of <span class="match term0">LNX</span> PDZ1 domain resulted in loss of ubiquitylation and subsequent degradation of the PTBi form of <span class="match term1">Numb</span>	RING	1	Training data	H.sapiens
1257	LNX1_HUMAN	CXD2_HUMAN	Q8TBB1	Q9UKL4	LNX1	GJD2	MEDLINE	30295974	Furthermore, cotransfection of cultured cells with <span class="match term1">Cx36</span> and E3 ubiquitin ligase-competent <span class="match term0">LNX1</span> and LNX2 isoforms led to loss of <span class="match term1">Cx36</span>-containing gap junctions between cells, whereas these junctions persisted following transfection with isoforms of these proteins that lack ligase activity.	RING	1	Other	H.sapiens
1258	LNX1_HUMAN	KCNA4_HUMAN	Q8TBB1	P22459	LNX1	KCNA4	MEDLINE	22889411	UbiNet 2.0	RING	1	Other	H.sapiens
1259	LNX1_HUMAN	SUFU_HUMAN	Q8TBB1	Q9UMX1	LNX1	SUFU	MEDLINE	33608498	We further show that the E3 ubiquitin ligase <span class="match term0">LNX1</span> plays a critical role in the SNEP1-mediated degradation of <span class="match term1">SuFu</span>	RING	1	Other	H.sapiens
1260	LNX1_HUMAN	NMDZ1_HUMAN	Q8TBB1	Q05586	LNX1	GRIN1	MEDLINE	22889411	UbiNet 2.0	RING	1	Other	H.sapiens
1261	LNX1_HUMAN	PQBP1_HUMAN	Q8TBB1	O60828	LNX1	PQBP1	MEDLINE	22889411	UbiNet 2.0	RING	1	Other	H.sapiens
1262	LNX1_HUMAN	CLD17_HUMAN	Q8TBB1	P56750	LNX1	CLDN17	MEDLINE	22889411	UbiNet 2.0	RING	1	Other	H.sapiens
1263	LNX1_HUMAN	5HT2B_HUMAN	Q8TBB1	P41595	LNX1	HTR2B	MEDLINE	22889411	UbiNet 2.0	RING	1	Other	H.sapiens
1264	LNX1_HUMAN	SRC_HUMAN	Q8TBB1	P12931	LNX1	SRC	MEDLINE	17936276	Moreover, c-<span class="match term1">Src</span> itself is ubiquitinated by <span class="match term0">LNX1</span>, suggesting an interdependent regulation of c-<span class="match term1">Src</span> and <span class="match term0">LNX1</span>	RING	1	Training data	H.sapiens
1265	LNX1_HUMAN	CD8A_HUMAN	Q8TBB1	P01732	LNX1	CD8A	MEDLINE	22045731	UbiNet 2.0	RING	1	Training data	H.sapiens
1266	LNX1_HUMAN	ZBT8A_HUMAN	Q8TBB1	Q96BR9	LNX1	ZBTB8A	MEDLINE	19668196	UbiNet 2.0	RING	1	Training data	H.sapiens
1267	LNX2_HUMAN	CXD2_HUMAN	Q8N448	Q9UKL4	LNX2	GJD2	MEDLINE	30295974	E3 ubiquitin ligases LNX1 and <span class="match term0">LNX2</span> localize at neuronal gap junctions formed by <span class="match term1">connexin36</span> in rodent brain and molecularly interact with <span class="match term1">connexin36</span>	RING	1	Other	H.sapiens
1268	LNX2_HUMAN	NUMB_HUMAN	Q8N448	P49757	LNX2	NUMB	MEDLINE	26451611	Moreover we have demonstrated the ubiquitination of cell fate determinant protein, <span class="match term1">Numb</span> by <span class="match term0">LNX2</span>	RING	1	Other	H.sapiens
1269	LRSM1_HUMAN	ABL1_HUMAN	Q6UWE0	P00519	LRSAM1	ABL1	MEDLINE	32098768	BBR inhibited the activity of <span class="match term1">BCR-ABL</span> and <span class="match term1">BCR-ABL</span> with the T315I mutation, and it also degraded these proteins via the autophagic lysosome pathway by recruiting E3 ubiquitin-protein ligase <span class="match term0">LRSAM1</span>	RING	1	Other	H.sapiens
1270	LRSM1_HUMAN	TS101_HUMAN	Q6UWE0	Q99816	LRSAM1	TSG101	MEDLINE	15256501	Bivalent binding of <span class="match term1">Tsg101</span> to a tandem tetrapeptide motif (PTAP) and to a central region of <span class="match term0">Tal</span> is essential for <span class="match term0">Tal</span>-mediated ubiquitylation of <span class="match term1">Tsg101</span>	RING	1	Training data	H.sapiens
1271	LRSM1_HUMAN	UBE3A_HUMAN	Q6UWE0	Q05086	LRSAM1	UBE3A	MEDLINE	33207262	<span class="match term0">LRSAM1</span> E3 ubiquitin ligase promotes proteasomal clearance of <span class="match term1">E6-AP</span> protein	RING	1	Other	H.sapiens
1272	MALT1_HUMAN	NEMO_HUMAN	Q9UDY8	Q9Y6K9	MALT1	IKBKG	MEDLINE	15125833	The <span class="match term0">MALT1</span> oligomers bind to TRAF6, induce TRAF6 oligomerization, and activate the ligase activity of TRAF6 to polyubiquitinate <span class="match term1">NEMO</span>	HECT	1	Training data	H.sapiens
1273	M3K1_HUMAN	MK03_HUMAN	Q13233	P27361	MAP3K1	MAPK3	MEDLINE	12049732	The PHD domain of <span class="match term0">MEKK1</span> acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of <span class="match term1">ERK1</span>/2	RING	1	Training data	H.sapiens
1274	M3K1_HUMAN	JUN_HUMAN	Q13233	P05412	MAP3K1	JUN	MEDLINE	17101801	<span class="match term0">MEKK1</span> mediates the ubiquitination and degradation of c-<span class="match term1">Jun</span> in response to osmotic stress	RING	1	Training data	H.sapiens
1275	M3K1_HUMAN	MK01_HUMAN	Q13233	P28482	MAP3K1	MAPK1	MEDLINE	12049732	The PHD domain of <span class="match term0">MEKK1</span> acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2	RING	1	Training data	H.sapiens
1276	M3K1_HUMAN	FOSL2_HUMAN	Q13233	P15408	MAP3K1	FOSL2	MEDLINE	15558021	<span class="match term0">MEKK1</span> also regulates Fra-2 protein stability by inducing Fra-2 ubiquitination and degradation	RING	1	Training data	H.sapiens
1277	M3K1_HUMAN	DTX1_HUMAN	Q13233	Q86Y01	MAP3K1	DTX1	MEDLINE	15684388	Deltex1 interacted directly with <span class="match term0">MEKK1</span>(C) and stimulated the ubiquitination of <span class="match term0">MEKK1</span>(C) as shown by in vivo and in vitro ubiquitination analysis	RING	1	Training data	H.sapiens
1278	MARH1_HUMAN	2B1F_HUMAN	Q8TCQ1	P01911	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1279	MARH1_HUMAN	2B17_HUMAN	Q8TCQ1	P13761	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1280	MARH1_HUMAN	DRB3_HUMAN	Q8TCQ1	P79483	MARCHF1	HLA-DRB3	UniProt	MARH1_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1281	MARH1_HUMAN	C2TA_HUMAN	Q8TCQ1	P33076	MARCHF1	CIITA	MEDLINE	19880452	UbiNet 2.0	RING	1	Training data	H.sapiens
1282	MARH1_HUMAN	DRB4_HUMAN	Q8TCQ1	P13762	MARCHF1	HLA-DRB4	UniProt	MARH1_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II	RING	1	Training data	H.sapiens
1283	MARH1_HUMAN	2B18_HUMAN	Q8TCQ1	Q30134	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1284	MARH1_HUMAN	DRA_HUMAN	Q8TCQ1	P01903	MARCHF1	HLA-DRA	UniProt	MARH1_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> or MARCH8 at Lys-244 leading to down-regulation of MHC class II	RING	1	Training data	H.sapiens
1285	MARH1_HUMAN	2B1A_HUMAN	Q8TCQ1	Q30167	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1286	MARH1_HUMAN	2B13_HUMAN	Q8TCQ1	P01912	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1287	MARH1_HUMAN	2B1G_HUMAN	Q8TCQ1	Q29974	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1288	MARH1_HUMAN	2B19_HUMAN	Q8TCQ1	Q9TQE0	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1289	MARH1_HUMAN	DRB5_HUMAN	Q8TCQ1	Q30154	MARCHF1	HLA-DRB5	UniProt	MARH1_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1290	MARH1_HUMAN	FAS_HUMAN	Q8TCQ1	P49327	MARCHF1	FASN	UniProt	MARH1_HUMAN	E3 ubiquitin-protein ligase that may mediate ubiquitination of TFRC, CD86 and <span class="match term1">FAS</span>, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies	RING	1	Training data	H.sapiens
1291	MARH1_HUMAN	2B11_HUMAN	Q8TCQ1	P04229	MARCHF1	HLA-DRB1	UniProt	2B11_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1292	MARH1_HUMAN	2B1B_HUMAN	Q8TCQ1	P20039	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1293	MARH1_HUMAN	2B1C_HUMAN	Q8TCQ1	Q95IE3	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1294	MARH1_HUMAN	2B1E_HUMAN	Q8TCQ1	Q9GIY3	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1295	MARH1_HUMAN	2B14_HUMAN	Q8TCQ1	P13760	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1296	MARH1_HUMAN	TFR1_HUMAN	Q8TCQ1	P02786	MARCHF1	TFRC	UniProt	MARH1_HUMAN	E3 ubiquitin-protein ligase that may mediate ubiquitination of <span class="match term1">TFRC</span>, CD86 and FAS, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies	RING	1	Training data	H.sapiens
1297	MARH1_HUMAN	CD86_HUMAN	Q8TCQ1	P42081	MARCHF1	CD86	MEDLINE	21220452	The TM region of CD83 blocks interleukin 10-driven, <span class="match term0">MARCH1</span>-dependent ubiquitination and degradation of MHC class II and <span class="match term1">CD86</span> in DCs	RING	1	Training data	H.sapiens
1298	MARH1_HUMAN	CD4_HUMAN	Q8TCQ1	P01730	MARCHF1	CD4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1299	MARH1_HUMAN	2B1D_HUMAN	Q8TCQ1	Q5Y7A7	MARCHF1	HLA-DRB1	UniProt	MARH8_HUMAN	Ubiquitinated by <span class="match term0">MARCH1</span> and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1300	MARHB_HUMAN	CD4_HUMAN	A6NNE9	P01730	MARCHF11	CD4	MEDLINE	17604280	<span class="match term0">MARCH-XI</span> possesses an E3 ubiquitin ligase activity that targets <span class="match term1">CD4</span> for ubiquitination	RING	1	Training data	H.sapiens
1301	MARH2_HUMAN	ERGI3_HUMAN	Q9P0N8	Q9Y282	MARCHF2	ERGIC3	MEDLINE	31142615	Here, we report that <span class="match term0">MARCH2</span> directs ubiquitination and subsequent degradation of <span class="match term1">ERGIC3</span> and that <span class="match term0">MARCH2</span> depletion increases endogenous <span class="match term1">ERGIC3</span> levels	RING	1	Other	H.sapiens
1302	MARH2_HUMAN	CD86_HUMAN	Q9P0N8	P42081	MARCHF2	CD86	UniProt	MARH2_HUMAN	E3 ubiquitin-protein ligase that may mediate ubiquitination of TFRC and <span class="match term1">CD86</span>, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies	RING	1	Training data	H.sapiens
1303	MARH2_HUMAN	DLG1_HUMAN	Q9P0N8	Q12959	MARCHF2	DLG1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1304	MARH2_HUMAN	CFTR_HUMAN	Q9P0N8	P13569	MARCHF2	CFTR	MEDLINE	23818989	UbiNet 2.0	RING	1	Training data	H.sapiens
1305	MARH2_HUMAN	TFR1_HUMAN	Q9P0N8	P02786	MARCHF2	TFRC	UniProt	MARH2_HUMAN	E3 ubiquitin-protein ligase that may mediate ubiquitination of <span class="match term1">TFRC</span> and CD86, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies	RING	1	Training data	H.sapiens
1306	MARH4_HUMAN	CD4_HUMAN	Q9P2E8	P01730	MARCHF4	CD4	UniProt	MARH4_HUMAN	E3 ubiquitin-protein ligase that may mediate ubiquitination of MHC-I and <span class="match term1">CD4</span>, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies	RING	1	Training data	H.sapiens
1307	MARH4_HUMAN	DRB_HUMAN	Q9P2E8	P01911	MARCHF4	HLA-DRB1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1308	MARH4_HUMAN	2B1E_HUMAN	Q9P2E8	Q9GIY3	MARCHF4	HLA-DRB1	MEDLINE	14722266	14722266	RING	1	Other	H.sapiens
1309	MARH5_HUMAN	FIS1_HUMAN	Q9NX47	Q9Y3D6	MARCHF5	FIS1	UniProt	MARH5_HUMAN	Ubiquitinated by <span class="match term0">MARCH5</span>	RING	1	Training data	H.sapiens
1310	MARH5_HUMAN	UTRO_HUMAN	Q9NX47	P46939	MARCHF5	UTRN	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1311	MARH5_HUMAN	DNM1L_HUMAN	Q9NX47	O00429	MARCHF5	DNM1L	MEDLINE	16936636	We also show that <span class="match term0">MARCH-V</span> promotes ubiquitination of <span class="match term1">Drp1</span>	RING	1	Training data	H.sapiens
1312	MARH5_HUMAN	ATX3_HUMAN	Q9NX47	P54252	MARCHF5	ATXN3	MEDLINE	20851218	UbiNet 2.0	RING	1	Training data	H.sapiens
1313	MARH5_HUMAN	MFN1_HUMAN	Q9NX47	Q8IWA4	MARCHF5	MFN1	UniProt	MARH5_HUMAN	Ubiquitinated by <span class="match term0">MARCH5</span>	RING	1	Training data	H.sapiens
1314	MARH5_HUMAN	TANK_HUMAN	Q9NX47	Q92844	MARCHF5	TANK	MEDLINE	32296023	UbiNet 2.0	RING	1	Other	H.sapiens
1315	MARH5_HUMAN	MARH5_HUMAN	Q9NX47	Q9NX47	MARCHF5	MARCHF5	UniProt	MARH5_HUMAN	Ubiquitinated by <span class="match term0">MARCH5</span> (By similarity)	RING	1	Training data	H.sapiens
1316	MARH5_HUMAN	MAP1B_HUMAN	Q9NX47	P46821	MARCHF5	MAP1B	MEDLINE	22308378	Mitochondrial ubiquitin ligase <span class="match term0">MITOL</span> blocks S-nitrosylated <span class="match term1">MAP1B</span>-light chain 1-mediated mitochondrial dysfunction and neuronal cell death	RING	1	Other	H.sapiens
1317	MARH5_HUMAN	TR10A_HUMAN	Q9NX47	O00220	MARCHF5	TNFRSF10A	MEDLINE	23300075	UbiNet 2.0	RING	1	Training data	H.sapiens
1318	MARH5_HUMAN	MFN2_HUMAN	Q9NX47	O95140	MARCHF5	MFN2	MEDLINE	23727017	UbiNet 2.0	RING	1	Other	H.sapiens
1319	MARH5_HUMAN	MCL1_HUMAN	Q9NX47	Q07820	MARCHF5	MCL1	MEDLINE	32484436	We show here in prostate cancer cells that increased NOXA, mediated by kinase inhibitor activation of an integrated stress response, drives the degradation of <span class="match term1">MCL1</span>, and identify the mitochondria-associated ubiquitin ligase <span class="match term0">MARCH5</span> as the primary mediator of this NOXA-dependent <span class="match term1">MCL1</span> degradation	RING	1	Other	H.sapiens
1320	MARH5_HUMAN	C2TA_HUMAN	Q9NX47	P33076	MARCHF5	CIITA	MEDLINE	18389477	UbiNet 2.0	RING	1	Training data	H.sapiens
1321	MARH5_HUMAN	SODC_HUMAN	Q9NX47	P00441	MARCHF5	SOD1	MEDLINE	19741096	UbiNet 2.0	RING	1	Other	H.sapiens
1322	MARH5_HUMAN	MAVS_HUMAN	Q9NX47	Q7Z434	MARCHF5	MAVS	MEDLINE	31881323	Dual targeting of RIG-I and <span class="match term1">MAVS</span> by <span class="match term0">MARCH5</span> mitochondria ubiquitin ligase in innate immunity	RING	1	Other	H.sapiens
1323	MARH6_HUMAN	IOD2_HUMAN	O60337	Q92813	MARCHF6	DIO2	MEDLINE	19651899	A highly efficient <span class="match term0">TEB4</span> knockdown (&gt;90% reduction in mRNA and protein levels) decreased <span class="match term1">D2</span> ubiquitination and increased <span class="match term1">D2</span> activity and protein levels by about fourfold	RING	1	Training data	H.sapiens
1324	MARH6_HUMAN	ERG1_HUMAN	O60337	Q14534	MARCHF6	SQLE	MEDLINE	32170014	UbiNet 2.0	RING	1	Other	H.sapiens
1325	MARH6_HUMAN	MARH6_HUMAN	O60337	O60337	MARCHF6	MARCHF6	MEDLINE	15673284	hUbiquitome	RING	1	Other	H.sapiens
1326	MARH7_HUMAN	MDM2_HUMAN	Q9H992	Q00987	MARCHF7	MDM2	MEDLINE	29295817	<span class="match term0">MARCH7</span> catalyzes Lys63-linked polyubiquitination of <span class="match term1">Mdm2</span>, which impedes <span class="match term1">Mdm2</span> autoubiquitination and degradation, thereby leading to the stabilization of <span class="match term1">Mdm2</span>	RING	1	Other	H.sapiens
1327	MARH7_HUMAN	MARH7_HUMAN	Q9H992	Q9H992	MARCHF7	MARCHF7	MEDLINE	18410486	In this study, we show that <span class="match term0">MARCH7</span> readily undergoes autoubiquitylation and associates with two deubiquitylating enzymes - ubiquitin-specific protease (USP)9X in the cytosol and USP7 in the nucleus	RING	1	Training data	H.sapiens
1328	MARH7_HUMAN	TAU_HUMAN	Q9H992	P10636	MARCHF7	MAPT	MEDLINE	24905733	UbiNet 2.0	RING	1	Other	H.sapiens
1329	MARH8_HUMAN	2B1E_HUMAN	Q5T0T0	Q9GIY3	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1330	MARH8_HUMAN	-	Q5T0T0	-	MARCHF8	NS2	MEDLINE	30759391	UbiNet 2.0	RING	1	Other	H.sapiens
1331	MARH8_HUMAN	2B1F_HUMAN	Q5T0T0	P01911	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1332	MARH8_HUMAN	2B1D_HUMAN	Q5T0T0	Q5Y7A7	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1333	MARH8_HUMAN	DRA_HUMAN	Q5T0T0	P01903	MARCHF8	HLA-DRA	UniProt	MARH8_HUMAN	Ubiquitinated by MARCH1 or <span class="match term0">MARCH8</span> at Lys-244 leading to down-regulation of MHC class II	RING	1	Training data	H.sapiens
1334	MARH8_HUMAN	IL1AP_HUMAN	Q5T0T0	Q9NPH3	MARCHF8	IL1RAP	MEDLINE	22904187	The E3 ubiquitin ligase <span class="match term0">MARCH8</span> negatively regulates IL-1beta-induced NF-kappaB activation by targeting the <span class="match term1">IL1RAP</span> coreceptor for ubiquitination and degradation	RING	1	Other	H.sapiens
1335	MARH8_HUMAN	2B18_HUMAN	Q5T0T0	Q30134	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1336	MARH8_HUMAN	DRB5_HUMAN	Q5T0T0	Q30154	MARCHF8	HLA-DRB5	UniProt	MARH8_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1337	MARH8_HUMAN	2B19_HUMAN	Q5T0T0	Q9TQE0	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1338	MARH8_HUMAN	MAVS_HUMAN	Q5T0T0	Q7Z434	MARCHF8	MAVS	MEDLINE	29165031	Recently, we have revealed that IFN (interferon)-induced BST2 recruits the E3 ubiquitin ligase <span class="match term0">MARCH8</span> to catalyze the K27-linked ubiquitination of <span class="match term1">MAVS</span> for CALCOCO2-directed autophagic degradation, hence inhibiting DDX58-mediated type I interferon signaling through a negative feedback loop.	RING	1	Other	H.sapiens
1339	MARH8_HUMAN	DRB3_HUMAN	Q5T0T0	P79483	MARCHF8	HLA-DRB3	UniProt	MARH8_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1340	MARH8_HUMAN	2B11_HUMAN	Q5T0T0	P04229	MARCHF8	HLA-DRB1	UniProt	2B11_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1341	MARH8_HUMAN	DRB4_HUMAN	Q5T0T0	P13762	MARCHF8	HLA-DRB4	UniProt	MARH8_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II	RING	1	Training data	H.sapiens
1342	MARH8_HUMAN	CD86_HUMAN	Q5T0T0	P42081	MARCHF8	CD86	UniProt	MARH8_HUMAN	E3 ubiquitin-protein ligase that may regulate immune responses by promoting ubiquitination of MHC-II and <span class="match term1">CD86</span>, which leads to their subsequent endocytosis and lysosomal degradation	RING	1	Training data	H.sapiens
1343	MARH8_HUMAN	SODC_HUMAN	Q5T0T0	P00441	MARCHF8	SOD1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1344	MARH8_HUMAN	2B1B_HUMAN	Q5T0T0	P20039	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1345	MARH8_HUMAN	ATX3_HUMAN	Q5T0T0	P54252	MARCHF8	ATXN3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1346	MARH8_HUMAN	2B1C_HUMAN	Q5T0T0	Q95IE3	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1347	MARH8_HUMAN	CADH1_HUMAN	Q5T0T0	P12830	MARCHF8	CDH1	MEDLINE	33540066	We demonstrated that <span class="match term0">MARCH8</span> interacts with and ubiquitinates <span class="match term1">CDH1</span> and beta2M	RING	1	Other	H.sapiens
1348	MARH8_HUMAN	TFR1_HUMAN	Q5T0T0	P02786	MARCHF8	TFRC	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1349	MARH8_HUMAN	2B1A_HUMAN	Q5T0T0	Q30167	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1350	MARH8_HUMAN	2B14_HUMAN	Q5T0T0	P13760	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1351	MARH8_HUMAN	A2MG_HUMAN	Q5T0T0	P01023	MARCHF8	A2M	MEDLINE	33540066	We demonstrated that <span class="match term0">MARCH8</span> interacts with and ubiquitinates CDH1 and <span class="match term1">beta2M</span>	RING	1	Other	H.sapiens
1352	MARH8_HUMAN	2B17_HUMAN	Q5T0T0	P13761	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1353	MARH8_HUMAN	CP3A4_HUMAN	Q5T0T0	P08684	MARCHF8	CYP3A4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1354	MARH8_HUMAN	FAS_HUMAN	Q5T0T0	P49327	MARCHF8	FASN	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1355	MARH8_HUMAN	2B1G_HUMAN	Q5T0T0	Q29974	MARCHF8	HLA-DRB1	UniProt	MARH1_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1356	MARH8_HUMAN	2B13_HUMAN	Q5T0T0	P01912	MARCHF8	HLA-DRB1	UniProt	2B13_HUMAN	Ubiquitinated by MARCH1 and <span class="match term0">MARCH8</span> at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II (Probable)	RING	1	Training data	H.sapiens
1357	MARH8_HUMAN	HG2A_HUMAN	Q5T0T0	P04233	MARCHF8	CD74	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1358	MARH8_HUMAN	4F2_HUMAN	Q5T0T0	P08195	MARCHF8	SLC3A2	MEDLINE	21757542	UbiNet 2.0	RING	1	Training data	H.sapiens
1359	MARH8_HUMAN	C2TA_HUMAN	Q5T0T0	P33076	MARCHF8	CIITA	MEDLINE	19566897	UbiNet 2.0	RING	1	Training data	H.sapiens
1360	MARH9_HUMAN	IGHD_HUMAN	Q86YJ5	P01880	MARCHF9	IGHD	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1361	MARH9_HUMAN	CEIP2_HUMAN	Q86YJ5	Q9UHN6	MARCHF9	CEMIP2	MEDLINE	19457934	UbiNet 2.0	RING	1	Training data	H.sapiens
1362	MARH9_HUMAN	PTPRF_HUMAN	Q86YJ5	P10586	MARCHF9	PTPRF	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1363	MARH9_HUMAN	PTPRA_HUMAN	Q86YJ5	P18433	MARCHF9	PTPRA	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1364	MARH9_HUMAN	ICAM1_HUMAN	Q86YJ5	P05362	MARCHF9	ICAM1	MEDLINE	17174307	<span class="match term0">MARCH-IX</span> expression causes ubiquitination and downregulation of <span class="match term1">ICAM-1</span> and a short alternative transcript of <span class="match term0">MARCH-IX</span> lacking the RING-CH domain, termed <span class="match term0">MARCH-IX</span> RINGless, is shown to act as a positive regulator of <span class="match term0">MARCH-IX</span> activity	RING	1	Training data	H.sapiens
1365	MARH9_HUMAN	FCRLB_HUMAN	Q86YJ5	Q6BAA4	MARCHF9	FCRLB	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1366	MARH9_HUMAN	DQA1_HUMAN	Q86YJ5	P01909	MARCHF9	HLA-DQA1	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1367	MARH9_HUMAN	FCRL2_HUMAN	Q86YJ5	Q96LA5	MARCHF9	FCRL2	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1368	MARH9_HUMAN	PLXC1_HUMAN	Q86YJ5	O60486	MARCHF9	PLXNC1	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1369	MARH9_HUMAN	PTPRJ_HUMAN	Q86YJ5	Q12913	MARCHF9	PTPRJ	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1370	MARH9_HUMAN	VAMP8_HUMAN	Q86YJ5	Q9BV40	MARCHF9	VAMP8	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1371	MARH9_HUMAN	LIRB1_HUMAN	Q86YJ5	Q8NHL6	MARCHF9	LILRB1	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1372	MARH9_HUMAN	CD4_HUMAN	Q86YJ5	P01730	MARCHF9	CD4	UniProt	MARH9_HUMAN	E3 ubiquitin-protein ligase that may mediate ubiquitination of MHC-I, <span class="match term1">CD4</span> and ICAM1, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies	RING	1	Training data	H.sapiens
1373	MARH9_HUMAN	SLAF1_HUMAN	Q86YJ5	Q13291	MARCHF9	SLAMF1	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1374	MARH9_HUMAN	DQB1_HUMAN	Q86YJ5	P01920	MARCHF9	HLA-DQB1	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1375	MARH9_HUMAN	FCG2B_HUMAN	Q86YJ5	P31994	MARCHF9	FCGR2B	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1376	MARH9_HUMAN	PVR_HUMAN	Q86YJ5	P15151	MARCHF9	PVR	High-throughput	19457934	2009_Hor	RING	1	Training data	H.sapiens
1377	MDM2_HUMAN	P53_HUMAN	Q00987	P04637	MDM2	TP53	MEDLINE	12080472	Taken together, these results suggest that <span class="match term0">Mdm2</span> activation of E2F1 occurs through the repression of <span class="match term1">p53</span>-dependent transcription of p21, a <span class="match term1">p53</span>-target gene and cyclin dependent kinase inhibitor	RING	1	Training data	H.sapiens
1378	MDM2_HUMAN	EID1_HUMAN	Q00987	Q9Y6B2	MDM2	EID1	MEDLINE	11073989	Ubiquitination of <span class="match term1">EID-1</span> requires an intact C-terminal region that is also necessary for stable binding to p300 and pRB, two proteins that bind to the ubiquitin ligase <span class="match term0">MDM2</span>	RING	1	Training data	H.sapiens
1379	MDM2_HUMAN	CDN1A_HUMAN	Q00987	P38936	MDM2	CDKN1A	MEDLINE	10698510	Tissue and cell-specific expression of the p53-target genes: bax, fas, <span class="match term0">mdm2</span> and <span class="match term1">waf1</span>/p21, before and following ionising irradiation in mice	RING	1	Training data	H.sapiens
1380	MDM2_HUMAN	GNL3_HUMAN	Q00987	Q9BVP2	MDM2	GNL3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1381	MDM2_HUMAN	CCNE1_HUMAN	Q00987	P24864	MDM2	CCNE1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1382	MDM2_HUMAN	MDM4_HUMAN	Q00987	O15151	MDM2	MDM4	MEDLINE	16227609	DNA damage-induced phosphorylation of <span class="match term1">MdmX</span> at serine 367 activates p53 by targeting <span class="match term1">MdmX</span> for <span class="match term0">Mdm2</span>-dependent degradation	RING	1	Training data	H.sapiens
1383	MDM2_HUMAN	TERT_HUMAN	Q00987	O14746	MDM2	TERT	MEDLINE	20453884	UbiNet 2.0	RING	1	Training data	H.sapiens
1384	MDM2_HUMAN	PSMD4_HUMAN	Q00987	P55036	MDM2	PSMD4	MEDLINE	19240029	UbiNet 2.0	RING	1	Other	H.sapiens
1385	MDM2_HUMAN	MDM2_HUMAN	Q00987	Q00987	MDM2	MDM2	MEDLINE	18234968	The negative effect of SS18-SSX1 expression on p53 was mediated by its ability to promote <span class="match term0">HDM2</span> stabilization through inhibition of <span class="match term0">HDM2</span> autoubiquitination	RING	1	Training data	H.sapiens
1386	MDM2_HUMAN	RIR2B_HUMAN	Q00987	Q7LG56	MDM2	RRM2B	MEDLINE	19015526	UbiNet 2.0	RING	1	Other	H.sapiens
1387	MDM2_HUMAN	ARRB2_HUMAN	Q00987	P32121	MDM2	ARRB2	UniProt	MDM2_HUMAN	Ubiquitinated by <span class="match term0">MDM2</span>; the ubiquitination is required for rapid internalization of ADRB2	RING	1	Training data	H.sapiens
1388	MDM2_HUMAN	DYR_HUMAN	Q00987	P00374	MDM2	DHFR	MEDLINE	18451149	Here, we describe the identification of a novel substrate for the <span class="match term0">MDM2</span> ubiquitin ligase: dihydrofolate reductase (<span class="match term1">DHFR</span>)	RING	1	Other	H.sapiens
1389	MDM2_HUMAN	CBP_HUMAN	Q00987	Q92793	MDM2	CREBBP	MEDLINE	21374733	Moreover, P300/<span class="match term1">CBP</span>-associated factor (PCAF), an ubiquitin ligase 3 for <span class="match term0">Mdm2</span>, was observed to participate in <span class="match term0">Mdm2</span> ubiquitination by PKCdelta inhibition and knock-down of PCAF rescued <span class="match term0">Mdm2</span> diminution.	RING	1	Training data	H.sapiens
1390	MDM2_HUMAN	HEXI1_HUMAN	Q00987	O94992	MDM2	HEXIM1	MEDLINE	19617712	UbiNet 2.0	RING	1	Training data	H.sapiens
1391	MDM2_HUMAN	KAT2B_HUMAN	Q00987	Q92831	MDM2	KAT2B	MEDLINE	19176998	Interestingly as well, a <span class="match term1">PCAF</span> deletion mutant that lacks E3 ligase activity towards <span class="match term0">Mdm2</span> also enhances Chk2 degradation	RING	1	Training data	H.sapiens
1392	MDM2_HUMAN	AQP2_HUMAN	Q00987	P41181	MDM2	AQP2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1393	MDM2_HUMAN	DYRK2_HUMAN	Q00987	Q92630	MDM2	DYRK2	MEDLINE	19965871	Under normal conditions, nuclear and not cytoplasmic <span class="match term1">DYRK2</span> is ubiquitinated by <span class="match term0">MDM2</span>, resulting in its constitutive degradation	RING	1	Other	H.sapiens
1394	MDM2_HUMAN	FOXO4_HUMAN	Q00987	P98177	MDM2	FOXO4	MEDLINE	18665269	UbiNet 2.0	RING	1	Training data	H.sapiens
1395	MDM2_HUMAN	ARBK1_HUMAN	Q00987	P25098	MDM2	ADRBK1	MEDLINE	17006543	Moreover, we find that activation of the PI3K/Akt pathway by insulin-like growth factor-1 alters <span class="match term0">Mdm2</span>-mediated GRK2 degradation, leading to enhanced GRK2 stability and increased kinase levels	RING	1	Training data	H.sapiens
1396	MDM2_HUMAN	HUWE1_HUMAN	Q00987	Q7Z6Z7	MDM2	HUWE1	MEDLINE	30818224	UbiNet 2.0	RING	1	Other	H.sapiens
1397	MDM2_HUMAN	L2GL1_HUMAN	Q00987	Q15334	MDM2	LLGL1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1398	MDM2_HUMAN	TTF1_HUMAN	Q00987	Q15361	MDM2	TTF1	MEDLINE	22383580	UbiNet 2.0	RING	1	Training data	H.sapiens
1399	MDM2_HUMAN	DAXX_HUMAN	Q00987	Q9UER7	MDM2	DAXX	MEDLINE	20153724	UbiNet 2.0	RING	1	Training data	H.sapiens
1400	MDM2_HUMAN	RB_HUMAN	Q00987	P06400	MDM2	RB1	MEDLINE	17297463	We have recently shown that <span class="match term0">MDM2</span> interacts with <span class="match term1">Rb</span> and promotes proteasome-dependent <span class="match term1">Rb</span> degradation	RING	1	Training data	H.sapiens
1401	MDM2_HUMAN	ESR2_HUMAN	Q00987	Q92731	MDM2	ESR2	MEDLINE	22349818	UbiNet 2.0	RING	1	Training data	H.sapiens
1402	MDM2_HUMAN	NFAT5_HUMAN	Q00987	O94916	MDM2	NFAT5	MEDLINE	16338656	UbiNet 2.0	RING	1	Training data	H.sapiens
1403	MDM2_HUMAN	EP300_HUMAN	Q00987	Q09472	MDM2	EP300	MEDLINE	10207051	<span class="match term0">MDM2</span> did not promote the degradation of p73 but instead disrupted the interaction of p73, but not of p53, with <span class="match term1">p300</span>/CBP by competing with p73 for binding to the <span class="match term1">p300</span>/CBP N terminus	RING	1	Training data	H.sapiens
1404	MDM2_HUMAN	DCX_HUMAN	Q00987	O43602	MDM2	DCX	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1405	MDM2_HUMAN	DDX24_HUMAN	Q00987	Q9GZR7	MDM2	DDX24	MEDLINE	24980433	<span class="match term0">MDM2</span> mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase <span class="match term1">DDX24</span>.	RING	1	Other	H.sapiens
1406	MDM2_HUMAN	RS2_HUMAN	Q00987	P15880	MDM2	RPS2	MEDLINE	31928715	<span class="match term1">RPS2</span> is ubiquitinated by <span class="match term0">MDM2</span> and the ubiquitinated status of <span class="match term1">RPS2</span> regulates the stability of p53, which is activated in response to cellular stresses such as DNA damage, oxidative stress, and especially ribosomal stress	RING	1	Other	H.sapiens
1407	MDM2_HUMAN	RUNX3_HUMAN	Q00987	Q13761	MDM2	RUNX3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1408	MDM2_HUMAN	H2B2E_HUMAN	Q00987	Q16778	MDM2	H2BC21	MEDLINE	15546622	UbiNet 2.0	RING	1	Other	H.sapiens
1409	MDM2_HUMAN	NUCL_HUMAN	Q00987	P19338	MDM2	NCL	MEDLINE	28478507	<span class="match term0">MDM2</span> Degrades Deacetylated <span class="match term1">Nucleolin</span> Through Ubiquitination to Promote Glioma Stem-Like Cell Enrichment for Chemotherapeutic Resistance	RING	1	Other	H.sapiens
1410	MDM2_HUMAN	IRS1_HUMAN	Q00987	P35568	MDM2	IRS1	MEDLINE	15456867	In summary, we have found the following: (i) beta-arrestin-1 can alter insulin signaling by inhibiting insulin-induced proteasomal degradation of <span class="match term1">IRS-1</span>; (ii) beta-arrestin-1 decreases the rate of ubiquitination of <span class="match term1">IRS-1</span> by competitively binding to endogenous <span class="match term0">Mdm2</span>, an E3 ligase that can ubiquitinate <span class="match term1">IRS-1</span>; (iii) dephosphorylation of S412 on beta-arrestin and the amino terminus of beta-arrestin-1 are required for this effect of beta-arrestin on <span class="match term1">IRS-1</span> degradation; and (iv) inhibition of beta-arrestin-1 leads to enhanced <span class="match term1">IRS-1</span> degradation and accentuated cellular insulin resistance	RING	1	Training data	H.sapiens
1411	MDM2_HUMAN	HIF1A_HUMAN	Q00987	Q16665	MDM2	HIF1A	MEDLINE	10640274	UbiNet 2.0	RING	1	Other	H.sapiens
1412	MDM2_HUMAN	HIPK2_HUMAN	Q00987	Q9H2X6	MDM2	HIPK2	MEDLINE	17349959	<span class="match term0">MDM2</span>-regulated degradation of <span class="match term1">HIPK2</span> prevents p53Ser46 phosphorylation and DNA damage-induced apoptosis	RING	1	Training data	H.sapiens
1413	MDM2_HUMAN	KAT5_HUMAN	Q00987	Q92993	MDM2	KAT5	MEDLINE	15640443	We also show that HDAC1 and <span class="match term0">Mdm2</span> function co-operatively to reduce AR-mediated transcription that is attenuated by the HAT activity of the AR co-activator <span class="match term1">Tip60</span>, suggesting interplay between acetylation status and receptor ubiquitylation in AR regulation	RING	1	Training data	H.sapiens
1414	MDM2_HUMAN	CADH1_HUMAN	Q00987	P12830	MDM2	CDH1	MEDLINE	16980628	Blocking endocytosis with dominant-negative mutants of dynamin abolished the association of <span class="match term0">MDM2</span> with E-cadherin, prevented E-cadherin degradation, and attenuated cell motility as observed by fluorescence microscopy	RING	1	Training data	H.sapiens
1415	MDM2_HUMAN	RL26_HUMAN	Q00987	P61254	MDM2	RPL26	MEDLINE	18951086	<span class="match term0">Mdm2</span> binds <span class="match term1">L26</span> and drives its polyubiquitylation and proteasomal degradation	RING	1	Training data	H.sapiens
1416	MDM2_HUMAN	IRF2_HUMAN	Q00987	P14316	MDM2	IRF2	MEDLINE	19032150	Role of <span class="match term0">Mdm2</span> acid domain interactions in recognition and ubiquitination of the transcription factor <span class="match term1">IRF-2</span>.	RING	1	Other	H.sapiens
1417	MDM2_HUMAN	PGAM2_HUMAN	Q00987	P15259	MDM2	PGAM2	MEDLINE	24567357	UbiNet 2.0	RING	1	Other	H.sapiens
1418	MDM2_HUMAN	JMY_HUMAN	Q00987	Q8N9B5	MDM2	JMY	UniProt	MDM2_HUMAN	Ubiquitinated by <span class="match term0">MDM2</span>, leading to its subsequent degradation by the proteasome	RING	1	Training data	H.sapiens
1419	MDM2_HUMAN	ARRB1_HUMAN	Q00987	P49407	MDM2	ARRB1	UniProt	MDM2_HUMAN	Ubiquitinated by <span class="match term0">MDM2</span>; the ubiquitination is required for rapid internalization of ADRB2	RING	1	Training data	H.sapiens
1420	MDM2_HUMAN	RT07_HUMAN	Q00987	Q9Y2R9	MDM2	MRPS7	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1421	MDM2_HUMAN	APEX1_HUMAN	Q00987	P27695	MDM2	APEX1	MEDLINE	19219073	<span class="match term1">APE1</span> ubiquitination occurred specifically at Lys residues near the N-terminus, and was markedly enhanced by mouse double minute 2 (<span class="match term0">MDM2</span>), the major intracellular p53 inhibitor	RING	1	Training data	H.sapiens
1422	MDM2_HUMAN	RARA_HUMAN	Q00987	P10276	MDM2	RARA	MEDLINE	26776160	In this study, we discover that murine double minute-2 (<span class="match term0">MDM2</span>) acts as an E3 ubiquitin ligase to target RARalpha for degradation	RING	1	Other	H.sapiens
1423	MDM2_HUMAN	ANDR_HUMAN	Q00987	P10275	MDM2	AR	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1424	MDM2_HUMAN	NFAC2_HUMAN	Q00987	Q13469	MDM2	NFATC2	MEDLINE	20009572	<span class="match term0">HDM2</span> negatively regulates cell migration by targeting NFAT (a transcription factor) for ubiquitination and degradation, while SCF(beta-TRCP) ubiquitinates Snail (a transcriptional repressor of E-cadherin) to inhibit cell migration	RING	1	Training data	H.sapiens
1425	MDM2_HUMAN	SNAI1_HUMAN	Q00987	O95863	MDM2	SNAI1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1426	MDM2_HUMAN	UT2_HUMAN	Q00987	Q15849	MDM2	SLC14A2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1427	MDM2_HUMAN	FOXP3_HUMAN	Q00987	Q9BZS1	MDM2	FOXP3	MEDLINE	32636834	Mechanistically, <span class="match term0">MDM2</span> interacts with <span class="match term1">FOXP3</span>, and mainly mediates monoubiquitination and polyubiquitination of <span class="match term1">FOXP3</span>, thus stabilizing the protein level of <span class="match term1">FOXP3</span>	RING	1	Other	H.sapiens
1428	MDM2_HUMAN	E2F1_HUMAN	Q00987	Q01094	MDM2	E2F1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1429	MDM2_HUMAN	NUMB_HUMAN	Q00987	P49757	MDM2	NUMB	MEDLINE	12646252	Mammalian <span class="match term1">Numb</span> is a target protein of <span class="match term0">Mdm2</span>, ubiquitin ligase.	RING	1	Other	H.sapiens
1430	MDM2_HUMAN	PBX1_HUMAN	Q00987	P40424	MDM2	PBX1	MEDLINE	23044487	UbiNet 2.0	RING	1	Other	H.sapiens
1431	MDM2_HUMAN	FOXO3_HUMAN	Q00987	O43524	MDM2	FOXO3	MEDLINE	19321440	UbiNet 2.0	RING	1	Training data	H.sapiens
1432	MDM2_HUMAN	IRF1_HUMAN	Q00987	P10914	MDM2	IRF1	MEDLINE	23134341	UbiNet 2.0	RING	1	Other	H.sapiens
1433	MDM2_HUMAN	FOXO1_HUMAN	Q00987	Q12778	MDM2	FOXO1	MEDLINE	19321440	UbiNet 2.0	RING	1	Training data	H.sapiens
1434	MDM2_HUMAN	NR0B2_HUMAN	Q00987	Q15466	MDM2	NR0B2	MEDLINE	22575647	UbiNet 2.0	RING	1	Training data	H.sapiens
1435	MDM2_HUMAN	ATF3_HUMAN	Q00987	P18847	MDM2	ATF3	MEDLINE	20592017	Here, we demonstrate that mouse double minute 2 (<span class="match term0">MDM2</span>) is a bona fide E3 ubiquitin ligase for <span class="match term1">ATF3</span> and regulates <span class="match term1">ATF3</span> expression by promoting its degradation	RING	1	Other	H.sapiens
1436	MDM2_HUMAN	PBIP1_HUMAN	Q00987	Q96AQ6	MDM2	PBXIP1	MEDLINE	24488098	UbiNet 2.0	RING	1	Other	H.sapiens
1437	MDM2_HUMAN	NOL3_HUMAN	Q00987	O60936	MDM2	NOL3	MEDLINE	17142834	This activity requires a functioning <span class="match term0">MDM2</span> ring finger domain because the <span class="match term0">MDM2</span>(C464A) mutant was unable to direct <span class="match term1">ARC</span> degradation	RING	1	Training data	H.sapiens
1438	MDM2_HUMAN	IEX1_HUMAN	Q00987	P46695	MDM2	IER3	MEDLINE	26973248	Here, we demonstrate that <span class="match term0">MDM2</span> is an E3 ligase that interacts with <span class="match term1">IER3</span> and promotes its ubiquitination, followed by proteasomal degradation	RING	1	Other	H.sapiens
1439	MDM2_HUMAN	DPOLQ_HUMAN	Q00987	O75417	MDM2	POLQ	MEDLINE	22056306	UbiNet 2.0	RING	1	Training data	H.sapiens
1440	MDM2_HUMAN	IGF1R_HUMAN	Q00987	P08069	MDM2	IGF1R	MEDLINE	12821780	<span class="match term0">Mdm2</span>-dependent ubiquitination and degradation of the insulin-like growth factor 1 receptor	RING	1	Training data	H.sapiens
1441	MDM2_HUMAN	FUS_HUMAN	Q00987	P35637	MDM2	FUS	MEDLINE	31632968	Moreover, the E3 ubiquitin-protein ligase <span class="match term0">MDM2</span> interacts with and down regulates <span class="match term1">FUS</span>, while the RRM and Znf_RanBP2 domains of <span class="match term1">FUS</span> facilitate its binding with <span class="match term0">MDM2</span>.	RING	1	Other	H.sapiens
1442	MDM2_HUMAN	P73_HUMAN	Q00987	O15350	MDM2	TP73	MEDLINE	26025930	<span class="match term0">MDM2</span> mediates <span class="match term1">p73</span> ubiquitination: a new molecular mechanism for suppression of <span class="match term1">p73</span> function	RING	1	Other	H.sapiens
1443	MDM2_HUMAN	ARPC3_HUMAN	Q00987	O15145	MDM2	ARPC3	MEDLINE	17142834	UbiNet 2.0	RING	1	Training data	H.sapiens
1444	MDM2_HUMAN	XRCC6_HUMAN	Q00987	P12956	MDM2	XRCC6	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1445	MDM2_HUMAN	HBP1_HUMAN	Q00987	O60381	MDM2	HBP1	MEDLINE	30816344	<span class="match term0">MDM2</span> facilitates <span class="match term1">HBP1</span> proteasomal degradation by ubiquitinating <span class="match term1">HBP1</span>, regardless of p53 status, thus attenuating the transcriptional inhibition of <span class="match term1">HBP1</span> in the expression of its target genes, such as the DNA methyltransferase DNMT1 and histone methyltransferase EZH2, which results in global DNA hypermethylation and histone hypermethylation and ultimately genome instability	RING	1	Other	H.sapiens
1446	MDM2_HUMAN	DLG4_HUMAN	Q00987	P78352	MDM2	DLG4	MEDLINE	14642282	PSD-95 interacts with and is ubiquitinated by the E3 ligase <span class="match term0">Mdm2</span>	RING	1	Training data	H.sapiens
1447	MDM2_HUMAN	PER2_HUMAN	Q00987	O15055	MDM2	PER2	MEDLINE	30425162	We identified <span class="match term1">PER2</span> as a previously uncharacterized substrate for the ubiquitin ligase mouse double minute 2 homolog (<span class="match term0">MDM2</span>) and found that <span class="match term0">MDM2</span> targeted <span class="match term1">PER2</span> for degradation in a manner independent of <span class="match term1">PER2</span> phosphorylation	RING	1	Other	H.sapiens
1448	MDM2_HUMAN	GCR_HUMAN	Q00987	P04150	MDM2	NR3C1	MEDLINE	12897156	UbiNet 2.0	RING	1	Training data	H.sapiens
1449	MDM2_HUMAN	PDE4D_HUMAN	Q00987	Q08499	MDM2	PDE4D	MEDLINE	19372219	UbiNet 2.0	RING	1	Training data	H.sapiens
1450	MDM2_HUMAN	STAT3_HUMAN	Q00987	P40763	MDM2	STAT3	MEDLINE	33660414	Mechanistically, MAPSK3 interacted with <span class="match term0">MDM2</span> to promote <span class="match term1">STAT3</span> degradation via the ubiquitin-proteasome pathway	RING	1	Other	H.sapiens
1451	MDM2_HUMAN	WRN_HUMAN	Q00987	Q14191	MDM2	WRN	MEDLINE	30532073	<span class="match term0">MDM2</span> induces ubiquitination of <span class="match term1">WRN</span> and dramatically downregulates the levels of <span class="match term1">WRN</span> protein in human cells	RING	1	Other	H.sapiens
1452	MDM2_HUMAN	RS27A_HUMAN	Q00987	P62979	MDM2	RPS27A	MEDLINE	21561866	UbiNet 2.0	RING	1	Other	H.sapiens
1453	MDM2_HUMAN	GA45A_HUMAN	Q00987	P24522	MDM2	GADD45A	MEDLINE	23563151	Here, we demonstrated that <span class="match term0">MDM2</span> was an E3 ubiquitin ligase for GADD45alpha	RING	1	Other	H.sapiens
1454	MDM2_HUMAN	MAPK2_HUMAN	Q00987	P49137	MDM2	MAPKAPK2	MEDLINE	34272277	<span class="match term1">MK2</span> degradation is mediated by the E3 ubiquitin ligase <span class="match term0">MDM2</span>, and we identify four lysine residues in <span class="match term1">MK2</span> that are directly ubiquitinated by <span class="match term0">MDM2</span>	RING	1	Other	H.sapiens
1455	MDM2_HUMAN	NOTC1_HUMAN	Q00987	P46531	MDM2	NOTCH1	MEDLINE	23252402	Non-degradative ubiquitination of the <span class="match term1">Notch1</span> receptor by the E3 ligase <span class="match term0">MDM2</span> activates the Notch signalling pathway.	RING	1	Other	H.sapiens
1456	MDM2_HUMAN	BI2L1_HUMAN	Q00987	Q9UHR4	MDM2	BAIAP2L1	MEDLINE	21887275	UbiNet 2.0	RING	1	Other	H.sapiens
1457	MDM2_HUMAN	TELT_HUMAN	Q00987	O15273	MDM2	TCAP	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1458	MDM2_HUMAN	ARI2_HUMAN	Q00987	O95376	MDM2	ARIH2	MEDLINE	22940738	UbiNet 2.0	RING	1	Training data	H.sapiens
1459	MDM2_HUMAN	HIPK1_HUMAN	Q00987	Q86Z02	MDM2	HIPK1	MEDLINE	22173032	UbiNet 2.0	RING	1	Training data	H.sapiens
1460	MDM4_HUMAN	MDM2_HUMAN	O15151	Q00987	MDM4	MDM2	MEDLINE	11568180	We also find that this transcriptionally inactive E2F-1 mutant is capable of degrading the <span class="match term0">MDMX</span>-related protein <span class="match term1">MDM2</span> and the <span class="match term0">MDMX</span> isoform <span class="match term0">MDMX</span>-S	RING	1	Training data	H.sapiens
1461	MDM4_HUMAN	P53_HUMAN	O15151	P04637	MDM4	TP53	MEDLINE	12393902	UbiNet 2.0	RING	1	Training data	H.sapiens
1462	MDM4_HUMAN	CDN1A_HUMAN	O15151	P38936	MDM4	CDKN1A	MEDLINE	18086887	Although the <span class="match term0">MDMX</span> effect was independent of MDM2, they synergistically promoted <span class="match term1">p21</span> degradation when coexpressed in cells	RING	1	Training data	H.sapiens
1463	MEX3B_HUMAN	SPN1_HUMAN	Q6ZN04	O95149	MEX3B	SNUPN	MEDLINE	24326307	UbiNet 2.0	Other	1	Other	H.sapiens
1464	MEX3C_HUMAN	DDX58_HUMAN	Q5U5Q3	O95786	MEX3C	DDX58	MEDLINE	30095198	Recent evidence has suggested that human <span class="match term0">MEX-3C</span> has a strong bondage with carcinogenesis and the <span class="match term0">MEX-3C</span>-mediated ubiquitination of <span class="match term1">RIG-I</span> is essential for the antiviral innate immune response	RING	1	Other	H.sapiens
1465	MGRN1_HUMAN	TS101_HUMAN	O60291	Q99816	MGRN1	TSG101	MEDLINE	17229889	UbiNet 2.0	RING	1	Training data	H.sapiens
1466	MIB1_HUMAN	DAPK1_HUMAN	Q86YT6	P53355	MIB1	DAPK1	MEDLINE	12351649	A death-associated protein kinase (<span class="match term1">DAPK</span>)-interacting protein, <span class="match term0">DIP-1</span>, is an E3 ubiquitin ligase that promotes tumor necrosis factor-induced apoptosis and regulates the cellular levels of <span class="match term1">DAPK</span>	RING	1	Training data	H.sapiens
1467	MIB1_HUMAN	E41L5_HUMAN	Q86YT6	Q9HCM4	MIB1	EPB41L5	MEDLINE	31462741	<span class="match term0">MIB1</span> binds to and ubiquitinates <span class="match term1">EPB41L5</span> resulting in its degradation	RING	1	Other	H.sapiens
1468	MIB1_HUMAN	EDAR_HUMAN	Q86YT6	Q9UNE0	MIB1	EDAR	MEDLINE	20176925	UbiNet 2.0	RING	1	Training data	H.sapiens
1469	MIB1_HUMAN	SMN_HUMAN	Q86YT6	Q16637	MIB1	SMN1	MEDLINE	23615451	UbiNet 2.0	RING	1	Training data	H.sapiens
1470	MIB1_HUMAN	PCM1_HUMAN	Q86YT6	Q15154	MIB1	PCM1	MEDLINE	24121310	UbiNet 2.0	RING	1	Training data	H.sapiens
1471	MIB1_HUMAN	DLL4_HUMAN	Q86YT6	Q9NR61	MIB1	DLL4	UniProt	MIB1_HUMAN	Ubiquitinated by MIB (<span class="match term0">MIB1</span> or MIB2), leading to its endocytosis and subsequent degradation (By similarity)	RING	1	Training data	H.sapiens
1472	MIB1_HUMAN	DLL1_HUMAN	Q86YT6	O00548	MIB1	DLL1	UniProt	MIB1_HUMAN	Ubiquitinated by MIB (<span class="match term0">MIB1</span> or MIB2), leading to its endocytosis and subsequent degradation (By similarity)	RING	1	Training data	H.sapiens
1473	MIB1_HUMAN	DLL3_HUMAN	Q86YT6	Q9NYJ7	MIB1	DLL3	UniProt	MIB1_HUMAN	Ubiquitinated by MIB (<span class="match term0">MIB1</span> or MIB2), leading to its endocytosis and subsequent degradation (By similarity)	RING	1	Training data	H.sapiens
1474	MIB1_HUMAN	TBK1_HUMAN	Q86YT6	Q9UHD2	MIB1	TBK1	MEDLINE	21903422	Detailed mechanistic analysis defined a role for mind bomb (<span class="match term0">MIB</span>) E3 ligases in K63-linked ubiquitination of <span class="match term1">TBK1</span>, a kinase that phosphorylates IRF transcription factors controlling interferon production	RING	1	Other	H.sapiens
1475	MIB1_HUMAN	CE290_HUMAN	Q86YT6	O15078	MIB1	CEP290	MEDLINE	24121310	UbiNet 2.0	RING	1	Training data	H.sapiens
1476	MIB1_HUMAN	CP131_HUMAN	Q86YT6	Q9UPN4	MIB1	CEP131	MEDLINE	24121310	UbiNet 2.0	RING	1	Training data	H.sapiens
1477	MIB1_HUMAN	BLM_HUMAN	Q86YT6	P54132	MIB1	BLM	MEDLINE	24239288	UbiNet 2.0	RING	1	Other	H.sapiens
1478	MIB1_HUMAN	MIB1_HUMAN	Q86YT6	Q86YT6	MIB1	MIB1	MEDLINE	12351649	The RING finger motifs of <span class="match term0">DIP-1</span> have E3 ligase activity that can auto-ubiquitinate <span class="match term0">DIP-1</span> in vitro	RING	1	Training data	H.sapiens
1479	MIB1_HUMAN	JAG1_HUMAN	Q86YT6	P78504	MIB1	JAG1	MEDLINE	25747658	UbiNet 2.0	RING	1	Other	H.sapiens
1480	MIB2_HUMAN	NEMO_HUMAN	Q96AX9	Q9Y6K9	MIB2	IKBKG	MEDLINE	21896478	UbiNet 2.0	RING	1	Training data	H.sapiens
1481	MIB2_HUMAN	DLL4_HUMAN	Q96AX9	Q9NR61	MIB2	DLL4	UniProt	MIB2_HUMAN	Ubiquitinated by MIB (MIB1 or <span class="match term0">MIB2</span>), leading to its endocytosis and subsequent degradation (By similarity)	RING	1	Training data	H.sapiens
1482	MIB2_HUMAN	XDH_HUMAN	Q96AX9	P47989	MIB2	XDH	MEDLINE	15824097	UbiNet 2.0	RING	1	Training data	H.sapiens
1483	MIB2_HUMAN	DLL3_HUMAN	Q96AX9	Q9NYJ7	MIB2	DLL3	UniProt	MIB2_HUMAN	Ubiquitinated by MIB (MIB1 or <span class="match term0">MIB2</span>), leading to its endocytosis and subsequent degradation (By similarity)	RING	1	Training data	H.sapiens
1484	MIB2_HUMAN	CYLD_HUMAN	Q96AX9	Q9NQC7	MIB2	CYLD	MEDLINE	25565632	To dissect <span class="match term1">CYLD</span> function we used a proteomics approach to identify <span class="match term1">CYLD</span> interacting proteins and identified <span class="match term0">MIB2</span>, an ubiquitin ligase enzyme involved in Notch signalling, as a protein which interacts with <span class="match term1">CYLD</span>	RING	1	Other	H.sapiens
1485	MIB2_HUMAN	TBK1_HUMAN	Q96AX9	Q9UHD2	MIB2	TBK1	MEDLINE	21903422	UbiNet 2.0	RING	1	Other	H.sapiens
1486	MIB2_HUMAN	DLL1_HUMAN	Q96AX9	O00548	MIB2	DLL1	UniProt	MIB2_HUMAN	Ubiquitinated by MIB (MIB1 or <span class="match term0">MIB2</span>), leading to its endocytosis and subsequent degradation (By similarity)	RING	1	Training data	H.sapiens
1487	TRI18_HUMAN	PP2AA_HUMAN	O15344	P67775	MID1	PPP2CA	MEDLINE	11685209	<span class="match term1">PP2Ac</span> accumulation is caused by an impairment of a newly identified E3 ubiquitin ligase activity of the <span class="match term0">MID1</span> protein that normally targets <span class="match term1">PP2Ac</span> for degradation through binding to its alpha4 regulatory subunit in an embryonic fibroblast line derived from a fetus with OS	RING	1	Training data	H.sapiens
1488	TRI18_HUMAN	UCHL1_HUMAN	O15344	P54829	MID1	STK36	MEDLINE	25278022	25278022	RING	1	Other	H.sapiens
1489	TRI18_HUMAN	STING_HUMAN	O15344	Q9NRP7	MID1	PPP2R4	MEDLINE	25207814	25207814	RING	1	Other	H.sapiens
1490	TRI18_HUMAN	IGBP1_HUMAN	O15344	P78318	MID1	IGBP1	MEDLINE	22613722	22613722	RING	1	Other	H.sapiens
1491	TRI18_HUMAN	UB2D1_HUMAN	O15344	P51668	MID1	UBE2D1	MEDLINE	21296087	21296087	RING	1	Other	H.sapiens
1492	TRI18_HUMAN	IRF3_HUMAN	O15344	Q14653	MID1	IRF3	MEDLINE	33513265	Ubiquitin E3 Ligase <span class="match term0">MID1</span> Inhibits the Innate Immune Response by Ubiquitinating <span class="match term1">IRF3</span>	RING	1	Other	H.sapiens
1493	TRI18_HUMAN	PP2AB_HUMAN	O15344	P62714	MID1	PPP2CB	MEDLINE	11685209	hUbiquitome	RING	1	Other	H.sapiens
1494	MKRN1_HUMAN	CDN1A_HUMAN	Q9UHC7	P38936	MKRN1	CDKN1A	MEDLINE	19536131	Under severe stress conditions, however, <span class="match term0">MKRN1</span> primarily induced the efficient degradation of <span class="match term1">p21</span>	RING	1	Training data	H.sapiens
1495	MKRN1_HUMAN	P53_HUMAN	Q9UHC7	P04637	MKRN1	TP53	UniProt	MKRN1_HUMAN	Ubiquitinated by <span class="match term0">MKRN1</span> at Lys-291 and Lys-292, which leads to proteasomal degradation	RING	1	Training data	H.sapiens
1496	MKRN1_HUMAN	DPOG1_HUMAN	Q9UHC7	P54098	MKRN1	POLG	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1497	MKRN1_HUMAN	FLIP1_HUMAN	Q9UHC7	Q7Z7B0	MKRN1	FILIP1	UniProt	MKRN1_HUMAN	These substrates include <span class="match term1">FILIP1</span>, p53/TP53, CDKN1A and TERT.	RING	1	Training data	H.sapiens
1498	MKRN1_HUMAN	ARF_HUMAN	Q9UHC7	Q8N726	MKRN1	CDKN2A	MEDLINE	23104211	UbiNet 2.0	RING	1	Training data	H.sapiens
1499	MKRN1_HUMAN	KCNH1_HUMAN	Q9UHC7	O95259	MKRN1	KCNH1	MEDLINE	33647316	<span class="match term0">MKRN1</span> promotes polyubiquitination and ER-associated proteasomal degradation of immature <span class="match term1">Eag1</span> proteins	RING	1	Other	H.sapiens
1500	MKRN1_HUMAN	RS10_HUMAN	Q9UHC7	P46783	MKRN1	RPS10	MEDLINE	31640799	Ubiquitin remnant profiling and in vitro ubiquitylation assays uncover PABPC1 and ribosomal protein <span class="match term1">RPS10</span> as direct ubiquitylation substrates of <span class="match term0">MKRN1</span>	RING	1	Other	H.sapiens
1501	MKRN1_HUMAN	PABP1_HUMAN	Q9UHC7	P11940	MKRN1	PABPC1	MEDLINE	31640799	Ubiquitin remnant profiling and in vitro ubiquitylation assays uncover <span class="match term1">PABPC1</span> and ribosomal protein RPS10 as direct ubiquitylation substrates of <span class="match term0">MKRN1</span>	RING	1	Other	H.sapiens
1502	MKRN1_HUMAN	POLG_WNV	Q9UHC7	P06935	MKRN1	-	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1503	MKRN1_HUMAN	TERT_HUMAN	Q9UHC7	O14746	MKRN1	TERT	MEDLINE	15805468	Furthermore, we have used the yeast two-hybrid method to identify a novel RING finger gene (<span class="match term0">MKRN1</span>) encoding an E3 ligase that mediates ubiquitination of hTERT	RING	1	Training data	H.sapiens
1504	MKRN2_HUMAN	P53_HUMAN	Q9H000	P04637	MKRN2	TP53	MEDLINE	32194692	The ubiquitination of <span class="match term1">P53</span> by <span class="match term0">MKRN2</span> was detected by in vitro ubiquitination assays	SINGLE_OTHER	1	Other	H.sapiens
1505	MKRN2_HUMAN	IF2B3_HUMAN	Q9H000	O00425	MKRN2	IGF2BP3	MEDLINE	32560817	Ubiquitination of <span class="match term1">IGF2BP3</span> by E3 ligase <span class="match term0">MKRN2</span> regulates the proliferation and migration of human neuroblastoma SHSY5Y cells	SINGLE_OTHER	1	Other	H.sapiens
1506	MKRN3_HUMAN	PABP1_HUMAN	Q13064	P11940	MKRN3	PABPC1	MEDLINE	34143182	The tumor suppressor function of <span class="match term0">MKRN3</span> is dependent on its E3 ligase activity, and <span class="match term0">MKRN3</span> missense mutations identified in patients substantially compromise <span class="match term0">MKRN3</span>-mediated <span class="match term1">PABPC1</span> ubiquitination	RING	1	Other	H.sapiens
1507	3MG_HUMAN	HM20B_HUMAN	P29372	Q9P0W2	MPG	HMG20B	MEDLINE	28760657	UbiNet 2.0	Other	1	Other	H.sapiens
1508	3MG_HUMAN	UB2D1_HUMAN	P29372	P51668	MPG	UBE2D1	MEDLINE	21296087	UbiNet 2.0	Other	1	Other	H.sapiens
1509	3MG_HUMAN	PRM2_HUMAN	P29372	P04554	MPG	PRM2	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
1510	3MG_HUMAN	PP2AB_HUMAN	P29372	P62714	MPG	PPP2CB	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
1511	3MG_HUMAN	PP2AA_HUMAN	P29372	P67775	MPG	PPP2CA	MEDLINE	25207814	UbiNet 2.0	Other	1	Other	H.sapiens
1512	3MG_HUMAN	STK36_HUMAN	P29372	Q9NRP7	MPG	STK36	MEDLINE	25278022	UbiNet 2.0	Other	1	Other	H.sapiens
1513	3MG_HUMAN	IGBP1_HUMAN	P29372	P78318	MPG	IGBP1	MEDLINE	22613722	UbiNet 2.0	Other	1	Other	H.sapiens
1514	3MG_HUMAN	PTPA_HUMAN	P29372	Q15257	MPG	PTPA	MEDLINE	25207814	UbiNet 2.0	Other	1	Other	H.sapiens
1515	MSL2_HUMAN	P53_HUMAN	Q9HCI7	P04637	MSL2	TP53	MEDLINE	19033443	Here we describe <span class="match term0">MSL2</span>, a novel E3 ligase for <span class="match term1">p53</span> that promotes ubiquitin-dependent cytoplasmic <span class="match term1">p53</span> localization	RING	1	Training data	H.sapiens
1516	MSL2_HUMAN	H2B1C_HUMAN	Q9HCI7	P62807	MSL2	H2BC4	MEDLINE	16627869	UbiNet 2.0	RING	1	Training data	H.sapiens
1517	MSL2_HUMAN	H2B2E_HUMAN	Q9HCI7	Q16778	MSL2	H2BC21	MEDLINE	21726816	The RING finger protein <span class="match term0">MSL2</span> in the MOF complex is an E3 ubiquitin ligase for <span class="match term1">H2B</span> K34 and is involved in crosstalk with H3 K4 and K79 methylation.	RING	1	Other	H.sapiens
1518	MUL1_HUMAN	AKT1_HUMAN	Q969V5	P31749	MUL1	AKT1	MEDLINE	22410793	<span class="match term1">Akt</span> was found to directly interact with <span class="match term0">MULAN</span> and to be ubiquitinated by <span class="match term0">MULAN</span> in vitro and in vivo	RING	1	Other	H.sapiens
1519	MUL1_HUMAN	MUL1_HUMAN	Q969V5	Q969V5	MUL1	MUL1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1520	MUL1_HUMAN	DNM1L_HUMAN	Q969V5	O00429	MUL1	DNM1L	MEDLINE	19407830	Furthermore, we show that <span class="match term1">DRP1</span> is a substrate for <span class="match term0">MAPL</span>, providing a direct link between <span class="match term0">MAPL</span> and the fission machinery	RING	1	Training data	H.sapiens
1521	MUL1_HUMAN	P73_HUMAN	Q969V5	O15350	MUL1	TP73	MEDLINE	26435500	Ubiquitination-dependent degradation of <span class="match term1">p73</span> by the mitochondrial E3 ubiquitin ligase Hades.	RING	1	Other	H.sapiens
1522	MUL1_HUMAN	BIP_HUMAN	Q969V5	P11021	MUL1	HSPA5	MEDLINE	29260979	<span class="match term1">HSPA5</span> negatively regulates lysosomal activity through ubiquitination of <span class="match term0">MUL1</span> in head and neck cancer	RING	1	Other	H.sapiens
1523	MUL1_HUMAN	ULK1_HUMAN	Q969V5	O75385	MUL1	ULK1	MEDLINE	26018823	Mitochondrial outer-membrane E3 ligase <span class="match term0">MUL1</span> ubiquitinates <span class="match term1">ULK1</span> and regulates selenite-induced mitophagy	RING	1	Other	H.sapiens
1524	MUL1_HUMAN	P53_HUMAN	Q969V5	P04637	MUL1	TP53	MEDLINE	31235254	UbiNet 2.0	RING	1	Training data	H.sapiens
1525	MYCB2_HUMAN	TSC2_HUMAN	O75592	P49815	MYCBP2	TSC2	MEDLINE	14559897	Therefore, we hypothesize that <span class="match term0">Pam</span>, through its interaction with tuberin, could regulate the ubiquitination and proteasomal degradation of the tuberin-hamartin complex particularly in the CNS	RING	1	Training data	H.sapiens
1526	MYCB2_HUMAN	NMNA2_HUMAN	O75592	Q9BZQ4	MYCBP2	NMNAT2	MEDLINE	29997255	29997255	RING	1	Other	H.sapiens
1527	MYLIP_HUMAN	LDLR_HUMAN	Q8WY64	P01130	MYLIP	LDLR	UniProt	MYLIP_HUMAN	Ubiquitinated by <span class="match term0">MYLIP</span> leading to degradation	RING	1	Training data	H.sapiens
1528	MYLIP_HUMAN	MYLIP_HUMAN	Q8WY64	Q8WY64	MYLIP	MYLIP	UniProt	MYLIP_HUMAN	Autoubiquitinated	RING	1	Training data	H.sapiens
1529	MYLIP_HUMAN	LRP8_HUMAN	Q8WY64	Q14114	MYLIP	LRP8	MEDLINE	20427281	UbiNet 2.0	RING	1	Training data	H.sapiens
1530	MYLIP_HUMAN	VLDLR_HUMAN	Q8WY64	P98155	MYLIP	VLDLR	MEDLINE	20427281	UbiNet 2.0	RING	1	Training data	H.sapiens
1531	NAT10_HUMAN	MDM2_HUMAN	Q9H0A0	Q00987	NAT10	MDM2	MEDLINE	26882543	<span class="match term0">NAT10</span> regulates p53 activation through acetylating p53 at K120 and ubiquitinating <span class="match term1">Mdm2</span>	Other	1	Other	H.sapiens
1532	NEDD4_HUMAN	ARRS_HUMAN	P46934	P10523	NEDD4	SAG	MEDLINE	25216516	<span class="match term1">SAG</span>/RBX2 is a novel substrate of <span class="match term0">NEDD4</span>-1 E3 ubiquitin ligase and mediates <span class="match term0">NEDD4</span>-1 induced chemosensitization.	HECT	1	Other	H.sapiens
1533	NEDD4_HUMAN	LYN_HUMAN	P46934	P07948	NEDD4	LYN	MEDLINE	10683340	These findings suggest that LMP2A recruits <span class="match term0">Nedd4</span>-like ubiquitin-protein ligases and B-cell signal transduction molecules, resulting in the degradation of LMP2A and <span class="match term1">Lyn</span> by a ubiquitin-dependent mechanism	HECT	1	Training data	H.sapiens
1534	NEDD4_HUMAN	PPARG_HUMAN	P46934	P37231	NEDD4	PPARG	MEDLINE	23549616	These data indicate that <span class="match term0">NEDD4</span>-1 is the E3 ubiquitin ligase responsible for <span class="match term1">PPARgamma</span> ubiquitination	HECT	1	Other	H.sapiens
1535	NEDD4_HUMAN	LGR4_HUMAN	P46934	Q9BXB1	NEDD4	LGR4	MEDLINE	31867777	UbiNet 2.0	HECT	1	Other	H.sapiens
1536	NEDD4_HUMAN	THOC1_HUMAN	P46934	Q96FV9	NEDD4	THOC1	MEDLINE	23460917	The <span class="match term1">Thoc1</span> encoded ribonucleoprotein is a substrate for the <span class="match term0">NEDD4</span>-1 E3 ubiquitin protein ligase.	HECT	1	Other	H.sapiens
1537	NEDD4_HUMAN	SRC_HUMAN	P46934	P12931	NEDD4	SRC	MEDLINE	12907674	UbiNet 2.0	HECT	1	Training data	H.sapiens
1538	NEDD4_HUMAN	RASN_HUMAN	P46934	P01111	NEDD4	NRAS	MEDLINE	24746824	UbiNet 2.0	HECT	1	Other	H.sapiens
1539	NEDD4_HUMAN	CXA1_HUMAN	P46934	P17302	NEDD4	GJA1	MEDLINE	19835873	Data presented in this manuscript are consistent with a new molecular model in which <span class="match term0">Nedd4</span>-mediated ubiquitination of <span class="match term1">Cx43</span> is required to recruit Eps15, through its ubiquitin-interacting motif, and targets ubiquitinated <span class="match term1">Cx43</span> to the endocytic pathway	HECT	1	Training data	H.sapiens
1540	NEDD4_HUMAN	AKT3_HUMAN	P46934	Q9Y243	NEDD4	AKT3	MEDLINE	23195959	UbiNet 2.0	HECT	1	Training data	H.sapiens
1541	NEDD4_HUMAN	SC6A3_HUMAN	P46934	Q01959	NEDD4	SLC6A3	MEDLINE	20051513	UbiNet 2.0	HECT	1	Other	H.sapiens
1542	NEDD4_HUMAN	PTEN_HUMAN	P46934	P60484	NEDD4	PTEN	MEDLINE	18498243	Crucial role of the C-terminus of <span class="match term1">PTEN</span> in antagonizing <span class="match term0">NEDD4</span>-1-mediated <span class="match term1">PTEN</span> ubiquitination and degradation	HECT	1	Training data	H.sapiens
1543	NEDD4_HUMAN	RNF11_HUMAN	P46934	Q9Y3C5	NEDD4	RNF11	MEDLINE	19953087	UbiNet 2.0	HECT	1	Other	H.sapiens
1544	NEDD4_HUMAN	AKT2_HUMAN	P46934	P31751	NEDD4	AKT2	MEDLINE	23195959	UbiNet 2.0	HECT	1	Training data	H.sapiens
1545	NEDD4_HUMAN	TTYH2_HUMAN	P46934	Q9BSA4	NEDD4	TTYH2	MEDLINE	18577513	The ubiquitin-protein ligase <span class="match term0">Nedd4</span>-2 differentially interacts with and regulates members of the Tweety family of chloride ion channels.	HECT	1	Other	H.sapiens
1546	NEDD4_HUMAN	XIAP_HUMAN	P46934	P98170	NEDD4	XIAP	MEDLINE	31383789	However, Dex decreased the amount of <span class="match term0">NEDD4</span> adhering to <span class="match term1">XIAP</span>, thus protecting <span class="match term1">XIAP</span> protein from <span class="match term0">NEDD4</span>-mediated ubiquitination and degradation	HECT	1	Other	H.sapiens
1547	NEDD4_HUMAN	NTRK1_HUMAN	P46934	P04629	NEDD4	NTRK1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1548	NEDD4_HUMAN	RASH_HUMAN	P46934	P01112	NEDD4	HRAS	MEDLINE	24746824	UbiNet 2.0	HECT	1	Other	H.sapiens
1549	NEDD4_HUMAN	EPS15_HUMAN	P46934	P42566	NEDD4	EPS15	MEDLINE	17013377	Furthermore, we demonstrate that the in vivo ubiquitination of members of the <span class="match term0">Nedd4</span> family of E3 ligases correlates with their ability to monoubiquitinate <span class="match term1">eps15</span>	HECT	1	Training data	H.sapiens
1550	NEDD4_HUMAN	TNR18_HUMAN	P46934	Q9Y5U5	NEDD4	TNFRSF18	MEDLINE	31824170	Discussion: In summary, our findings demonstrated that E3 ligase <span class="match term0">NEDD4</span> mediates ubiquitination and degradation of <span class="match term1">GITR</span> and suppresses T-cell-mediated-killings on melanoma cells	HECT	1	Other	H.sapiens
1551	NEDD4_HUMAN	ADRB2_HUMAN	P46934	P07550	NEDD4	ADRB2	MEDLINE	18544533	Among the various catalytically inactive E3 ubiquitin ligase mutants that we tested, a dominant negative <span class="match term0">Nedd4</span> specifically inhibited isoproterenol-induced ubiquitination and degradation of the beta(2)AR in HEK-293 cells	HECT	1	Training data	H.sapiens
1552	NEDD4_HUMAN	GGA3_HUMAN	P46934	Q9NZ52	NEDD4	GGA3	MEDLINE	17116753	Interestingly, <span class="match term0">Nedd4</span> is also able to ubiquitinate <span class="match term1">GGA3</span>	HECT	1	Training data	H.sapiens
1553	NEDD4_HUMAN	NFIP2_HUMAN	P46934	Q9NV92	NEDD4	NDFIP2	MEDLINE	15252135	Ubiquitination of <span class="match term1">N4WBP5A</span> is enhanced by <span class="match term0">Nedd4</span> and <span class="match term0">Nedd4</span>-2 expression	HECT	1	Training data	H.sapiens
1554	NEDD4_HUMAN	RPGF2_HUMAN	P46934	Q9Y4G8	NEDD4	RAPGEF2	MEDLINE	11598133	<span class="match term1">CNrasGEF</span> is ubiquitinated in cells, and this ubiquitination is augmented upon overexpression of wt-<span class="match term0">Nedd4</span> but is inhibited in cells overexpressing a catalytically inactive <span class="match term0">Nedd4</span> (<span class="match term0">Nedd4</span>(CS)) or in cells expressing CNrasGEFDelta2PY, which cannot bind <span class="match term0">Nedd4</span>	HECT	1	Training data	H.sapiens
1555	NEDD4_HUMAN	Q2F514_HBV	P46934	Q2F514	NEDD4	X	MEDLINE	33767993	Our findings suggest that <span class="match term0">NEDD4</span> exerts a tumor-suppressive effect in HBV-associated HCC by acting as an E3 ubiquitin ligase for HBx degradation and provide new insights into the function of <span class="match term0">NEDD4</span>.	HECT	1	Other	H.sapiens
1556	NEDD4_HUMAN	EAA3_HUMAN	P46934	P43005	NEDD4	SLC1A1	MEDLINE	18539596	At the cellular level, chronic morphine induced the PTEN (phosphatase and tensin homolog deleted on chromosome Ten)-mediated up-regulation of the ubiquitin E3 ligase <span class="match term0">Nedd4</span> via cAMP/protein kinase A signaling, leading to <span class="match term1">EAAC1</span> ubiquitination and proteasomal degradation	HECT	1	Training data	H.sapiens
1557	NEDD4_HUMAN	LAPM5_HUMAN	P46934	Q13571	NEDD4	LAPTM5	MEDLINE	19953087	UbiNet 2.0	HECT	1	Training data	H.sapiens
1558	NEDD4_HUMAN	DCNL1_HUMAN	P46934	Q96GG9	NEDD4	DCUN1D1	MEDLINE	21813641	UbiNet 2.0	HECT	1	Training data	H.sapiens
1559	NEDD4_HUMAN	SYUA_HUMAN	P46934	P37840	NEDD4	SNCA	MEDLINE	21953697	UbiNet 2.0	HECT	1	Training data	H.sapiens
1560	NEDD4_HUMAN	SPY2_HUMAN	P46934	O43597	NEDD4	SPRY2	MEDLINE	19864419	UbiNet 2.0	HECT	1	Training data	H.sapiens
1561	NEDD4_HUMAN	NFIP1_HUMAN	P46934	Q9BT67	NEDD4	NDFIP1	MEDLINE	20962770	<span class="match term0">Nedd4</span> family interacting protein 1 (<span class="match term1">Ndfip1</span>) is an adaptor protein that regulates Itch, an E3 ubiquitin ligase that ubiquitylates JunB, thereby preventing interleukin (IL)-4 and IL-5 production	HECT	1	Training data	H.sapiens
1562	NEDD4_HUMAN	MDM2_HUMAN	P46934	Q00987	NEDD4	MDM2	MEDLINE	24413081	As a result, <span class="match term0">NEDD4</span>-1-mediated ubiquitination stabilizes <span class="match term1">Mdm2</span>	HECT	1	Other	H.sapiens
1563	NEDD4_HUMAN	MTMR4_HUMAN	P46934	Q9NYA4	NEDD4	MTMR4	MEDLINE	19125695	The inositol phosphatase <span class="match term1">MTMR4</span> is a novel target of the ubiquitin ligase <span class="match term0">Nedd4</span>	HECT	1	Training data	H.sapiens
1564	NEDD4_HUMAN	SCNNB_HUMAN	P46934	P51168	NEDD4	SCNN1B	MEDLINE	19953087	UbiNet 2.0	HECT	1	Other	H.sapiens
1565	NEDD4_HUMAN	TMIG2_HUMAN	P46934	Q96BF3	NEDD4	TMIGD2	MEDLINE	33962630	CONCLUSIONS: <span class="match term0">NEDD4</span> ubiquitin E3 ligase binds to and mediates polyubiquitination of <span class="match term1">IGPR-1</span> leading to its lysosomal-dependent degradation	HECT	1	Other	H.sapiens
1566	NEDD4_HUMAN	NEDD4_HUMAN	P46934	P46934	NEDD4	NEDD4	MEDLINE	18772139	Consistent with this, we uncovered that the C2 domain of <span class="match term0">Nedd4</span> is ubiquitinated itself and as such is recruited by the ubiquitin-interacting motif of gamma2-adaptin for subsequent ubiquitin conjugation	HECT	1	Training data	H.sapiens
1567	NEDD4_HUMAN	DTX1_HUMAN	P46934	Q86Y01	NEDD4	DTX1	MEDLINE	15620649	UbiNet 2.0	HECT	1	Training data	H.sapiens
1568	NEDD4_HUMAN	PAX7_HUMAN	P46934	P23759	NEDD4	PAX7	MEDLINE	26304770	UbiNet 2.0	HECT	1	Other	H.sapiens
1569	NEDD4_HUMAN	LAP4A_HUMAN	P46934	Q15012	NEDD4	LAPTM4A	MEDLINE	34297722	RNF152 is a transmembrane E3 ligase that ubiquitinates itself, whereas <span class="match term1">LAPTM4A</span> uses its carboxyl-terminal PY motifs to recruit <span class="match term0">NEDD4</span>-1 for ubiquitination	HECT	1	Other	H.sapiens
1570	NEDD4_HUMAN	VGFR2_HUMAN	P46934	P35968	NEDD4	KDR	MEDLINE	15060076	UbiNet 2.0	HECT	1	Training data	H.sapiens
1571	NEDD4_HUMAN	KLF15_HUMAN	P46934	Q9UIH9	NEDD4	KLF15	MEDLINE	33687156	The <span class="match term1">KLF15</span>-triggered gene expression program, including atrogenes and FoxOs, was regulated via <span class="match term1">KLF15</span> ubiquitination by the E3 ubiquitin ligase <span class="match term0">NEDD4</span>	HECT	1	Other	H.sapiens
1572	NEDD4_HUMAN	LATS1_HUMAN	P46934	O95835	NEDD4	LATS1	MEDLINE	24107629	<span class="match term0">NEDD4</span> E3 ligase inhibits the activity of the Hippo pathway by targeting <span class="match term1">LATS1</span> for degradation.	HECT	1	Other	H.sapiens
1573	NEDD4_HUMAN	MYCN_HUMAN	P46934	P04198	NEDD4	MYCN	MEDLINE	23175188	Importantly, <span class="match term0">NEDD4</span> directly bound to Myc oncoproteins and targeted Myc oncoproteins for ubiquitination and degradation, and small-molecule SIRT2 inhibitors reactivated <span class="match term0">NEDD4</span> gene expression, reduced <span class="match term1">N-Myc</span> and c-Myc protein expression, and suppressed neuroblastoma and pancreatic cancer cell proliferation	HECT	1	Other	H.sapiens
1574	NEDD4_HUMAN	IGF1R_HUMAN	P46934	P08069	NEDD4	IGF1R	MEDLINE	18286479	Grb10 and <span class="match term0">Nedd4</span>, unlike the IGF-IR, which is targeted for lysosomal degradation are not degraded and likely directed into recycling endosomes	HECT	1	Training data	H.sapiens
1575	NEDD4_HUMAN	SQSTM_HUMAN	P46934	Q13501	NEDD4	SQSTM1	MEDLINE	29021346	Taken together, our studies show that <span class="match term0">NEDD4</span> is an autophagic E3 ubiquitin ligase that ubiquitylates <span class="match term1">SQSTM1</span>, facilitating <span class="match term1">SQSTM1</span>-mediated inclusion body autophagy.	HECT	1	Other	H.sapiens
1576	NEDD4_HUMAN	ANDR_HUMAN	P46934	P10275	NEDD4	AR	MEDLINE	18703514	The mutant PMEPA1 (PY1/2 motif mutation) that is impaired in <span class="match term0">NEDD4</span> recruitment shows attenuated <span class="match term1">AR</span> ubiquitination and <span class="match term1">AR</span> protein down-regulation	HECT	1	Training data	H.sapiens
1577	NEDD4_HUMAN	NMDE4_HUMAN	P46934	O15399	NEDD4	GRIN2D	MEDLINE	23639431	UbiNet 2.0	HECT	1	Training data	H.sapiens
1578	NEDD4_HUMAN	TS101_HUMAN	P46934	Q99816	NEDD4	TSG101	MEDLINE	15126635	<span class="match term0">Nedd4</span>.1-mediated ubiquitination and subsequent recruitment of <span class="match term1">Tsg101</span> ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding	HECT	1	Training data	H.sapiens
1579	NEDD4_HUMAN	WBP2_HUMAN	P46934	Q969T9	NEDD4	WBP2	MEDLINE	26371805	UbiNet 2.0	HECT	1	Other	H.sapiens
1580	NEDD4_HUMAN	AP1G2_HUMAN	P46934	O75843	NEDD4	AP1G2	MEDLINE	18772139	Consistent with this, we uncovered that the C2 domain of <span class="match term0">Nedd4</span> is ubiquitinated itself and as such is recruited by the ubiquitin-interacting motif of gamma2-adaptin for subsequent ubiquitin conjugation	HECT	1	Training data	H.sapiens
1581	NEDD4_HUMAN	ACK1_HUMAN	P46934	Q07912	NEDD4	TNK2	MEDLINE	19144635	103, 9796-9801 ), our result suggest that EGF receptor-mediated <span class="match term1">ACK1</span> activation allows <span class="match term0">Nedd4</span>-2 to drive kinase degradation	HECT	1	Training data	H.sapiens
1582	NEDD4_HUMAN	ERBB4_HUMAN	P46934	Q15303	NEDD4	ERBB4	MEDLINE	19193720	<span class="match term0">Nedd4</span> mediates <span class="match term1">ErbB4</span> JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cells	HECT	1	Training data	H.sapiens
1583	NEDD4_HUMAN	SL9A1_HUMAN	P46934	P19634	NEDD4	SLC9A1	MEDLINE	20855896	Fibroblasts derived from beta-arrestin-1 and <span class="match term0">Nedd4</span>-1 knock-out mice show loss of <span class="match term1">NHE1</span> ubiquitylation, increased plasmalemmal <span class="match term1">NHE1</span> levels and greatly enhanced <span class="match term1">NHE1</span> transport compared with wild-type fibroblasts.	HECT	1	Training data	H.sapiens
1584	NEDD4_HUMAN	MAF_HUMAN	P46934	O75444	NEDD4	MAF	MEDLINE	29467225	In conclusion, this study highlights that TMEPAI decreases c-<span class="match term1">Maf</span> stability by recruiting the ubiquitin ligase <span class="match term0">NEDD4</span> to c-<span class="match term1">Maf</span> for proteasomal degradation	HECT	1	Other	H.sapiens
1585	NEDD4_HUMAN	KSYK_HUMAN	P46934	P43405	NEDD4	SYK	MEDLINE	11046148	LMP2A enhances Lyn and <span class="match term1">Syk</span> ubiquitination in vivo in a fashion that depends on the activity of <span class="match term0">Nedd4</span> family members and correlates with destabilization of the Lyn tyrosine kinase	HECT	1	Training data	H.sapiens
1586	NEDD4_HUMAN	BCL10_HUMAN	P46934	O95999	NEDD4	BCL10	MEDLINE	15082780	The HECT domain ubiquitin ligases <span class="match term0">NEDD4</span> and Itch promote ubiquitination and degradation of <span class="match term1">Bcl10</span>, thus downmodulating NF-kappa B activation	HECT	1	Training data	H.sapiens
1587	NEDD4_HUMAN	CDN1A_HUMAN	P46934	P38936	NEDD4	CDKN1A	MEDLINE	31831018	UbiNet 2.0	HECT	1	Other	H.sapiens
1588	NEDD4_HUMAN	SPDYA_HUMAN	P46934	Q5MJ70	NEDD4	SPDYA	MEDLINE	19054764	The cyclin-dependent kinase activator, Spy1A, is targeted for degradation by the ubiquitin ligase <span class="match term0">NEDD4</span>.	HECT	1	Other	H.sapiens
1589	NEDD4_HUMAN	PAR1_HUMAN	P46934	P25116	NEDD4	F2R	MEDLINE	26391660	UbiNet 2.0	HECT	1	Training data	H.sapiens
1590	NEDD4_HUMAN	EGFR_HUMAN	P46934	P00533	NEDD4	EGFR	MEDLINE	20086093	RNA interference (RNAi) knockdown of <span class="match term0">Nedd4</span>-1, not <span class="match term0">Nedd4</span>-2, inhibited degradation of both <span class="match term1">EGFR</span> and ACK, and overexpression of ACK mutants that are deficient in either binding to or ubiquitination by <span class="match term0">Nedd4</span>-1 blocked EGF-induced degradation of <span class="match term1">EGFR</span>	HECT	1	Training data	H.sapiens
1591	NEDD4_HUMAN	COPT1_HUMAN	P46934	O15431	NEDD4	SLC31A1	MEDLINE	34278744	In support of an oncogenic role for <span class="match term1">CTR1</span>, the authors find that <span class="match term1">CTR1</span> is abnormally elevated in breast cancer, and is subjected by <span class="match term0">NEDD4</span> like E3 ubiquitin protein ligase (Nedd4l)-mediated negative regulation through ubiquitination and subsequent degradation	HECT	1	Other	H.sapiens
1592	NEDD4_HUMAN	AMOT_HUMAN	P46934	Q4VCS5	NEDD4	AMOT	MEDLINE	22385262	UbiNet 2.0	HECT	1	Training data	H.sapiens
1593	NEDD4_HUMAN	SCN5A_HUMAN	P46934	Q14524	NEDD4	SCN5A	MEDLINE	15217910	UbiNet 2.0	HECT	1	Other	H.sapiens
1594	NEDD4_HUMAN	RASK_HUMAN	P46934	P01116	NEDD4	KRAS	MEDLINE	24746824	UbiNet 2.0	HECT	1	Other	H.sapiens
1595	NEDD4_HUMAN	XPO1_HUMAN	P46934	O14980	NEDD4	XPO1	MEDLINE	31326389	In addition, <span class="match term0">NEDD4</span> could promote the interaction between <span class="match term1">XPO1</span> and RanBP3 via K63-linked ubiquitination of <span class="match term1">XPO1</span>	HECT	1	Other	H.sapiens
1596	NEDD4_HUMAN	PDC6I_HUMAN	P46934	Q8WUM4	NEDD4	PDCD6IP	MEDLINE	20519395	UbiNet 2.0	HECT	1	Training data	H.sapiens
1597	NEDD4_HUMAN	LGR5_HUMAN	P46934	O75473	NEDD4	LGR5	MEDLINE	31867777	UbiNet 2.0	HECT	1	Other	H.sapiens
1598	NEDD4_HUMAN	ERRFI_HUMAN	P46934	Q9UJM3	NEDD4	ERRFI1	MEDLINE	27557663	UbiNet 2.0	HECT	1	Other	H.sapiens
1599	NEDD4_HUMAN	NOTC1_HUMAN	P46934	P46531	NEDD4	NOTCH1	MEDLINE	15620649	UbiNet 2.0	HECT	1	Training data	H.sapiens
1600	NEDD4_HUMAN	IRS2_HUMAN	P46934	Q9Y4H2	NEDD4	IRS2	MEDLINE	28126338	We concluded that USP15 attenuates IGF-I signaling by antagonizing <span class="match term0">Nedd4</span>-induced <span class="match term1">IRS-2</span> ubiquitination.	HECT	1	Other	H.sapiens
1601	NEDD4_HUMAN	TBK1_HUMAN	P46934	Q9UHD2	NEDD4	TBK1	MEDLINE	34257412	Mechanically <span class="match term0">NEDD4</span> catalyzes the K27-linked poly-ubiquitination of <span class="match term1">TBK1</span> at K344, which serves as a recognition signal for cargo receptor NDP52-mediated selective autophagic degradation	HECT	1	Other	H.sapiens
1602	NEDD4_HUMAN	PI51A_HUMAN	P46934	Q99755	NEDD4	PIP5K1A	MEDLINE	29851245	<span class="match term0">NEDD4</span>-induced degradative ubiquitination of phosphatidylinositol 4-phosphate 5-kinase alpha and its implication in breast cancer cell proliferation.	HECT	1	Other	H.sapiens
1603	NEDD4_HUMAN	FGFR1_HUMAN	P46934	P11362	NEDD4	FGFR1	MEDLINE	21765395	UbiNet 2.0	HECT	1	Training data	H.sapiens
1604	NEDD4_HUMAN	IFM3_HUMAN	P46934	Q01628	NEDD4	IFITM3	MEDLINE	26263374	Here, we demonstrate that the E3 ubiquitin ligase <span class="match term0">NEDD4</span> ubiquitinates <span class="match term1">IFITM3</span> in cells and in vitro	HECT	1	Other	H.sapiens
1605	NEDD4_HUMAN	A8MYT4_HUMAN	P46934	A8MYT4	NEDD4	PIK3C3	MEDLINE	32101753	Here, we report that the E3 ubiquitin ligase <span class="match term0">NEDD4</span>-1 promotes the autophagy flux by targeting <span class="match term1">VPS34</span>	HECT	1	Other	H.sapiens
1606	NEDD4_HUMAN	H31_HUMAN	P46934	P68431	NEDD4	H3C1	MEDLINE	28300060	H3 ubiquitination by <span class="match term0">NEDD4</span> regulates H3 acetylation and tumorigenesis.	HECT	1	Other	H.sapiens
1607	NEDD4_HUMAN	SCNNG_HUMAN	P46934	P51170	NEDD4	SCNN1G	MEDLINE	17013377	UbiNet 2.0	HECT	1	Other	H.sapiens
1608	NEDD4_HUMAN	MDR1_HUMAN	P46934	P08183	NEDD4	ABCB1	MEDLINE	26006083	The treated <span class="match term1">ABCB1</span> had reduced mobility on SDS-PAGE, and mass spectrometry identified eight lysine residues, K271, K272, K575, K685, K877, K885	HECT	1	Other	H.sapiens
1609	NEDD4_HUMAN	ABC3G_HUMAN	P46934	Q9HC16	NEDD4	APOBEC3G	MEDLINE	15581898	<span class="match term1">APOBEC3G</span> ubiquitination by <span class="match term0">Nedd4</span>-1 favors its packaging into HIV-1 particles	HECT	1	Training data	H.sapiens
1610	NEDD4_HUMAN	RBX2_HUMAN	P46934	Q9UBF6	NEDD4	RNF7	MEDLINE	25216516	SAG/<span class="match term1">RBX2</span> is a novel substrate of <span class="match term0">NEDD4</span>-1 E3 ubiquitin ligase and mediates <span class="match term0">NEDD4</span>-1 induced chemosensitization	HECT	1	Other	H.sapiens
1611	NEDD4_HUMAN	BECN1_HUMAN	P46934	Q14457	NEDD4	BECN1	MEDLINE	21936852	We establish <span class="match term0">Nedd4</span> as a novel binding partner of <span class="match term1">Beclin 1</span> and demonstrate that <span class="match term0">Nedd4</span> polyubiquitinates <span class="match term1">Beclin 1</span> with Lys11- and Lys63-linked chains	HECT	1	Other	H.sapiens
1612	NEDD4_HUMAN	ERBB3_HUMAN	P46934	P21860	NEDD4	ERBB3	MEDLINE	24662824	In this study, we identified <span class="match term0">NEDD4</span> (neural precursor cell expressed, developmentally downregulated 4) as a novel interaction partner and ubiquitin E3 ligase of human <span class="match term1">HER3</span>.	HECT	1	Other	H.sapiens
1613	NEDD4_HUMAN	DP13A_HUMAN	P46934	Q9UKG1	NEDD4	APPL1	MEDLINE	21320486	We determined that the ubiquitin ligase <span class="match term0">Nedd4</span> enhances polyubiquitination of <span class="match term1">APPL1</span>, and the ubiquitin molecules attached to <span class="match term1">APPL1</span> are linked through lysine-63	HECT	1	Training data	H.sapiens
1614	NEDD4_HUMAN	BRAT1_HUMAN	P46934	Q6PJG6	NEDD4	BRAT1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1615	NEDD4_HUMAN	GUCD1_HUMAN	P46934	Q96NT3	NEDD4	GUCD1	MEDLINE	24743017	A yeast two-hybrid interaction assay, aimed at identifying any relevant interaction partners of <span class="match term1">GUCD1</span>, revealed direct interactions with <span class="match term0">NEDD4</span>-1 (E3 ubiquitin protein ligase neural precursor cell expressed, developmentally downregulated gene 4), resulting in control of <span class="match term1">GUCD1</span> stability	HECT	1	Other	H.sapiens
1616	NEDD4_HUMAN	PSMD4_HUMAN	P46934	P55036	NEDD4	PSMD4	MEDLINE	19240029	We discovered that, unlike typical substrates of Ub ligases (E3s), <span class="match term1">S5a</span> can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, Siah2, Parkin, APC, and SCF(betaTRCP1)), the U-box E3, CHIP, and HECT domain E3s (E6AP and <span class="match term0">Nedd4</span>) when assayed with UbcH5 or related Ub-conjugating enzymes	HECT	1	Other	H.sapiens
1617	NEDD4_HUMAN	MYC_HUMAN	P46934	P01106	NEDD4	MYC	MEDLINE	23175188	UbiNet 2.0	HECT	1	Training data	H.sapiens
1618	NEDD4_HUMAN	GRIA1_HUMAN	P46934	P42261	NEDD4	GRIA1	MEDLINE	21148011	Finally, we show that ubiquitination of <span class="match term1">GluA1</span> by <span class="match term0">Nedd4</span>-1 becomes more prevalent as neurons mature.	HECT	1	Other	H.sapiens
1619	NEDD4_HUMAN	HGS_HUMAN	P46934	O14964	NEDD4	HGS	MEDLINE	12230472	Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and <span class="match term1">Hgs</span>, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by <span class="match term0">Nedd4</span>.	HECT	1	Other	H.sapiens
1620	NEDD4_HUMAN	RPB1_HUMAN	P46934	P24928	NEDD4	POLR2A	MEDLINE	10490634	A human WW domain-containing hect (WW-hect) E3 protein closely related to Rsp5, <span class="match term0">Rpf1</span>/hNedd4, also binds and ubiquitinates both yeast and human <span class="match term1">Rpb1</span> in vitro, suggesting that <span class="match term0">Rpf1</span> and/or another WW-hect E3 protein mediates UV-induced degradation of the large subunit of polymerase II in human cells	HECT	1	Training data	H.sapiens
1621	NEDD4_HUMAN	DVL2_HUMAN	P46934	O14641	NEDD4	DVL2	MEDLINE	31867777	UbiNet 2.0	HECT	1	Other	H.sapiens
1622	NEDD4_HUMAN	SAV1_HUMAN	P46934	Q9H4B6	NEDD4	SAV1	MEDLINE	25692647	UbiNet 2.0	HECT	1	Other	H.sapiens
1623	NEDD4_HUMAN	PROM1_HUMAN	P46934	O43490	NEDD4	PROM1	MEDLINE	29760280	We observed that <span class="match term1">CD133</span> was monoubiquitinated and demonstrated that the E3 ligase <span class="match term0">Nedd4</span> was required for <span class="match term1">CD133</span> ubiquitination.	HECT	1	Other	H.sapiens
1624	NEDD4_HUMAN	MAR1_HUMAN	P46934	Q16655	NEDD4	MLANA	MEDLINE	15703212	Both <span class="match term0">NEDD4</span> and Itch participate in the degradation of Melan-A	HECT	1	Training data	H.sapiens
1625	NEDD4_HUMAN	ANX13_HUMAN	P46934	P27216	NEDD4	ANXA13	MEDLINE	10871286	UbiNet 2.0	HECT	1	Training data	H.sapiens
1626	NEDD4_HUMAN	AKT1_HUMAN	P46934	P31749	NEDD4	AKT1	MEDLINE	23195959	UbiNet 2.0	HECT	1	Training data	H.sapiens
1627	NEDD4_HUMAN	N4BP1_HUMAN	P46934	O75113	NEDD4	N4BP1	MEDLINE	17114934	This observation, together with the monoubiquitination of <span class="match term0">Nedd4</span>-BP1 by the ubiquitin ligase <span class="match term0">Nedd4</span> suggests that the NYN domain proteins of eukaryotes are regulated by monoubiquitination	HECT	1	Training data	H.sapiens
1628	NEDD4_HUMAN	KI26B_HUMAN	P46934	Q2KJY2	NEDD4	KIF26B	MEDLINE	22768111	UbiNet 2.0	HECT	1	Training data	H.sapiens
1629	NEDD4_HUMAN	TFG_HUMAN	P46934	Q92734	NEDD4	TFG	MEDLINE	33176158	Ubiquitin enrichment coupled proteomics revealed that NAB2 stimulates ubiquitination of trafficking-associated proteins, most likely through modulating the substrate specificity of <span class="match term0">Nedd4</span>, providing a putative protein network involved in the NAB2 mechanism and revealing trafficking scaffold protein <span class="match term1">TFG</span> as a <span class="match term0">Nedd4</span> substrate.	HECT	1	Other	H.sapiens
1630	NED4L_HUMAN	TGFR1_HUMAN	Q96PU5	P36897	NEDD4L	TGFBR1	MEDLINE	15817471	Alternatively, I-Smads elicit degradation of the TGF-beta receptor by recruiting the WW and HECT domain E3 ligases, Smurfs, WWP1, or <span class="match term0">NEDD4-2</span>	HECT	1	Training data	H.sapiens
1631	NED4L_HUMAN	AMOT_HUMAN	Q96PU5	Q4VCS5	NEDD4L	AMOT	MEDLINE	22385262	UbiNet 2.0	HECT	1	Training data	H.sapiens
1632	NED4L_HUMAN	SCNNA_HUMAN	Q96PU5	P37088	NEDD4L	SCNN1A	MEDLINE	18322022	<span class="match term0">Nedd4-2</span> reduces the half-life of ENaC subunits and enhances the ubiquitination of alpha, beta, and gammaENaC subunits when expressed alone or together suggesting that each subunit is a target for <span class="match term0">Nedd4-2</span>-mediated ubiquitination	HECT	1	Training data	H.sapiens
1633	NED4L_HUMAN	SPHK2_HUMAN	Q96PU5	Q9NRA0	NEDD4L	SPHK2	MEDLINE	34305532	Ubiquitination of <span class="match term1">SphK2</span> mediated by <span class="match term0">NEDD4L</span> overexpression suppressed glioma cell viability and invasion but promoted glioma apoptosis	HECT	1	Other	H.sapiens
1634	NED4L_HUMAN	SGK1_HUMAN	Q96PU5	O00141	NEDD4L	SGK1	MEDLINE	18094676	A main mechanism by which <span class="match term1">Sgk1</span> exerts this de-repression is the phosphorylation of the ubiquitin ligase <span class="match term0">Nedd4-2</span> that is thereby prevented from ubiquitylating ENaC	HECT	1	Training data	H.sapiens
1635	NED4L_HUMAN	APBB1_HUMAN	Q96PU5	O00213	NEDD4L	APBB1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1636	NED4L_HUMAN	S38A2_HUMAN	Q96PU5	Q96QD8	NEDD4L	SLC38A2	MEDLINE	17003038	UbiNet 2.0	HECT	1	Training data	H.sapiens
1637	NED4L_HUMAN	SC6A3_HUMAN	Q96PU5	Q01959	NEDD4L	SLC6A3	MEDLINE	20051513	Moreover, a fragment of the <span class="match term0">Nedd4-2</span> molecule containing WW3, WW4, and HECT domains was sufficient for fully potentiating PKC-dependent ubiquitination of <span class="match term1">DAT</span>	HECT	1	Training data	H.sapiens
1638	NED4L_HUMAN	CRCM1_HUMAN	Q96PU5	Q96D31	NEDD4L	ORAI1	MEDLINE	22682960	UbiNet 2.0	HECT	1	Training data	H.sapiens
1639	NED4L_HUMAN	TRAF3_HUMAN	Q96PU5	Q13114	NEDD4L	TRAF3	MEDLINE	33608556	E3 ligase <span class="match term0">Nedd4l</span> promotes antiviral innate immunity by catalyzing K29-linked cysteine ubiquitination of <span class="match term1">TRAF3</span>	HECT	1	Other	H.sapiens
1640	NED4L_HUMAN	NTRK1_HUMAN	Q96PU5	P04629	NEDD4L	NTRK1	MEDLINE	16701206	The binding of <span class="match term0">Nedd4-2</span> to <span class="match term1">TrkA</span> through a PPXY motif leads to the ubiquitination and downregulation of <span class="match term1">TrkA</span>	HECT	1	Training data	H.sapiens
1641	NED4L_HUMAN	SCN3A_HUMAN	Q96PU5	Q9NY46	NEDD4L	SCN3A	UniProt	NED4L_HUMAN	May be ubiquitinated by <span class="match term0">NEDD4L</span>; which would promote its endocytosis	HECT	1	Training data	H.sapiens
1642	NED4L_HUMAN	SCNNB_HUMAN	Q96PU5	P51168	NEDD4L	SCNN1B	MEDLINE	17502380	UbiNet 2.0	HECT	1	Training data	H.sapiens
1643	NED4L_HUMAN	E2AK4_HUMAN	Q96PU5	Q9P2K8	NEDD4L	EIF2AK4	MEDLINE	25589675	UbiNet 2.0	HECT	1	Other	H.sapiens
1644	NED4L_HUMAN	AKT1_HUMAN	Q96PU5	P31749	NEDD4L	AKT1	MEDLINE	32322280	Moreover, <span class="match term0">RSP5</span> mediated K63-linked ubiquitination of <span class="match term1">Akt</span> instead of K48-linked ubiquitination.	HECT	1	Other	H.sapiens
1645	NED4L_HUMAN	NFIP2_HUMAN	Q96PU5	Q9NV92	NEDD4L	NDFIP2	MEDLINE	15252135	Ubiquitination of <span class="match term1">N4WBP5A</span> is enhanced by Nedd4 and <span class="match term0">Nedd4-2</span> expression	HECT	1	Training data	H.sapiens
1646	NED4L_HUMAN	CRTC3_HUMAN	Q96PU5	Q6UUV7	NEDD4L	CRTC3	MEDLINE	29505301	<span class="match term0">NEDD4L</span> limits cAMP signaling through ubiquitination of CREB-regulated transcription coactivator 3.	HECT	1	Other	H.sapiens
1647	NED4L_HUMAN	P53_HUMAN	Q96PU5	P04637	NEDD4L	TP53	MEDLINE	29323264	We demonstrated that <span class="match term1">p53</span> degradation occurred not only via Mdm2, but also via another unexpected E3 ubiquitin ligase, <span class="match term0">Nedd4-2</span>	HECT	1	Other	H.sapiens
1648	NED4L_HUMAN	SCN9A_HUMAN	Q96PU5	Q15858	NEDD4L	SCN9A	UniProt	NED4L_HUMAN	Ubiquitinated by <span class="match term0">NEDD4L</span>; which may promote its endocytosis	HECT	1	Training data	H.sapiens
1649	NED4L_HUMAN	RCAN1_HUMAN	Q96PU5	P53805	NEDD4L	RCAN1	MEDLINE	22426484	UbiNet 2.0	HECT	1	Training data	H.sapiens
1650	NED4L_HUMAN	SMAD3_HUMAN	Q96PU5	P84022	NEDD4L	SMAD3	MEDLINE	19917253	UbiNet 2.0	HECT	1	Training data	H.sapiens
1651	NED4L_HUMAN	SCN8A_HUMAN	Q96PU5	Q9UQD0	NEDD4L	SCN8A	UniProt	NED4L_HUMAN	May be ubiquitinated by <span class="match term0">NEDD4L</span>; which would promote its endocytosis (By similarity)	HECT	1	Training data	H.sapiens
1652	NED4L_HUMAN	PFKAP_HUMAN	Q96PU5	Q01813	NEDD4L	PFKP	MEDLINE	32679544	<span class="match term0">NEDD4L</span> upregulation elicited by KLF3 deficiency in VSMCs increases the ubiquitination and degradation of <span class="match term1">PFKP</span> by <span class="match term0">NEDD4L</span>;	HECT	1	Other	H.sapiens
1653	NED4L_HUMAN	LGR4_HUMAN	Q96PU5	Q9BXB1	NEDD4L	LGR4	MEDLINE	31867777	UbiNet 2.0	HECT	1	Other	H.sapiens
1654	NED4L_HUMAN	TTYH2_HUMAN	Q96PU5	Q9BSA4	NEDD4L	TTYH2	MEDLINE	18577513	We have also shown that <span class="match term0">Nedd4-2</span>-mediated ubiquitination of <span class="match term1">TTYH2</span> is a critical regulator of cell surface and total cellular levels of this protein	HECT	1	Training data	H.sapiens
1655	NED4L_HUMAN	TGFR2_HUMAN	Q96PU5	P37173	NEDD4L	TGFBR2	MEDLINE	15817471	UbiNet 2.0	HECT	1	Training data	H.sapiens
1656	NED4L_HUMAN	TRPV6_HUMAN	Q96PU5	Q9H1D0	NEDD4L	TRPV6	MEDLINE	20843805	UbiNet 2.0	HECT	1	Training data	H.sapiens
1657	NED4L_HUMAN	NTRK2_HUMAN	Q96PU5	Q16620	NEDD4L	NTRK2	MEDLINE	16701206	UbiNet 2.0	HECT	1	Training data	H.sapiens
1658	NED4L_HUMAN	OCLN_HUMAN	Q96PU5	Q16625	NEDD4L	OCLN	MEDLINE	20504882	UbiNet 2.0	HECT	1	Training data	H.sapiens
1659	NED4L_HUMAN	DVL2_HUMAN	Q96PU5	O14641	NEDD4L	DVL2	MEDLINE	31867777	UbiNet 2.0	HECT	1	Training data	H.sapiens
1660	NED4L_HUMAN	SCN5A_HUMAN	Q96PU5	Q14524	NEDD4L	SCN5A	UniProt	NED4L_HUMAN	Ubiquitinated by <span class="match term0">NEDD4L</span>; which promotes its endocytosis	HECT	1	Training data	H.sapiens
1661	NED4L_HUMAN	PSPC1_HUMAN	Q96PU5	Q8WXF1	NEDD4L	PSPC1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1662	NED4L_HUMAN	TS101_HUMAN	Q96PU5	Q99816	NEDD4L	TSG101	MEDLINE	18321968	<span class="match term0">NEDD4L</span> stimulation also required <span class="match term1">TSG101</span> and resulted in ubiquitylation of several ESCRT-I subunits, including <span class="match term1">TSG101</span>	HECT	1	Training data	H.sapiens
1663	NED4L_HUMAN	BEST1_HUMAN	Q96PU5	O76090	NEDD4L	BEST1	MEDLINE	31036321	The E3 ubiquitin ligase, <span class="match term0">NEDD4L</span> (NEDD4-2) regulates bestrophin-1 (<span class="match term1">BEST1</span>) by ubiquitin-dependent proteolysis	HECT	1	Other	H.sapiens
1664	NED4L_HUMAN	NRAM2_HUMAN	Q96PU5	P49281	NEDD4L	SLC11A2	MEDLINE	19706893	We identify <span class="match term0">Nedd4-2</span> as an E3 ligase recruited by Ndfip1 for the ubiquitination of <span class="match term1">DMT1</span> within human neurons	HECT	1	Training data	H.sapiens
1665	NED4L_HUMAN	SMAD2_HUMAN	Q96PU5	Q15796	NEDD4L	SMAD2	MEDLINE	19917253	Through its WW domain, <span class="match term0">Nedd4L</span> specifically recognizes a TGF-beta-induced phosphoThr-ProTyr motif in the linker region, resulting in <span class="match term1">Smad2</span>/3 polyubiquitination and degradation	HECT	1	Training data	H.sapiens
1666	NED4L_HUMAN	BRAT1_HUMAN	Q96PU5	Q6PJG6	NEDD4L	BRAT1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1667	NED4L_HUMAN	P63_HUMAN	Q96PU5	Q9H3D4	NEDD4L	TP63	MEDLINE	16908849	UbiNet 2.0	HECT	1	Training data	H.sapiens
1668	NED4L_HUMAN	SCN2A_HUMAN	Q96PU5	Q99250	NEDD4L	SCN2A	UniProt	NED4L_HUMAN	May be ubiquitinated by <span class="match term0">NEDD4L</span>; which would promote its endocytosis (By similarity)	HECT	1	Training data	H.sapiens
1669	NED4L_HUMAN	CLCN5_HUMAN	Q96PU5	P51795	NEDD4L	CLCN5	UniProt	NED4L_HUMAN	Ubiquitinated by <span class="match term0">NEDD4L</span> in the presence of albumin; which promotes endocytosis and proteasomal degradation	HECT	1	Training data	H.sapiens
1670	NED4L_HUMAN	HGS_HUMAN	Q96PU5	O14964	NEDD4L	HGS	MEDLINE	20675381	UbiNet 2.0	HECT	1	Training data	H.sapiens
1671	NED4L_HUMAN	MRP1_HUMAN	Q96PU5	P33527	NEDD4L	ABCC1	MEDLINE	32140187	Further, TRIM2 and <span class="match term0">NEDD4L</span> were predicted as E3 ligases to regulate ubiquitination of vimentin and <span class="match term1">MRP1</span>, respectively	HECT	1	Other	H.sapiens
1672	NED4L_HUMAN	NED4L_HUMAN	Q96PU5	Q96PU5	NEDD4L	NEDD4L	MEDLINE	18498246	ENaC ubiquitination, in turn, appears to promote <span class="match term0">Nedd4-2</span> self-ubiquitination	HECT	1	Training data	H.sapiens
1673	NED4L_HUMAN	SCNAA_HUMAN	Q96PU5	Q9Y5Y9	NEDD4L	SCN10A	UniProt	NED4L_HUMAN	Ubiquitinated by <span class="match term0">NEDD4L</span>; which promotes its endocytosis (By similarity)	HECT	1	Training data	H.sapiens
1674	NED4L_HUMAN	KCNH2_HUMAN	Q96PU5	Q12809	NEDD4L	KCNH2	MEDLINE	21463633	UbiNet 2.0	HECT	1	Training data	H.sapiens
1675	NED4L_HUMAN	IL6RB_HUMAN	Q96PU5	P40189	NEDD4L	IL6ST	MEDLINE	33769697	Mechanistically, <span class="match term0">NEDD4L</span> directly interacts with <span class="match term1">GP130</span> and mediates its Lys-27-linked ubiquitination and proteasomal degradation	HECT	1	Other	H.sapiens
1676	NED4L_HUMAN	MERL_HUMAN	Q96PU5	P35240	NEDD4L	NF2	MEDLINE	33058421	<span class="match term1">Merlin</span> ubiquitination is mediated by the E3 ubiquitin ligase, <span class="match term0">NEDD4L</span>, which requires a scaffold protein, AMOTL1, to approach <span class="match term1">Merlin</span>.	HECT	1	Other	H.sapiens
1677	NED4L_HUMAN	SCNNG_HUMAN	Q96PU5	P51170	NEDD4L	SCNN1G	MEDLINE	14556380	Both beta- and gamma-<span class="match term1">ENaC</span> participate in negative regulation by interacting with <span class="match term0">Nedd4-2</span>, an E3 ubiquitin-ligase	HECT	1	Training data	H.sapiens
1678	NED4L_HUMAN	ACK1_HUMAN	Q96PU5	Q07912	NEDD4L	TNK2	MEDLINE	19144635	103, 9796-9801 ), our result suggest that EGF receptor-mediated <span class="match term1">ACK1</span> activation allows <span class="match term0">Nedd4-2</span> to drive kinase degradation	HECT	1	Training data	H.sapiens
1679	NED4L_HUMAN	LGR5_HUMAN	Q96PU5	O75473	NEDD4L	LGR5	MEDLINE	31867777	UbiNet 2.0	HECT	1	Other	H.sapiens
1680	NED4L_HUMAN	STK35_HUMAN	Q96PU5	Q8TDR2	NEDD4L	STK35	MEDLINE	33117809	<span class="match term1">STK35</span> Is Ubiquitinated by <span class="match term0">NEDD4L</span> and Promotes Glycolysis and Inhibits Apoptosis Through Regulating the AKT Signaling Pathway, Influencing Chemoresistance of Colorectal Cancer	HECT	1	Other	H.sapiens
1681	NED4L_HUMAN	RHOB_HUMAN	Q96PU5	P62745	NEDD4L	RHOB	MEDLINE	26949039	UbiNet 2.0	HECT	1	Other	H.sapiens
1682	NED4L_HUMAN	OGG1_HUMAN	Q96PU5	O15527	NEDD4L	OGG1	MEDLINE	33282879	The E3 Ubiquitin Ligase <span class="match term0">NEDD4L</span> Targets <span class="match term1">OGG1</span> for Ubiquitylation and Modulates the Cellular DNA Damage Response	HECT	1	Other	H.sapiens
1683	NED4L_HUMAN	S22A8_HUMAN	Q96PU5	Q8TCC7	NEDD4L	SLC22A8	MEDLINE	29487013	In the current study, we showed that treatment of <span class="match term1">hOAT3</span>-expressing cells with AG490 resulted in an enhanced <span class="match term1">hOAT3</span> ubiquitination and degradation, which was accompanied by a strengthened association of <span class="match term0">Nedd4-2</span> with <span class="match term1">hOAT3</span> and a reduction in <span class="match term0">Nedd4-2</span> phosphorylation	HECT	1	Other	H.sapiens
1684	NED4L_HUMAN	KCNA3_HUMAN	Q96PU5	P22001	NEDD4L	KCNA3	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1685	NED4L_HUMAN	EAA1_HUMAN	Q96PU5	P43003	NEDD4L	SLC1A3	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
1686	NED4L_HUMAN	PSPC_HUMAN	Q96PU5	P11686	NEDD4L	SFTPC	MEDLINE	19423771	hUbiquitome	HECT	1	Other	H.sapiens
1687	NEUL1_HUMAN	PDE9A_HUMAN	O76050	O76083	NEURL1	PDE9A	MEDLINE	31068605	Using a yeast two-hybrid screen, we have identified a cGMP-hydrolysing phosphodiesterase, <span class="match term1">PDE9A</span>, as a novel interactor and substrate of Neuralized E3 ubiquitin protein ligase 1 (<span class="match term0">NEURL1</span>)	RING	1	Other	H.sapiens
1688	NEU1B_HUMAN	DLL3_HUMAN	A8MQ27	Q9NYJ7	NEURL1B	DLL3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1689	NEU1B_HUMAN	DLL1_HUMAN	A8MQ27	O00548	NEURL1B	DLL1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1690	NEU1B_HUMAN	EDAR_HUMAN	A8MQ27	Q9UNE0	NEURL1B	EDAR	MEDLINE	20176925	UbiNet 2.0	RING	1	Training data	H.sapiens
1691	NEU1B_HUMAN	DLL4_HUMAN	A8MQ27	Q9NR61	NEURL1B	DLL4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1692	NEUL2_HUMAN	CTNB1_HUMAN	Q9BR09	P35222	NEURL2	CTNNB1	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	H.sapiens
1693	NHLC1_HUMAN	PPR3C_HUMAN	Q6VVB1	Q9UQK1	NHLRC1	PPP1R3C	MEDLINE	18029386	Here, we show that the laforin-<span class="match term0">malin</span> complex downregulates <span class="match term1">PTG</span>-induced glycogen synthesis in FTO2B hepatoma cells through a mechanism involving ubiquitination and degradation of <span class="match term1">PTG</span>	RING	1	Training data	H.sapiens
1694	NHLC1_HUMAN	EPM2A_HUMAN	Q6VVB1	O95278	NHLRC1	EPM2A	UniProt	NHLC1_HUMAN	Ubiquitinated by <span class="match term0">NHLRC1</span>/malin in a <span class="match term1">EPM2A</span>/laforin-dependent manner (By similarity)	RING	1	Training data	H.sapiens
1695	NHLC1_HUMAN	GDE_HUMAN	Q6VVB1	P35573	NHLRC1	AGL	UniProt	NHLC1_HUMAN	Polyubiquitinates <span class="match term0">EPM2A</span>/laforin and ubiquitinates <span class="match term1">AGL</span> and targets them for proteasome-dependent degradation	RING	1	Training data	H.sapiens
1696	NHLC1_HUMAN	EP2A2_HUMAN	Q6VVB1	B3EWF7	NHLRC1	EPM2A	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1697	NHLC1_HUMAN	DVL2_HUMAN	Q6VVB1	O14641	NHLRC1	DVL2	MEDLINE	22223637	UbiNet 2.0	RING	1	Other	H.sapiens
1698	NOSIP_HUMAN	PP2AA_HUMAN	Q9Y314	P67775	NOSIP	PPP2CA	MEDLINE	25546391	UbiNet 2.0	UBOX	1	Other	H.sapiens
1699	NOSIP_HUMAN	EPOR_HUMAN	Q9Y314	P19235	NOSIP	EPOR	MEDLINE	12746455	This receptor-associated ubiquitin ligase, RUL, co-precipitated with <span class="match term1">EpoR</span> from mammalian cells and mediated ubiquitination of <span class="match term1">EpoR</span>	UBOX	1	Training data	H.sapiens
1700	OSTM1_HUMAN	GNAI3_HUMAN	Q86WC4	P08754	OSTM1	GNAI3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1701	PRKN2_HUMAN	SEPT5_HUMAN	O60260	Q99719	PARK2	PRKN	UniProt	PRKN2_HUMAN	As wild-type <span class="match term0">PARK2</span>, but not familial-linked <span class="match term0">PARK2</span> mutants, ubiquinates mouse SEPT5 and promotes its degradation, it has been sugested that a deficiency in SEPT5 degradation may contribute to the development of early onset Parkinson disease 2 (<span class="match term0">PARK2</span>)	RING	1	Training data	H.sapiens
1702	PRKN2_HUMAN	SYUA_HUMAN	O60260	P37840	PARK2	SNCA	MEDLINE	17883392	Similar to recently conducted studies on alpha-synuclein processing, both macroautophagy and the proteasome participate in parkin degradation, with the proteasome playing the predominant role for normal parkin turnover and macroautophagy being more important in the degradation of aggregated parkin	RING	1	Training data	H.sapiens
1703	PRKN2_HUMAN	CCNE1_HUMAN	O60260	P24864	PARK2	CCNE1	MEDLINE	19946270	<span class="match term0">PARK2</span> mutations in cancer decrease <span class="match term0">PARK2</span>'s E3 ligase activity, compromising its ability to ubiquitinate cyclin E and resulting in mitotic instability	RING	1	Training data	H.sapiens
1704	PRKN2_HUMAN	GPR37_HUMAN	O60260	O15354	PARK2	GPR37	MEDLINE	19218498	The orphan G-protein-coupled receptor 37 (<span class="match term1">GPR37</span>) is a substrate of parkin, and its insoluble aggregates accumulate in brain tissue samples of Parkinson's disease patients, including Lewy bodies and neurites	RING	1	Training data	H.sapiens
1705	PRKN2_HUMAN	SNCAP_HUMAN	O60260	Q9Y6H5	PARK2	SNCAIP	UniProt	PRKN2_HUMAN	Familial mutations in <span class="match term0">PARK2</span> disrupt the ubiquitination of <span class="match term1">SNCAIP</span> and the formation of the ubiquitin-positive inclusions	RING	1	Training data	H.sapiens
1706	PRKN2_HUMAN	PRKN2_HUMAN	O60260	O60260	PARK2	PARK2	UniProt	PRKN2_HUMAN	Inhibits both auto-ubiquitination of <span class="match term0">PARK2</span> and ubiquitination of target proteins by <span class="match term0">PARK2</span> (By similarity)	RING	1	Training data	H.sapiens
1707	PRKN2_HUMAN	AIMP2_HUMAN	O60260	Q13155	PARK2	AIMP2	UniProt	PRKN2_HUMAN	Ubiquitinated by <span class="match term0">PARK2</span>, leading to its degradation by the proteasome	RING	1	Training data	H.sapiens
1708	PRKN2_HUMAN	PARK7_HUMAN	O60260	Q99497	PARK2	PARK7	MEDLINE	20634198	TRAF6 promotes atypical ubiquitination of mutant <span class="match term1">DJ-1</span> and alpha-synuclein and is localized to Lewy bodies in sporadic Parkinson's disease brains	RING	1	Training data	H.sapiens
1709	PRKN2_HUMAN	H2B1J_HUMAN	O60260	O95147	PARK2	NEK2	MEDLINE	26387737	26387737	RING	1	Other	H.sapiens
1710	PRKN2_HUMAN	2AAA_HUMAN	O60260	P46527	PARK2	HSD17B10	MEDLINE	25591737	25591737	RING	1	Other	H.sapiens
1711	PRKN2_HUMAN	RAD51_HUMAN	O60260	Q99714	PARK2	PTPN5	MEDLINE	25583483	25583483	RING	1	Other	H.sapiens
1712	PRKN2_HUMAN	PINK1_HUMAN	O60260	Q9BXM7	PARK2	PINK1	MEDLINE	22724072	22724072	RING	1	Other	H.sapiens
1713	PRKN2_HUMAN	MFN1_HUMAN	O60260	Q8IWA4	PARK2	MFN1	MEDLINE	21615408	21615408	RING	1	Other	H.sapiens
1714	PRKN2_HUMAN	ZN746_HUMAN	O60260	Q6NUN9	PARK2	ZNF746	MEDLINE	21376232	21376232	RING	1	Other	H.sapiens
1715	PRKN2_HUMAN	RBP2_HUMAN	O60260	P49792	PARK2	RANBP2	MEDLINE	16332688	Furthermore, Parkin controls the intracellular levels of sumoylated HDAC4, as a result of the ubiquitination and degradation of <span class="match term1">RanBP2</span>	RING	1	Training data	H.sapiens
1716	PRKN2_HUMAN	DNM1L_HUMAN	O60260	O00429	PARK2	DNM1L	MEDLINE	21292769	21292769	RING	1	Other	H.sapiens
1717	PRKN2_HUMAN	NEMO_HUMAN	O60260	Q9Y6K9	PARK2	IKBKG	MEDLINE	19880420	19880420	RING	1	Other	H.sapiens
1718	PRKN2_HUMAN	PSMD4_HUMAN	O60260	P55036	PARK2	PSMD4	MEDLINE	19240029	19240029	RING	1	Other	H.sapiens
1719	PRKN2_HUMAN	PICK1_HUMAN	O60260	Q9NRD5	PARK2	PICK1	MEDLINE	17553932	17553932	RING	1	Other	H.sapiens
1720	PRKN2_HUMAN	LIMK1_HUMAN	O60260	P53667	PARK2	LIMK1	MEDLINE	17512523	Furthermore, in the cells co-transfected with parkin and p38, <span class="match term1">LIMK1</span> significantly decreased p38-ubiquitination by parkin	RING	1	Training data	H.sapiens
1721	PRKN2_HUMAN	SIM2_HUMAN	O60260	Q14190	PARK2	SIM2	MEDLINE	17360614	In Parkin, the IBR domain has been shown to augment binding of the E2 proteins UbcH7 and UbcH8, and the subsequent ubiquitination of the proteins synphilin-1, Sept5, and <span class="match term1">SIM2</span>	RING	1	Training data	H.sapiens
1722	PRKN2_HUMAN	EPS15_HUMAN	O60260	P42566	PARK2	EPS15	MEDLINE	16862145	16862145	RING	1	Other	H.sapiens
1723	PRKN2_HUMAN	TBB5_HUMAN	O60260	P07437	PARK2	TUBB	MEDLINE	12716939	The binding between parkin and tubulin apparently led to increased ubiquitination and accelerated degradation of alpha- and beta-tubulins in HEK293 cells	RING	1	Training data	H.sapiens
1724	PARP1_HUMAN	SIAH1_HUMAN	P09874	Q8IUQ4	PARP1	SIAH1	MEDLINE	29949759	At the protein level, <span class="match term0">PARP1</span> promotes <span class="match term1">Siah1</span> proteolysis, likely through inducing PARylation-dependent ubiquitination (PARdU) of <span class="match term1">Siah1</span>	Other	1	Other	H.sapiens
1725	PAXI1_HUMAN	PCNA_HUMAN	Q6ZW49	P12004	PAXIP1	PCNA	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
1726	PCGF1_HUMAN	H2A1_HUMAN	Q9BSM1	P0C0S8	PCGF1	H2AC11	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1727	PDLI2_HUMAN	TF65_HUMAN	Q96JY6	Q04206	PDLIM2	RELA	MEDLINE	19052146	<span class="match term0">PDLIM2</span> (Mystique/SLIM) is a postsynaptic density-95/discs large/zonula occludens-1-Lin-11, Isl-1, Mec-3 (PDZ-LIM) domain protein expressed in the nucleus of T lymphocytes, where it promotes degradation of the <span class="match term1">p65</span> subunit of NF-kappaB	SINGLE_OTHER	1	Training data	H.sapiens
1728	PDLI2_HUMAN	STAT1_HUMAN	Q96JY6	P42224	PDLIM2	STAT1	MEDLINE	20889505	UbiNet 2.0	SINGLE_OTHER	1	Training data	H.sapiens
1729	PZRN3_HUMAN	MUSK_HUMAN	Q9UPQ7	O15146	PDZRN3	MUSK	UniProt	PZRN3_HUMAN	Ubiquitinated by <span class="match term0">PDZRN3</span>	RING	1	Training data	H.sapiens
1730	PELI1_HUMAN	RBP1_HUMAN	Q96FA3	Q15311	PELI1	RALBP1	MEDLINE	19734906	Notably, <span class="match term0">Peli1</span> bound to and ubiquitinated <span class="match term1">RIP1</span>, a signaling molecule that mediates IKK activation induced by the TLR3 and TLR4 adaptor TRIF	RING	1	Training data	H.sapiens
1731	PELI1_HUMAN	IRAK1_HUMAN	Q96FA3	P51617	PELI1	IRAK1	MEDLINE	16884718	In support of this hypothesis we show that Pellino proteins induce <span class="match term1">IRAK</span>-1 polyubiquitination in a RING-dependent manner	RING	1	Training data	H.sapiens
1732	PELI1_HUMAN	M3K14_HUMAN	Q96FA3	Q99558	PELI1	MAP3K14	MEDLINE	29555915	Mechanically, <span class="match term0">Peli1</span> functions as an E3 ligase to associate with NF-kappaB inducing kinase (<span class="match term1">NIK</span>) and mediates <span class="match term1">NIK</span> Lys48 ubiquitination and degradation	RING	1	Other	H.sapiens
1733	PELI1_HUMAN	RIPK3_HUMAN	Q96FA3	Q9Y572	PELI1	RIPK3	MEDLINE	30269743	However, while screening for <span class="match term1">RIP3</span>-binding proteins, we discovered that pellino E3 ubiquitin protein ligase 1 (<span class="match term0">PELI1</span>) also interacts directly with <span class="match term1">RIP3</span> protein; further investigation in this study revealed that <span class="match term0">PELI1</span> also targets <span class="match term1">RIP3</span> for proteasome-dependent degradation	RING	1	Other	H.sapiens
1734	PELI1_HUMAN	MDM4_HUMAN	Q96FA3	O15151	PELI1	MDM4	MEDLINE	29523541	<span class="match term0">Peli1</span> bound <span class="match term1">Mdmx</span> in vitro and in vivo and promoted high levels of ubiquitination of <span class="match term1">Mdmx</span>	RING	1	Other	H.sapiens
1735	PELI1_HUMAN	TRAF3_HUMAN	Q96FA3	Q13114	PELI1	TRAF3	MEDLINE	23603814	UbiNet 2.0	RING	1	Training data	H.sapiens
1736	PELI1_HUMAN	RIPK1_HUMAN	Q96FA3	Q13546	PELI1	RIPK1	MEDLINE	19734906	UbiNet 2.0	RING	1	Training data	H.sapiens
1737	PELI1_HUMAN	BCL6_HUMAN	Q96FA3	P41182	PELI1	BCL6	MEDLINE	25295537	<span class="match term0">PELI1</span> directly interacted with the oncoprotein B cell chronic lymphocytic leukemia (<span class="match term1">BCL6</span>) and induced lysine 63-mediated <span class="match term1">BCL6</span> polyubiquitination	RING	1	Other	H.sapiens
1738	PELI3_HUMAN	IRAK1_HUMAN	Q8N2H9	P51617	PELI3	IRAK1	MEDLINE	12874243	UbiNet 2.0	RING	1	Training data	H.sapiens
1739	PELI3_HUMAN	RIPK2_HUMAN	Q8N2H9	O43353	PELI3	RIPK2	MEDLINE	23892723	Pellino3 ubiquitinates <span class="match term1">RIP2</span> and mediates Nod2-induced signaling and protective effects in colitis.	RING	1	Other	H.sapiens
1740	PELI3_HUMAN	TRAF6_HUMAN	Q8N2H9	Q9Y4K3	PELI3	TRAF6	MEDLINE	23042151	UbiNet 2.0	RING	1	Other	H.sapiens
1741	PEX10_HUMAN	PEX5_HUMAN	O60683	P50542	PEX10	PEX5	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1742	PEX12_HUMAN	PEX5_HUMAN	O00623	P50542	PEX12	PEX5	MEDLINE	19687296	UbiNet 2.0	RING	1	Training data	H.sapiens
1743	PIAS2_HUMAN	STAT1_HUMAN	O75928	P42224	PIAS2	STAT1	MEDLINE	12764129	We demonstrate that <span class="match term1">STAT1</span> is a substrate for SUMO modification and that <span class="match term0">PIASx</span>-alpha, but not PIAS1, functions as an E3 ligase to promote <span class="match term1">STAT1</span> modification	RING	1	Training data	H.sapiens
1744	PIAS4_HUMAN	TYY1_HUMAN	Q8N2W9	P25490	PIAS4	YY1	MEDLINE	17353273	We also discovered that <span class="match term0">PIASy</span>, a SUMO E3 ligase, is a novel <span class="match term1">YY1</span>-interacting protein and can stimulate the sumoylation of <span class="match term1">YY1</span> both in vitro and in vivo	RING	1	Training data	H.sapiens
1745	PIAS4_HUMAN	ETS1_HUMAN	Q8N2W9	P14921	PIAS4	ETS1	MEDLINE	17456046	Deletion analysis showed that the TAD (transcriptional activation domain), which has been identified as the interaction domain with <span class="match term0">PIASy</span>, was also required for <span class="match term1">Ets-1</span> ubiquitination and proteasomal degradation	RING	1	Training data	H.sapiens
1746	PINK1_HUMAN	VDAC1_HUMAN	Q9BXM7	P21796	PINK1	VDAC1	MEDLINE	32047033	Here, we demonstrate that <span class="match term1">VDAC1</span> can be either mono- or polyubiquitinated by Parkin in a <span class="match term0">PINK1</span>-dependent manner	Other	1	Other	H.sapiens
1747	PJA1_HUMAN	SUZ12_HUMAN	Q8NG27	Q15022	PJA1	SUZ12	MEDLINE	21513699	UbiNet 2.0	RING	1	Training data	H.sapiens
1748	PJA1_HUMAN	FOXR2_HUMAN	Q8NG27	Q6PJQ5	PJA1	FOXR2	MEDLINE	33839405	This current study found that E3 ligase <span class="match term0">PJA1</span> regulates ubiquitin-mediated degradation of <span class="match term1">FOXR2</span> and predicts good outcome of patients with LAC	RING	1	Other	H.sapiens
1749	PJA1_HUMAN	ELF1_HUMAN	Q8NG27	P32519	PJA1	ELF1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1750	PJA1_HUMAN	EZH2_HUMAN	Q8NG27	Q15910	PJA1	EZH2	MEDLINE	21513699	<span class="match term0">PRAJA1</span> is a ubiquitin ligase for the polycomb repressive complex 2 proteins.	RING	1	Other	H.sapiens
1751	PJA1_HUMAN	MAGD1_HUMAN	Q8NG27	Q9Y5V3	PJA1	MAGED1	UniProt	PJA1_HUMAN	Ubiquitinates <span class="match term1">MAGED1</span> antigen leading to its subsequent degradation by proteosome (By similarity)	RING	1	Training data	H.sapiens
1752	PJA1_HUMAN	TADBP_HUMAN	Q8NG27	Q13148	PJA1	TARDBP	MEDLINE	32686212	These results indicate that <span class="match term0">PJA1</span> is one of the principal E3 ubiquitin ligases for <span class="match term1">TDP-43</span> to counteract its aggregation propensity and could be a potential therapeutic target for ALS and FTLD.	RING	1	Other	H.sapiens
1753	PJA1_HUMAN	SMAD3_HUMAN	Q8NG27	P84022	PJA1	SMAD3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1754	PJA2_HUMAN	KAP1_HUMAN	O43164	P31321	PJA2	PRKAR1B	MEDLINE	21423175	UbiNet 2.0	RING	1	Training data	H.sapiens
1755	PJA2_HUMAN	KAP2_HUMAN	O43164	P13861	PJA2	PRKAR2A	MEDLINE	21423175	UbiNet 2.0	RING	1	Training data	H.sapiens
1756	PJA2_HUMAN	KAP0_HUMAN	O43164	P10644	PJA2	PRKAR1A	MEDLINE	21423175	UbiNet 2.0	RING	1	Training data	H.sapiens
1757	PJA2_HUMAN	KAP3_HUMAN	O43164	P31323	PJA2	PRKAR2B	MEDLINE	21423175	UbiNet 2.0	RING	1	Training data	H.sapiens
1758	PJA2_HUMAN	KSR1_HUMAN	O43164	Q8IVT5	PJA2	KSR1	MEDLINE	34372882	<span class="match term0">PJA2</span> reduced <span class="match term1">KSR1</span> by ubiquitination	RING	1	Other	H.sapiens
1759	PJA2_HUMAN	PJA2_HUMAN	O43164	O43164	PJA2	PJA2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1760	PJA2_HUMAN	MFHA1_HUMAN	O43164	Q9Y4C4	PJA2	MFHAS1	MEDLINE	30013073	Correction: Ubiquitylation of <span class="match term1">MFHAS1</span> by the ubiquitin ligase <span class="match term0">praja2</span> promotes M1 macrophage polarization by activating JNK and p38 pathways	RING	1	Other	H.sapiens
1761	PML_HUMAN	H31_HUMAN	P29590	P68431	PML	H3C12	MEDLINE	29471350	29471350	RING	1	Other	H.sapiens
1762	PPARA_HUMAN	BCL2_HUMAN	Q07869	P10415	PPARA	BCL2	MEDLINE	26556865	In this process, <span class="match term0">PPARalpha</span>/C102 was critical for <span class="match term0">PPARalpha</span> binding to BH3 domain of <span class="match term1">Bcl2</span>, subsequently, <span class="match term0">PPARalpha</span> transferred K48-linked polyubiquitin to lysine-22 site of <span class="match term1">Bcl2</span> resulting in its ubiquitination and proteasome-dependent degradation	RING	1	Other	H.sapiens
1763	PPARG_HUMAN	MUC1_HUMAN	P37231	P15941	PPARG	MUC1	MEDLINE	24292674	<span class="match term0">PPARgamma</span> E3 ubiquitin ligase regulates <span class="match term1">MUC1</span>-C oncoprotein stability	RING	1	Other	H.sapiens
1764	PPARG_HUMAN	SELS_HUMAN	P37231	Q9BQE4	PPARG	SELENOS	MEDLINE	30082770	Here, we report that <span class="match term0">PPARgamma</span> directly interacts with both <span class="match term1">SelS</span> and SelK via its ligand-binding domain to induce ubiquitination and degradation of the selenoproteins	RING	1	Other	H.sapiens
1765	PPARG_HUMAN	SELK_HUMAN	P37231	Q9Y6D0	PPARG	SELENOK	MEDLINE	30082770	Here, we report that <span class="match term0">PPARgamma</span> directly interacts with both SelS and <span class="match term1">SelK</span> via its ligand-binding domain to induce ubiquitination and degradation of the selenoproteins	RING	1	Other	H.sapiens
1766	PPARG_HUMAN	TF65_HUMAN	P37231	Q04206	PPARG	RELA	MEDLINE	23250430	The ligand-binding domain of <span class="match term0">PPARgamma</span> interacts with the Rel Homology Domain region of NFkappaB/<span class="match term1">p65</span> to undergo robust ubiquitination and degradation that was independent of <span class="match term0">PPARgamma</span> transcriptional activity	RING	1	Other	H.sapiens
1767	PPIL2_HUMAN	SNAI1_HUMAN	Q13356	O95863	PPIL2	SNAI1	MEDLINE	29352246	U-box ubiquitin ligase <span class="match term0">PPIL2</span> suppresses breast cancer invasion and metastasis by altering cell morphology and promoting <span class="match term1">SNAI1</span> ubiquitination and degradation	UBOX	1	Other	H.sapiens
1768	PRC1_HUMAN	H2A1A_HUMAN	O43663	Q96QV6	PRC1	H2AC1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1769	PRC1_HUMAN	H2A1H_HUMAN	O43663	Q96KK5	PRC1	H2AC12	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1770	PRC1_HUMAN	H2AX_HUMAN	O43663	P16104	PRC1	H2AX	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1771	PRC1_HUMAN	RING2_HUMAN	O43663	Q99496	PRC1	RNF2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1772	PRC1_HUMAN	H2AZ_HUMAN	O43663	P0C0S5	PRC1	H2AZ1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1773	PRC1_HUMAN	H2A1B_HUMAN	O43663	P04908	PRC1	H2AC4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1774	PRC1_HUMAN	H2A2A_HUMAN	O43663	Q6FI13	PRC1	H2AC18	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1775	PRKN_HUMAN	-	O60260	-	PRKN	cyclin-D	MEDLINE	32296023	UbiNet 2.0	RBR	1	Other	H.sapiens
1776	PRKN_HUMAN	SEPT4_HUMAN	O60260	O43236	PRKN	SEPTIN4	MEDLINE	22792159	UbiNet 2.0	RBR	1	Training data	H.sapiens
1777	PRKN_HUMAN	UBP30_HUMAN	O60260	Q70CQ3	PRKN	USP30	MEDLINE	22199232	E3Net	RBR	1	Other	H.sapiens
1778	PRKN_HUMAN	ATX3_HUMAN	O60260	P54252	PRKN	ATXN3	MEDLINE	22199232	E3Net	RBR	1	Other	H.sapiens
1779	PRKN_HUMAN	CCNE2_HUMAN	O60260	O96020	PRKN	CCNE2	MEDLINE	12628165	UbiNet 2.0	RBR	1	Training data	H.sapiens
1780	PRKN_HUMAN	FAF1_HUMAN	O60260	Q9UNN5	PRKN	FAF1	MEDLINE	23307929	UbiNet 2.0	RBR	1	Training data	H.sapiens
1781	PRKN_HUMAN	SQSTM_HUMAN	O60260	Q13501	PRKN	SQSTM1	MEDLINE	26746706	UbiNet 2.0	RBR	1	Other	H.sapiens
1782	PRKN_HUMAN	BCL2_HUMAN	O60260	P10415	PRKN	BCL2	MEDLINE	20889974	UbiNet 2.0	RBR	1	Training data	H.sapiens
1783	PRKN_HUMAN	VPS35_HUMAN	O60260	Q96QK1	PRKN	VPS35	MEDLINE	29893854	<span class="match term0">Parkin</span> mediates the ubiquitination of <span class="match term1">VPS35</span> and modulates retromer-dependent endosomal sorting.	RBR	1	Other	H.sapiens
1784	PRKN_HUMAN	UCHL1_HUMAN	O60260	P09936	PRKN	UCHL1	MEDLINE	25403879	<span class="match term0">Parkin</span>-mediated K63-polyubiquitination targets <span class="match term1">ubiquitin C-terminal hydrolase L1</span> for degradation by the autophagy-lysosome system.	RBR	1	Other	H.sapiens
1785	PRKN_HUMAN	G37L1_HUMAN	O60260	O60883	PRKN	GPR37L1	MEDLINE	18241051	UbiNet 2.0	RBR	1	Training data	H.sapiens
1786	PRKN_HUMAN	HIF1A_HUMAN	O60260	Q16665	PRKN	HIF1A	MEDLINE	29180628	29180628	RBR	1	Other	H.sapiens
1787	PRKN_HUMAN	MIRO1_HUMAN	O60260	Q8IXI2	PRKN	RHOT1	MEDLINE	26254304	UbiNet 2.0	RBR	1	Other	H.sapiens
1788	PRKN_HUMAN	TBA1B_HUMAN	O60260	P68363	PRKN	TUBA1B	MEDLINE	18195004	UbiNet 2.0	RBR	1	Training data	H.sapiens
1789	PRKN_HUMAN	PTN5_HUMAN	O60260	P54829	PRKN	PTPN5	MEDLINE	25583483	<span class="match term1">STEP61</span> is a substrate of the E3 ligase <span class="match term0">parkin</span> and is upregulated in Parkinson's disease.	RBR	1	Other	H.sapiens
1790	PRKN_HUMAN	MFN2_HUMAN	O60260	O95140	PRKN	MFN2	MEDLINE	20871098	UbiNet 2.0	RBR	1	Training data	H.sapiens
1791	PRKN_HUMAN	ERBB4_HUMAN	O60260	Q15303	PRKN	ERBB4	MEDLINE	15632191	UbiNet 2.0	RBR	1	Training data	H.sapiens
1792	PRKN_HUMAN	CISD1_HUMAN	O60260	Q9NZ45	PRKN	CISD1	MEDLINE	31110043	UbiNet 2.0	RBR	1	Other	H.sapiens
1793	PRKN_HUMAN	PDCD2_HUMAN	O60260	Q16342	PRKN	PDCD2	MEDLINE	22199232	E3Net	RBR	1	Other	H.sapiens
1794	PRKN_HUMAN	TOM20_HUMAN	O60260	Q15388	PRKN	TOMM20	MEDLINE	22199232	E3Net	RBR	1	Other	H.sapiens
1795	PRKN_HUMAN	DDIT4_HUMAN	O60260	Q9NX09	PRKN	DDIT4	MEDLINE	25101677	UbiNet 2.0	RBR	1	Other	H.sapiens
1796	PRKN_HUMAN	VDAC1_HUMAN	O60260	P21796	PRKN	VDAC1	MEDLINE	22199232	E3Net	RBR	1	Other	H.sapiens
1797	PRKN_HUMAN	NLRP3_HUMAN	O60260	Q96P20	PRKN	NLRP3	MEDLINE	33527027	Collectively, <span class="match term0">PARK2</span> negatively regulates <span class="match term1">NLRP3</span> protein via ubiquitination	RBR	1	Other	H.sapiens
1798	PRKN_HUMAN	SERA_HUMAN	O60260	O43175	PRKN	PHGDH	MEDLINE	32478681	<span class="match term0">Parkin</span> ubiquitinates phosphoglycerate dehydrogenase to suppress serine synthesis and tumor progression.	RBR	1	Other	H.sapiens
1799	PRKN_HUMAN	SH3G3_HUMAN	O60260	Q99963	PRKN	SH3GL3	MEDLINE	20064468	UbiNet 2.0	RBR	1	Training data	H.sapiens
1800	PRKN_HUMAN	SYT11_HUMAN	O60260	Q9BT88	PRKN	SYT11	MEDLINE	12925569	UbiNet 2.0	RBR	1	Training data	H.sapiens
1801	PRKN_HUMAN	CHIP_HUMAN	O60260	Q9UNE7	PRKN	STUB1	MEDLINE	22199232	E3Net	RBR	1	Other	H.sapiens
1802	PRKN_HUMAN	B2CL1_HUMAN	O60260	Q07817	PRKN	BCL2L1	MEDLINE	33431795	Mechanism dissection indicates that while androgens/androgen receptor (AR) can decrease BCL-2 expression to induce cell death, yet they can also simultaneously increase anti-apoptosis <span class="match term1">BCL-XL</span> protein expression via decreasing its potential E3 ubiquitin ligase, <span class="match term0">PARK2</span>, through transcriptionally increasing the miR-493-3p expression to target <span class="match term0">PARK2</span>	RBR	1	Other	H.sapiens
1803	PRKN_HUMAN	YAP1_HUMAN	O60260	P46937	PRKN	YAP1	MEDLINE	32863938	Co-IP and ubiquitination assays revealed that <span class="match term0">PARK2</span> could interact with <span class="match term1">YAP</span> in the cytosol and promotes <span class="match term1">YAP</span> K48-linked ubiquitination at K90 sites	RBR	1	Other	H.sapiens
1804	PRKN_HUMAN	HXK1_HUMAN	O60260	P19367	PRKN	HK1	MEDLINE	23068103	Mitochondrial hexokinase <span class="match term1">HKI</span> is a novel substrate of the <span class="match term0">Parkin</span> ubiquitin ligase.	RBR	1	Other	H.sapiens
1805	PRKN_HUMAN	TANK_HUMAN	O60260	Q92844	PRKN	TANK	MEDLINE	31558697	UbiNet 2.0	RBR	1	Other	H.sapiens
1806	PRKN_HUMAN	CCNB1_HUMAN	O60260	P14635	PRKN	CCNB1	MEDLINE	26387737	UbiNet 2.0	RBR	1	Other	H.sapiens
1807	PRKN_HUMAN	NEK2_HUMAN	O60260	P51955	PRKN	NEK2	MEDLINE	26387737	UbiNet 2.0	RBR	1	Other	H.sapiens
1808	PRKN_HUMAN	MIRO2_HUMAN	O60260	Q8IXI1	PRKN	RHOT2	MEDLINE	22078885	UbiNet 2.0	RBR	1	Training data	H.sapiens
1809	PRKN_HUMAN	TRAF6_HUMAN	O60260	Q9Y4K3	PRKN	TRAF6	MEDLINE	31558697	UbiNet 2.0	RBR	1	Other	H.sapiens
1810	PRKN_HUMAN	SH3G2_HUMAN	O60260	Q99962	PRKN	SH3GL2	MEDLINE	20064468	UbiNet 2.0	RBR	1	Training data	H.sapiens
1811	PRKN_HUMAN	FUBP1_HUMAN	O60260	Q96AE4	PRKN	FUBP1	MEDLINE	16672220	UbiNet 2.0	RBR	1	Training data	H.sapiens
1812	PRKN_HUMAN	PLCG1_HUMAN	O60260	P19174	PRKN	PLCG1	MEDLINE	18671761	UbiNet 2.0	RBR	1	Training data	H.sapiens
1813	PRKN_HUMAN	BAX_HUMAN	O60260	Q07812	PRKN	BAX	MEDLINE	22460798	UbiNet 2.0	RBR	1	Training data	H.sapiens
1814	PRKN_HUMAN	ERBB3_HUMAN	O60260	P21860	PRKN	ERBB3	MEDLINE	15632191	UbiNet 2.0	RBR	1	Training data	H.sapiens
1815	PRKN_HUMAN	SYPH_HUMAN	O60260	P08247	PRKN	SYP	MEDLINE	16135753	UbiNet 2.0	RBR	1	Training data	H.sapiens
1816	PRKN_HUMAN	TADBP_HUMAN	O60260	Q13148	PRKN	TARDBP	MEDLINE	23258539	UbiNet 2.0	RBR	1	Training data	H.sapiens
1817	PRKN2_HUMAN	Q99648_HUMAN	O60260	Q99648	PRKN	CDCrel-1	MEDLINE	11078524	hUbiquitome	RING	1	Other	H.sapiens
1818	PRP19_HUMAN	RFA2_HUMAN	Q9UMS4	P15927	PRPF19	RPA2	MEDLINE	24332808	UbiNet 2.0	DWD	1	Other	H.sapiens
1819	PRP19_HUMAN	RFA1_HUMAN	Q9UMS4	P27694	PRPF19	RPA1	MEDLINE	24332808	UbiNet 2.0	DWD	1	Other	H.sapiens
1820	PRP19_HUMAN	YBOX1_HUMAN	Q9UMS4	P67809	PRPF19	YBX1	MEDLINE	33361760	Further studies revealed that circRNA-SORE binds the master oncogenic protein <span class="match term1">YBX1</span> in the cytoplasm, which prevents <span class="match term1">YBX1</span> nuclear interaction with the E3 ubiquitin ligase <span class="match term0">PRP19</span> and thus blocks <span class="match term0">PRP19</span>-mediated <span class="match term1">YBX1</span> degradation	DWD	1	Other	H.sapiens
1821	PRP19_HUMAN	PRPF3_HUMAN	Q9UMS4	O43395	PRPF19	PRPF3	MEDLINE	20595234	UbiNet 2.0	DWD	1	Other	H.sapiens
1822	PTPA_HUMAN	BMI1_HUMAN	Q15257	P35226	PTPA	BMI1	MEDLINE	33463265	<span class="match term0">PP2A</span> mediates the ubiquitination/degradation of <span class="match term1">BMI1</span>, which is revealed by changes in the physical interaction of <span class="match term0">PP2A</span> and <span class="match term1">BMI1</span>	Other	1	Other	H.sapiens
1823	RB40C_HUMAN	RACK1_HUMAN	Q96S21	P63244	RAB40C	RACK1	MEDLINE	30112187	<span class="match term0">RAB40C</span> regulates <span class="match term1">RACK1</span> stability via the ubiquitin-proteasome system	SOCS_VHL_BC-box	1	Other	H.sapiens
1824	RACK1_HUMAN	HIF1A_HUMAN	P63244	Q16665	RACK1	HIF1A	MEDLINE	17244529	<span class="match term0">RACK1</span> competes with HSP90 for binding to <span class="match term1">HIF-1alpha</span> and is required for O(2)-independent and HSP90 inhibitor-induced degradation of <span class="match term1">HIF-1alpha</span>.	Other	1	Other	H.sapiens
1825	RACK1_HUMAN	CLC1B_HUMAN	P63244	Q9P126	RACK1	CLEC1B	MEDLINE	19785988	UbiNet 2.0	Other	1	Other	H.sapiens
1826	RAD18_HUMAN	PCNA_HUMAN	Q9NS91	P12004	RAD18	PCNA	MEDLINE	12226657	<span class="match term1">PCNA</span> is mono-ubiquitinated through RAD6 and <span class="match term0">RAD18</span>, modified by lysine-63-linked multi-ubiquitination--which additionally requires MMS2, UBC13 and RAD5--and is conjugated to SUMO by UBC9	RING	1	Training data	H.sapiens
1827	RAD18_HUMAN	FACD2_HUMAN	Q9NS91	Q9BXW9	RAD18	FANCD2	MEDLINE	20675655	UbiNet 2.0	RING	1	Training data	H.sapiens
1828	RAD18_HUMAN	TP53B_HUMAN	Q9NS91	Q12888	RAD18	TP53BP1	MEDLINE	19228710	<span class="match term0">RAD18</span> associates with <span class="match term1">53BP1</span> and is recruited to DSB sites in a <span class="match term1">53BP1</span>-dependent manner specifically during G1-phase, <span class="match term0">RAD18</span> monoubiquitinates KBD domain of <span class="match term1">53BP1</span> at lysine 1268 in vitro	RING	1	Other	H.sapiens
1829	RAD18_HUMAN	P53_HUMAN	Q9NS91	P04637	RAD18	TP53	MEDLINE	33083020	Mechanistic studies found that LINC00355 that mainly located in the nucleus, acting as a transcriptional activator, promoted transcription of <span class="match term0">RAD18</span> and UBE3C, which both bind to <span class="match term1">P53</span> and mediate the ubiquitination and degradation of <span class="match term1">P53</span>	RING	1	Other	H.sapiens
1830	RAD18_HUMAN	RAD18_HUMAN	Q9NS91	Q9NS91	RAD18	RAD18	MEDLINE	15509568	Multiple ubiquitinated bands of <span class="match term0">Rad18</span> were detected in vitro in the presence of E1, E2 (Rad6), and methylated ubiquitin, indicating that <span class="match term0">Rad18</span> was monoubiquitinated at multiple sites through autoubiquitination	RING	1	Training data	H.sapiens
1831	RAD18_HUMAN	RFC2_HUMAN	Q9NS91	P35250	RAD18	RFC2	MEDLINE	18245774	Furthermore <span class="match term1">RFC2</span> was ubiquitylated by the RAD6-<span class="match term0">RAD18</span> complex in vitro, and its modification was inhibited in the presence of RPA	RING	1	Training data	H.sapiens
1832	RD23A_HUMAN	TWST1_HUMAN	P54725	Q15672	RAD23A	TWIST1	MEDLINE	31487504	Our experiments reveal that: <span class="match term0">HR23A</span> interacts with <span class="match term1">Twist1</span>, and this promotes the ubiquitin-mediated proteasomal degradation of <span class="match term1">Twist1</span>	Other	1	Other	H.sapiens
1833	RAG1_HUMAN	IMA1_HUMAN	P15918	P52292	RAG1	KPNA2	MEDLINE	19118899	This is the first putative substrate identified for the <span class="match term0">RAG1</span> ubiquitin ligase, and to our knowledge it is the first reported case of ubiquitylation of KPNA1	RING	1	Other	H.sapiens
1834	RAG1_HUMAN	IMA5_HUMAN	P15918	P52294	RAG1	KPNA1	MEDLINE	19118899	UbiNet 2.0	RING	1	Training data	H.sapiens
1835	RAG1_HUMAN	H31T_HUMAN	P15918	Q16695	RAG1	H3-4	MEDLINE	20122409	The RING domain of <span class="match term0">RAG1</span> ubiquitylates histone H3: a novel activity in chromatin-mediated regulation of V(D)J joining.	RING	1	Other	H.sapiens
1836	RAG1_HUMAN	RAG1_HUMAN	P15918	P15918	RAG1	RAG1	MEDLINE	14671314	Autoubiquitylation of the V(D)J recombinase protein <span class="match term0">RAG1</span>	RING	1	Training data	H.sapiens
1837	RAG1_HUMAN	C9JYI4_HUMAN	P15918	C9JYI4	RAG1	KPNA1	MEDLINE	19118899	hUbiquitome	RING	1	Other	H.sapiens
1838	RBBP6_HUMAN	GRB2_HUMAN	Q7Z6E9	P62993	RBBP6	GRB2	MEDLINE	34348893	<span class="match term1">GRB2</span> K109 ubiquitination by E3 ubiquitin ligase <span class="match term0">RBBP6</span> releases MRE11 promoting HDR	RING	1	Other	H.sapiens
1839	RBBP6_HUMAN	ZBT38_HUMAN	Q7Z6E9	Q8NAP3	RBBP6	ZBTB38	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1840	RBBP6_HUMAN	YBOX1_HUMAN	Q7Z6E9	P67809	RBBP6	YBX1	MEDLINE	18851979	<span class="match term0">RBBP6</span> interacts with multifunctional protein <span class="match term1">YB-1</span> through its RING finger domain, leading to ubiquitination and proteosomal degradation of <span class="match term1">YB-1</span>	RING	1	Training data	H.sapiens
1841	HOIL1_HUMAN	HOIL1_HUMAN	Q9BYM8	Q9BYM8	RBCK1	RBCK1	MEDLINE	18303026	UbiNet 2.0	RING	1	Training data	H.sapiens
1842	HOIL1_HUMAN	RIPK1_HUMAN	Q9BYM8	Q13546	RBCK1	RIPK1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1843	HOIL1_HUMAN	TRI25_HUMAN	Q9BYM8	Q14258	RBCK1	TRIM25	MEDLINE	21292167	UbiNet 2.0	RING	1	Training data	H.sapiens
1844	HOIL1_HUMAN	IRF3_HUMAN	Q9BYM8	Q14653	RBCK1	IRF3	MEDLINE	18711448	Furthermore, viral infection leads to induction of <span class="match term0">RBCK1</span> and subsequent degradation of <span class="match term1">IRF3</span>	RING	1	Training data	H.sapiens
1845	HOIL1_HUMAN	NEMO_HUMAN	Q9BYM8	Q9Y6K9	RBCK1	IKBKG	MEDLINE	19675569	UbiNet 2.0	RING	1	Training data	H.sapiens
1846	HOIL1_HUMAN	TAB2_HUMAN	Q9BYM8	Q9NYJ8	RBCK1	TAB2	MEDLINE	17449468	<span class="match term0">RBCK1</span> negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting <span class="match term1">TAB2</span>/3 for degradation	RING	1	Training data	H.sapiens
1847	HOIL1_HUMAN	TAB3_HUMAN	Q9BYM8	Q8N5C8	RBCK1	TAB3	MEDLINE	17449468	<span class="match term0">RBCK1</span> negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation.	RING	1	Training data	H.sapiens
1848	HOIL1_HUMAN	IREB2_HUMAN	Q9BYM8	P48200	RBCK1	IREB2	MEDLINE	16275334	Through studies analyzing iron-mediated degradation of iron regulatory protein 2 (<span class="match term1">IRP2</span>), a central regulator of iron metabolism in mammalian cells, we have identified a RING finger protein, <span class="match term0">HOIL-1</span>, as an ubiquitin ligase recognizing <span class="match term1">IRP2</span> through a signal created by heme-mediated oxidative modification of the protein	RING	1	Training data	H.sapiens
1849	HOIL1_HUMAN	BACH1_HUMAN	Q9BYM8	O14867	RBCK1	BACH1	MEDLINE	17682061	UbiNet 2.0	RING	1	Training data	H.sapiens
1850	HOIL1_HUMAN	NR1I2_HUMAN	Q9BYM8	O75469	RBCK1	NR1I2	MEDLINE	23160820	UbiNet 2.0	RING	1	Training data	H.sapiens
1851	HOIL1_HUMAN	KPCA_HUMAN	Q9BYM8	P17252	RBCK1	PRKCA	MEDLINE	25118570	UbiNet 2.0	RING	1	Other	H.sapiens
1852	RBX1_HUMAN	RPB1_HUMAN	P62877	P24928	RBX1	POLR2A	MEDLINE	30349055	<span class="match term0">RBX1</span> modifies <span class="match term1">POLR2A</span> by the K63-linked ubiquitination.	RING	1	Other	H.sapiens
1853	RBX1_HUMAN	KS6B1_HUMAN	P62877	P23443	RBX1	RPS6KB1	MEDLINE	18279656	UbiNet 2.0	RING	1	Training data	H.sapiens
1854	RBX1_HUMAN	NF2L2_HUMAN	P62877	Q16236	RBX1	NFE2L2	MEDLINE	23274085	UbiNet 2.0	RING	1	Training data	H.sapiens
1855	RBX1_HUMAN	ESR1_HUMAN	P62877	P03372	RBX1	ESR1	MEDLINE	20130088	UbiNet 2.0	RING	1	Training data	H.sapiens
1856	RBX1_HUMAN	SUFU_HUMAN	P62877	Q9UMX1	RBX1	SUFU	MEDLINE	33499884	Mechanistically, <span class="match term0">ROC1</span> was able to target suppressor of fused homolog (<span class="match term1">SUFU</span>) for ubiquitin-dependent degradation, allowing Gli2 release from the <span class="match term1">SUFU</span> complex to activate the SHH pathway	RING	1	Other	H.sapiens
1857	RC3H1_HUMAN	ICOS_HUMAN	Q5TC82	Q9Y6W8	RC3H1	ICOS	MEDLINE	18172933	<span class="match term0">Roquin</span> normally limits <span class="match term1">Icos</span> expression by promoting the degradation of <span class="match term1">Icos</span> messenger RNA.A conserved segment in the unusually long <span class="match term1">ICOS</span> 3' untranslated mRNA is essential for regulation by <span class="match term0">Roquin</span>	RING	1	Training data	H.sapiens
1858	ZN363_HUMAN	CDN1B_HUMAN	Q96PM5	P46527	RCHY1	CDKN1B	MEDLINE	21236467	Our results suggest that <span class="match term0">Pirh2</span> mediates the degradation of p27(<span class="match term1">Kip1</span>) and participates in cell proliferation in human HCC	RING	1	Training data	H.sapiens
1859	ZN363_HUMAN	ITCH_HUMAN	Q96PM5	Q96J02	RCHY1	ITCH	MEDLINE	33569599	This down-regulation is shown to involve the ubiquitination of <span class="match term1">AIP4</span> by <span class="match term0">Pirh2</span>	RING	1	Other	H.sapiens
1860	ZN363_HUMAN	COPE_HUMAN	Q96PM5	O14579	RCHY1	COPE	MEDLINE	17721809	<span class="match term0">PIRH2</span> promotes the ubiquitylation of <span class="match term1">epsilon-COP</span> in vitro and in vivo and consequently promotes the degradation of <span class="match term1">epsilon-COP</span>	RING	1	Training data	H.sapiens
1861	ZN363_HUMAN	HDAC1_HUMAN	Q96PM5	Q13547	RCHY1	HDAC1	MEDLINE	18344599	<span class="match term0">Pirh2</span> is a RING finger type ubiquitin ligase which ubiquitylates various proteins including p53, p27(Kip1), <span class="match term1">HDAC1</span>, and epsilon-COP	RING	1	Training data	H.sapiens
1862	ZN363_HUMAN	GORAB_HUMAN	Q96PM5	Q5T7V8	RCHY1	GORAB	MEDLINE	20598683	A newly identified <span class="match term0">Pirh2</span> substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination	RING	1	Training data	H.sapiens
1863	ZN363_HUMAN	CHK2_HUMAN	Q96PM5	O96017	RCHY1	CHEK2	MEDLINE	23449389	UbiNet 2.0	RING	1	Training data	H.sapiens
1864	ZN363_HUMAN	P63_HUMAN	Q96PM5	Q9H3D4	RCHY1	TP63	MEDLINE	23235527	UbiNet 2.0	RING	1	Training data	H.sapiens
1865	ZN363_HUMAN	SRPRB_HUMAN	Q96PM5	Q9Y5M8	RCHY1	SRPRB	MEDLINE	18344599	<span class="match term0">Pirh2</span> interacts with and ubiquitylates signal recognition particle receptor beta subunit	RING	1	Training data	H.sapiens
1866	ZN363_HUMAN	P53_HUMAN	Q96PM5	P04637	RCHY1	TP53	MEDLINE	19895323	It has been suggested that measles virus phosphoprotein may inhibit ubiquitination of <span class="match term0">Pirh2</span>, which has been reported to be overexpressed in lung carcinoma and is responsible for degrading the cell cycle regulator <span class="match term1">p53</span>	RING	1	Training data	H.sapiens
1867	ZN363_HUMAN	ELAV1_HUMAN	Q96PM5	Q15717	RCHY1	ELAVL1	MEDLINE	34091597	We demonstrated that <span class="match term0">Pirh2</span> ubiquitinated the <span class="match term1">HuR</span> protein facilitating its proteasome-mediated degradation in cells.	RING	1	Other	H.sapiens
1868	ZN363_HUMAN	SRP09_HUMAN	Q96PM5	P49458	RCHY1	SRP9	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1869	ZN363_HUMAN	POLH_HUMAN	Q96PM5	Q9Y253	RCHY1	POLH	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1870	ZN363_HUMAN	DPOLQ_HUMAN	Q96PM5	O75417	RCHY1	POLQ	MEDLINE	21791603	UbiNet 2.0	RING	1	Training data	H.sapiens
1871	ZN363_HUMAN	P73_HUMAN	Q96PM5	O15350	RCHY1	TP73	MEDLINE	21994467	UbiNet 2.0	RING	1	Training data	H.sapiens
1872	RFFL_HUMAN	RIPK1_HUMAN	Q8WZ73	Q13546	RFFL	RIPK1	MEDLINE	18450452	UbiNet 2.0	RING	1	Other	H.sapiens
1873	RFFL_HUMAN	RFFL_HUMAN	Q8WZ73	Q8WZ73	RFFL	RFFL	UniProt	RFFL_HUMAN	Auto-ubiquitinated (in vitro) (By similarity)	RING	1	Training data	H.sapiens
1874	RFFL_HUMAN	CASPA_HUMAN	Q8WZ73	Q92851	RFFL	CASP10	MEDLINE	15069192	UbiNet 2.0	RING	1	Training data	H.sapiens
1875	RFFL_HUMAN	CASP8_HUMAN	Q8WZ73	Q14790	RFFL	CASP8	MEDLINE	15069192	UbiNet 2.0	RING	1	Training data	H.sapiens
1876	RFFL_HUMAN	CFTR_HUMAN	Q8WZ73	P13569	RFFL	CFTR	MEDLINE	29503157	<span class="match term0">RFFL</span> retrieves the unfolded <span class="match term1">CFTR</span> from the PM for lysosomal degradation by chaperone-independent K63-linked poly-ubiquitination	RING	1	Other	H.sapiens
1877	RFFL_HUMAN	PRR5L_HUMAN	Q8WZ73	Q6MZQ0	RFFL	PRR5L	MEDLINE	22609986	UbiNet 2.0	RING	1	Training data	H.sapiens
1878	RFFL_HUMAN	P53_HUMAN	Q8WZ73	P04637	RFFL	TP53	MEDLINE	17121812	CARPs physically interact with and ubiquitinate <span class="match term1">p53</span>, targeting it for degradation in the absence of MDM2. Unlike MDM2 or other E3 ligases known to target <span class="match term1">p53</span>, CARP1 and <span class="match term0">CARP2</span> appear to target phosphorylated <span class="match term1">p53</span> for ubiquitination and degradation.	RING	1	Training data	H.sapiens
1879	RFFL_HUMAN	1433S_HUMAN	Q8WZ73	P31947	RFFL	SFN	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1880	RFPLA_HUMAN	CCNB1_HUMAN	A6NLU0	P14635	RFPL4A	CCNB1	MEDLINE	12525704	UbiNet 2.0	RING	1	Training data	H.sapiens
1881	COP1_HUMAN	MIRO1_HUMAN	Q8NHY2	P14635	RFWD2	CDKN1B	MEDLINE	26254224	26254224	DWD	1	Other	H.sapiens
1882	RFWD3_HUMAN	P53_HUMAN	Q6PCD5	P04637	RFWD3	TP53	UniProt	RFWD3_HUMAN	Ubiquitinated by <span class="match term0">RFWD3</span>, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/<span class="match term1">TP53</span> that are not targeted to the proteasome	RING	1	Training data	H.sapiens
1883	RFWD3_HUMAN	RAD51_HUMAN	Q6PCD5	Q06609	RFWD3	RAD51	MEDLINE	33842359	We further demonstrated the decrease of homologous recombination (HR)-associated <span class="match term1">Rad51</span> in the transformed cells was related to the increase of its ubiquitination regulated by E3 ligase <span class="match term0">RFWD3</span> for the radiosensitization, which was opposite to normal cells, indicating that <span class="match term0">RFWD3</span>-dependent ubiquitination on <span class="match term1">Rad51</span> was involved in the VPA-mediated radio-bidirectional effect	RING	1	Other	H.sapiens
1884	RHBT1_HUMAN	PDE5A_HUMAN	O94844	O76074	RHOBTB1	PDE5A	MEDLINE	30896450	UbiNet 2.0	BTB_OTHER	1	Other	H.sapiens
1885	RHBT3_HUMAN	CCNE1_HUMAN	O94955	P24864	RHOBTB3	CCNE1	MEDLINE	24145166	Golgi-associated <span class="match term0">RhoBTB3</span> targets cyclin E for ubiquitylation and promotes cell cycle progression.	Other	1	Other	H.sapiens
1886	RICTR_HUMAN	SGK1_HUMAN	Q6R327	O00141	RICTOR	SGK1	MEDLINE	20832730	Moreover, as part of a feedback mechanism, phosphorylation of <span class="match term0">Rictor</span> at T1135 by multiple AGC kinases disrupts the interaction between <span class="match term0">Rictor</span> and Cullin-1 to impair <span class="match term1">SGK1</span> ubiquitination	RING	1	Training data	H.sapiens
1887	RING1_HUMAN	H2A1_HUMAN	Q06587	P0C0S8	RING1	H2AC11	MEDLINE	16359901	UbiNet 2.0	RING	1	Training data	H.sapiens
1888	RING1_HUMAN	SMRCD_HUMAN	Q06587	Q9H4L7	RING1	SMARCAD1	MEDLINE	29888761	Interestingly, T906 phosphorylation is also important for <span class="match term1">SMARCAD1</span> ubiquitination by <span class="match term0">RING1</span> at K905	RING	1	Other	H.sapiens
1889	RNF12_HUMAN	LDB2_HUMAN	Q9NVW2	O43679	RLIM	LDB2	UniProt	RNF12_HUMAN	Ubiquitinated by <span class="match term0">RLIM</span>/RNF12, leading to its degradation by the proteasome (By similarity)	RING	1	Training data	H.sapiens
1890	RNF12_HUMAN	LMO4_HUMAN	Q9NVW2	P61968	RLIM	LMO4	MEDLINE	31801865	<span class="match term0">RLIM</span> is an E3 ubiquitin ligase that leads to the ubiquitination and degradation of several transcription regulators, such as LMO2, <span class="match term1">LMO4</span>, LHX2, LHX3, LDB1 and the telomeric protein TRF1	RING	1	Other	H.sapiens
1891	RNF12_HUMAN	LDB1_HUMAN	Q9NVW2	Q86U70	RLIM	LDB1	MEDLINE	17437998	Finally, SSBP2 was demonstrated to inhibit <span class="match term1">Ldb1</span> and Lmo2 interaction with the E3 ubiquitin ligase <span class="match term0">RLIM</span>, prevent <span class="match term0">RLIM</span>-mediated <span class="match term1">Ldb1</span> ubiquitination, and protect <span class="match term1">Ldb1</span> and Lmo2 from proteasomal degradation	RING	1	Training data	H.sapiens
1892	RNF12_HUMAN	RNF12_HUMAN	Q9NVW2	Q9NVW2	RLIM	RLIM	MEDLINE	31801865	UbiNet 2.0	RING	1	Other	H.sapiens
1893	RNF12_HUMAN	HDAC2_HUMAN	Q9NVW2	Q92769	RLIM	HDAC2	MEDLINE	12840003	Ubc8 gene expression is induced by both VPA and TSA, whereas only TSA simultaneously reduces <span class="match term0">RLIM</span> protein levels and therefore fails to induce <span class="match term1">HDAC2</span> degradation	RING	1	Training data	H.sapiens
1894	RNF12_HUMAN	STMN1_HUMAN	Q9NVW2	P16949	RLIM	STMN1	MEDLINE	24686088	Here we identified the <span class="match term0">Rlim</span>, a Ring H2 zinc finger protein with intrinsic ubiquitin ligase activity, as a Stathmin-interacting protein that could increase Stathmin turnover through binding with this targeted protein and then induce its degradation by proteasome in a ubiquitin-dependent manner	RING	1	Other	H.sapiens
1895	RNF12_HUMAN	ZFP42_HUMAN	Q9NVW2	Q96MM3	RLIM	ZFP42	MEDLINE	22596162	UbiNet 2.0	RING	1	Training data	H.sapiens
1896	RNF12_HUMAN	LIMK1_HUMAN	Q9NVW2	P53667	RLIM	LIMK1	UniProt	RNF12_HUMAN	Also polyubiquitinated by <span class="match term0">RLIM</span> (By similarity)	RING	1	Training data	H.sapiens
1897	RNF12_HUMAN	MDM2_HUMAN	Q9NVW2	Q00987	RLIM	MDM2	MEDLINE	26926424	UbiNet 2.0	RING	1	Other	H.sapiens
1898	RNF12_HUMAN	LHX3_HUMAN	Q9NVW2	Q9UBR4	RLIM	LHX3	MEDLINE	31801865	<span class="match term0">RLIM</span> is an E3 ubiquitin ligase that leads to the ubiquitination and degradation of several transcription regulators, such as LMO2, LMO4, LHX2, <span class="match term1">LHX3</span>, LDB1 and the telomeric protein TRF1	RING	1	Other	H.sapiens
1899	RNF12_HUMAN	LHX2_HUMAN	Q9NVW2	P50458	RLIM	LHX2	MEDLINE	31801865	<span class="match term0">RLIM</span> is an E3 ubiquitin ligase that leads to the ubiquitination and degradation of several transcription regulators, such as LMO2, LMO4, <span class="match term1">LHX2</span>, LHX3, LDB1 and the telomeric protein TRF1	RING	1	Other	H.sapiens
1900	RNF12_HUMAN	TERF1_HUMAN	Q9NVW2	P54274	RLIM	TERF1	MEDLINE	31801865	<span class="match term0">RLIM</span> is an E3 ubiquitin ligase that leads to the ubiquitination and degradation of several transcription regulators, such as LMO2, LMO4, LHX2, LHX3, LDB1 and the telomeric protein <span class="match term1">TRF1</span>	RING	1	Other	H.sapiens
1901	RNF12_HUMAN	TF3B_HUMAN	Q9NVW2	Q92994	RLIM	BRF1	MEDLINE	30413534	<span class="match term0">RNF12</span> catalyzes <span class="match term1">BRF1</span> ubiquitination and regulates RNA polymerase III-dependent transcription	RING	1	Other	H.sapiens
1902	RNF12_HUMAN	RBTN2_HUMAN	Q9NVW2	P25791	RLIM	LMO2	MEDLINE	31801865	<span class="match term0">RLIM</span> is an E3 ubiquitin ligase that leads to the ubiquitination and degradation of several transcription regulators, such as <span class="match term1">LMO2</span>, LMO4, LHX2, LHX3, LDB1 and the telomeric protein TRF1	RING	1	Other	H.sapiens
1903	RNF11_HUMAN	SMUF2_HUMAN	Q9Y3C5	Q9HAU4	RNF11	SMURF2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1904	RNF11_HUMAN	RNF11_HUMAN	Q9Y3C5	Q9Y3C5	RNF11	RNF11	MEDLINE	14562029	hUbiquitome	RING	1	Other	H.sapiens
1905	RN111_HUMAN	SMAD7_HUMAN	Q6ZNA4	O15105	RNF111	SMAD7	MEDLINE	18808420	<span class="match term0">Arkadia</span>, a RING-type E3 ubiquitin ligase, induces the ubiquitination and degradation of <span class="match term1">Smad7</span> and corepressors, c-Ski and SnoN, to enhance TGF-beta family signaling	RING	1	Training data	H.sapiens
1906	RN111_HUMAN	SKI_HUMAN	Q6ZNA4	P12755	RNF111	SKI	MEDLINE	18950738	<span class="match term0">Arkadia</span> bound Smad2/3 via <span class="match term1">Ski</span> to induce the ubiquitination of Smad2/3	RING	1	Training data	H.sapiens
1907	RN111_HUMAN	SKIL_HUMAN	Q6ZNA4	P12757	RNF111	SKIL	MEDLINE	18808420	<span class="match term0">Arkadia</span>, a RING-type E3 ubiquitin ligase, induces the ubiquitination and degradation of Smad7 and corepressors, c-Ski and <span class="match term1">SnoN</span>, to enhance TGF-beta family signaling	RING	1	Training data	H.sapiens
1908	RN111_HUMAN	PML_HUMAN	Q6ZNA4	P29590	RNF111	PML	MEDLINE	23530056	UbiNet 2.0	RING	1	Training data	H.sapiens
1909	RN111_HUMAN	NF2L2_HUMAN	Q6ZNA4	Q16236	RNF111	NFE2L2	MEDLINE	29597191	<span class="match term0">Arkadia</span> (RING Finger Protein 111) Mediates Sumoylation-Dependent Stabilization of <span class="match term1">Nrf2</span> Through K48-Linked Ubiquitination	RING	1	Other	H.sapiens
1910	RN111_HUMAN	SMAD3_HUMAN	Q6ZNA4	P84022	RNF111	SMAD3	MEDLINE	18950738	UbiNet 2.0	RING	1	Training data	H.sapiens
1911	RN111_HUMAN	SUMO2_HUMAN	Q6ZNA4	P61956	RNF111	SUMO2	MEDLINE	23530056	<span class="match term0">Arkadia</span>, a novel SUMO-targeted ubiquitin ligase involved in PML degradation.	RING	1	Other	H.sapiens
1912	RN111_HUMAN	SMAD2_HUMAN	Q6ZNA4	Q15796	RNF111	SMAD2	MEDLINE	18950738	UbiNet 2.0	RING	1	Training data	H.sapiens
1913	RN115_HUMAN	MET_HUMAN	Q9Y4L5	P08581	RNF115	MET	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1914	RN115_HUMAN	FLT3_HUMAN	Q9Y4L5	P36888	RNF115	FLT3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1915	RN115_HUMAN	MAVS_HUMAN	Q9Y4L5	Q7Z434	RNF115	MAVS	MEDLINE	33139700	<span class="match term0">RNF115</span> constitutively interacts with and induces K48-linked ubiquitination and proteasomal degradation of homeostatic <span class="match term1">MAVS</span> in uninfected cells, whereas associates with and catalyzes K63-linked ubiquitination of MITA after HSV-1 infection	RING	1	Other	H.sapiens
1916	RN115_HUMAN	CXCR4_HUMAN	Q9Y4L5	P61073	RNF115	CXCR4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1917	RN115_HUMAN	EGFR_HUMAN	Q9Y4L5	P00533	RNF115	EGFR	MEDLINE	23418353	UbiNet 2.0	RING	1	Other	H.sapiens
1918	RN115_HUMAN	RN115_HUMAN	Q9Y4L5	Q9Y4L5	RNF115	RNF115	MEDLINE	17462600	In the ligand-induced degradation of EGF receptor (EGFR), Rabring7 accelerated the degradation of EGFR, whereas Rabring7C229S inhibited the degradation induced by cCbl, another E3 ligase	RING	1	Training data	H.sapiens
1919	RN123_HUMAN	CDN1B_HUMAN	Q5XPI4	P46527	RNF123	CDKN1B	UniProt	RN123_HUMAN	Deubiquitinates and prevents proteasomal degradation of <span class="match term0">RNF123</span> which in turn stimulates <span class="match term1">CDKN1B</span> ubiquitin-dependent degradation thereby playing a role in cell proliferation	RING	1	Training data	H.sapiens
1920	RN123_HUMAN	CBX5_HUMAN	Q5XPI4	P45973	RNF123	CBX5	MEDLINE	23077635	UbiNet 2.0	RING	1	Training data	H.sapiens
1921	RN123_HUMAN	NFKB1_HUMAN	Q5XPI4	P19838	RNF123	NFKB1	MEDLINE	25860612	Here, we identify <span class="match term0">KPC1</span> as the Ub ligase (E3) that binds to the ankyrin repeats domain of <span class="match term1">p105</span>, ubiquitinates it, and mediates its processing both under basal conditions and following signaling	RING	1	Other	H.sapiens
1922	RN123_HUMAN	CBX1_HUMAN	Q5XPI4	P83916	RNF123	CBX1	MEDLINE	23077635	UbiNet 2.0	RING	1	Training data	H.sapiens
1923	RN125_HUMAN	DDX58_HUMAN	Q96EQ8	O95786	RNF125	DDX58	MEDLINE	17719635	By analyzing this regulatory circuit, we found that UbcH8 and ISG15 are functional regulators of <span class="match term0">RNF125</span> E3 ligase activity, which regulates the level of ubiquitin and ISG15 conjugation of <span class="match term1">RIG-I</span>	RING	1	Training data	H.sapiens
1924	RN125_HUMAN	NLRP3_HUMAN	Q96EQ8	Q96P20	RNF125	NLRP3	MEDLINE	31999304	We also identify <span class="match term0">RNF125</span> as an additional E3 ubiquitin ligase that initiates K63-linked ubiquitination of the <span class="match term1">NLRP3</span> LRR domain	RING	1	Other	H.sapiens
1925	RN125_HUMAN	IFIH1_HUMAN	Q96EQ8	Q9BYX4	RNF125	IFIH1	MEDLINE	17460044	Further, <span class="match term0">RNF125</span> conjugates ubiquitin to <span class="match term1">MDA5</span>, a family protein of RIG-I as well as IPS-1, which is also a downstream protein of RIG-I signaling that results in suppressing the functions of these proteins	RING	1	Training data	H.sapiens
1926	RN125_HUMAN	P53_HUMAN	Q96EQ8	P04637	RNF125	TP53	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1927	RN125_HUMAN	MAVS_HUMAN	Q96EQ8	Q7Z434	RNF125	MAVS	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1928	RN125_HUMAN	JAK1_HUMAN	Q96EQ8	P23458	RNF125	JAK1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1929	RN125_HUMAN	ILRL2_HUMAN	Q96EQ8	Q9HB29	RNF125	IL1RL2	MEDLINE	29176319	Mutations of Lys568 and Lys569 in the C-terminal tail of <span class="match term1">IL-1Rrp2</span> decrease ubiquitination by <span class="match term0">RNF125</span> and increase the steady-state levels of <span class="match term1">IL-1Rrp2</span>	RING	1	Other	H.sapiens
1930	RN125_HUMAN	RN125_HUMAN	Q96EQ8	Q96EQ8	RNF125	RNF125	MEDLINE	17990982	hUbiquitome	RING	1	Other	H.sapiens
1931	RN126_HUMAN	PTEN_HUMAN	Q9BV68	P60484	RNF126	PTEN	MEDLINE	33664240	The in vivo ubiquitination assay showed that <span class="match term0">RNF126</span> specifically regulates <span class="match term1">PTEN</span> stability through poly-ubiquitination	RING	1	Other	H.sapiens
1932	RN126_HUMAN	CDN1A_HUMAN	Q9BV68	P38936	RNF126	CDKN1A	MEDLINE	23026136	UbiNet 2.0	RING	1	Other	H.sapiens
1933	RN126_HUMAN	MET_HUMAN	Q9BV68	P08581	RNF126	MET	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1934	RN126_HUMAN	CXCR4_HUMAN	Q9BV68	P61073	RNF126	CXCR4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1935	RN126_HUMAN	AICDA_HUMAN	Q9BV68	Q9GZX7	RNF126	AICDA	MEDLINE	23277564	Solubility-based genetic screen identifies RING finger protein 126 as an E3 ligase for activation-induced cytidine deaminase.	RING	1	Other	H.sapiens
1936	RN126_HUMAN	P53_HUMAN	Q9BV68	P04637	RNF126	TP53	MEDLINE	33149608	Overexpression of <span class="match term0">RNF126</span> Promotes the Development of Colorectal Cancer via Enhancing <span class="match term1">p53</span> Ubiquitination and Degradation	RING	1	Other	H.sapiens
1937	RN126_HUMAN	FLT3_HUMAN	Q9BV68	P36888	RNF126	FLT3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1938	RN126_HUMAN	EGFR_HUMAN	Q9BV68	P00533	RNF126	EGFR	MEDLINE	23418353	<span class="match term0">RNF126</span> and Rabring7 associate with the <span class="match term1">EGFR</span> through a ubiquitin-binding zinc finger domain and both E3 ubiquitin ligases promote ubiquitylation of <span class="match term1">EGFR</span>.	RING	1	Other	H.sapiens
1939	RN128_HUMAN	CD40L_HUMAN	Q8TEB7	P29965	RNF128	CD40LG	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1940	RN128_HUMAN	P53_HUMAN	Q8TEB7	P04637	RNF128	TP53	MEDLINE	31715145	<span class="match term0">RNF128</span> is an E3 ubiquitin ligase that targets <span class="match term1">p53</span> for degradation	RING	1	Other	H.sapiens
1941	RN128_HUMAN	CD44_HUMAN	Q8TEB7	P16070	RNF128	CD44	MEDLINE	30832692	Downregulation of <span class="match term0">RNF128</span> activates Wnt/beta-catenin signaling to induce cellular EMT and stemness via <span class="match term1">CD44</span> and CTTN ubiquitination in melanoma	RING	1	Other	H.sapiens
1942	RN128_HUMAN	GDIR1_HUMAN	Q8TEB7	P52565	RNF128	ARHGDIA	MEDLINE	17114425	<span class="match term0">GRAIL</span> was subsequently demonstrated to bind and ubiquitinate <span class="match term1">RhoGDI</span>, although <span class="match term0">GRAIL</span>-mediated ubiquitination of <span class="match term1">RhoGDI</span> did not result in proteosomal degradation.	RING	1	Training data	H.sapiens
1943	RN128_HUMAN	ARPC5_HUMAN	Q8TEB7	O15511	RNF128	ARPC5	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1944	RN128_HUMAN	GDIR2_HUMAN	Q8TEB7	P52566	RNF128	ARHGDIB	MEDLINE	17114425	<span class="match term0">GRAIL</span> was subsequently demonstrated to bind and ubiquitinate RhoGDI, although <span class="match term0">GRAIL</span>-mediated ubiquitination of RhoGDI did not result in proteosomal degradation.	RING	1	Training data	H.sapiens
1945	RN128_HUMAN	COR1A_HUMAN	Q8TEB7	P31146	RNF128	CORO1A	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1946	RN128_HUMAN	CD83_HUMAN	Q8TEB7	Q01151	RNF128	CD83	MEDLINE	19542455	The transmembrane E3 ligase <span class="match term0">GRAIL</span> ubiquitinates and degrades <span class="match term1">CD83</span> on CD4 T cells	RING	1	Training data	H.sapiens
1947	RNF13_HUMAN	SNAPN_HUMAN	O43567	O95295	RNF13	SNAPIN	MEDLINE	22890573	UbiNet 2.0	RING	1	Training data	H.sapiens
1948	RNF13_HUMAN	RNF13_HUMAN	O43567	O43567	RNF13	RNF13	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1949	GOLI_HUMAN	VAMP3_HUMAN	Q86XS8	Q15836	RNF130	VAMP3	MEDLINE	23353890	UbiNet 2.0	RING	1	Training data	H.sapiens
1950	RN135_HUMAN	DDX58_HUMAN	Q8IUD6	O95786	RNF135	DDX58	MEDLINE	19017631	Our data suggest that Riplet/<span class="match term0">RNF135</span> is a novel factor of the <span class="match term1">RIG-I</span> pathway that is involved in the evoking of human innate immunity against RNA virus infection, and activates <span class="match term1">RIG-I</span> through ubiquitination of its C-terminal region	RING	1	Training data	H.sapiens
1951	RN138_HUMAN	TF7L2_HUMAN	Q8WVD3	Q9NQB0	RNF138	TCF7L2	MEDLINE	16714285	Here, we show that <span class="match term0">NARF</span> induces the ubiquitylation of TCF/LEF in vitro and in vivo, and functions as an E3 ubiquitin-ligase that specifically cooperates with the E2 conjugating enzyme E2-25K	RING	1	Training data	H.sapiens
1952	RN138_HUMAN	CTIP_HUMAN	Q8WVD3	Q99708	RNF138	RBBP8	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1953	RN138_HUMAN	LEF1_HUMAN	Q8WVD3	Q9UJU2	RNF138	LEF1	MEDLINE	16714285	Here, we show that <span class="match term0">NARF</span> induces the ubiquitylation of TCF/LEF in vitro and in vivo, and functions as an E3 ubiquitin-ligase that specifically cooperates with the E2 conjugating enzyme E2-25K	RING	1	Training data	H.sapiens
1954	RN138_HUMAN	RN138_HUMAN	Q8WVD3	Q8WVD3	RNF138	RNF138	MEDLINE	16714285	UbiNet 2.0	RING	1	Training data	H.sapiens
1955	RN138_HUMAN	XRCC5_HUMAN	Q8WVD3	P13010	RNF138	XRCC5	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1956	RN139_HUMAN	INSI1_HUMAN	Q8WU17	O15503	RNF139	INSIG1	MEDLINE	20068067	UbiNet 2.0	RING	1	Training data	H.sapiens
1957	RN139_HUMAN	RN139_HUMAN	Q8WU17	Q8WU17	RNF139	RNF139	MEDLINE	12032852	hUbiquitome	RING	1	Other	H.sapiens
1958	RNF14_HUMAN	RNF14_HUMAN	Q9UBS8	Q9UBS8	RNF14	RNF14	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1959	R144A_HUMAN	HSP72_HUMAN	P50876	P54652	RNF144A	HSPA2	MEDLINE	31406303	Collectively, these findings reveal a previously unappreciated role for <span class="match term0">RNF144A</span> in suppression of breast cancer growth and metastasis, and identify <span class="match term0">RNF144A</span> as the first, to our knowledge, E3 ubiquitin ligase for <span class="match term1">HSPA2</span> in human cancer.	SINGLE_OTHER	1	Other	H.sapiens
1960	R144A_HUMAN	EGFR_HUMAN	P50876	P00533	RNF144A	EGFR	MEDLINE	30171075	<span class="match term0">RNF144A</span> promotes <span class="match term1">EGFR</span> ubiquitination, maintains <span class="match term1">EGFR</span> protein, and prolongs EGF/<span class="match term1">EGFR</span> signaling during EGF stimulation	SINGLE_OTHER	1	Other	H.sapiens
1961	R144A_HUMAN	PRKDC_HUMAN	P50876	P78527	RNF144A	PRKDC	MEDLINE	24979766	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
1962	R144B_HUMAN	BAX_HUMAN	Q7Z419	Q07812	RNF144B	BAX	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1963	R144B_HUMAN	CDN1A_HUMAN	Q7Z419	P38936	RNF144B	CDKN1A	MEDLINE	16427630	Together with a recent report showing that <span class="match term0">p53RFP</span> is involved in ubiquitination and degradation of <span class="match term1">p21</span>, a p53 downstream protein promoting growth arrest and antagonizing apoptosis, our findings suggest that <span class="match term0">p53RFP</span> is involved in switching a cell from p53-mediated growth arrest to apoptosis	RING	1	Training data	H.sapiens
1964	R144B_HUMAN	TYW4_HUMAN	Q7Z419	O60294	RNF144B	LCMT2	MEDLINE	12853982	UbiNet 2.0	RING	1	Training data	H.sapiens
1965	R144B_HUMAN	NPM_HUMAN	Q7Z419	P06748	RNF144B	NPM1	MEDLINE	20864535	UbiNet 2.0	RING	1	Training data	H.sapiens
1966	RN145_HUMAN	HMDH_HUMAN	Q96MT1	P04035	RNF145	HMGCR	MEDLINE	30543180	We find that <span class="match term0">RNF145</span> and gp78 independently co-ordinate <span class="match term1">HMGCR</span> ubiquitination and degradation	RING	1	Other	H.sapiens
1967	RN146_HUMAN	XRCC6_HUMAN	Q9NTX7	P12956	RNF146	XRCC6	MEDLINE	21825151	UbiNet 2.0	RING	1	Other	H.sapiens
1968	RN146_HUMAN	3BP5L_HUMAN	Q9NTX7	Q7L8J4	RNF146	SH3BP5L	MEDLINE	34128958	Using proximity-dependent biotin identification (BioID) interaction proteomics, we have identified <span class="match term1">SH3BP5</span> and its paralogue <span class="match term1">SH3BP5L</span> as new substrates of the poly-ADP-ribose polymerase Tankyrase and the E3 ligase <span class="match term0">RNF146</span>	RING	1	Other	H.sapiens
1969	RN146_HUMAN	3BP5_HUMAN	Q9NTX7	O60239	RNF146	SH3BP5	MEDLINE	34128958	Using proximity-dependent biotin identification (BioID) interaction proteomics, we have identified <span class="match term1">SH3BP5</span> and its paralogue <span class="match term1">SH3BP5L</span> as new substrates of the poly-ADP-ribose polymerase Tankyrase and the E3 ligase <span class="match term0">RNF146</span>	RING	1	Other	H.sapiens
1970	RN146_HUMAN	AXIN1_HUMAN	Q9NTX7	O15169	RNF146	AXIN1	MEDLINE	21478859	UbiNet 2.0	RING	1	Training data	H.sapiens
1971	RN146_HUMAN	XRCC1_HUMAN	Q9NTX7	P18887	RNF146	XRCC1	MEDLINE	21825151	UbiNet 2.0	RING	1	Other	H.sapiens
1972	RN146_HUMAN	CASC3_HUMAN	Q9NTX7	O15234	RNF146	CASC3	MEDLINE	21478859	UbiNet 2.0	RING	1	Training data	H.sapiens
1973	RN146_HUMAN	TNKS1_HUMAN	Q9NTX7	O95271	RNF146	TNKS	MEDLINE	21478859	UbiNet 2.0	RING	1	Training data	H.sapiens
1974	RN146_HUMAN	TNKS2_HUMAN	Q9NTX7	Q9H2K2	RNF146	TNKS2	MEDLINE	21478859	UbiNet 2.0	RING	1	Training data	H.sapiens
1975	RN146_HUMAN	GO45_HUMAN	Q9NTX7	Q9H2G9	RNF146	BLZF1	MEDLINE	21478859	UbiNet 2.0	RING	1	Training data	H.sapiens
1976	RN146_HUMAN	AXIN2_HUMAN	Q9NTX7	Q9Y2T1	RNF146	AXIN2	MEDLINE	21383061	UbiNet 2.0	RING	1	Training data	H.sapiens
1977	RN146_HUMAN	PARP1_HUMAN	Q9NTX7	P09874	RNF146	PARP1	MEDLINE	21825151	UbiNet 2.0	RING	1	Training data	H.sapiens
1978	RN149_HUMAN	BRAF_HUMAN	Q8NC42	P15056	RNF149	BRAF	MEDLINE	22628551	UbiNet 2.0	RING	1	Training data	H.sapiens
1979	RN152_HUMAN	RHEB_HUMAN	Q8N8N0	Q15382	RNF152	RHEB	MEDLINE	32296023	UbiNet 2.0	RING	1	Other	H.sapiens
1980	RN152_HUMAN	RRAGA_HUMAN	Q8N8N0	Q7L523	RNF152	RRAGA	MEDLINE	25936802	Ubiquitination by <span class="match term0">RNF152</span> generates an anchor on <span class="match term1">RagA</span> to recruit its inhibitor GATOR1, a GAP complex for Rag GTPases	RING	1	Other	H.sapiens
1981	RN152_HUMAN	TSN12_HUMAN	Q8N8N0	O95859	RNF152	TSPAN12	MEDLINE	33602225	Mechanistically, <span class="match term0">RNF152</span> interacted with <span class="match term1">TSPAN12</span> and targeted it for ubiquitination and proteasomal degradation, thereby inhibiting <span class="match term1">TSPAN12</span>-dependent CXCL6 expression and HCC progression	RING	1	Other	H.sapiens
1982	RN167_HUMAN	CAST1_HUMAN	Q9H6Y7	Q8WTX7	RNF167	CASTOR1	MEDLINE	33594058	<span class="match term0">RNF167</span> activates mTORC1 and promotes tumorigenesis by targeting <span class="match term1">CASTOR1</span> for ubiquitination and degradation	RING	1	Other	H.sapiens
1983	RN167_HUMAN	S22AI_HUMAN	Q9H6Y7	Q96BI1	RNF167	SLC22A18	MEDLINE	16314844	UbiNet 2.0	RING	1	Training data	H.sapiens
1984	RN168_HUMAN	H2AY_HUMAN	Q8IYW5	O75367	RNF168	MACROH2A1	MEDLINE	32424115	Here, we report that <span class="match term0">RNF168</span> ubiquitinates the non-canonical H2A variants H2AZ and <span class="match term1">macroH2A1</span>/2 at the divergent N-terminal tail lysine residue	RING	1	Other	H.sapiens
1985	RN168_HUMAN	H2AW_HUMAN	Q8IYW5	Q9P0M6	RNF168	MACROH2A2	MEDLINE	32424115	Here, we report that <span class="match term0">RNF168</span> ubiquitinates the non-canonical H2A variants H2AZ and macroH2A1/2 at the divergent N-terminal tail lysine residue	RING	1	Other	H.sapiens
1986	RN168_HUMAN	RHOC_HUMAN	Q8IYW5	P08134	RNF168	RHOC	MEDLINE	33865221	Importantly, we here reported that <span class="match term0">RNF168</span> directly interacted with Ras homolog gene family member C (<span class="match term1">RHOC</span>) and induced its ubiquitination to promote <span class="match term1">RHOC</span> degradation	RING	1	Other	H.sapiens
1987	RN168_HUMAN	H2A1_HUMAN	Q8IYW5	P0C0S8	RNF168	H2AC11	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1988	RN168_HUMAN	H2A2C_HUMAN	Q8IYW5	Q16777	RNF168	H2AC20	MEDLINE	19203578	UbiNet 2.0	RING	1	Other	H.sapiens
1989	RN168_HUMAN	H2A2A_HUMAN	Q8IYW5	Q6FI13	RNF168	H2AC18	MEDLINE	32424115	<span class="match term0">RNF168</span> catalyzes <span class="match term1">H2A</span> and H2AX ubiquitination on lysine 13/15 (K13/K15) upon DNA damage and promotes the accrual of downstream repair factors at damaged chromatin	RING	1	Other	H.sapiens
1990	RN168_HUMAN	H2AX_HUMAN	Q8IYW5	P16104	RNF168	H2AX	MEDLINE	22980979	UbiNet 2.0	RING	1	Training data	H.sapiens
1991	RN168_HUMAN	H2AZ_HUMAN	Q8IYW5	P0C0S5	RNF168	H2AZ1	MEDLINE	32424115	Here, we report that <span class="match term0">RNF168</span> ubiquitinates the non-canonical H2A variants <span class="match term1">H2AZ</span> and macroH2A1/2 at the divergent N-terminal tail lysine residue	RING	1	Other	H.sapiens
1992	RN168_HUMAN	KDM4A_HUMAN	Q8IYW5	O75164	RNF168	KDM4A	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
1993	RN168_HUMAN	RN168_HUMAN	Q8IYW5	Q8IYW5	RNF168	RNF168	MEDLINE	19203578	hUbiquitome	RING	1	Other	H.sapiens
1994	RN170_HUMAN	ITPR1_HUMAN	Q96K19	Q14643	RNF170	ITPR1	MEDLINE	21610068	UbiNet 2.0	RING	1	Training data	H.sapiens
1995	RN180_HUMAN	CCN4_HUMAN	Q86T96	O95388	RNF180	CCN4	MEDLINE	33553163	Our findings revealed a crucial role of <span class="match term0">RNF180</span> in suppressing tumor growth by ubiquitinating <span class="match term1">WISP1</span> in CRC.	RING	1	Other	H.sapiens
1996	RN180_HUMAN	PLK2_HUMAN	Q86T96	Q9NYY3	RNF180	PLK2	MEDLINE	33482186	Ring finger protein 180 (<span class="match term0">RNF180</span>), an E3 ubiquitin ligase, interacted with <span class="match term1">PLK2</span> and induced the ubiquitination of <span class="match term1">PLK2</span>	RING	1	Other	H.sapiens
1997	RN180_HUMAN	ZIC2_HUMAN	Q86T96	O95409	RNF180	ZIC2	UniProt	RN180_HUMAN	Ubiquitinated by <span class="match term0">RNF180</span>, leading to its degradation	RING	1	Training data	H.sapiens
1998	RN180_HUMAN	RHOC_HUMAN	Q86T96	P08134	RNF180	RHOC	MEDLINE	33082325	We subsequently demonstrated that <span class="match term0">RNF180</span> could directly combine with <span class="match term1">RhoC</span> and promote the ubiquitination and degradation of <span class="match term1">RhoC</span> protein in GC cells	RING	1	Other	H.sapiens
1999	RN181_HUMAN	ESR1_HUMAN	Q9P0P0	P03372	RNF181	ESR1	MEDLINE	32973333	Immuno-precipitation assays indicate that <span class="match term0">RNF181</span> associates with <span class="match term1">ERalpha</span> and promotes its stability possibly via inducing <span class="match term1">ERalpha</span> K63-linked poly-ubiquitination	RING	1	Other	H.sapiens
2000	RN181_HUMAN	ITA2B_HUMAN	Q9P0P0	P08514	RNF181	ITGA2B	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2001	RN181_HUMAN	RN181_HUMAN	Q9P0P0	Q9P0P0	RNF181	RNF181	MEDLINE	18331836	hUbiquitome	RING	1	Other	H.sapiens
2002	RN182_HUMAN	TF65_HUMAN	Q8N6D2	Q04206	RNF182	RELA	MEDLINE	31432514	The E3 ubiquitin ligase <span class="match term0">RNF182</span> inhibits TLR-triggered cytokine production through promoting <span class="match term1">p65</span> ubiquitination and degradation	RING	1	Other	H.sapiens
2003	RN182_HUMAN	VATL_HUMAN	Q8N6D2	P27449	RNF182	ATP6V0C	MEDLINE	18298843	A novel brain-enriched E3 ubiquitin ligase <span class="match term0">RNF182</span> is up regulated in the brains of Alzheimer's patients and targets <span class="match term1">ATP6V0C</span> for degradation	RING	1	Training data	H.sapiens
2004	RN183_HUMAN	B2CL1_HUMAN	Q96D59	Q07817	RNF183	BCL2L1	MEDLINE	29507230	Furthermore, <span class="match term0">RNF183</span> interacts with <span class="match term1">Bcl-xL</span>, an antiapoptotic member of the Bcl-2 family, and polyubiquitinates <span class="match term1">Bcl-xL</span> for degradation	RING	1	Other	H.sapiens
2005	RN183_HUMAN	AT1B1_HUMAN	Q96D59	P05026	RNF183	ATP1B1	MEDLINE	31732153	Hypertonicity-responsive ubiquitin ligase <span class="match term0">RNF183</span> promotes Na, K-ATPase lysosomal degradation through ubiquitination of its beta1 subunit.	RING	1	Other	H.sapiens
2006	RN183_HUMAN	TR10B_HUMAN	Q96D59	O14763	RNF183	TNFRSF10B	MEDLINE	31889078	Inflammatory bowel disease-associated ubiquitin ligase <span class="match term0">RNF183</span> promotes lysosomal degradation of <span class="match term1">DR5</span> and TRAIL-induced caspase activation.	RING	1	Other	H.sapiens
2007	RN185_HUMAN	SEC20_HUMAN	Q96GF1	Q12981	RNF185	BNIP1	MEDLINE	21931693	UbiNet 2.0	RING	1	Training data	H.sapiens
2008	RN185_HUMAN	DVL2_HUMAN	Q96GF1	O14641	RNF185	DVL2	MEDLINE	24727453	The E3 ligase <span class="match term0">RNF185</span> negatively regulates osteogenic differentiation by targeting <span class="match term1">Dvl2</span> for degradation.	RING	1	Other	H.sapiens
2009	RN185_HUMAN	PRAF3_HUMAN	Q96GF1	O75915	RNF185	ARL6IP5	MEDLINE	29481911	In conclusion, our findings highlight the following: (1) <span class="match term0">RNF185</span> promotes GC metastasis by mediating <span class="match term1">JWA</span> degradation via a ubiquitin-proteasome pathway; (2) the K158 site of <span class="match term1">JWA</span> is essential for its ubiquitination in GC cells	RING	1	Other	H.sapiens
2010	RN185_HUMAN	TIRR_HUMAN	Q96GF1	Q9BRJ7	RNF185	NUDT16L1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2011	RN185_HUMAN	CFTR_HUMAN	Q96GF1	P13569	RNF185	CFTR	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2012	RN186_HUMAN	SESN2_HUMAN	Q9NXI6	P58004	RNF186	SESN2	MEDLINE	31586034	The RING-type E3 ligase <span class="match term0">RNF186</span> ubiquitinates <span class="match term1">Sestrin-2</span> and thereby controls nutrient sensing	RING	1	Other	H.sapiens
2013	RN187_HUMAN	YAP1_HUMAN	Q5TA31	P46937	RNF187	YAP1	MEDLINE	32198343	Immuno-precipitation assay shows that <span class="match term0">RNF187</span> associates with <span class="match term1">YAP</span>, promoting its degradation possibly via inducing <span class="match term1">YAP</span> K48-dependent poly-ubiquitination	RING	1	Other	H.sapiens
2014	RN19A_HUMAN	SODC_HUMAN	Q9NV58	P00441	RNF19A	SOD1	UniProt	RN19A_HUMAN	Unlike wild-type protein, the pathogenics variants <span class="match term1">ALS1</span> Arg-38, Arg-47, Arg-86 and Ala-94 are polyubiquitinated by <span class="match term0">RNF19A</span>; which leads to their proteasomal degradation	RING	1	Training data	H.sapiens
2015	RN19A_HUMAN	P53_HUMAN	Q9NV58	P04637	RNF19A	TP53	MEDLINE	34184814	<span class="match term0">RNF19A</span> interacted with <span class="match term1">p53</span>, shortened <span class="match term1">p53</span> half-life and mediated <span class="match term1">p53</span> ubiquitin-degradation	RING	1	Other	H.sapiens
2016	RN19A_HUMAN	CASR_HUMAN	Q9NV58	P41180	RNF19A	CASR	UniProt	RN19A_HUMAN	Ubiquitinated by <span class="match term0">RNF19A</span>; which induces proteasomal degradation	RING	1	Training data	H.sapiens
2017	RN19A_HUMAN	SNCAP_HUMAN	Q9NV58	Q9Y6H5	RNF19A	SNCAIP	MEDLINE	18004887	Parkin is a multidomain E3 ligase that contains an N-terminal ubiquitin-like domain that interacts with, and effects the ubiquitination of, substrates such as cyclin E, p38 and synphilin	RING	1	Training data	H.sapiens
2018	RN19A_HUMAN	TRAF6_HUMAN	Q9NV58	Q9Y4K3	RNF19A	TRAF6	MEDLINE	29215004	NLRP11 attenuates Toll-like receptor signalling by targeting <span class="match term1">TRAF6</span> for degradation via the ubiquitin ligase <span class="match term0">RNF19A</span>	RING	1	Other	H.sapiens
2019	RN19A_HUMAN	RN19A_HUMAN	Q9NV58	Q9NV58	RNF19A	RNF19A	MEDLINE	11237715	hUbiquitome	RING	1	Other	H.sapiens
2020	RN19B_HUMAN	UCKL1_HUMAN	Q6ZMZ0	Q9NWZ5	RNF19B	UCKL1	MEDLINE	16709802	We demonstrated decreased protein expression and enhanced ubiquitination of URKL-1 in the presence of <span class="match term0">NKLAM</span>	RING	1	Training data	H.sapiens
2021	RING2_HUMAN	H2A2A_HUMAN	Q99496	Q6FI13	RNF2	H2AC18	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2022	RING2_HUMAN	H2A1_HUMAN	Q99496	P0C0S8	RNF2	H2AC11	MEDLINE	16702407	UbiNet 2.0	RING	1	Training data	H.sapiens
2023	RING2_HUMAN	H2AX_HUMAN	Q99496	P16104	RNF2	H2AX	MEDLINE	21676867	<span class="match term0">RNF2</span>-BMI1 interacts with <span class="match term1">H2AX</span> in a DNA damage-dependent manner and is required for monoubiquitination of <span class="match term1">H2AX</span> at Lys(119)/Lys(120)	RING	1	Other	H.sapiens
2024	RING2_HUMAN	RING2_HUMAN	Q99496	Q99496	RNF2	RNF2	MEDLINE	22910419	UbiNet 2.0	RING	1	Training data	H.sapiens
2025	RING2_HUMAN	GEMI_HUMAN	Q99496	O75496	RNF2	GMNN	MEDLINE	20697353	UbiNet 2.0	RING	1	Training data	H.sapiens
2026	RING2_HUMAN	H2A2C_HUMAN	Q99496	Q16777	RNF2	H2AC20	MEDLINE	20351251	UbiNet 2.0	RING	1	Other	H.sapiens
2027	RING2_HUMAN	RYBP_HUMAN	Q99496	Q8N488	RNF2	RYBP	MEDLINE	17070805	UbiNet 2.0	RING	1	Training data	H.sapiens
2028	RING2_HUMAN	AMRA1_HUMAN	Q99496	Q9C0C7	RNF2	AMBRA1	MEDLINE	24980959	Here, we found that <span class="match term0">RNF2</span> associates with <span class="match term1">AMBRA1</span> to act as an E3 ligase to ubiquitinate <span class="match term1">AMBRA1</span> via K48 linkage	RING	1	Other	H.sapiens
2029	RING2_HUMAN	H2AZ_HUMAN	Q99496	P0C0S5	RNF2	H2AZ1	MEDLINE	17636032	UbiNet 2.0	RING	1	Training data	H.sapiens
2030	RING2_HUMAN	RIR1_HUMAN	Q99496	P23921	RNF2	RRM1	MEDLINE	24614341	Here, we identified the E3 ubiquitin-protein ligases <span class="match term0">RNF2</span> and Bmi1 to associate with <span class="match term1">RRM1</span> with subsequent poly-ubiquitination at either position 48 or 63 of ubiquitin	RING	1	Other	H.sapiens
2031	RING2_HUMAN	RASFA_HUMAN	Q99496	A6NK89	RNF2	RASSF10	MEDLINE	34224728	Furthermore, we demonstrate that <span class="match term1">RASSF10</span> is a substrate for the E3 ligase <span class="match term0">RNF2</span> and show that an NPM dependent downregulation of RNF2 expression is critical to maintain stable RASSF10 levels in cells for efficient mitotic arrest	RING	1	Other	H.sapiens
2032	BRE1A_HUMAN	H2B2E_HUMAN	Q5VTR2	Q16778	RNF20	H2BC21	MEDLINE	21443952	UbiNet 2.0	RING	1	Other	H.sapiens
2033	BRE1A_HUMAN	PA2G4_HUMAN	Q5VTR2	Q9UQ80	RNF20	PA2G4	MEDLINE	19037095	We identified <span class="match term0">hBre1</span> acting as an E3 ligase for <span class="match term1">Ebp1</span> and increasing its polyubiquitination	RING	1	Training data	H.sapiens
2034	BRE1A_HUMAN	H2B1A_HUMAN	Q5VTR2	Q96A08	RNF20	HIST1H2BA	UniProt	BRE1A_HUMAN	Monoubiquitination of Lys-122 by the <span class="match term0">RNF20</span>/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation	RING	1	Training data	H.sapiens
2035	BRE1A_HUMAN	H2B1C_HUMAN	Q5VTR2	P62807	RNF20	H2BC4	MEDLINE	16307923	UbiNet 2.0	RING	1	Training data	H.sapiens
2036	RN208_HUMAN	VIME_HUMAN	Q9H0X6	P08670	RNF208	VIM	MEDLINE	31862882	Mechanistically, <span class="match term0">RNF208</span> specifically polyubiquitinated the Lys97 residue within the head domain of <span class="match term1">Vimentin</span> through interaction with the Ser39 residue of phosphorylated <span class="match term1">Vimentin</span>, which exists as a soluble form, eventually facilitating proteasomal degradation of <span class="match term1">Vimentin</span>	RING	1	Other	H.sapiens
2037	RN213_HUMAN	DHE3_HUMAN	Q63HN8	P00367	RNF213	GLUD1	MEDLINE	34269483	Following amino acid deprivation or mTORC1 inhibition, <span class="match term1">GDH1</span> translocates from mitochondria to the cytoplasm, where it becomes ubiquitinated and degraded via the E3 ligase <span class="match term0">RNF213</span>	RING	1	Other	H.sapiens
2038	RN216_HUMAN	TLR8_HUMAN	Q9NWF9	Q9NR97	RNF216	TLR8	MEDLINE	31385713	We show a novel role for Ring Finger Protein 216 (<span class="match term0">RNF216</span>), and E3-ligase which targets <span class="match term1">TLR8</span> for ubiquitination and degradation	RING	1	Other	H.sapiens
2039	RN216_HUMAN	TLR9_HUMAN	Q9NWF9	Q9NR96	RNF216	TLR9	MEDLINE	15107846	UbiNet 2.0	RING	1	Training data	H.sapiens
2040	RN216_HUMAN	TRAF3_HUMAN	Q9NWF9	Q13114	RNF216	TRAF3	MEDLINE	15107846	UbiNet 2.0	RING	1	Training data	H.sapiens
2041	RN216_HUMAN	TLR4_HUMAN	Q9NWF9	O00206	RNF216	TLR4	MEDLINE	15107846	UbiNet 2.0	RING	1	Training data	H.sapiens
2042	RN216_HUMAN	RIPK1_HUMAN	Q9NWF9	Q13546	RNF216	RIPK1	MEDLINE	16968706	UbiNet 2.0	RING	1	Training data	H.sapiens
2043	RN216_HUMAN	RN216_HUMAN	Q9NWF9	Q9NWF9	RNF216	RNF216	UniProt	RN216_HUMAN	Auto-ubiquitinated	RING	1	Training data	H.sapiens
2044	RN220_HUMAN	SIN3B_HUMAN	Q5VTB9	O75182	RNF220	SIN3B	MEDLINE	20170641	Co-expression of <span class="match term0">RNF220</span> promotes the ubiquitination and proteasomal degradation of <span class="match term1">Sin3B</span>	RING	1	Training data	H.sapiens
2045	RN220_HUMAN	RN220_HUMAN	Q5VTB9	Q5VTB9	RNF220	RNF220	UniProt	RN220_HUMAN	Auto-ubiquitinated; leads to proteasomal degradation (By similarity)	RING	1	Training data	H.sapiens
2046	RN220_HUMAN	SIN3A_HUMAN	Q5VTB9	Q96ST3	RNF220	SIN3A	MEDLINE	30500349	<span class="match term0">RNF220</span> protein is an E3 ligase promoting the ubiquitination and proteasomal degradation of <span class="match term1">SIN3</span> Transcription Regulator Family Member B (SIN3B), a chromatin-associated protein, which is primarily expressed in the nucleus of germ cells and plays a vital role in chromatin condensation	RING	1	Other	H.sapiens
2047	RNF25_HUMAN	NKD2_HUMAN	Q96BH1	Q969F2	RNF25	NKD2	MEDLINE	18757723	UbiNet 2.0	RING	1	Training data	H.sapiens
2048	RNF26_HUMAN	STK36_HUMAN	Q9BY78	P09936	RNF26	TMEM173	MEDLINE	25254379	25254379	RING	1	Other	H.sapiens
2049	RNF26_HUMAN	SQSTM_HUMAN	Q9BY78	Q13501	RNF26	SQSTM1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2050	RNF26_HUMAN	IRF3_HUMAN	Q9BY78	Q14653	RNF26	IRF3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2051	RNF26_HUMAN	STING_HUMAN	Q9BY78	Q86WV6	RNF26	STING1	MEDLINE	25254379	In expression screens, we identified RING finger protein 26 (<span class="match term0">RNF26</span>), an E3 ubiquitin ligase, could mediate polyubiquitination of <span class="match term1">MITA</span>	RING	1	Other	H.sapiens
2052	RNF31_HUMAN	KPCB_HUMAN	Q96EP0	P05771	RNF31	PRKCB	MEDLINE	17069764	LUBAC efficiently ubiquitinated activated PKC in vitro, and degradation of activated PKCalpha was delayed in HOIL-1L-deficient cells.	RING	1	Training data	H.sapiens
2053	RNF31_HUMAN	TRAF1_HUMAN	Q96EP0	Q13077	RNF31	TRAF1	MEDLINE	25996949	UbiNet 2.0	RING	1	Other	H.sapiens
2054	RNF31_HUMAN	KPCA_HUMAN	Q96EP0	P17252	RNF31	PRKCA	MEDLINE	17069764	LUBAC efficiently ubiquitinated activated PKC in vitro, and degradation of activated <span class="match term1">PKCalpha</span> was delayed in HOIL-1L-deficient cells.	RING	1	Training data	H.sapiens
2055	RNF31_HUMAN	CASP1_HUMAN	Q96EP0	P29466	RNF31	CASP1	MEDLINE	32122970	UbiNet 2.0	RING	1	Other	H.sapiens
2056	RNF31_HUMAN	NR0B1_HUMAN	Q96EP0	P51843	RNF31	NR0B1	MEDLINE	19237537	Our data suggest that <span class="match term0">RNF31</span> functions to stabilize <span class="match term1">DAX-1</span>, which might be linked to <span class="match term1">DAX-1</span> monoubiquitination	RING	1	Training data	H.sapiens
2057	RNF31_HUMAN	TRI25_HUMAN	Q96EP0	Q14258	RNF31	TRIM25	MEDLINE	21292167	UbiNet 2.0	RING	1	Training data	H.sapiens
2058	RNF31_HUMAN	NEMO_HUMAN	Q96EP0	Q9Y6K9	RNF31	IKBKG	MEDLINE	24469399	UbiNet 2.0	RING	1	Other	H.sapiens
2059	RNF31_HUMAN	RIPK1_HUMAN	Q96EP0	Q13546	RNF31	RIPK1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2060	RNF31_HUMAN	DDX58_HUMAN	Q96EP0	O95786	RNF31	DDX58	MEDLINE	21292167	UbiNet 2.0	RING	1	Training data	H.sapiens
2061	RNF34_HUMAN	CASPA_HUMAN	Q969K3	Q92851	RNF34	CASP10	MEDLINE	15069192	UbiNet 2.0	RING	1	Training data	H.sapiens
2062	RNF34_HUMAN	P53_HUMAN	Q969K3	P04637	RNF34	TP53	MEDLINE	17121812	CARPs physically interact with and ubiquitinate <span class="match term1">p53</span>, targeting it for degradation in the absence of MDM2. Unlike MDM2 or other E3 ligases known to target <span class="match term1">p53</span>, <span class="match term0">CARP1</span> and CARP2 appear to target phosphorylated <span class="match term1">p53</span> for ubiquitination and degradation.	RING	1	Training data	H.sapiens
2063	RNF34_HUMAN	PRGC1_HUMAN	Q969K3	Q9UBK2	RNF34	PPARGC1A	MEDLINE	22064484	UbiNet 2.0	RING	1	Training data	H.sapiens
2064	RNF34_HUMAN	NOD1_HUMAN	Q969K3	Q9Y239	RNF34	NOD1	MEDLINE	25012219	CONCLUSION: These findings confirm that <span class="match term0">RNF34</span> is a negative regulator of the <span class="match term1">NOD1</span> pathway through direct interaction and ubiquitination of <span class="match term1">NOD1</span>, and suggest a novel regulatory mechanism of <span class="match term1">NOD1</span>.	RING	1	Other	H.sapiens
2065	RNF34_HUMAN	RIPK1_HUMAN	Q969K3	Q13546	RNF34	RIPK1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2066	RNF34_HUMAN	CASP8_HUMAN	Q969K3	Q14790	RNF34	CASP8	MEDLINE	15069192	UbiNet 2.0	RING	1	Training data	H.sapiens
2067	RNF38_HUMAN	LDB1_HUMAN	Q9H0F5	Q86U70	RNF38	LDB1	MEDLINE	32021282	And in this study, we confirmed that <span class="match term1">LDB1</span> was a novel substrate of <span class="match term0">RNF38</span>, and <span class="match term1">LDB1</span> was reported to be elevated in CRC and its high expression was associated with poor prognosis of CRC patients.	RING	1	Other	H.sapiens
2068	RNF38_HUMAN	P53_HUMAN	Q9H0F5	P04637	RNF38	TP53	MEDLINE	23973461	UbiNet 2.0	RING	1	Training data	H.sapiens
2069	RNF38_HUMAN	PTN6_HUMAN	Q9H0F5	P29350	RNF38	PTPN6	MEDLINE	30112836	Further studies showed that <span class="match term0">RNF38</span> interacts with the nonreceptor tyrosine phosphatase SH2-containing protein tyrosine phosphatase 1 (<span class="match term1">SHP-1</span>) and induces the polyubiquitination of <span class="match term1">SHP-1</span>, which leads to destabilization of <span class="match term1">SHP-1</span> and promotion of STAT3 signaling in gastric cancer cells	RING	1	Other	H.sapiens
2070	RNF38_HUMAN	RUNX1_HUMAN	Q9H0F5	Q01196	RNF38	RUNX1	MEDLINE	30309654	In this study, we showed that a nuclear ubiquitin ligase <span class="match term0">RNF38</span> induced ubiquitination of <span class="match term1">RUNX1</span>	RING	1	Other	H.sapiens
2071	RNF39_HUMAN	DDX3X_HUMAN	Q9H2S5	O00571	RNF39	DDX3X	MEDLINE	33674311	Here, we show that the E3 ubiquitin ligase <span class="match term0">RNF39</span> inhibits RLR pathways through mediating K48-linked ubiquitination and proteasomal degradation of <span class="match term1">DDX3X</span>	RING	1	Other	H.sapiens
2072	RNF4_HUMAN	PML_HUMAN	P78317	P29590	RNF4	PML	MEDLINE	20943951	These studies indicate that arsenic induces the rapid reorganization of the cell nucleus by SUMO modification of nuclear body-associated <span class="match term1">PML</span> and uptake of the ubiquitin E3 ligase <span class="match term0">RNF4</span> leading to the ubiquitin-mediated degradation of <span class="match term1">PML</span>	RING	1	Training data	H.sapiens
2073	RNF4_HUMAN	SP1_HUMAN	P78317	P08047	RNF4	SP1	MEDLINE	21983342	21983342	RING	1	Other	H.sapiens
2074	RNF4_HUMAN	ZN746_HUMAN	P78317	Q6NUN9	RNF4	ZNF746	MEDLINE	32197837	Conversely, the SUMO E3 ligase PIASy inhibited the <span class="match term0">RNF4</span>-mediated ubiquitination of <span class="match term1">PARIS</span> and blocked the <span class="match term0">RNF4</span>-mediated relief of <span class="match term1">PARIS</span>-mediated transcriptional repression.	RING	1	Other	H.sapiens
2075	RNF4_HUMAN	RNF4_HUMAN	P78317	P78317	RNF4	RNF4	MEDLINE	14987998	UbiNet 2.0	RING	1	Training data	H.sapiens
2076	RNF4_HUMAN	CENPI_HUMAN	P78317	Q92674	RNF4	CENPI	MEDLINE	20212317	UbiNet 2.0	RING	1	Training data	H.sapiens
2077	RNF4_HUMAN	CTIP_HUMAN	P78317	Q99708	RNF4	RBBP8	MEDLINE	33723063	SUMO-modified hyperphosphorylated <span class="match term1">CtIP</span> is targeted by the SUMO-dependent E3 ubiquitin ligase <span class="match term0">RNF4</span> for polyubiquitination and subsequent degradation	RING	1	Other	H.sapiens
2078	RNF4_HUMAN	SUMO2_HUMAN	P78317	P61956	RNF4	SUMO2	MEDLINE	18408734	<span class="match term0">RNF4</span> is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation.	RING	1	Other	H.sapiens
2079	RNF4_HUMAN	PARP1_HUMAN	P78317	P09874	RNF4	PARP1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2080	RNF4_HUMAN	ETV4_HUMAN	P78317	P43268	RNF4	ETV4	UniProt	RNF4_HUMAN	Probably polyubiquitinated by <span class="match term0">RNF4</span> and deubiquitinated by USP2	RING	1	Training data	H.sapiens
2081	RNF4_HUMAN	EPAS1_HUMAN	P78317	Q99814	RNF4	EPAS1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2082	RNF4_HUMAN	DAND5_HUMAN	P78317	Q8N907	RNF4	DAND5	MEDLINE	21983342	UbiNet 2.0	RING	1	Other	H.sapiens
2083	RNF4_HUMAN	ATX1_HUMAN	P78317	P54253	RNF4	ATXN1	MEDLINE	24882209	UbiNet 2.0	RING	1	Other	H.sapiens
2084	BRE1B_HUMAN	STX1A_HUMAN	O75150	Q16623	RNF40	STX1A	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2085	BRE1B_HUMAN	H2B2E_HUMAN	O75150	Q16778	RNF40	H2BC21	MEDLINE	16307923	UbiNet 2.0	RING	1	Other	H.sapiens
2086	BRE1B_HUMAN	H2B1A_HUMAN	O75150	Q96A08	RNF40	H2BC1	MEDLINE	16307923	UbiNet 2.0	RING	1	Training data	H.sapiens
2087	BRE1B_HUMAN	PA2G4_HUMAN	O75150	Q9UQ80	RNF40	PA2G4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2088	RNF41_HUMAN	ZAP70_HUMAN	Q9H4P4	P43403	RNF41	ZAP70	MEDLINE	32034311	Publisher Correction: K33-linked polyubiquitination of <span class="match term1">Zap70</span> by <span class="match term0">Nrdp1</span> controls CD8+ T cell activation	RING	1	Other	H.sapiens
2089	RNF41_HUMAN	ERBB3_HUMAN	Q9H4P4	P21860	RNF41	ERBB3	MEDLINE	15632191	Interaction between human parkin and the mammalian RING finger protein homologue <span class="match term0">Nrdp1</span>/FLRF, a ubiquitin-protein isopeptide ligase that ubiquitinates <span class="match term1">ErbB3</span> and ErbB4, was validated by in vitro binding assay, co-immunoprecipitation, and immunofluorescence co-localization	RING	1	Training data	H.sapiens
2090	RNF41_HUMAN	PRKN2_HUMAN	Q9H4P4	O60260	RNF41	PARK2	MEDLINE	19800834	The E3 ubiquitin ligase <span class="match term0">Nrdp1</span> is shown to interact with the N terminal of Parkin (the first 76 amino acids) and catalyze degradation of Parkin via the ubiquitin-proteasome pathway, suggesting that <span class="match term0">Nrdp1</span> may be involved in the development of PD via the regulation of Parkin, We believe we are the first to have screened PD patients for mutations in the <span class="match term0">Nrdp1</span> gene to determine the association between these variants and PD	RING	1	Training data	H.sapiens
2091	RNF41_HUMAN	CEBPB_HUMAN	Q9H4P4	P17676	RNF41	CEBPB	MEDLINE	22707723	UbiNet 2.0	RING	1	Training data	H.sapiens
2092	RNF41_HUMAN	BIRC6_HUMAN	Q9H4P4	Q9NR09	RNF41	BIRC6	MEDLINE	15314180	UbiNet 2.0	RING	1	Training data	H.sapiens
2093	RNF41_HUMAN	CYBP_HUMAN	Q9H4P4	Q9HB71	RNF41	CACYBP	MEDLINE	31754404	<span class="match term0">RNF41</span> recruited <span class="match term1">CACYBP</span> by its C-terminal substrate binding domain, subsequently ubiquitinating <span class="match term1">CACYBP</span> and promoting its degradation in both proteasome- and lysosome-dependent pathways	RING	1	Other	H.sapiens
2094	RNF41_HUMAN	TBK1_HUMAN	Q9H4P4	Q9UHD2	RNF41	TBK1	MEDLINE	19483718	UbiNet 2.0	RING	1	Training data	H.sapiens
2095	RNF41_HUMAN	RNF41_HUMAN	Q9H4P4	Q9H4P4	RNF41	RNF41	MEDLINE	15314180	These observations suggest that <span class="match term0">Nrdp1</span> self-ubiquitination and stability could play an important role in regulating the activity of this protein	RING	1	Training data	H.sapiens
2096	RNF41_HUMAN	IRF3_HUMAN	Q9H4P4	Q14653	RNF41	IRF3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2097	RNF41_HUMAN	PERE_HUMAN	Q9H4P4	P11678	RNF41	EPX	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2098	RNF41_HUMAN	ERBB4_HUMAN	Q9H4P4	Q15303	RNF41	ERBB4	MEDLINE	15632191	Interaction between human parkin and the mammalian RING finger protein homologue <span class="match term0">Nrdp1</span>/FLRF, a ubiquitin-protein isopeptide ligase that ubiquitinates ErbB3 and <span class="match term1">ErbB4</span>, was validated by in vitro binding assay, co-immunoprecipitation, and immunofluorescence co-localization	RING	1	Training data	H.sapiens
2099	RNF41_HUMAN	MYD88_HUMAN	Q9H4P4	Q99836	RNF41	MYD88	MEDLINE	19483718	UbiNet 2.0	RING	1	Training data	H.sapiens
2100	RNF41_HUMAN	ZN746_HUMAN	Q9H4P4	Q6NUN9	RNF41	ZNF746	MEDLINE	18541373	UbiNet 2.0	RING	1	Training data	H.sapiens
2101	RNF43_HUMAN	RNF43_HUMAN	Q68DV7	Q68DV7	RNF43	RNF43	MEDLINE	18313049	UbiNet 2.0	RING	1	Training data	H.sapiens
2102	RNF43_HUMAN	AKP8L_HUMAN	Q68DV7	Q9ULX6	RNF43	AKAP8L	MEDLINE	18313049	<span class="match term1">HAP95</span> is ubiquitylated and subjected to a proteasome-dependent degradation pathway, however, the experiments in which 293 cells expressing both <span class="match term0">RNF43</span> and <span class="match term1">HAP95</span> were treated with a proteasome inhibitor, MG132, show that <span class="match term1">HAP95</span> is unlikely to serve as a substrate of <span class="match term0">RNF43</span> ubiquitin ligase	RING	1	Training data	H.sapiens
2103	RNF43_HUMAN	FZD5_HUMAN	Q68DV7	Q13467	RNF43	FZD5	MEDLINE	22895187	UbiNet 2.0	RING	1	Other	H.sapiens
2104	RNF5_HUMAN	SCAP_HUMAN	Q99942	Q12770	RNF5	SCAP	MEDLINE	32054686	Mechanistic studies revealed that <span class="match term0">RNF5</span> binds to the transmembrane domain of <span class="match term1">SCAP</span> and ubiquitinates the Lys-305 located in cytosolic loop 2 of <span class="match term1">SCAP</span>	RING	1	Other	H.sapiens
2105	RNF5_HUMAN	PAXI_HUMAN	Q99942	P49023	RNF5	PXN	MEDLINE	12861019	<span class="match term0">RNF5</span> requires intact RING and C-terminal domains to mediate paxillin ubiquitination	RING	1	Training data	H.sapiens
2106	RNF5_HUMAN	MAVS_HUMAN	Q99942	Q7Z434	RNF5	MAVS	MEDLINE	20483786	UbiNet 2.0	RING	1	Other	H.sapiens
2107	RNF5_HUMAN	SOPA_SALTY	Q99942	Q8ZNR3	RNF5	sopA	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2108	RNF5_HUMAN	STING_HUMAN	Q99942	Q86WV6	RNF5	STING1	MEDLINE	19285439	UbiNet 2.0	RING	1	Training data	H.sapiens
2109	RNF5_HUMAN	S26A4_HUMAN	Q99942	O43511	RNF5	SLC26A4	MEDLINE	22750442	UbiNet 2.0	RING	1	Training data	H.sapiens
2110	RNF5_HUMAN	JKAMP_HUMAN	Q99942	Q9P055	RNF5	JKAMP	MEDLINE	19269966	Regulation of endoplasmic reticulum-associated degradation by <span class="match term0">RNF5</span>-dependent ubiquitination of JNK-associated membrane protein (<span class="match term1">JAMP</span>)	RING	1	Training data	H.sapiens
2111	RNF5_HUMAN	IRF3_HUMAN	Q99942	Q14653	RNF5	IRF3	MEDLINE	33684176	JMJD6 negatively regulates cytosolic RNA induced antiviral signaling by recruiting <span class="match term0">RNF5</span> to promote activated <span class="match term1">IRF3</span> K48 ubiquitination	RING	1	Other	H.sapiens
2112	RNF5_HUMAN	CFTR_HUMAN	Q99942	P13569	RNF5	CFTR	MEDLINE	21148293	JB12 cooperates with cytosolic Hsc70 and the ubiquitin ligase <span class="match term0">RMA1</span> to target <span class="match term1">CFTR</span> and <span class="match term1">CFTR</span> F508 for degradation	RING	1	Training data	H.sapiens
2113	RNF5_HUMAN	UB2L3_HUMAN	Q99942	P68036	RNF5	UBE2L3	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2114	RNF6_HUMAN	ANDR_HUMAN	Q9Y252	P10275	RNF6	AR	MEDLINE	19345326	<span class="match term0">RNF6</span> induces <span class="match term1">AR</span> ubiquitination and promotes <span class="match term1">AR</span> transcriptional activity	RING	1	Training data	H.sapiens
2115	RNF6_HUMAN	LIMK1_HUMAN	Q9Y252	P53667	RNF6	LIMK1	MEDLINE	17188549	<span class="match term0">Rnf6</span> is an E3 ubiquitin ligase responsible for <span class="match term1">LIMK</span> degradation in neurons	RING	1	Training data	H.sapiens
2116	RNF6_HUMAN	MAD1_HUMAN	Q9Y252	Q05195	RNF6	MXD1	MEDLINE	34094667	Lastly, <span class="match term0">RNF6</span> promoted the degradation of <span class="match term1">MAD1</span> via the ubiquitin-proteasome pathway, and this reduction in the <span class="match term1">MAD1</span> levels enabled c-Myc to promote the Warburg effect in PC	RING	1	Other	H.sapiens
2117	RNF6_HUMAN	FOXA1_HUMAN	Q9Y252	P55317	RNF6	FOXA1	MEDLINE	30496760	<span class="match term0">RNF6</span> facilitates metastasis and radioresistance in hepatocellular carcinoma through ubiquitination of <span class="match term1">FoxA1</span>	RING	1	Other	H.sapiens
2118	RNF6_HUMAN	TLE3_HUMAN	Q9Y252	Q04726	RNF6	TLE3	MEDLINE	29374067	<span class="match term0">RNF6</span> Promotes Colorectal Cancer by Activating the Wnt/beta-Catenin Pathway via Ubiquitination of <span class="match term1">TLE3</span>	RING	1	Other	H.sapiens
2119	RNF6_HUMAN	LIMS1_HUMAN	Q9Y252	P48059	RNF6	LIMS1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2120	RNF6_HUMAN	NR0B2_HUMAN	Q9Y252	Q15466	RNF6	NR0B2	MEDLINE	30323630	Further studies showed that <span class="match term0">RNF6</span> regulated the stability of <span class="match term1">SHP</span>-1 by inducing its polyubiquitination	RING	1	Other	H.sapiens
2121	RNF8_HUMAN	NONO_HUMAN	O76064	Q15233	RNF8	NONO	MEDLINE	30445466	We found that: (i) <span class="match term0">RNF8</span> ubiquitinates <span class="match term1">NONO</span> and (ii) UV radiation triggers <span class="match term1">NONO</span> ubiquitination and its subsequent degradation	RING	1	Other	H.sapiens
2122	RNF8_HUMAN	CTNB1_HUMAN	O76064	P35222	RNF8	CTNNB1	MEDLINE	32549753	In addition, <span class="match term0">RNF8</span> interacted with <span class="match term1">beta-catenin</span> and facilitated its nuclear translocation by conjugating K63 polyubiquitination on it	RING	1	Other	H.sapiens
2123	RNF8_HUMAN	NBN_HUMAN	O76064	O60934	RNF8	NBN	MEDLINE	23115235	We identified a novel interaction of the E3 ubiquitin ligase <span class="match term0">RNF8</span> with <span class="match term1">Nbs1</span>, a key regulator of DNA double-strand break (DSB) repair	RING	1	Other	H.sapiens
2124	RNF8_HUMAN	OTUB1_HUMAN	O76064	Q96FW1	RNF8	OTUB1	MEDLINE	21130715	UbiNet 2.0	RING	1	Training data	H.sapiens
2125	RNF8_HUMAN	CHK2_HUMAN	O76064	O96017	RNF8	CHEK2	MEDLINE	22266820	UbiNet 2.0	RING	1	Other	H.sapiens
2126	RNF8_HUMAN	H2A2C_HUMAN	O76064	Q16777	RNF8	H2AC20	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2127	RNF8_HUMAN	BLM_HUMAN	O76064	P54132	RNF8	BLM	MEDLINE	23708797	UbiNet 2.0	RING	1	Training data	H.sapiens
2128	RNF8_HUMAN	H2AX_HUMAN	O76064	P16104	RNF8	H2AFX	MEDLINE	20385748	Moreover, similar to H2AX but different from 53BP1 deficiency, <span class="match term0">RNF8</span>(-/-) males are sterile, and this is associated with defective ubiquitylation of the XY chromatin	RING	1	Training data	H.sapiens
2129	RNF8_HUMAN	H2A1A_HUMAN	O76064	Q96QV6	RNF8	HIST1H2AA	UniProt	RNF8_HUMAN	Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases <span class="match term0">RNF8</span> and RNF168, leading to the recruitment of repair proteins to sites of DNA damage	RING	1	Training data	H.sapiens
2130	RNF8_HUMAN	H2A2B_HUMAN	O76064	Q8IUE6	RNF8	H2AC21	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2131	RNF8_HUMAN	KMT5A_HUMAN	O76064	Q9NQR1	RNF8	KMT5A	MEDLINE	33710666	<span class="match term1">KMT5A</span> is a newly identified substrate of <span class="match term0">RNF8</span> in vitro and in vivo.	RING	1	Other	H.sapiens
2132	RNF8_HUMAN	PCNA_HUMAN	O76064	P12004	RNF8	PCNA	MEDLINE	18948756	<span class="match term1">PCNA</span> is ubiquitinated by <span class="match term0">RNF8</span>	RING	1	Training data	H.sapiens
2133	RNF8_HUMAN	TPP1_HUMAN	O76064	O14773	RNF8	TPP1	MEDLINE	22101936	UbiNet 2.0	RING	1	Training data	H.sapiens
2134	RNF8_HUMAN	RECQ4_HUMAN	O76064	O94761	RNF8	RECQL4	MEDLINE	33674555	<span class="match term0">RNF8</span> ubiquitinates <span class="match term1">RecQL4</span> and promotes its dissociation from DNA double strand breaks	RING	1	Other	H.sapiens
2135	RNF8_HUMAN	LMBL2_HUMAN	O76064	Q969R5	RNF8	L3MBTL2	MEDLINE	31225475	In this paper we identify lethal(3) malignant brain tumor like 2 (<span class="match term1">L3MBTL2</span>) as the substrate of <span class="match term0">RNF8</span>	RING	1	Other	H.sapiens
2136	RNF8_HUMAN	RNF8_HUMAN	O76064	O76064	RNF8	RNF8	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2137	RNF8_HUMAN	XRCC5_HUMAN	O76064	P13010	RNF8	XRCC5	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2138	RNF8_HUMAN	KDM4A_HUMAN	O76064	O75164	RNF8	KDM4A	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2139	RNF8_HUMAN	H2A1_HUMAN	O76064	P0C0S8	RNF8	H2AC11	MEDLINE	18001824	UbiNet 2.0	RING	1	Training data	H.sapiens
2140	RNF8_HUMAN	DPOD4_HUMAN	O76064	Q9HCU8	RNF8	POLD4	MEDLINE	23233665	UbiNet 2.0	RING	1	Training data	H.sapiens
2141	RNF8_HUMAN	PML_HUMAN	O76064	P29590	RNF8	PML	MEDLINE	23708797	UbiNet 2.0	RING	1	Training data	H.sapiens
2142	RNF8_HUMAN	H2B1A_HUMAN	O76064	Q96A08	RNF8	H2BC1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2143	RNFT2_HUMAN	IL3RA_HUMAN	Q96EX2	P26951	RNFT2	IL3RA	MEDLINE	31990690	Here we found that <span class="match term0">RNFT2</span> (RING finger transmembrane-domain containing protein 2, also TMEM118), a previously uncharacterized RING finger ubiquitin E3 ligase, negatively regulated IL3-dependent cellular responses through <span class="match term1">IL3Ralpha</span> ubiquitination and degradation in the proteasome	RING	1	Other	H.sapiens
2144	RSAD2_HUMAN	IRAK1_HUMAN	Q8WXG1	P51617	RSAD2	IRAK1	MEDLINE	31921110	Furthermore, dual-luciferase reporter and Co-IP assays showed gD and <span class="match term0">viperin</span> interaction leaded to the increase of IRF7-mediated IFN-beta expression through promoting <span class="match term0">viperin</span> and <span class="match term1">IRAK1</span> interaction and facilitating K63-linked <span class="match term1">IRAK1</span> polyubiquitination	Other	1	Other	H.sapiens
2145	ARRS_HUMAN	IKBA_HUMAN	P10523	P25963	SAG	NFKBIA	MEDLINE	23136067	UbiNet 2.0	Other	1	Training data	H.sapiens
2146	ARRS_HUMAN	CDN1B_HUMAN	P10523	P46527	SAG	CDKN1B	MEDLINE	23136067	UbiNet 2.0	Other	1	Training data	H.sapiens
2147	ARRS_HUMAN	HIF1A_HUMAN	P10523	Q16665	SAG	HIF1A	MEDLINE	23136067	UbiNet 2.0	Other	1	Training data	H.sapiens
2148	ARRS_HUMAN	JUN_HUMAN	P10523	P05412	SAG	JUN	MEDLINE	23136067	UbiNet 2.0	Other	1	Training data	H.sapiens
2149	ARRS_HUMAN	UB2R1_HUMAN	P10523	P49427	SAG	CDC34	MEDLINE	10851089	UbiNet 2.0	Other	1	Training data	H.sapiens
2150	ARRS_HUMAN	APR_HUMAN	P10523	Q13794	SAG	PMAIP1	MEDLINE	23136067	UbiNet 2.0	Other	1	Training data	H.sapiens
2151	ARRS_HUMAN	DPTOR_HUMAN	P10523	Q8TB45	SAG	DEPTOR	MEDLINE	23136067	UbiNet 2.0	Other	1	Training data	H.sapiens
2152	ARRS_HUMAN	NF1_HUMAN	P10523	P21359	SAG	NF1	MEDLINE	23136067	UbiNet 2.0	Other	1	Training data	H.sapiens
2153	SH3R1_HUMAN	KCNJ1_HUMAN	Q7Z6J0	P48048	SH3RF1	KCNJ1	MEDLINE	19710010	UbiNet 2.0	RING	1	Training data	H.sapiens
2154	SH3R1_HUMAN	HEY2_HUMAN	Q7Z6J0	Q9UBP5	SH3RF1	HEY2	MEDLINE	17420289	UbiNet 2.0	RING	1	Training data	H.sapiens
2155	SH3R1_HUMAN	HGS_HUMAN	Q7Z6J0	O14964	SH3RF1	HGS	MEDLINE	16084064	Finally, we demonstrate that JNK1 does not interact with <span class="match term1">Hrs</span> under the conditions of <span class="match term0">POSH</span> interacted with <span class="match term1">Hrs</span>, but instead reduces the <span class="match term0">POSH</span>-catalyzed ubiquitination of <span class="match term1">Hrs</span> and their reciprocal interaction	RING	1	Training data	H.sapiens
2156	SH3R1_HUMAN	KCNJ2_HUMAN	Q7Z6J0	P63252	SH3RF1	KCNJ2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2157	SH3R1_HUMAN	HERP1_HUMAN	Q7Z6J0	Q15011	SH3RF1	HERPUD1	MEDLINE	17420289	UbiNet 2.0	RING	1	Other	H.sapiens
2158	SH3R1_HUMAN	PDC6I_HUMAN	Q7Z6J0	Q8WUM4	SH3RF1	PDCD6IP	MEDLINE	19393081	RESULTS: In this study we identified <span class="match term1">ALIX</span> as a <span class="match term0">POSH</span> ubiquitination substrate in human cells: <span class="match term0">POSH</span> induces the ubiquitination of <span class="match term1">ALIX</span> that is modified on several lysine residues in vivo and in vitro	RING	1	Training data	H.sapiens
2159	SH3R1_HUMAN	SH3R1_HUMAN	Q7Z6J0	Q7Z6J0	SH3RF1	SH3RF1	MEDLINE	15659549	hUbiquitome	RING	1	Other	H.sapiens
2160	SHRPN_HUMAN	YAP1_HUMAN	Q9H0F6	P46937	SHARPIN	YAP1	MEDLINE	31884247	Immuno-precipitation assay shows that <span class="match term0">SHARPIN</span> associates with <span class="match term1">YAP</span>, promoting <span class="match term1">YAP</span> degradation possibly via inducing <span class="match term1">YAP</span> K48-dependent poly-ubiquitination	Other	1	Other	H.sapiens
2161	SHPRH_HUMAN	PCNA_HUMAN	Q149N8	P12004	SHPRH	PCNA	UniProt	SHPRH_HUMAN	Acts together with the E3 ligases, HLTF or <span class="match term0">SHPRH</span>, in the 'Lys-63'-linked poly-ubiquitination of <span class="match term1">PCNA</span> upon genotoxic stress, which is required for DNA repair (By similarity)	RING	1	Training data	H.sapiens
2162	SIAH1_HUMAN	EGLN1_HUMAN	Q8IUQ4	Q9GZT9	SIAH1	EGLN1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2163	SIAH1_HUMAN	COM1_HUMAN	Q8IUQ4	Q99708	SIAH1	RBBP8	MEDLINE	14654780	Our results suggest that p21(Waf-1/Cip-1) induction by <span class="match term0">SIAH-1</span> could not be mediated by <span class="match term1">CtIP</span> degradation	RING	1	Training data	H.sapiens
2164	SIAH1_HUMAN	SYUA_HUMAN	Q8IUQ4	P37840	SIAH1	SNCA	MEDLINE	18065497	Our findings suggest that <span class="match term0">Siah-1</span>-mediated alpha-synuclein ubiquitination may play a critical role in Lewy body formation and PD pathogenesis	RING	1	Training data	H.sapiens
2165	SIAH1_HUMAN	EGLN2_HUMAN	Q8IUQ4	Q96KS0	SIAH1	EGLN2	MEDLINE	17047048	UbiNet 2.0	RING	1	Training data	H.sapiens
2166	SIAH1_HUMAN	CYBP_HUMAN	Q8IUQ4	Q9HB71	SIAH1	CACYBP	MEDLINE	20181957	UbiNet 2.0	RING	1	Other	H.sapiens
2167	SIAH1_HUMAN	HIPK2_HUMAN	Q8IUQ4	Q9H2X6	SIAH1	HIPK2	MEDLINE	19250734	Degradation of <span class="match term1">HIPK2</span> by <span class="match term0">Siah1</span> was blocked by forced expression of either Mixed Lineage Kinase-3 or Epstein-Barr viral protein LMP-1, as well as by DNA damaging stimuli	RING	1	Training data	H.sapiens
2168	SIAH1_HUMAN	OBF1_HUMAN	Q8IUQ4	Q16633	SIAH1	POU2AF1	UniProt	SIAH1_HUMAN	Ubiquitinated; mediated by <span class="match term0">SIAH1</span> or SIAH2 and leading to its subsequent proteasomal degradation (Probable)	RING	1	Training data	H.sapiens
2169	SIAH1_HUMAN	CTNB1_HUMAN	Q8IUQ4	P35222	SIAH1	CTNNB1	MEDLINE	12147676	Moreover, ES uses a pathway independent of the <span class="match term0">Siah1</span> protein in targeting <span class="match term1">beta-catenin</span> for proteasome-mediated degradation	RING	1	Training data	H.sapiens
2170	SIAH1_HUMAN	ELL_HUMAN	Q8IUQ4	P55199	SIAH1	ELL	MEDLINE	32152128	Mechanistically, we show that p300-mediated site-specific acetylation increases, whereas HDAC3-mediated deacetylation decreases, <span class="match term1">ELL</span> stability through polyubiquitylation by the E3 ubiquitin ligase <span class="match term0">Siah1</span>	RING	1	Other	H.sapiens
2171	SIAH1_HUMAN	ELL2_HUMAN	Q8IUQ4	O00472	SIAH1	ELL2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2172	SIAH1_HUMAN	MARE3_HUMAN	Q8IUQ4	Q9UPY8	SIAH1	MAPRE3	MEDLINE	19696028	The ubiquitin-protein isopeptide ligase <span class="match term0">SIAH-1</span> facilitates <span class="match term1">EB3</span> polyubiquitination and subsequent proteasome-mediated degradation, whereas <span class="match term0">SIAH-1</span> knockdown increases <span class="match term1">EB3</span> stability and steady-state levels	RING	1	Training data	H.sapiens
2173	SIAH1_HUMAN	HIF1A_HUMAN	Q8IUQ4	Q16665	SIAH1	HIF1A	MEDLINE	17047048	Here, we explore the mechanism for <span class="match term1">HIF1alpha</span> activation by LMP1 in nasopharyngeal epithelial cells: LMP1 up-regulates the level of <span class="match term0">Siah1</span> E3 ubiquitin ligase by enhancing its stability, which subsequently induces proteasomal degradation of prolyl HIF-hydroxylases 1 and 3 that normally mark <span class="match term1">HIF1alpha</span> for degradation	RING	1	Training data	H.sapiens
2174	SIAH1_HUMAN	SNCAP_HUMAN	Q8IUQ4	Q9Y6H5	SIAH1	SNCAIP	MEDLINE	14506261	<span class="match term0">Siah-1</span> facilitated synphilin-1 degradation via the ubiquitin-proteasome pathway more efficiently than Parkin	RING	1	Training data	H.sapiens
2175	SIAH1_HUMAN	PML_HUMAN	Q8IUQ4	P29590	SIAH1	PML	UniProt	SIAH1_HUMAN	Ubiquitinated; mediated by <span class="match term0">SIAH1</span> or SIAH2 and leading to its subsequent proteasomal degradation	RING	1	Training data	H.sapiens
2176	SIAH1_HUMAN	NUMB_HUMAN	Q8IUQ4	P49757	SIAH1	NUMB	MEDLINE	18213731	Seven-in-absentia homologue 1 (<span class="match term0">Siah1</span>) is an E3 ubiquitin ligase that regulates the ubiquitination and proteasome-dependent degradation of a number of proteins	RING	1	Training data	H.sapiens
2177	SIAH1_HUMAN	S10AA_HUMAN	Q8IUQ4	P60903	SIAH1	S100A10	MEDLINE	29321312	The E3 Ubiquitin Ligase <span class="match term0">Siah-1</span> Suppresses Avian Reovirus Infection by Targeting <span class="match term1">p10</span> for Degradation	RING	1	Other	H.sapiens
2178	SIAH1_HUMAN	MYB_HUMAN	Q8IUQ4	P10242	SIAH1	MYB	UniProt	SIAH1_HUMAN	Ubiquitinated; mediated by <span class="match term0">SIAH1</span> and leading to its subsequent proteasomal degradation (Probable)	RING	1	Training data	H.sapiens
2179	SIAH1_HUMAN	EGLN3_HUMAN	Q8IUQ4	Q9H6Z9	SIAH1	EGLN3	MEDLINE	17047048	UbiNet 2.0	RING	1	Training data	H.sapiens
2180	SIAH1_HUMAN	AFF1_HUMAN	Q8IUQ4	P51825	SIAH1	AFF1	MEDLINE	15221006	The underlying oncogenic mechanism involves the two E3 ubiquitin ligases <span class="match term0">SIAH1</span> and SIAH2, the N-terminal portion of <span class="match term1">AF4</span> and the protection of the <span class="match term1">AF4</span>.MLL fusion protein against proteosomal degradation	RING	1	Training data	H.sapiens
2181	SIAH1_HUMAN	AKT3_HUMAN	Q8IUQ4	Q9Y243	SIAH1	AKT3	MEDLINE	31471318	Here we show <span class="match term0">Siah1</span> as an ubiquitin ligase that preferentially interacts with <span class="match term1">Akt3</span> and facilitates ubiquitination and degradation of <span class="match term1">Akt3</span>	RING	1	Other	H.sapiens
2182	SIAH1_HUMAN	TERF2_HUMAN	Q8IUQ4	Q15554	SIAH1	TERF2	MEDLINE	21057505	UbiNet 2.0	RING	1	Other	H.sapiens
2183	SIAH1_HUMAN	XIAP_HUMAN	Q8IUQ4	P98170	SIAH1	XIAP	MEDLINE	21185211	UbiNet 2.0	RING	1	Training data	H.sapiens
2184	SIAH1_HUMAN	ACK1_HUMAN	Q8IUQ4	Q07912	SIAH1	TNK2	MEDLINE	23208506	UbiNet 2.0	RING	1	Training data	H.sapiens
2185	SIAH1_HUMAN	IFI27_HUMAN	Q8IUQ4	P40305	SIAH1	IFI27	MEDLINE	29024247	CacyBP/SIP inhibits the migration and invasion behaviors of glioblastoma cells through activating <span class="match term0">Siah1</span> mediated ubiquitination and degradation of cytoplasmic <span class="match term1">p27</span>	RING	1	Other	H.sapiens
2186	SIAH1_HUMAN	HIF1N_HUMAN	Q8IUQ4	Q9NWT6	SIAH1	HIF1AN	MEDLINE	18280659	Immunoprecipitation assay and ubiquitination assay revealed that <span class="match term0">Siah-1</span> interacted with, and ubiquitinated FIH	RING	1	Training data	H.sapiens
2187	SIAH1_HUMAN	PLCE1_HUMAN	Q8IUQ4	Q9P212	SIAH1	PLCE1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2188	SIAH1_HUMAN	BAG1_HUMAN	Q8IUQ4	Q99933	SIAH1	BAG1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2189	SIAH1_HUMAN	SYPH_HUMAN	Q8IUQ4	P08247	SIAH1	SYP	UniProt	SIAH1_HUMAN	Ubiquitinated; mediated by <span class="match term0">SIAH1</span> or SIAH2 and leading to its subsequent proteasomal degradation (By similarity)	RING	1	Training data	H.sapiens
2190	SIAH1_HUMAN	STAR_HUMAN	Q8IUQ4	P49675	SIAH1	STAR	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2191	SIAH1_HUMAN	FLT3_HUMAN	Q8IUQ4	P36888	SIAH1	FLT3	MEDLINE	20508617	UbiNet 2.0	RING	1	Training data	H.sapiens
2192	SIAH1_HUMAN	KHDR3_HUMAN	Q8IUQ4	O75525	SIAH1	KHDRBS3	MEDLINE	15163637	Rodent T-STAR orthologues (also known as etoile or <span class="match term1">SLM2</span>) were not targeted for degradation by <span class="match term0">SIAH1</span>	RING	1	Training data	H.sapiens
2193	SIAH1_HUMAN	ZEB1_HUMAN	Q8IUQ4	P37275	SIAH1	ZEB1	MEDLINE	25528765	The ubiquitin ligase Siah is a novel regulator of <span class="match term1">Zeb1</span> in breast cancer.	RING	1	Other	H.sapiens
2194	SIAH1_HUMAN	TRIB3_HUMAN	Q8IUQ4	Q96RU7	SIAH1	TRIB3	MEDLINE	18276110	Cotransfection of <span class="match term0">SIAH1</span> could withdraw up-regulation of TGF-beta signaling by <span class="match term1">TRB3</span>, suggesting <span class="match term0">SIAH1</span>-induced degradation of <span class="match term1">TRB3</span> represents a potential regulatory mechanism for TGF-beta signaling	RING	1	Training data	H.sapiens
2195	SIAH1_HUMAN	KIF22_HUMAN	Q8IUQ4	Q14807	SIAH1	KIF22	MEDLINE	20144232	Previously, we reported that <span class="match term0">SIAH-1</span> induces the degradation of Kid (<span class="match term1">KIF22</span>), a chromokinesin protein implicated in the normal progression of mitosis and meiosis, by the ubiquitin proteasome pathway	RING	1	Training data	H.sapiens
2196	SIAH1_HUMAN	GRM5_HUMAN	Q8IUQ4	P41594	SIAH1	GRM5	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2197	SIAH1_HUMAN	DCC_HUMAN	Q8IUQ4	P43146	SIAH1	DCC	MEDLINE	9858595	In the course of defining <span class="match term0">Siah-1</span> sequences required for <span class="match term1">DCC</span> degradation, we found that <span class="match term0">Siah-1</span> is itself rapidly degraded via the proteasome pathway, and RING domain mutations stabilized the <span class="match term0">Siah-1</span> protein	RING	1	Training data	H.sapiens
2198	SIAH1_HUMAN	KLF10_HUMAN	Q8IUQ4	Q13118	SIAH1	KLF10	MEDLINE	12072443	Co-expression of <span class="match term0">SIAH1</span> results in proteasomal degradation of <span class="match term1">TIEG1</span> but not of the related factor TIEG2	RING	1	Training data	H.sapiens
2199	SIAH1_HUMAN	JADE1_HUMAN	Q8IUQ4	Q6IE81	SIAH1	JADE1	MEDLINE	23001567	UbiNet 2.0	RING	1	Training data	H.sapiens
2200	SIAH1_HUMAN	PKD1_HUMAN	Q8IUQ4	P98161	SIAH1	PKD1	MEDLINE	15284290	Furthermore, ubiquitination and degradation of <span class="match term1">PKD1</span>-C are increased in the presence of <span class="match term0">Siah-1</span>, and overexpression of <span class="match term0">Siah-1</span> protein promotes the degradation of polycystin-1 via the ubiquitin-proteasome pathway	RING	1	Training data	H.sapiens
2201	SIAH2_HUMAN	TINF2_HUMAN	O43255	Q9BSI4	SIAH2	TINF2	MEDLINE	22064479	UbiNet 2.0	RING	1	Training data	H.sapiens
2202	SIAH2_HUMAN	BAG1_HUMAN	O43255	Q99933	SIAH2	BAG1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2203	SIAH2_HUMAN	LATS2_HUMAN	O43255	Q9NRM7	SIAH2	LATS2	MEDLINE	25438054	UbiNet 2.0	RING	1	Other	H.sapiens
2204	SIAH2_HUMAN	TANK_HUMAN	O43255	Q92844	SIAH2	TANK	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2205	SIAH2_HUMAN	EGLN3_HUMAN	O43255	Q9H6Z9	SIAH2	EGLN3	MEDLINE	16958618	The RING (really interesting new gene) finger E3 ligase <span class="match term0">Siah2</span> preferentially targets <span class="match term1">PHD3</span> for degradation	RING	1	Training data	H.sapiens
2206	SIAH2_HUMAN	SYUA_HUMAN	O43255	P37840	SIAH2	SNCA	MEDLINE	18070888	Suppression of SIAH expression by short hairpin RNA to SIAH-1 and SIAH-2 abolished alpha-synuclein monoubiquitylation in dopaminergic cells, indicating that endogenous SIAH ubiquitylates alpha-synuclein	RING	1	Training data	H.sapiens
2207	SIAH2_HUMAN	SH3K1_HUMAN	O43255	Q96B97	SIAH2	SH3KBP1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2208	SIAH2_HUMAN	SENP7_HUMAN	O43255	Q9BQF6	SIAH2	SENP7	MEDLINE	31825833	In steady state, but not IBD, <span class="match term1">SENP7</span> expression was negatively regulated by a direct interaction and ubiquitination by <span class="match term0">SIAH2</span>	RING	1	Other	H.sapiens
2209	SIAH2_HUMAN	CHK2_HUMAN	O43255	O96017	SIAH2	CHEK2	MEDLINE	26751770	<span class="match term1">CHK2</span> stability is regulated by the E3 ubiquitin ligase <span class="match term0">SIAH2</span>.	RING	1	Other	H.sapiens
2210	SIAH2_HUMAN	HIF1A_HUMAN	O43255	Q16665	SIAH2	HIF1A	MEDLINE	22055192	UbiNet 2.0	RING	1	Training data	H.sapiens
2211	SIAH2_HUMAN	DCC_HUMAN	O43255	P43146	SIAH2	DCC	UniProt	SIAH2_HUMAN	Ubiquitinated; mediated by SIAH1 or <span class="match term0">SIAH2</span> and leading to its subsequent proteasomal degradation (Probable)	RING	1	Training data	H.sapiens
2212	SIAH2_HUMAN	P53_HUMAN	O43255	P04637	SIAH2	TP53	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2213	SIAH2_HUMAN	CDN1B_HUMAN	O43255	P46527	SIAH2	CDKN1B	MEDLINE	21734459	UbiNet 2.0	RING	1	Training data	H.sapiens
2214	SIAH2_HUMAN	SPY2_HUMAN	O43255	O43597	SIAH2	SPRY2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2215	SIAH2_HUMAN	ASPP2_HUMAN	O43255	Q13625	SIAH2	TP53BP2	MEDLINE	23644657	Here we demonstrate that under hypoxic conditions, the ubiquitin ligase Siah (seven in absentia homolog)2 controls <span class="match term1">ASPP2</span> availability, with concomitant effect on epithelial cell polarity	RING	1	Other	H.sapiens
2216	SIAH2_HUMAN	MYPT1_HUMAN	O43255	O14974	SIAH2	PPP1R12A	MEDLINE	19744480	These findings suggest a novel mechanism whereby the ability of MP to modulate myosin light chain might be regulated by the degradation of its targeting subunit <span class="match term1">MYPT1</span> through the <span class="match term0">SIAH2</span>-ubiquitin-proteasomal pathway	RING	1	Training data	H.sapiens
2217	SIAH2_HUMAN	PML_HUMAN	O43255	P29590	SIAH2	PML	UniProt	SIAH2_HUMAN	Ubiquitinated; mediated by SIAH1 or <span class="match term0">SIAH2</span> and leading to its subsequent proteasomal degradation	RING	1	Training data	H.sapiens
2218	SIAH2_HUMAN	AKAP1_HUMAN	O43255	Q92667	SIAH2	AKAP1	MEDLINE	18323779	In addition, we show that overexpression of <span class="match term0">Siah2</span> or oxygen and glucose deprivation (OGD) promotes <span class="match term0">Siah2</span>-mediated ubiquitination and proteolysis of <span class="match term1">AKAP121</span>	RING	1	Training data	H.sapiens
2219	SIAH2_HUMAN	OBF1_HUMAN	O43255	Q16633	SIAH2	POU2AF1	UniProt	SIAH2_HUMAN	Ubiquitinated; mediated by SIAH1 or <span class="match term0">SIAH2</span> and leading to its subsequent proteasomal degradation (Probable)	RING	1	Training data	H.sapiens
2220	SIAH2_HUMAN	KIF15_HUMAN	O43255	Q9NS87	SIAH2	KIF15	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2221	SIAH2_HUMAN	SYPH_HUMAN	O43255	P08247	SIAH2	SYP	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2222	SIAH2_HUMAN	NRF1_HUMAN	O43255	Q16656	SIAH2	NRF1	MEDLINE	30833558	The hypoxia-activated E3 ligase <span class="match term0">SIAH2</span> spatially downregulates nuclear-encoded mitochondrial gene expression including pyruvate dehydrogenase beta via degrading <span class="match term1">NRF1</span> (Nuclear Respiratory Factor 1) through ubiquitination on lysine 230, resulting in enhanced Warburg effect, metabolic reprogramming and pro-tumor immune response	RING	1	Other	H.sapiens
2223	SIAH2_HUMAN	DYRK2_HUMAN	O43255	Q92630	SIAH2	DYRK2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2224	SIAH2_HUMAN	EGLN1_HUMAN	O43255	Q9GZT9	SIAH2	EGLN1	MEDLINE	19546213	Whereas PHD1 and PHD3 proteolysis has been shown to be regulated by <span class="match term0">Siah2</span> ubiquitin E3 ligase-mediated polyubiquitylation and proteasomal destruction, protein regulation of the main oxygen sensor responsible for hypoxia-inducible factor alpha regulation, <span class="match term1">PHD2</span>, remained unknown	RING	1	Training data	H.sapiens
2225	SIAH2_HUMAN	SNCAP_HUMAN	O43255	Q9Y6H5	SIAH2	SNCAIP	MEDLINE	17982729	UbiNet 2.0	RING	1	Training data	H.sapiens
2226	SIAH2_HUMAN	PIAS1_HUMAN	O43255	O75925	SIAH2	PIAS1	MEDLINE	17533377	We demonstrate that <span class="match term0">hSiah2</span> regulates specifically the proteasome-dependent degradation of Pias proteins.	RING	1	Training data	H.sapiens
2227	SIAH2_HUMAN	EGLN2_HUMAN	O43255	Q96KS0	SIAH2	EGLN2	MEDLINE	15210114	UbiNet 2.0	RING	1	Other	H.sapiens
2228	SIAH2_HUMAN	PPARG_HUMAN	O43255	P37231	SIAH2	PPARG	MEDLINE	22294748	UbiNet 2.0	RING	1	Training data	H.sapiens
2229	SIAH2_HUMAN	NCOR1_HUMAN	O43255	O75376	SIAH2	NCOR1	MEDLINE	16141343	Our results illustrate a mechanism by which the estrogen-ER complex markedly reduces the level of <span class="match term1">N-CoR</span> through a process involving the up-regulation of <span class="match term0">Siah2</span> and the subsequent targeting of <span class="match term1">N-CoR</span> for proteasomal degradation	RING	1	Training data	H.sapiens
2230	SIAH2_HUMAN	PLCE1_HUMAN	O43255	Q9P212	SIAH2	PLCE1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2231	SIAH2_HUMAN	PSMD4_HUMAN	O43255	P55036	SIAH2	PSMD4	MEDLINE	19240029	We discovered that, unlike typical substrates of Ub ligases (E3s), <span class="match term1">S5a</span> can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, <span class="match term0">Siah2</span>, Parkin, APC, and SCF(betaTRCP1)), the U-box E3, CHIP, and HECT domain E3s (E6AP and Nedd4) when assayed with UbcH5 or related Ub-conjugating enzymes	RING	1	Other	H.sapiens
2232	SIAH2_HUMAN	HDAC3_HUMAN	O43255	O15379	SIAH2	HDAC3	MEDLINE	20691163	UbiNet 2.0	RING	1	Training data	H.sapiens
2233	SIAH2_HUMAN	ANDR_HUMAN	O43255	P10275	SIAH2	AR	MEDLINE	23518348	UbiNet 2.0	RING	1	Training data	H.sapiens
2234	SIAH2_HUMAN	ZEB1_HUMAN	O43255	P37275	SIAH2	ZEB1	MEDLINE	25528765	The ubiquitin ligase Siah is a novel regulator of <span class="match term1">Zeb1</span> in breast cancer.	RING	1	Other	H.sapiens
2235	SIAH2_HUMAN	TRAF2_HUMAN	O43255	Q12933	SIAH2	TRAF2	MEDLINE	12411493	hUbiquitome	RING	1	Other	H.sapiens
2236	SIVA_HUMAN	ARF_HUMAN	O15304	Q8N726	SIVA1	CDKN2A	MEDLINE	23462994	UbiNet 2.0	Other	1	Other	H.sapiens
2237	SIVA_HUMAN	XIAP_HUMAN	O15304	P98170	SIVA1	XIAP	MEDLINE	32015347	We describe how <span class="match term0">SIVA-1</span> regulates FAIM-L function by disrupting the interaction of FAIM-L with <span class="match term1">XIAP</span>, thereby promoting <span class="match term1">XIAP</span> ubiquitination, caspase-3 activation and neuronal death	Other	1	Other	H.sapiens
2238	SKP2_HUMAN	BRCA1_HUMAN	Q13309	P38398	SKP2	BRCA1	MEDLINE	25659039	Moreover, we show that <span class="match term1">BRCA1</span> is ubiquitinated by SCF(<span class="match term0">Skp2</span>) and that abrogation of Chk2 phosphorylation impairs its ubiquitination	F-box	1	Other	H.sapiens
2239	SKP2_HUMAN	ESR1_HUMAN	Q13309	P03372	SKP2	ESR1	MEDLINE	23770852	UbiNet 2.0	F-box	1	Other	H.sapiens
2240	SKP2_HUMAN	CDN1B_HUMAN	Q13309	P46527	SKP2	CDKN1B	MEDLINE	19112177	HINT1 directly interacts with the SCF(<span class="match term0">SKP2</span>) ubiquitin ligase complex and inhibits the ubiquitylation of p27(<span class="match term1">KIP1</span>)	F-box	1	Training data	H.sapiens
2241	SKP2_HUMAN	VE2_HPV18	Q13309	P06790	SKP2	E2	MEDLINE	19828607	The human papillomavirus type 18 <span class="match term1">E2</span> protein is a cell cycle-dependent target of the SCFSkp2 ubiquitin ligase.	F-box	1	Other	H.sapiens
2242	SKP2_HUMAN	CEBPA_HUMAN	Q13309	P49715	SKP2	CEBPA	MEDLINE	34002296	In recent independent studies, we showed that CDK2 and <span class="match term0">SKP2</span> downregulated <span class="match term1">C/EBPalpha</span> expression in an ubiquitin-dependent proteasome degradation manner leading to differentiation block in AML	F-box	1	Other	H.sapiens
2243	SKP2_HUMAN	DCTN6_HUMAN	Q13309	O00399	SKP2	DCTN6	MEDLINE	33989513	Cyclin A acts as an activator and substrate recruitment factor of CDK2, while <span class="match term0">Skp2</span> mediates the ubiquitination and subsequent destruction of the CDK inhibitor protein <span class="match term1">p27</span>	F-box	1	Other	H.sapiens
2244	SKP2_HUMAN	CDN1A_HUMAN	Q13309	P38936	SKP2	CDKN1A	MEDLINE	12393444	As for this mechanism, GATA-2 was found to inhibit ubiquitin/proteasome-dependent degradation of p21(<span class="match term1">WAF1</span>) and p27(Kip1) and to induce their accumulation by repressing the expression of <span class="match term0">Skp2</span> and Cul1, both of which are components of the ubiquitin ligase for p21(<span class="match term1">WAF1</span>) and p27(Kip1)	F-box	1	Training data	H.sapiens
2245	SKP2_HUMAN	RB_HUMAN	Q13309	P06400	SKP2	RB1	MEDLINE	17187060	Here, we report a novel interaction between <span class="match term1">pRB</span> and the anaphase-promoting complex/cyclosome (APC/C) that controls p27(Kip1) stability by targeting <span class="match term0">Skp2</span> for ubiquitin-mediated degradation	F-box	1	Training data	H.sapiens
2246	SKP2_HUMAN	RBL2_HUMAN	Q13309	Q08999	SKP2	RBL2	MEDLINE	12435635	Furthermore, in vitro polyubiquitination of <span class="match term1">p130</span> by SCF(<span class="match term0">Skp2</span>) was specifically dependent on phosphorylation of <span class="match term1">p130</span> on Serine 672	F-box	1	Training data	H.sapiens
2247	SKP2_HUMAN	TAL1_HUMAN	Q13309	P17542	SKP2	TAL1	MEDLINE	17962192	Ubiquitination and degradation of <span class="match term1">Tal1</span>/SCL are induced by notch signaling and depend on <span class="match term0">Skp2</span> and CHIP	F-box	1	Training data	H.sapiens
2248	SKP2_HUMAN	YAP1_HUMAN	Q13309	P46937	SKP2	YAP1	MEDLINE	29891922	Here, we report that <span class="match term1">YAP</span> is subject to non-proteolytic, K63-linked polyubiquitination by the SCFSKP2 E3 ligase complex (<span class="match term0">SKP2</span>), which is reversed by the deubiquitinase OTUD1	F-box	1	Other	H.sapiens
2249	SKP2_HUMAN	E2F1_HUMAN	Q13309	Q01094	SKP2	E2F1	MEDLINE	11245432	In contrast to substrates of the SKP1-Cullin 1-F box (SCF) complexes, in vitro ubiquitination of <span class="match term1">E2F1</span> by CUL1-ROC1 ligase does not require <span class="match term1">E2F1</span> phosphorylation, is not stimulated by overexpression of F box protein <span class="match term0">SKP2</span>, and is not affected by immunodepletion of SKP1 or mutations in CUL1 disrupting SKPI binding	F-box	1	Training data	H.sapiens
2250	SKP2_HUMAN	CDK9_HUMAN	Q13309	P50750	SKP2	CDK9	MEDLINE	11689688	<span class="match term1">CDK9</span> ubiquitination was modulated by cyclin T1 and p45(<span class="match term0">SKP2</span>)	F-box	1	Training data	H.sapiens
2251	SKP2_HUMAN	VE7_HPV16	Q13309	P03129	SKP2	E7	MEDLINE	15113913	The papillomavirus <span class="match term1">E7</span> oncoprotein is ubiquitinated by UbcH7 and Cullin 1- and <span class="match term0">Skp2</span>-containing E3 ligase.	F-box	1	Other	H.sapiens
2252	SKP2_HUMAN	AKT2_HUMAN	Q13309	P31751	SKP2	AKT2	MEDLINE	22632973	The <span class="match term0">Skp2</span>-SCF E3 ligase regulates Akt ubiquitination, glycolysis, herceptin sensitivity, and tumorigenesis.	F-box	1	Other	H.sapiens
2253	SKP2_HUMAN	PSMD9_HUMAN	Q13309	O00233	SKP2	PSMD9	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
2254	SKP2_HUMAN	JAK3_HUMAN	Q13309	P52333	SKP2	JAK3	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
2255	SKP2_HUMAN	CARM1_HUMAN	Q13309	Q86X55	SKP2	CARM1	MEDLINE	27309807;27867975	27309807:27867975	F-box	1	Other	H.sapiens
2256	SKP2_HUMAN	RND3_HUMAN	Q13309	P61587	SKP2	RND3	MEDLINE	24045951	The Rho family member <span class="match term1">RhoE</span> interacts with <span class="match term0">Skp2</span> and is degraded at the proteasome during cell cycle progression.	F-box	1	Other	H.sapiens
2257	SKP2_HUMAN	PDCD4_HUMAN	Q13309	Q53EL6	SKP2	PDCD4	MEDLINE	30760284	CONCLUSIONS: We identify <span class="match term1">PDCD4</span> as an important ubiquitination substrate of <span class="match term0">SKP2</span>	F-box	1	Other	H.sapiens
2258	SKP2_HUMAN	A9UEZ6_HUMAN	Q13309	A9UEZ6	SKP2	BCR/ABL fusion	MEDLINE	31044085	UbiNet 2.0	F-box	1	Other	H.sapiens
2259	SKP2_HUMAN	MYC_HUMAN	Q13309	P01106	SKP2	MYC	MEDLINE	15103331	The F-box protein <span class="match term0">Skp2</span> mediates c-<span class="match term1">Myc</span> ubiquitylation by binding to the MB2 domain	F-box	1	Training data	H.sapiens
2260	SKP2_HUMAN	CCNE1_HUMAN	Q13309	P24864	SKP2	CCNE1	MEDLINE	11237742	In vivo, expression of <span class="match term0">SKP2</span> induced cyclin E polyubiquitination and degradation	F-box	1	Training data	H.sapiens
2261	SKP2_HUMAN	CCNA2_HUMAN	Q13309	P20248	SKP2	CCNA2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
2262	SKP2_HUMAN	SPDYA_HUMAN	Q13309	Q5MJ70	SKP2	SPDYA	MEDLINE	19622356	RINGO/Speedy A is degraded by the proteasome and the process involves the ubiquitin ligase SCF(<span class="match term0">Skp2</span>)	F-box	1	Training data	H.sapiens
2263	SKP2_HUMAN	CDN1C_HUMAN	Q13309	P49918	SKP2	CDKN1C	MEDLINE	20805359	Interestingly, FaDu cells with reduced cortactin levels also exhibited a significant diminution in RhoA expression and activity, together with decreased expression of <span class="match term0">Skp2</span>, a critical component of the SCF ubiquitin ligase that targets p27(Kip1) and <span class="match term1">p57</span>(Kip2) for degradation	F-box	1	Training data	H.sapiens
2264	SKP2_HUMAN	CDT1_HUMAN	Q13309	Q9H211	SKP2	CDT1	MEDLINE	12840033	The SCF(<span class="match term0">Skp2</span>) complex ubiquitinated <span class="match term1">Cdt1</span> both in vivo and in vitro	F-box	1	Training data	H.sapiens
2265	SKP2_HUMAN	BTG2_HUMAN	Q13309	P78543	SKP2	BTG2	MEDLINE	19615363	Leucine rich repeat (LRR) domain of <span class="match term0">Skp2</span> could bind to <span class="match term1">TIS21</span> C-terminus and facilitated <span class="match term1">TIS21</span> degradation via ubiquitin-proteasome pathway	F-box	1	Training data	H.sapiens
2266	SKP2_HUMAN	TFE2_HUMAN	Q13309	P15923	SKP2	TCF3	MEDLINE	PMC4306233	PMC4306233	F-box	1	Other	H.sapiens
2267	SKP2_HUMAN	SKP2_HUMAN	Q13309	Q13309	SKP2	SKP2	UniProt	SKP2_HUMAN	In association with DDB1 and <span class="match term0">SKP2</span> probably is involved in ubiquitination of CDKN1B/p27kip	F-box	1	Training data	H.sapiens
2268	SKP2_HUMAN	FBW1A_HUMAN	Q13309	Q9Y297	SKP2	BTRC	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
2269	SKP2_HUMAN	P53_HUMAN	Q13309	P04637	SKP2	TP53	MEDLINE	21127074	UbiNet 2.0	F-box	1	Training data	H.sapiens
2270	SKP2_HUMAN	BRCA2_HUMAN	Q13309	P51587	SKP2	BRCA2	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
2271	SKP2_HUMAN	RRAGA_HUMAN	Q13309	Q7L523	SKP2	RRAGA	MEDLINE	26051179	<span class="match term0">Skp2</span> E3 ligase drives K63-linked ubiquitination of <span class="match term1">RagA</span>, which facilitates GATOR1 recruitment and <span class="match term1">RagA</span>(GTP) hydrolysis, thereby providing a negative feedback loop to attenuate mTORC1 lysosomal recruitment and prevent mTORC1 hyperactivation	F-box	1	Other	H.sapiens
2272	SKP2_HUMAN	CDK8_HUMAN	Q13309	P49336	SKP2	CDK8	MEDLINE	22898779	UbiNet 2.0	F-box	1	Training data	H.sapiens
2273	SKP2_HUMAN	ELF4_HUMAN	Q13309	Q99607	SKP2	ELF4	UniProt	SKP2_HUMAN	SCF(<span class="match term0">SKP2</span>) directs ubiquination of ORC1L, CDT1, RBL2, <span class="match term1">ELF4</span>, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1	F-box	1	Training data	H.sapiens
2274	SKP2_HUMAN	UBP18_HUMAN	Q13309	Q9UMW8	SKP2	USP18	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
2275	SKP2_HUMAN	IKBE_HUMAN	Q13309	O00221	SKP2	NFKBIE	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
2276	SKP2_HUMAN	ICAM1_HUMAN	Q13309	P05362	SKP2	ICAM1	MEDLINE	28802579	Atorvastatin prevents endothelial dysfunction in high glucose condition through <span class="match term0">Skp2</span>-mediated degradation of FOXO1 and <span class="match term1">ICAM-1</span>.	F-box	1	Other	H.sapiens
2277	SKP2_HUMAN	DUS1_HUMAN	Q13309	P28562	SKP2	DUSP1	MEDLINE	19034960	Unrestrained extracellular signal-regulated kinase (ERK) activity linked to proteasomal degradation of dual-specificity phosphatase 1 (<span class="match term1">DUSP1</span>), a specific ERK inhibitor, by the CKS1-<span class="match term0">SKP2</span> ubiquitin ligase complex occurs in more aggressive HCC of F344 rats and humans	F-box	1	Training data	H.sapiens
2278	SKP2_HUMAN	KMT2A_HUMAN	Q13309	Q03164	SKP2	KMT2A	MEDLINE	17908926	UbiNet 2.0	F-box	1	Training data	H.sapiens
2279	SKP2_HUMAN	CYGB_HUMAN	Q13309	Q8WWM9	SKP2	CYGB	MEDLINE	28948618	Cell cycle-dependent regulation of cytoglobin by <span class="match term0">Skp2</span>.	F-box	1	Other	H.sapiens
2280	SKP2_HUMAN	IKBA_HUMAN	Q13309	P25963	SKP2	NFKBIA	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
2281	SKP2_HUMAN	FOXO3_HUMAN	Q13309	O43524	SKP2	FOXO3	MEDLINE	21841822	Deacetylation of <span class="match term1">FOXO3</span> by SIRT1 or SIRT2 leads to <span class="match term0">Skp2</span>-mediated <span class="match term1">FOXO3</span> ubiquitination and degradation.	F-box	1	Other	H.sapiens
2282	SKP2_HUMAN	SMAD4_HUMAN	Q13309	Q13485	SKP2	SMAD4	MEDLINE	15314162	Ubiquitination and proteolysis of cancer-derived <span class="match term1">Smad4</span> mutants by SCFSkp2	F-box	1	Training data	H.sapiens
2283	SKP2_HUMAN	TOB1_HUMAN	Q13309	P50616	SKP2	TOB1	MEDLINE	16951159	Degradation of <span class="match term1">Tob1</span> mediated by SCFSkp2-dependent ubiquitination	F-box	1	Training data	H.sapiens
2284	SKP2_HUMAN	MYBB_HUMAN	Q13309	P10244	SKP2	MYBL2	MEDLINE	10871850	Degradation of <span class="match term1">B-Myb</span> by ubiquitin-mediated proteolysis: involvement of the Cdc34-SCF(p45Skp2) pathway	F-box	1	Training data	H.sapiens
2285	SKP2_HUMAN	PHB_HUMAN	Q13309	P35232	SKP2	PHB	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
2286	SKP2_HUMAN	TWST1_HUMAN	Q13309	Q15672	SKP2	TWIST1	MEDLINE	28346424	UbiNet 2.0	F-box	1	Other	H.sapiens
2287	SKP2_HUMAN	NBN_HUMAN	Q13309	O60934	SKP2	NBN	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
2288	SKP2_HUMAN	SIPA1_HUMAN	Q13309	Q96FS4	SKP2	SIPA1	MEDLINE	21502543	UbiNet 2.0	F-box	1	Training data	H.sapiens
2289	SKP2_HUMAN	ING3_HUMAN	Q13309	Q9NXR8	SKP2	ING3	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
2290	SKP2_HUMAN	MEFV_HUMAN	Q13309	O15553	SKP2	MEFV	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
2291	SKP2_HUMAN	NKX31_HUMAN	Q13309	Q99801	SKP2	NKX3-1	MEDLINE	27065334	UbiNet 2.0	F-box	1	Other	H.sapiens
2292	SKP2_HUMAN	FOXO1_HUMAN	Q13309	Q12778	SKP2	FOXO1	UniProt	SKP2_HUMAN	SCF(<span class="match term0">SKP2</span>) directs ubiquination of ORC1L, CDT1, RBL2, ELF4, CDKN1A, RAG2, <span class="match term1">FOXO1A</span>, and probably MYC and TAL1	F-box	1	Training data	H.sapiens
2293	SKP2_HUMAN	RAG2_HUMAN	Q13309	P55895	SKP2	RAG2	UniProt	SKP2_HUMAN	SCF(<span class="match term0">SKP2</span>) directs ubiquination of ORC1L, CDT1, RBL2, ELF4, CDKN1A, <span class="match term1">RAG2</span>, FOXO1A, and probably MYC and TAL1	F-box	1	Training data	H.sapiens
2294	SKP2_HUMAN	SIR3_HUMAN	Q13309	Q9NTG7	SKP2	SIRT3	MEDLINE	24658274	UbiNet 2.0	F-box	1	Training data	H.sapiens
2295	SKP2_HUMAN	8ODP_HUMAN	Q13309	P36639	SKP2	NUDT1	MEDLINE	28947420	UbiNet 2.0	F-box	1	Other	H.sapiens
2296	SKP2_HUMAN	STK11_HUMAN	Q13309	Q15831	SKP2	STK11	MEDLINE	25728766	<span class="match term0">Skp2</span>-dependent ubiquitination and activation of <span class="match term1">LKB1</span> is essential for cancer cell survival under energy stress	F-box	1	Other	H.sapiens
2297	SKP2_HUMAN	TF7L1_HUMAN	Q13309	Q9HCS4	SKP2	TCF7L1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
2298	SKP2_HUMAN	CCND1_HUMAN	Q13309	P24385	SKP2	CCND1	MEDLINE	11439327	A splice variant of <span class="match term0">Skp2</span> is retained in the cytoplasm and fails to direct cyclin D1 ubiquitination in the uterine cancer cell line SK-UT	F-box	1	Training data	H.sapiens
2299	SKP2_HUMAN	CADH1_HUMAN	Q13309	P12830	SKP2	CDH1	MEDLINE	26474281	UbiNet 2.0	F-box	1	Other	H.sapiens
2300	SKP2_HUMAN	AKT1_HUMAN	Q13309	P31749	SKP2	AKT1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
2301	SKP2_HUMAN	BORA_HUMAN	Q13309	Q6PGQ7	SKP2	BORA	MEDLINE	26697838	UbiNet 2.0	F-box	1	Other	H.sapiens
2302	SKP2_HUMAN	FGD1_HUMAN	Q13309	P98174	SKP2	FGD1	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
2303	SKP2_HUMAN	RASF1_HUMAN	Q13309	Q9NS23	SKP2	RASSF1	MEDLINE	18071316	Here we show that <span class="match term0">Skp2</span>, an oncogenic subunit of the Skp1-Cul1-F-box ubiquitin ligase complex, interacts with, ubiquitinates, and promotes the degradation of <span class="match term1">RASSF1A</span> at the G1-S transition of the cell cycle	F-box	1	Training data	H.sapiens
2304	SKP2_HUMAN	ORC1_HUMAN	Q13309	Q13415	SKP2	ORC1	MEDLINE	24658274	UbiNet 2.0	F-box	1	Other	H.sapiens
2305	SKP2_HUMAN	CTNB1_HUMAN	Q13309	P35222	SKP2	CTNNB1	MEDLINE	22199232	E3Net	F-box	1	Other	H.sapiens
2306	SKP2_HUMAN	ACE2_HUMAN	Q13309	Q9BYF1	SKP2	ACE2	MEDLINE	33511555	BaP induces an aryl hydrocarbon receptor (AhR)-dependent upregulation of the ubiquitin E3 ligase <span class="match term0">Skp2</span> for <span class="match term1">ACE2</span> ubiquitination	F-box	1	Other	H.sapiens
2307	SMUF1_HUMAN	KLF2_HUMAN	Q9HCE7	Q9Y5W3	SMURF1	KLF2	MEDLINE	21382345	UbiNet 2.0	HECT	1	Training data	H.sapiens
2308	SMUF1_HUMAN	RHOA_HUMAN	Q9HCE7	P61586	SMURF1	RHOA	MEDLINE	14752271	<span class="match term0">Smurf1</span> thus provides a link between the control of cell polarity and ubiquitin-mediated <span class="match term1">RhoA</span> degradation during directional cell movements	HECT	1	Training data	H.sapiens
2309	SMUF1_HUMAN	SMAD7_HUMAN	Q9HCE7	O15105	SMURF1	SMAD7	MEDLINE	11278251	Here we show that <span class="match term0">Smurf1</span>, an E3 ubiquitin ligase for bone morphogenetic protein-specific Smads, also interacts with <span class="match term1">Smad7</span> and induces <span class="match term1">Smad7</span> ubiquitination and translocation into the cytoplasm	HECT	1	Training data	H.sapiens
2310	SMUF1_HUMAN	CCD69_HUMAN	Q9HCE7	A6NI79	SMURF1	CCDC69	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2311	SMUF1_HUMAN	TAB1_HUMAN	Q9HCE7	Q15750	SMURF1	TAB1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2312	SMUF1_HUMAN	HOIL1_HUMAN	Q9HCE7	Q9BYM8	SMURF1	RBCK1	MEDLINE	20804422	UbiNet 2.0	HECT	1	Training data	H.sapiens
2313	SMUF1_HUMAN	TLN1_HUMAN	Q9HCE7	Q9Y490	SMURF1	TLN1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2314	SMUF1_HUMAN	ITK_HUMAN	Q9HCE7	Q08881	SMURF1	ITK	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2315	SMUF1_HUMAN	SMAD6_HUMAN	Q9HCE7	O43541	SMURF1	SMAD6	MEDLINE	16299379	<span class="match term1">Smad6</span> enhances <span class="match term0">Smurf1</span>-induced Runx2 degradation in an ubiquitin-proteasome-dependent manner	HECT	1	Training data	H.sapiens
2316	SMUF1_HUMAN	LARGN_HUMAN	Q9HCE7	Q569H4	SMURF1	PRR16	MEDLINE	20804422	UbiNet 2.0	HECT	1	Training data	H.sapiens
2317	SMUF1_HUMAN	ANS4B_HUMAN	Q9HCE7	Q8N8V4	SMURF1	ANKS4B	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2318	SMUF1_HUMAN	MAVS_HUMAN	Q9HCE7	Q7Z434	SMURF1	MAVS	MEDLINE	23087404	UbiNet 2.0	HECT	1	Training data	H.sapiens
2319	SMUF1_HUMAN	ARBK2_HUMAN	Q9HCE7	P35626	SMURF1	ADRBK2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2320	SMUF1_HUMAN	M3K9_HUMAN	Q9HCE7	P80192	SMURF1	MAP3K9	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2321	SMUF1_HUMAN	RN114_HUMAN	Q9HCE7	Q9Y508	SMURF1	RNF114	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2322	SMUF1_HUMAN	NEK2_HUMAN	Q9HCE7	P51955	SMURF1	NEK2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2323	SMUF1_HUMAN	CF106_HUMAN	Q9HCE7	Q9H6K1	SMURF1	C6orf106	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2324	SMUF1_HUMAN	M4K5_HUMAN	Q9HCE7	Q9Y4K4	SMURF1	MAP4K5	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2325	SMUF1_HUMAN	UB2V1_HUMAN	Q9HCE7	Q13404	SMURF1	UBE2V1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2326	SMUF1_HUMAN	BMR1B_HUMAN	Q9HCE7	O00238	SMURF1	BMPR1B	MEDLINE	20558834	UbiNet 2.0	HECT	1	Training data	H.sapiens
2327	SMUF1_HUMAN	RD23A_HUMAN	Q9HCE7	P54725	SMURF1	RAD23A	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2328	SMUF1_HUMAN	MATK_HUMAN	Q9HCE7	P42679	SMURF1	MATK	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2329	SMUF1_HUMAN	RUNX2_HUMAN	Q9HCE7	Q13950	SMURF1	RUNX2	MEDLINE	17215250	The protein degradation of <span class="match term1">Runx2</span> is mediated by the E3 ubiquitin ligase <span class="match term0">Smurf1</span>	HECT	1	Training data	H.sapiens
2330	SMUF1_HUMAN	SLAI2_HUMAN	Q9HCE7	Q9P270	SMURF1	SLAIN2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2331	SMUF1_HUMAN	FGR_HUMAN	Q9HCE7	P09769	SMURF1	FGR	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2332	SMUF1_HUMAN	TAOK3_HUMAN	Q9HCE7	Q9H2K8	SMURF1	TAOK3	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2333	SMUF1_HUMAN	OTU6B_HUMAN	Q9HCE7	Q8N6M0	SMURF1	OTUD6B	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2334	SMUF1_HUMAN	ELOF1_HUMAN	Q9HCE7	P60002	SMURF1	ELOF1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2335	SMUF1_HUMAN	HIP1_HUMAN	Q9HCE7	O00291	SMURF1	HIP1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2336	SMUF1_HUMAN	Q8N519_HUMAN	Q9HCE7	Q8N519	SMURF1	-	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2337	SMUF1_HUMAN	KISS1_HUMAN	Q9HCE7	Q15726	SMURF1	KISS1	MEDLINE	30244247	The ubiquitin-dependent degradation of <span class="match term1">KISS-1</span> induced by <span class="match term0">Smurf1</span> and the activation of NF-kappaB signaling pathway might be involved in this process	HECT	1	Other	H.sapiens
2338	SMUF1_HUMAN	PADI4_HUMAN	Q9HCE7	Q9UM07	SMURF1	PADI4	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2339	SMUF1_HUMAN	SMAD1_HUMAN	Q9HCE7	Q15797	SMURF1	SMAD1	MEDLINE	14711801	Thus overexpression of <span class="match term0">Smurf1</span> specifically promotes <span class="match term1">Smad1</span> and Smad5 ubiquitination and degradation in embryonic lung epithelium, thereby modulating the effects of BMP4 on embryonic lung growth	HECT	1	Training data	H.sapiens
2340	SMUF1_HUMAN	FGF12_HUMAN	Q9HCE7	P61328	SMURF1	FGF12	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2341	SMUF1_HUMAN	TBX6_HUMAN	Q9HCE7	O95947	SMURF1	TBX6	MEDLINE	19561075	UbiNet 2.0	HECT	1	Training data	H.sapiens
2342	SMUF1_HUMAN	SCYL1_HUMAN	Q9HCE7	Q96KG9	SMURF1	SCYL1	MEDLINE	20804422	UbiNet 2.0	HECT	1	Training data	H.sapiens
2343	SMUF1_HUMAN	EPN1_HUMAN	Q9HCE7	Q9Y6I3	SMURF1	EPN1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2344	SMUF1_HUMAN	BMPR2_HUMAN	Q9HCE7	Q13873	SMURF1	BMPR2	MEDLINE	20558834	UbiNet 2.0	HECT	1	Training data	H.sapiens
2345	SMUF1_HUMAN	CG050_HUMAN	Q9HCE7	Q9BRJ6	SMURF1	C7orf50	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2346	SMUF1_HUMAN	GDF15_HUMAN	Q9HCE7	Q99988	SMURF1	GDF15	MEDLINE	18927080	Smad ubiquitin regulatory factor 1 (<span class="match term0">Smurf1</span>) and Smurf2 are E3 ubiquitin ligases, which suppress transforming growth factor-beta (TGF-beta) family signaling through degradation of Smads and receptors for TGF-beta and bone morphogenetic proteins	HECT	1	Training data	H.sapiens
2347	SMUF1_HUMAN	AXIN1_HUMAN	Q9HCE7	O15169	SMURF1	AXIN1	MEDLINE	23959799	UbiNet 2.0	HECT	1	Training data	H.sapiens
2348	SMUF1_HUMAN	PICAL_HUMAN	Q9HCE7	Q13492	SMURF1	PICALM	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2349	SMUF1_HUMAN	ING2_HUMAN	Q9HCE7	Q9H160	SMURF1	ING2	MEDLINE	20621832	HECT ubiquitin ligase <span class="match term0">Smurf1</span> targets the tumor suppressor <span class="match term1">ING2</span> for ubiquitination and degradation.	HECT	1	Other	H.sapiens
2350	SMUF1_HUMAN	ATX3_HUMAN	Q9HCE7	P54252	SMURF1	ATXN3	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2351	SMUF1_HUMAN	ENTR1_HUMAN	Q9HCE7	Q96C92	SMURF1	ENTR1	MEDLINE	20804422	UbiNet 2.0	HECT	1	Training data	H.sapiens
2352	SMUF1_HUMAN	ASCC2_HUMAN	Q9HCE7	Q9H1I8	SMURF1	ASCC2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2353	SMUF1_HUMAN	TGFR2_HUMAN	Q9HCE7	P37173	SMURF1	TGFBR2	MEDLINE	15817471	UbiNet 2.0	HECT	1	Training data	H.sapiens
2354	SMUF1_HUMAN	KPCG_HUMAN	Q9HCE7	P05129	SMURF1	PRKCG	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2355	SMUF1_HUMAN	F188A_HUMAN	Q9HCE7	Q9H8M7	SMURF1	FAM188A	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2356	SMUF1_HUMAN	BMR1A_HUMAN	Q9HCE7	P36894	SMURF1	BMPR1A	MEDLINE	20558834	UbiNet 2.0	HECT	1	Training data	H.sapiens
2357	SMUF1_HUMAN	CI078_HUMAN	Q9HCE7	Q9NZ63	SMURF1	C9orf78	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2358	SMUF1_HUMAN	SPART_HUMAN	Q9HCE7	Q8N0X7	SMURF1	SPART	MEDLINE	20804422	UbiNet 2.0	HECT	1	Training data	H.sapiens
2359	SMUF1_HUMAN	TOM1_HUMAN	Q9HCE7	O60784	SMURF1	TOM1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2360	SMUF1_HUMAN	UBP5_HUMAN	Q9HCE7	P45974	SMURF1	USP5	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2361	SMUF1_HUMAN	KC1D_HUMAN	Q9HCE7	P48730	SMURF1	CSNK1D	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2362	SMUF1_HUMAN	AN13A_HUMAN	Q9HCE7	Q8IZ07	SMURF1	ANKRD13A	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2363	SMUF1_HUMAN	ACVR1_HUMAN	Q9HCE7	Q04771	SMURF1	ACVR1	MEDLINE	31685442	FINDINGS: The deubiquitinase PSMD14 acts as a positive regulator for the initiation of the BMP6 signaling pathway through deubiquitinating K48-linked <span class="match term1">ALK2</span> type I receptor ubiquitination mediated by <span class="match term0">Smurf1</span> E3 ligase, resulting in increased stability of the <span class="match term1">ALK2</span>	HECT	1	Other	H.sapiens
2364	SMUF1_HUMAN	ZFAN5_HUMAN	Q9HCE7	O76080	SMURF1	ZFAND5	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2365	SMUF1_HUMAN	EPHA1_HUMAN	Q9HCE7	P21709	SMURF1	EPHA1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2366	SMUF1_HUMAN	UB2D1_HUMAN	Q9HCE7	P51668	SMURF1	UBE2D1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2367	SMUF1_HUMAN	SMAD5_HUMAN	Q9HCE7	Q99717	SMURF1	SMAD5	MEDLINE	12871975	<span class="match term0">Smurf1</span> facilitates myogenic differentiation and antagonizes the bone morphogenetic protein-2-induced osteoblast conversion by targeting <span class="match term1">Smad5</span> for degradation	HECT	1	Training data	H.sapiens
2368	SMUF1_HUMAN	Q8TB46_HUMAN	Q9HCE7	Q8TB46	SMURF1	ANKRD50	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2369	SMUF1_HUMAN	BTK_HUMAN	Q9HCE7	Q06187	SMURF1	BTK	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2370	SMUF1_HUMAN	FOXA2_HUMAN	Q9HCE7	Q9Y261	SMURF1	FOXA2	MEDLINE	31891682	Mechanistically, we found that SND1-induced <span class="match term1">FOXA2</span> ubiquitination resulted in degradation, mediated by the E3 ligase enzyme <span class="match term0">Smurf1</span>	HECT	1	Other	H.sapiens
2371	SMUF1_HUMAN	FES_HUMAN	Q9HCE7	P07332	SMURF1	FES	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2372	SMUF1_HUMAN	KRT36_HUMAN	Q9HCE7	O76013	SMURF1	KRT36	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2373	SMUF1_HUMAN	ADRM1_HUMAN	Q9HCE7	Q16186	SMURF1	ADRM1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2374	SMUF1_HUMAN	CUED1_HUMAN	Q9HCE7	Q9NWM3	SMURF1	CUEDC1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2375	SMUF1_HUMAN	UB2D3_HUMAN	Q9HCE7	P61077	SMURF1	UBE2D3	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2376	SMUF1_HUMAN	M3K10_HUMAN	Q9HCE7	Q02779	SMURF1	MAP3K10	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2377	SMUF1_HUMAN	RAC1_HUMAN	Q9HCE7	P63000	SMURF1	RAC1	MEDLINE	16472676	We found that <span class="match term0">Smurf1</span>, a HECT domain E3 ubiquitin ligase, could specifically target RhoA but not Cdc42 or <span class="match term1">Rac1</span> for degradation	HECT	1	Training data	H.sapiens
2378	SMUF1_HUMAN	TRAF4_HUMAN	Q9HCE7	Q9BUZ4	SMURF1	TRAF4	MEDLINE	19458200	Here, we identify tumor necrosis factor (TNF)-receptor-associated factor-4 (<span class="match term1">TRAF4</span>) as a new target of <span class="match term0">Smurf1</span>, which polyubiquitylates <span class="match term1">TRAF4</span> to trigger its proteasomal destruction	HECT	1	Training data	H.sapiens
2379	SMUF1_HUMAN	AN13D_HUMAN	Q9HCE7	Q6ZTN6	SMURF1	ANKRD13D	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2380	SMUF1_HUMAN	ODFP2_HUMAN	Q9HCE7	Q5BJF6	SMURF1	ODF2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2381	SMUF1_HUMAN	MOES_HUMAN	Q9HCE7	P26038	SMURF1	MSN	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2382	SMUF1_HUMAN	UBXN6_HUMAN	Q9HCE7	Q9BZV1	SMURF1	UBXN6	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2383	SMUF1_HUMAN	TRIB2_HUMAN	Q9HCE7	Q92519	SMURF1	TRIB2	MEDLINE	24089522	We performed a structure-function analysis of <span class="match term1">TRIB2</span> and identified a domain (amino acids 1-5) at the N terminus that interacted with the E3 ubiquitin ligase <span class="match term0">Smurf1</span> and was critical for protein stability	HECT	1	Other	H.sapiens
2384	SMUF1_HUMAN	CACO1_HUMAN	Q9HCE7	Q9P1Z2	SMURF1	CALCOCO1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2385	SMUF1_HUMAN	PTEN_HUMAN	Q9HCE7	P60484	SMURF1	PTEN	MEDLINE	32938489	CONCLUSION: This study reveals that IMP3 is overdressed in prostate cancer, which accelerates the progression of prostate cancer through activating PI3K/AKT/mTOR signaling pathway via increasing <span class="match term0">SMURF1</span>-mediated <span class="match term1">PTEN</span> ubiquitination.	HECT	1	Other	H.sapiens
2386	SMUF1_HUMAN	IMPCT_HUMAN	Q9HCE7	Q9P2X3	SMURF1	IMPACT	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2387	SMUF1_HUMAN	ANR50_HUMAN	Q9HCE7	Q9ULJ7	SMURF1	ANKRD50	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2388	SMUF1_HUMAN	RABE2_HUMAN	Q9HCE7	Q9H5N1	SMURF1	RABEP2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2389	SMUF1_HUMAN	PSMD4_HUMAN	Q9HCE7	P55036	SMURF1	PSMD4	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2390	SMUF1_HUMAN	FAF2_HUMAN	Q9HCE7	Q96CS3	SMURF1	FAF2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2391	SMUF1_HUMAN	TM1L2_HUMAN	Q9HCE7	Q6ZVM7	SMURF1	TOM1L2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2392	SMUF1_HUMAN	LCK_HUMAN	Q9HCE7	P06239	SMURF1	LCK	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2393	SMUF1_HUMAN	TNIK_HUMAN	Q9HCE7	Q9UKE5	SMURF1	TNIK	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2394	SMUF1_HUMAN	TBK1_HUMAN	Q9HCE7	Q9UHD2	SMURF1	TBK1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2395	SMUF1_HUMAN	TPM4_HUMAN	Q9HCE7	P67936	SMURF1	TPM4	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2396	SMUF1_HUMAN	FKBP3_HUMAN	Q9HCE7	Q00688	SMURF1	FKBP3	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2397	SMUF1_HUMAN	CIP4_HUMAN	Q9HCE7	Q15642	SMURF1	TRIP10	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2398	SMUF1_HUMAN	PGFRA_HUMAN	Q9HCE7	P16234	SMURF1	PDGFRA	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2399	SMUF1_HUMAN	UB2G1_HUMAN	Q9HCE7	P62253	SMURF1	UBE2G1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2400	SMUF1_HUMAN	UBQL2_HUMAN	Q9HCE7	Q9UHD9	SMURF1	UBQLN2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2401	SMUF1_HUMAN	UBE2K_HUMAN	Q9HCE7	P61086	SMURF1	UBE2K	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2402	SMUF1_HUMAN	RIOK3_HUMAN	Q9HCE7	O14730	SMURF1	RIOK3	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2403	SMUF1_HUMAN	TNIP2_HUMAN	Q9HCE7	Q8NFZ5	SMURF1	TNIP2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2404	SMUF1_HUMAN	UBAC1_HUMAN	Q9HCE7	Q9BSL1	SMURF1	UBAC1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2405	SMUF1_HUMAN	KPCA_HUMAN	Q9HCE7	P17252	SMURF1	PRKCA	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2406	SMUF1_HUMAN	ANXA6_HUMAN	Q9HCE7	P08133	SMURF1	ANXA6	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2407	SMUF1_HUMAN	TGFR1_HUMAN	Q9HCE7	P36897	SMURF1	TGFBR1	MEDLINE	12151385	Moreover, although <span class="match term0">Smurf1</span>(deltaC2) induced ubiquitination of Smad7, it failed to induce the ubiquitination and degradation of <span class="match term1">TbetaR-I</span> and did not enhance the inhibitory activity of Smad7	HECT	1	Training data	H.sapiens
2408	SMUF1_HUMAN	M3K2_HUMAN	Q9HCE7	Q9Y2U5	SMURF1	MAP3K2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2409	SMUF1_HUMAN	ERBB2_HUMAN	Q9HCE7	P04626	SMURF1	ERBB2	MEDLINE	33875644	JAC1 increased the ubiquitination of <span class="match term1">HER2</span> at the K716 site through the E3 ubiquitin ligase <span class="match term0">SMURF1</span> which was due to the decreased expression of NEDD4, the E3 ubiquitin ligase of <span class="match term0">SMURF1</span>	HECT	1	Other	H.sapiens
2410	SMUF1_HUMAN	UVRAG_HUMAN	Q9HCE7	Q9P2Y5	SMURF1	UVRAG	MEDLINE	30686098	Here we report that <span class="match term1">UVRAG</span> is ubiquitinated by <span class="match term0">SMURF1</span> at lysine residues 517 and 559, which decreases the association of <span class="match term1">UVRAG</span> with RUBCN and promotes autophagosome maturation	HECT	1	Other	H.sapiens
2411	SMUF1_HUMAN	Q7Z4L4_HUMAN	Q9HCE7	Q7Z4L4	SMURF1	TNIK	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2412	SMUF1_HUMAN	PPARG_HUMAN	Q9HCE7	P37231	SMURF1	PPARG	MEDLINE	30566427	Non-proteolytic ubiquitin modification of <span class="match term1">PPARgamma</span> by <span class="match term0">Smurf1</span> protects the liver from steatosis	HECT	1	Other	H.sapiens
2413	SMUF1_HUMAN	CSK22_HUMAN	Q9HCE7	P19784	SMURF1	CSNK2A2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2414	SMUF1_HUMAN	KPCI_HUMAN	Q9HCE7	P41743	SMURF1	PRKCI	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2415	SMUF1_HUMAN	MARK2_HUMAN	Q9HCE7	Q7KZI7	SMURF1	MARK2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2416	SMUF1_HUMAN	UBQL1_HUMAN	Q9HCE7	Q9UMX0	SMURF1	UBQLN1	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2417	SMUF1_HUMAN	SRC8_HUMAN	Q9HCE7	Q14247	SMURF1	CTTN	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2418	SMUF1_HUMAN	HOME2_HUMAN	Q9HCE7	Q9NSB8	SMURF1	HOMER2	High-throughput	20804422	2010_Andrews	HECT	1	Training data	H.sapiens
2419	SMUF2_HUMAN	SMAD4_HUMAN	Q9HAU4	Q13485	SMURF2	SMAD4	MEDLINE	15817471	We describe an equivalent mechanism of degradation of <span class="match term1">Smad4</span> by the above E3 ligases, via formation of ternary complexes between <span class="match term1">Smad4</span> and Smurfs, mediated by R-Smads (Smad2) or I-Smads (Smad6/7), acting as adaptors	HECT	1	Training data	H.sapiens
2420	SMUF2_HUMAN	SMAD1_HUMAN	Q9HAU4	Q15797	SMURF2	SMAD1	MEDLINE	11158580	<span class="match term0">Smurf2</span> selectively interacts with receptor-regulated Smads and preferentially targets <span class="match term1">Smad1</span> for ubiquitination and proteasome-mediated degradation	HECT	1	Training data	H.sapiens
2421	SMUF2_HUMAN	CTNB1_HUMAN	Q9HAU4	P35222	SMURF2	CTNNB1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2422	SMUF2_HUMAN	SMAD2_HUMAN	Q9HAU4	Q15796	SMURF2	SMAD2	MEDLINE	14507671	These data suggest that the decrease in <span class="match term1">Smad2</span> resulted from enhanced ubiquitin-dependent degradation of <span class="match term1">Smad2</span> mediated by <span class="match term0">Smurf2</span>, and is involved in the regulation of <span class="match term1">Smad2</span>-mediated TGF-beta signaling in nephritic glomeruli	HECT	1	Training data	H.sapiens
2423	SMUF2_HUMAN	BRE1A_HUMAN	Q9HAU4	Q5VTR2	SMURF2	RNF20	MEDLINE	22231558	UbiNet 2.0	HECT	1	Other	H.sapiens
2424	SMUF2_HUMAN	MD2L1_HUMAN	Q9HAU4	Q13257	SMURF2	MAD2L1	MEDLINE	18852296	UbiNet 2.0	HECT	1	Other	H.sapiens
2425	SMUF2_HUMAN	SMAD7_HUMAN	Q9HAU4	O15105	SMURF2	SMAD7	MEDLINE	15862290	Smad ubiquitination regulatory factor 2 (<span class="match term0">Smurf2</span>), a ubiquitin ligase for Smads, plays critical roles in the regulation of transforming growth factor-beta (TGF-beta)-Smad signaling via ubiquitin-dependent degradation of Smad2 and <span class="match term1">Smad7</span>	HECT	1	Training data	H.sapiens
2426	SMUF2_HUMAN	SMUF1_HUMAN	Q9HAU4	Q9HCE7	SMURF2	SMURF1	MEDLINE	20009572	<span class="match term1">Smurf1</span> regulates cell migration through ubiquitination of RhoA, talin head domain and hPEM2, while <span class="match term0">Smurf2</span> ubiquitinates <span class="match term1">Smurf1</span>, TGFbeta type I receptor and RaplB to modulate cell migration and adhesion	HECT	1	Training data	H.sapiens
2427	SMUF2_HUMAN	PARP1_HUMAN	Q9HAU4	P09874	SMURF2	PARP1	MEDLINE	32167680	We further study and prove that <span class="match term0">Smurf2</span> can promote <span class="match term1">PARP1</span> ubiquitination and degradation.	HECT	1	Other	H.sapiens
2428	SMUF2_HUMAN	SATB1_HUMAN	Q9HAU4	Q01826	SMURF2	SATB1	MEDLINE	30742943	Reversible regulation of <span class="match term1">SATB1</span> ubiquitination by USP47 and <span class="match term0">SMURF2</span> mediates colon cancer cell proliferation and tumor progression.	HECT	1	Other	H.sapiens
2429	SMUF2_HUMAN	RNF11_HUMAN	Q9HAU4	Q9Y3C5	SMURF2	RNF11	MEDLINE	14755250	Our results also demonstrate that AMSH is ubiquitinated by <span class="match term0">Smurf2</span> E3 ligase in the presence of <span class="match term1">RNF11</span> and that a consequent reduction in its steady-state level requires both <span class="match term1">RNF11</span> and <span class="match term0">Smurf2</span>	HECT	1	Training data	H.sapiens
2430	SMUF2_HUMAN	SKIL_HUMAN	Q9HAU4	P12757	SMURF2	SKIL	MEDLINE	15496141	However, in contrast with <span class="match term0">Smurf2</span>, NEDD4-2 failed to induce ubiquitination of <span class="match term1">SnoN</span> (Ski-related novel protein N), although NEDD4-2 bound to <span class="match term1">SnoN</span> via Smad2 more strongly than <span class="match term0">Smurf2</span>	HECT	1	Training data	H.sapiens
2431	SMUF2_HUMAN	RAP1B_HUMAN	Q9HAU4	P61224	SMURF2	RAP1B	MEDLINE	17318188	<span class="match term0">Smurf2</span> ubiquitinates inactive <span class="match term1">Rap1B</span> and initiates its degradation through the ubiquitin/proteasome pathway (UPS)	HECT	1	Training data	H.sapiens
2432	SMUF2_HUMAN	TNR1B_HUMAN	Q9HAU4	P20333	SMURF2	TNFRSF1B	MEDLINE	18671942	<span class="match term0">Smurf2</span> is a TRAF2 binding protein that triggers TNF-R2 ubiquitination and TNF-R2-induced JNK activation	HECT	1	Training data	H.sapiens
2433	SMUF2_HUMAN	TGFR1_HUMAN	Q9HAU4	P36897	SMURF2	TGFBR1	MEDLINE	17347560	In this study, we focused on Arkadia, <span class="match term0">Smurf2</span>, Smad7, and TGF-beta type I receptor (TbetaRI), principal molecules in the regulation of TGF-beta signaling, to understand the regulatory mechanism of ubiquitin-proteasomal degradation of TGF-beta signaling in the pathogenesis of renal fibrosis	HECT	1	Training data	H.sapiens
2434	SMUF2_HUMAN	STABP_HUMAN	Q9HAU4	O95630	SMURF2	STAMBP	MEDLINE	14755250	Our results also demonstrate that <span class="match term1">AMSH</span> is ubiquitinated by <span class="match term0">Smurf2</span> E3 ligase in the presence of RNF11 and that a consequent reduction in its steady-state level requires both RNF11 and <span class="match term0">Smurf2</span>	HECT	1	Training data	H.sapiens
2435	SMUF2_HUMAN	RHOA_HUMAN	Q9HAU4	P61586	SMURF2	RHOA	MEDLINE	21402695	UbiNet 2.0	HECT	1	Other	H.sapiens
2436	SMUF2_HUMAN	SMAD5_HUMAN	Q9HAU4	Q99717	SMURF2	SMAD5	MEDLINE	20484049	UbiNet 2.0	HECT	1	Other	H.sapiens
2437	SMUF2_HUMAN	KLF5_HUMAN	Q9HAU4	Q13887	SMURF2	KLF5	MEDLINE	21953463	UbiNet 2.0	HECT	1	Training data	H.sapiens
2438	SMUF2_HUMAN	ID3_HUMAN	Q9HAU4	Q02535	SMURF2	ID3	MEDLINE	21933340	UbiNet 2.0	HECT	1	Training data	H.sapiens
2439	SMUF2_HUMAN	H2AX_HUMAN	Q9HAU4	P16104	SMURF2	H2AX	MEDLINE	31533041	Suppression of PRMT5 occurs in methylthioadenosine phosphorylase (MTAP)-deficient glioblastoma cells and attenuates the expression of RNF168, leading to destabilization of <span class="match term1">H2AX</span> by E3 ubiquitin ligase <span class="match term0">SMURF2</span>	HECT	1	Other	H.sapiens
2440	SMUF2_HUMAN	TGFR2_HUMAN	Q9HAU4	P37173	SMURF2	TGFBR2	MEDLINE	22848678	UbiNet 2.0	HECT	1	Training data	H.sapiens
2441	SMUF2_HUMAN	RUNX2_HUMAN	Q9HAU4	Q13950	SMURF2	RUNX2	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2442	SMUF2_HUMAN	FBW1A_HUMAN	Q9HAU4	Q9Y297	SMURF2	BTRC	MEDLINE	24709419	UbiNet 2.0	HECT	1	Other	H.sapiens
2443	SMUF2_HUMAN	TRAF4_HUMAN	Q9HAU4	Q9BUZ4	SMURF2	TRAF4	MEDLINE	23973329	UbiNet 2.0	HECT	1	Other	H.sapiens
2444	SMUF2_HUMAN	GSK3B_HUMAN	Q9HAU4	P49841	SMURF2	GSK3B	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2445	SMUF2_HUMAN	TOP2A_HUMAN	Q9HAU4	P11388	SMURF2	TOP2A	MEDLINE	28611047	UbiNet 2.0	HECT	1	Other	H.sapiens
2446	SMUF2_HUMAN	SIR1_HUMAN	Q9HAU4	Q96EB6	SMURF2	SIRT1	MEDLINE	32361710	Here, we reported that the E3 ubiquitin ligase <span class="match term0">SMURF2</span> interacts with <span class="match term1">SIRT1</span> and mediates its ubiquitination and degradation	HECT	1	Other	H.sapiens
2447	SMUF2_HUMAN	EZH2_HUMAN	Q9HAU4	Q15910	SMURF2	EZH2	MEDLINE	31948940	Genotoxin treatments augmented <span class="match term1">EZH2</span> acetylation, leading to reduced association between <span class="match term1">EZH2</span> and its E3 ubiquitin ligase <span class="match term0">SMURF2</span>	HECT	1	Other	H.sapiens
2448	SMUF2_HUMAN	AXIN1_HUMAN	Q9HAU4	O15169	SMURF2	AXIN1	MEDLINE	20858899	Here, we show that <span class="match term0">Smurf2</span> is an E3 ubiquitin ligase for <span class="match term1">Axin</span>	HECT	1	Other	H.sapiens
2449	SMUF2_HUMAN	ID1_HUMAN	Q9HAU4	P41134	SMURF2	ID1	MEDLINE	21933340	UbiNet 2.0	HECT	1	Training data	H.sapiens
2450	SMUF2_HUMAN	MLXPL_HUMAN	Q9HAU4	Q9NP71	SMURF2	MLXIPL	MEDLINE	31409643	We observed that <span class="match term0">SMURF2</span> interacts with <span class="match term1">ChREBP</span> and promotes <span class="match term1">ChREBP</span> ubiquitination and degradation via the proteasome pathway	HECT	1	Other	H.sapiens
2451	SMUF2_HUMAN	SMAD3_HUMAN	Q9HAU4	P84022	SMURF2	SMAD3	MEDLINE	15108358	UbiNet 2.0	HECT	1	Training data	H.sapiens
2452	SMUF2_HUMAN	STALP_HUMAN	Q9HAU4	Q96FJ0	SMURF2	STAMBPL1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
2453	SMUF2_HUMAN	EGFR_HUMAN	Q9HAU4	P00533	SMURF2	EGFR	MEDLINE	21750651	UbiNet 2.0	HECT	1	Training data	H.sapiens
2454	SOCS1_HUMAN	JAK2_HUMAN	O15524	O60674	SOCS1	JAK2	MEDLINE	11278610	Degradation of <span class="match term1">JAK2</span> depended on its phosphorylation and its high affinity binding with <span class="match term0">SOCS1</span> through the kinase inhibitory region and the SH2 domain	SOCS_VHL_BC-box	1	Training data	H.sapiens
2455	SOCS1_HUMAN	TF65_HUMAN	O15524	Q04206	SOCS1	RELA	UniProt	SOCS1_HUMAN	Promotes ubiquitination of NF-kappa-B subunit <span class="match term1">RELA</span> and its subsequent proteasomal degradation	SOCS_VHL_BC-box	1	Training data	H.sapiens
2456	SOCS1_HUMAN	VAV_HUMAN	O15524	P15498	SOCS1	VAV1	MEDLINE	10747851	These results suggest that <span class="match term0">SOCS1</span> programs <span class="match term1">VAV</span> degradation by acting as a substrate-specific recognition component of a VCB-like ubiquitin ligase complex	SOCS_VHL_BC-box	1	Training data	H.sapiens
2457	SOCS1_HUMAN	IRS1_HUMAN	O15524	P35568	SOCS1	IRS1	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	H.sapiens
2458	SOCS1_HUMAN	LYN_HUMAN	O15524	P07948	SOCS1	LYN	MEDLINE	17905674	Intriguingly, phosphorylated Y314 also binds the suppressor of cytokine signalling 1 (<span class="match term0">SOCS1</span>), resulting in elevated ubiquitination and degradation of <span class="match term1">Lyn</span>	SOCS_VHL_BC-box	1	Training data	H.sapiens
2459	SOCS1_HUMAN	JAK1_HUMAN	O15524	P23458	SOCS1	JAK1	MEDLINE	32532301	IAV infection upregulated the suppressor of cytokine signaling (SOCS) protein <span class="match term0">SOCS1</span>, and <span class="match term0">SOCS1</span> mediated the ubiquitination and degradation of <span class="match term1">JAK1</span>	SOCS_VHL_BC-box	1	Other	H.sapiens
2460	SOCS1_HUMAN	IRS2_HUMAN	O15524	Q9Y4H2	SOCS1	IRS2	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	H.sapiens
2461	SOCS2_HUMAN	SOCS1_HUMAN	O14508	O15524	SOCS2	SOCS1	MEDLINE	17898043	UbiNet 2.0	Other	1	Training data	H.sapiens
2462	SOCS2_HUMAN	GHR_HUMAN	O14508	P10912	SOCS2	GHR	MEDLINE	21980433	The <span class="match term0">SOCS2</span> ubiquitin ligase complex regulates growth hormone receptor levels.	Other	1	Other	H.sapiens
2463	SOCS2_HUMAN	SOCS3_HUMAN	O14508	O14543	SOCS2	SOCS3	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2464	SOCS3_HUMAN	IRS2_HUMAN	O14543	Q9Y4H2	SOCS3	IRS2	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	H.sapiens
2465	SOCS3_HUMAN	JAK2_HUMAN	O14543	O60674	SOCS3	JAK2	MEDLINE	24438103	Reconstruction of an active <span class="match term0">SOCS3</span>-based E3 ubiquitin ligase complex in vitro: identification of the active components and <span class="match term1">JAK2</span> and gp130 as substrates.	SOCS_VHL_BC-box	1	Other	H.sapiens
2466	SOCS3_HUMAN	IRS1_HUMAN	O14543	P35568	SOCS3	IRS1	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	H.sapiens
2467	SOCS3_HUMAN	SIGL7_HUMAN	O14543	Q9Y286	SOCS3	SIGLEC7	MEDLINE	17138568	Following ligation, the ECS E3 ligase is recruited by <span class="match term0">SOCS3</span> to target Siglec 7 for proteasomal degradation, and <span class="match term0">SOCS3</span> expression is decreased concomitantly	SOCS_VHL_BC-box	1	Training data	H.sapiens
2468	SOCS3_HUMAN	IL6RB_HUMAN	O14543	P40189	SOCS3	IL6ST	MEDLINE	24438103	Reconstruction of an active <span class="match term0">SOCS3</span>-based E3 ubiquitin ligase complex in vitro: identification of the active components and JAK2 and <span class="match term1">gp130</span> as substrates.	SOCS_VHL_BC-box	1	Other	H.sapiens
2469	SOCS4_HUMAN	DAB1_HUMAN	Q8WXH5	O75553	SOCS4	DAB1	MEDLINE	24210661	UbiNet 2.0	SOCS_VHL_BC-box	1	Other	H.sapiens
2470	SOCS5_HUMAN	EGFR_HUMAN	O75159	P00533	SOCS5	EGFR	MEDLINE	15590694	Interestingly, <span class="match term1">EGFR</span> is degraded by <span class="match term0">SOCS5</span> prior to EGF treatment in a ligand- and c-Cbl-independent manner	SOCS_VHL_BC-box	1	Training data	H.sapiens
2471	SOCS5_HUMAN	STAT1_HUMAN	O75159	P42224	SOCS5	STAT1	MEDLINE	33391546	Overexpression of COL6A1 promoted OS cell migration and invasion via interacting with <span class="match term0">SOCS5</span> to suppress <span class="match term1">STAT1</span> expression and activation in an ubiquitination and proteasomal degradation manner	SOCS_VHL_BC-box	1	Other	H.sapiens
2472	SOCS6_HUMAN	KIT_HUMAN	O14544	P10721	SOCS6	KIT	MEDLINE	21030588	Structural basis for c-<span class="match term1">KIT</span> inhibition by the suppressor of cytokine signaling 6 (<span class="match term0">SOCS6</span>) ubiquitin ligase	SOCS_VHL_BC-box	1	Other	H.sapiens
2473	SOCS7_HUMAN	DAB1_HUMAN	O14512	O75553	SOCS7	DAB1	MEDLINE	24210661	24210661	SOCS_VHL_BC-box	1	Other	H.sapiens
2474	SPOP_HUMAN	BRD4_HUMAN	O43791	O60885	SPOP	BRD4	MEDLINE	28805820	Prostate cancer-associated <span class="match term0">SPOP</span> mutations confer resistance to BET inhibitors through stabilization of <span class="match term1">BRD4</span>.	Other	1	Other	H.sapiens
2475	SPOP_HUMAN	BMI1_HUMAN	O43791	P35226	SPOP	BMI1	MEDLINE	15897469	UbiNet 2.0	Other	1	Training data	H.sapiens
2476	SPOP_HUMAN	PTEN_HUMAN	O43791	P60484	SPOP	PTEN	MEDLINE	24656772	UbiNet 2.0	Other	1	Other	H.sapiens
2477	SPOP_HUMAN	BRMS1_HUMAN	O43791	Q9HCU9	SPOP	BRMS1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2478	SPOP_HUMAN	BRD3_HUMAN	O43791	Q15059	SPOP	BRD3	MEDLINE	28805821	Here we analyzed changes in the ubiquitin landscape induced by endometrial cancer-associated <span class="match term0">SPOP</span> mutations and identified BRD2, <span class="match term1">BRD3</span> and BRD4 proteins (BETs) as <span class="match term0">SPOP</span>-CUL3 substrates that are preferentially degraded by endometrial cancer-associated <span class="match term0">SPOP</span> mutants	Other	1	Other	H.sapiens
2479	SPOP_HUMAN	MYD88_HUMAN	O43791	Q99836	SPOP	MYD88	MEDLINE	31406379	The E3 ubiquitin ligase <span class="match term0">SPOP</span> controls resolution of systemic inflammation by triggering <span class="match term1">MYD88</span> degradation	Other	1	Other	H.sapiens
2480	SPOP_HUMAN	TIF1A_HUMAN	O43791	O15164	SPOP	TRIM24	MEDLINE	25278611	UbiNet 2.0	Other	1	Other	H.sapiens
2481	SPOP_HUMAN	ESR1_HUMAN	O43791	P03372	SPOP	ESR1	MEDLINE	25766326	UbiNet 2.0	Other	1	Training data	H.sapiens
2482	SPOP_HUMAN	DEK_HUMAN	O43791	P35659	SPOP	DEK	MEDLINE	25278611	UbiNet 2.0	Other	1	Other	H.sapiens
2483	SPOP_HUMAN	ILF3_HUMAN	O43791	Q12906	SPOP	ILF3	MEDLINE	31772275	Mechanistic studies showed that the EGF-MEK-ERK pathway mediates <span class="match term1">ILF3</span> phosphorylation, which hinders E3 ligase speckle-type POZ protein (<span class="match term0">SPOP</span>)-mediated poly-ubiquitination and degradation of <span class="match term1">ILF3</span>	Other	1	Other	H.sapiens
2484	SPOP_HUMAN	GLYR1_HUMAN	O43791	Q49A26	SPOP	GLYR1	MEDLINE	25278611	UbiNet 2.0	Other	1	Other	H.sapiens
2485	SPOP_HUMAN	CAPR1_HUMAN	O43791	Q14444	SPOP	CAPRIN1	MEDLINE	31771591	RESULTS: The cytoplasmic form of wild-type (WT) <span class="match term0">SPOP</span> recognizes and triggers ubiquitin-dependent degradation of <span class="match term1">Caprin1</span>	Other	1	Other	H.sapiens
2486	SPOP_HUMAN	TP53B_HUMAN	O43791	Q12888	SPOP	TP53BP1	MEDLINE	34144977	<span class="match term1">53BP1</span>-bound <span class="match term0">SPOP</span> induces polyubiquitination of <span class="match term1">53BP1</span>, eliciting <span class="match term1">53BP1</span> extraction from chromatin by a valosin-containing protein/p97 segregase complex	Other	1	Other	H.sapiens
2487	SPOP_HUMAN	NCOA3_HUMAN	O43791	Q9Y6Q9	SPOP	NCOA3	MEDLINE	21577200	UbiNet 2.0	Other	1	Other	H.sapiens
2488	SPOP_HUMAN	ERG_HUMAN	O43791	P11308	SPOP	ERG	MEDLINE	29202479	Recent reports suggest that <span class="match term0">SPOP</span> acts as a ubiquitin ligase for <span class="match term1">ERG</span> and propose that <span class="match term1">ERG</span> stabilization is the oncogenic effector of <span class="match term0">SPOP</span> mutation	Other	1	Other	H.sapiens
2489	SPOP_HUMAN	H2AY_HUMAN	O43791	O75367	SPOP	MACROH2A1	MEDLINE	15897469	UbiNet 2.0	Other	1	Training data	H.sapiens
2490	SPOP_HUMAN	ODPX_HUMAN	O43791	O00330	SPOP	PDHX	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2491	SPOP_HUMAN	LATS1_HUMAN	O43791	O95835	SPOP	LATS1	MEDLINE	32460168	Mechanistically, <span class="match term0">SPOP</span> specifically interacted with <span class="match term1">LATS1</span>, and promoted the poly-ubiquitination and subsequent degradation of <span class="match term1">LATS1</span> in a degron-dependent manner	Other	1	Other	H.sapiens
2492	SPOP_HUMAN	FADD_HUMAN	O43791	Q13158	SPOP	FADD	MEDLINE	30190126	We also found that ubiquitin ligase SPOP (speckle-type POZ protein) binds to <span class="match term1">FADD</span> and mediates its degradation, which can be blocked by MG132 treatment	Other	1	Other	H.sapiens
2493	SPOP_HUMAN	INF2_HUMAN	O43791	Q27J81	SPOP	INF2	MEDLINE	28448495	Here, we revealed that <span class="match term0">SPOP</span> recognizes a Ser/Thr (S/T)-rich motif in the C-terminal region of <span class="match term1">INF2</span> and triggers atypical polyubiquitination of <span class="match term1">INF2</span>	Other	1	Other	H.sapiens
2494	SPOP_HUMAN	DPPA2_HUMAN	O43791	Q7Z7J5	SPOP	DPPA2	MEDLINE	33862460	<span class="match term0">SPOP</span> suppresses testicular germ cell tumors progression through ubiquitination and degradation of <span class="match term1">DPPA2</span>	Other	1	Other	H.sapiens
2495	SPOP_HUMAN	JUN_HUMAN	O43791	P05412	SPOP	JUN	MEDLINE	19164706	UbiNet 2.0	Other	1	Training data	H.sapiens
2496	SPOP_HUMAN	DUS7_HUMAN	O43791	Q16829	SPOP	DUSP7	MEDLINE	24656772	UbiNet 2.0	Other	1	Other	H.sapiens
2497	SPOP_HUMAN	GLI2_HUMAN	O43791	P10070	SPOP	GLI2	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2498	SPOP_HUMAN	DAXX_HUMAN	O43791	Q9UER7	SPOP	DAXX	MEDLINE	16524876	UbiNet 2.0	Other	1	Training data	H.sapiens
2499	SPOP_HUMAN	CDC20_HUMAN	O43791	Q12834	SPOP	CDC20	MEDLINE	27780719	Here, we identified the <span class="match term1">Cdc20</span> oncoprotein as a novel ubiquitin substrate of <span class="match term0">SPOP</span>	Other	1	Other	H.sapiens
2500	SPOP_HUMAN	DUS6_HUMAN	O43791	Q16828	SPOP	DUSP6	MEDLINE	24656772	UbiNet 2.0	Other	1	Other	H.sapiens
2501	SPOP_HUMAN	CCNE1_HUMAN	O43791	P24864	SPOP	CCNE1	MEDLINE	30237511	UbiNet 2.0	Other	1	Other	H.sapiens
2502	SPOP_HUMAN	HIPK2_HUMAN	O43791	Q9H2X6	SPOP	HIPK2	MEDLINE	34133717	Here, we report that upon DNA damage, <span class="match term0">SPOP</span> is phosphorylated at Ser119 by the ATM serine/threonine kinase, which potentiates the binding of <span class="match term0">SPOP</span> to homeodomain-interacting protein kinase 2 (<span class="match term1">HIPK2</span>), resulting in a nondegradative ubiquitination of <span class="match term1">HIPK2</span>	Other	1	Other	H.sapiens
2503	SPOP_HUMAN	BRD2_HUMAN	O43791	P25440	SPOP	BRD2	MEDLINE	28805821	Here we analyzed changes in the ubiquitin landscape induced by endometrial cancer-associated <span class="match term0">SPOP</span> mutations and identified <span class="match term1">BRD2</span>, BRD3 and BRD4 proteins (BETs) as SPOP-CUL3 substrates that are preferentially degraded by endometrial cancer-associated SPOP mutants	Other	1	Other	H.sapiens
2504	SPOP_HUMAN	ZBTB3_HUMAN	O43791	Q9H5J0	SPOP	ZBTB3	MEDLINE	28805821	Here we analyzed changes in the ubiquitin landscape induced by endometrial cancer-associated <span class="match term0">SPOP</span> mutations and identified <span class="match term1">BRD2</span>,  <span class="match term1">BRD3</span> and BRD4 proteins (BETs) as SPOP-CUL3 substrates that are preferentially degraded by endometrial cancer-associated SPOP mutants	Other	1	Other	H.sapiens
2505	SPOP_HUMAN	FAS_HUMAN	O43791	P49327	SPOP	FASN	MEDLINE	30955223	Here, we provide evidence that <span class="match term1">FASN</span> is a substrate of <span class="match term0">SPOP</span> and that interaction of these proteins induces <span class="match term1">FASN</span> ubiquitination and proteasome-dependent degradation	Other	1	Other	H.sapiens
2506	SPOP_HUMAN	GLI3_HUMAN	O43791	P10071	SPOP	GLI3	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2507	SPOP_HUMAN	ANDR_HUMAN	O43791	P10275	SPOP	AR	MEDLINE	24508459;25274033	24508459;25274033	Other	1	Other	H.sapiens
2508	SPOP_HUMAN	NANOG_HUMAN	O43791	Q9H9S0	SPOP	NANOG	MEDLINE	31624231:30595538	31624231:30595538	Other	1	Other	H.sapiens
2509	SPOP_HUMAN	PD1L1_HUMAN	O43791	Q9NZQ7	SPOP	CD274	MEDLINE	29160310	Loss-of-function mutations in <span class="match term0">SPOP</span> compromise ubiquitination-mediated <span class="match term1">PD-L1</span> degradation, leading to increased <span class="match term1">PD-L1</span> levels and reduced numbers of tumour-infiltrating lymphocytes in mouse tumours and in primary human prostate cancer specimens	Other	1	Other	H.sapiens
2510	SPOP_HUMAN	HDAC6_HUMAN	O43791	Q9UBN7	SPOP	HDAC6	MEDLINE	28599312	Cullin 3SPOP ubiquitin E3 ligase promotes the poly-ubiquitination and degradation of <span class="match term1">HDAC6</span>	Other	1	Other	H.sapiens
2511	SPOP_HUMAN	KCNH2_HUMAN	O43791	Q12809	SPOP	KCNH2	MEDLINE	26344095	UbiNet 2.0	Other	1	Other	H.sapiens
2512	SPOP_HUMAN	SETD2_HUMAN	O43791	Q9BYW2	SPOP	SETD2	MEDLINE	27614073	We demonstrate that <span class="match term0">SPOP</span> is critically involved in <span class="match term1">SETD2</span> stability control and that the <span class="match term0">SPOP</span>/CUL3 complex is responsible for <span class="match term1">SETD2</span> polyubiquitination both in vivo and in vitro ChIP-Seq analysis and biochemical experiments demonstrate that modulation of <span class="match term0">SPOP</span> expression confers differential H3K36me3 on <span class="match term1">SETD2</span> target genes, and induce H3K36me3-coupled alternative splicing events	Other	1	Other	H.sapiens
2513	SPOP_HUMAN	PRGR_HUMAN	O43791	P06401	SPOP	PGR	MEDLINE	26693071	UbiNet 2.0	Other	1	Other	H.sapiens
2514	SPOP_HUMAN	GLI1_HUMAN	O43791	P08151	SPOP	GLI1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2515	SPSB2_HUMAN	NOS2_HUMAN	Q99619	P35228	SPSB2	NOS2	MEDLINE	20603330	20603330	SOCS_VHL_BC-box	1	Other	H.sapiens
2516	SPSB2_HUMAN	NANO2_HUMAN	Q99619	P60321	SPSB2	NANOS2	MEDLINE	20603330	UbiNet 2.0	SOCS_VHL_BC-box	1	Other	H.sapiens
2517	SPSB3_HUMAN	SNAI1_HUMAN	Q6PJ21	O95863	SPSB3	SNAI1	MEDLINE	29059170	In this study, we carried out a luciferase-based genome-wide screening using small interfering RNA library against ~200 of E3 ligases and ubiquitin-related genes and identified SOCS box protein <span class="match term0">SPSB3</span> as a novel E3 ligase component that targets <span class="match term1">SNAIL</span> into polyubiquitination and degradation in response to GSK-3beta phosphorylation of <span class="match term1">SNAIL</span>	SOCS_VHL_BC-box	1	Other	H.sapiens
2518	SQSTM_HUMAN	LDHA_HUMAN	Q13501	P00338	SQSTM1	LDHA	MEDLINE	32859246	CONCLUSIONS: Our data revealed a novel lysosomal pathway of <span class="match term1">LDHA</span> degradation, which is mediated by the binding of K63-ubiquitinated <span class="match term1">LDHA</span> to <span class="match term0">SQSTM1</span>	Other	1	Other	H.sapiens
2519	STABP_HUMAN	NLRP3_HUMAN	O95630	Q96P20	STAMBP	NLRP3	MEDLINE	33253913	These findings describe a unique mechanism of non-degradative ubiquitination of <span class="match term1">NLRP3</span> by <span class="match term0">STAMBP</span> to limit excessive inflammasome activation and to reduce injurious IL-1beta signaling.	SOCS_VHL_BC-box	1	Other	H.sapiens
2520	CHIP_HUMAN	HSP7C_HUMAN	Q9UNE7	P11142	STUB1	HSPA8	MEDLINE	20675402	<span class="match term0">CHIP</span> appears to sort newly synthesized Hsp90-unchaperoned BCR-ABL to the proteasome not only by inhibiting <span class="match term1">Hsc70</span> and thereby promoting Bag1 to bind BCR-ABL, but also by ubiquitinating BCR-ABL	UBOX	1	Training data	H.sapiens
2521	CHIP_HUMAN	PSMD4_HUMAN	Q9UNE7	P55036	STUB1	PSMD4	MEDLINE	19240029	Furthermore, if the <span class="match term1">S5a</span> UIM domains were fused to GST, the protein was rapidly ubiquitinated by MuRF1 and <span class="match term0">CHIP</span>	UBOX	1	Training data	H.sapiens
2522	CHIP_HUMAN	ANDR_HUMAN	Q9UNE7	P10275	STUB1	AR	MEDLINE	15107424	We found that <span class="match term0">CHIP</span> functions as a negative regulator of <span class="match term1">AR</span> transcriptional activity by promoting <span class="match term1">AR</span> degradation	UBOX	1	Training data	H.sapiens
2523	CHIP_HUMAN	SMG5_HUMAN	Q9UNE7	Q9UPR3	STUB1	SMG5	MEDLINE	16809764	Phosphorylated HDAC8 preferentially recruits Hsp70 to a complex that inhibits the <span class="match term0">CHIP</span> (C-terminal heat shock protein interacting protein) E3 ligase-mediated degradation of hEST1B	UBOX	1	Training data	H.sapiens
2524	CHIP_HUMAN	RUNX1_HUMAN	Q9UNE7	Q01196	STUB1	RUNX1	MEDLINE	19524548	Interestingly, we found that <span class="match term0">CHIP</span>-mediated degradation of <span class="match term1">Runx1</span> is independent of the molecular chaperone Hsp70/90	UBOX	1	Training data	H.sapiens
2525	CHIP_HUMAN	HIF1A_HUMAN	Q9UNE7	Q16665	STUB1	HIF1A	MEDLINE	19940151	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2526	CHIP_HUMAN	FOXP3_HUMAN	Q9UNE7	Q9BZS1	STUB1	FOXP3	MEDLINE	23973223	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2527	CHIP_HUMAN	TAU_HUMAN	Q9UNE7	P10636	STUB1	MAPT	MEDLINE	16807328	Based on these findings, we propose that polyubiquitination of <span class="match term1">tau</span> by <span class="match term0">CHIP</span> may facilitate the formation of insoluble filamentous <span class="match term1">tau</span> lesions	UBOX	1	Training data	H.sapiens
2528	CHIP_HUMAN	NANO2_HUMAN	Q9UNE7	P60321	STUB1	NANOS2	MEDLINE	22199232	E3Net	UBOX	1	Other	H.sapiens
2529	CHIP_HUMAN	CREM_HUMAN	Q9UNE7	Q03060	STUB1	CREM	MEDLINE	22267842	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2530	CHIP_HUMAN	M3K11_HUMAN	Q9UNE7	Q16584	STUB1	MAP3K11	MEDLINE	24912674	UbiNet 2.0	UBOX	1	Other	H.sapiens
2531	CHIP_HUMAN	SC6A4_HUMAN	Q9UNE7	P31645	STUB1	SLC6A4	MEDLINE	22199232	E3Net	UBOX	1	Other	H.sapiens
2532	CHIP_HUMAN	RAF1_HUMAN	Q9UNE7	P04049	STUB1	RAF1	MEDLINE	18922468	In the absence of S621 phosphorylation, <span class="match term1">CRAF</span> is degraded by the proteasome by mechanisms that do not uniquely rely on the E3 ubiquitin ligase <span class="match term0">CHIP</span>	UBOX	1	Training data	H.sapiens
2533	CHIP_HUMAN	GATA4_HUMAN	Q9UNE7	P43694	STUB1	GATA4	MEDLINE	22199232	E3Net	UBOX	1	Other	H.sapiens
2534	CHIP_HUMAN	BAG1_HUMAN	Q9UNE7	Q99933	STUB1	BAG1	MEDLINE	11676916	Consequently, <span class="match term1">BAG-1</span> promotes <span class="match term0">CHIP</span>-induced degradation of the glucocorticoid hormone receptor in vivo	UBOX	1	Training data	H.sapiens
2535	CHIP_HUMAN	NOS1_HUMAN	Q9UNE7	P29475	STUB1	NOS1	MEDLINE	15466472	Moreover, incubation of <span class="match term1">nNOS</span> with a purified system containing an E1 ubiquitin-activating enzyme, an E2 ubiquitin carrier protein conjugating enzyme (UbcH5a), <span class="match term0">CHIP</span>, glutathione S-transferase-tagged ubiquitin, and an ATP-generating system leads to the ubiquitylation of <span class="match term1">nNOS</span>	UBOX	1	Training data	H.sapiens
2536	CHIP_HUMAN	GCYA2_HUMAN	Q9UNE7	P33402	STUB1	GUCY1A2	MEDLINE	17873020	UbiNet 2.0	UBOX	1	Other	H.sapiens
2537	CHIP_HUMAN	CHIP_HUMAN	Q9UNE7	Q9UNE7	STUB1	STUB1	UniProt	CHIP_HUMAN	The FTSH1 precursor is ubiquitinated by <span class="match term0">CHIP</span> in the cytoplasm	UBOX	1	Training data	H.sapiens
2538	CHIP_HUMAN	IRF1_HUMAN	Q9UNE7	P10914	STUB1	IRF1	MEDLINE	20947504	UbiNet 2.0	UBOX	1	Other	H.sapiens
2539	CHIP_HUMAN	S100P_HUMAN	Q9UNE7	P25815	STUB1	S100P	MEDLINE	23344957	UbiNet 2.0	UBOX	1	Other	H.sapiens
2540	CHIP_HUMAN	ATCAY_HUMAN	Q9UNE7	Q86WG3	STUB1	ATCAY	MEDLINE	16275660	UbiNet 2.0	UBOX	1	Other	H.sapiens
2541	CHIP_HUMAN	EPHA2_HUMAN	Q9UNE7	P29317	STUB1	EPHA2	MEDLINE	19567782	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2542	CHIP_HUMAN	NOS2_HUMAN	Q9UNE7	P35228	STUB1	NOS2	MEDLINE	19362296	Furthermore, <span class="match term0">CHIP</span> promoted ubiquitination and proteasomal degradation of <span class="match term1">iNOS</span> by associating with <span class="match term1">iNOS</span>	UBOX	1	Training data	H.sapiens
2543	CHIP_HUMAN	ERBB2_HUMAN	Q9UNE7	P04626	STUB1	ERBB2	MEDLINE	18655187	In addition, the carboxyl terminus of Hsc70-interacting protein (<span class="match term0">CHIP</span>), a chaperone-dependent E3 ubiquitin ligase, played a crucial role in the quercetin-induced ubiquitination of <span class="match term1">Her-2</span>/neu	UBOX	1	Training data	H.sapiens
2544	CHIP_HUMAN	NOS3_HUMAN	Q9UNE7	P29474	STUB1	NOS3	MEDLINE	14507928	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2545	CHIP_HUMAN	NCOA3_HUMAN	Q9UNE7	Q9Y6Q9	STUB1	NCOA3	MEDLINE	19198599	Proteomic analysis identified the transcriptional co-activator <span class="match term1">SRC-3</span> (refs 13, 14, 15, 16, 17, 18, 19) as a direct target for ubiquitylation and degradation by <span class="match term0">CHIP</span>.	UBOX	1	Training data	H.sapiens
2546	CHIP_HUMAN	INSR_HUMAN	Q9UNE7	P06213	STUB1	INSR	MEDLINE	28431247	28431247	UBOX	1	Other	H.sapiens
2547	CHIP_HUMAN	DPOLB_HUMAN	Q9UNE7	P06746	STUB1	POLB	MEDLINE	19713937	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2548	CHIP_HUMAN	SNPH_HUMAN	Q9UNE7	O15079	STUB1	SNPH	MEDLINE	29898993	Using a global proteomics screen, we show that <span class="match term1">SNPH</span> associates with multiple regulators of ubiquitin-dependent responses and is ubiquitinated by the E3 ligase CHIP (or <span class="match term0">STUB1</span>) on Lys111 and Lys153 in the microtubule-binding domain	UBOX	1	Other	H.sapiens
2549	CHIP_HUMAN	ESR1_HUMAN	Q9UNE7	P03372	STUB1	ESR1	MEDLINE	19098309	These findings indicate that Csp not only regulates the exit of CFTR from the <span class="match term1">ER</span>, but that this action is accompanied by Hsc70/Hsp70 and <span class="match term0">CHIP</span>-mediated CFTR degradation	UBOX	1	Training data	H.sapiens
2550	CHIP_HUMAN	DLK1_HUMAN	Q9UNE7	P80370	STUB1	DLK1	MEDLINE	22199232	E3Net	UBOX	1	Other	H.sapiens
2551	CHIP_HUMAN	CP3A4_HUMAN	Q9UNE7	P08684	STUB1	CYP3A4	MEDLINE	19103148	<span class="match term1">CYP3A4</span> ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and <span class="match term0">CHIP</span> E3 ligases	UBOX	1	Training data	H.sapiens
2552	CHIP_HUMAN	NPM_HUMAN	Q9UNE7	P06748	STUB1	NPM1	MEDLINE	15126367	In line with these observations, the carboxyl hsp70-interacting ubiquitin ligase (<span class="match term0">CHIP</span>), was shown to increase basal ubiquitination and turnover of <span class="match term1">NPM</span>-ALK kinase, supporting a mechanism whereby <span class="match term1">NPM</span>-ALK proceeds rapidly toward hsp70-assisted ubiquitin-dependent proteasomal degradation, when chaperoning activity of hsp90 is prohibited by 17-AAG	UBOX	1	Training data	H.sapiens
2553	CHIP_HUMAN	CIP2A_HUMAN	Q9UNE7	Q8TCG1	STUB1	CIP2A	MEDLINE	24293411	UbiNet 2.0	UBOX	1	Other	H.sapiens
2554	CHIP_HUMAN	M3K12_HUMAN	Q9UNE7	Q12852	STUB1	MAP3K12	MEDLINE	16931512	Interestingly, the Hsp70 co-chaperone <span class="match term0">CHIP</span>, an E3 ubiquitin ligase, seems to be indispensable for this process since Hsp70 failed to induce <span class="match term1">DLK</span> degradation in COS-7 cells expressing a <span class="match term0">CHIP</span> mutant unable to catalyze ubiquitination or in immortalized fibroblasts derived from <span class="match term0">CHIP</span> knock-out mice	UBOX	1	Training data	H.sapiens
2555	CHIP_HUMAN	TAL1_HUMAN	Q9UNE7	P17542	STUB1	TAL1	MEDLINE	17962192	In contrast to the fact that the N-terminal tetratricopeptide region (TPR) domain of <span class="match term0">CHIP</span> is necessary and sufficient for E47 ubiquitination and degradation, <span class="match term0">CHIP</span> promoted <span class="match term1">Tal1</span> degradation with both chaperone binding and ubiquitin ligase activities, which are mediated by its TPR domain and U box, respectively	UBOX	1	Training data	H.sapiens
2556	CHIP_HUMAN	AHR_HUMAN	Q9UNE7	P35869	STUB1	AHR	MEDLINE	17209571	Our results suggest a model where the E3 ubiquitin ligase <span class="match term0">CHIP</span> cooperates with other ubiquitination factors to remodel native <span class="match term1">AhR</span>-hsp90 complexes and where co-chaperones such as the XAP2 may affect the ability of <span class="match term0">CHIP</span> to target <span class="match term1">AhR</span> complexes for ubiquitination	UBOX	1	Training data	H.sapiens
2557	CHIP_HUMAN	TRAF2_HUMAN	Q9UNE7	Q12933	STUB1	TRAF2	MEDLINE	21793045	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2558	CHIP_HUMAN	ERN1_HUMAN	Q9UNE7	O75460	STUB1	ERN1	MEDLINE	25225294	UbiNet 2.0	UBOX	1	Other	H.sapiens
2559	CHIP_HUMAN	ATX3_HUMAN	Q9UNE7	P54252	STUB1	ATXN3	MEDLINE	24106274	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2560	CHIP_HUMAN	DAPK1_HUMAN	Q9UNE7	P53355	STUB1	DAPK1	MEDLINE	17324930	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2561	CHIP_HUMAN	CFTR_HUMAN	Q9UNE7	P13569	STUB1	CFTR	MEDLINE	19625452	<span class="match term0">CHIP</span> and RMA1 recognize different regions of <span class="match term1">CFTR</span> and a large pool of nascent CFTRDeltaF508 is ubiquitinated by RMA1 before Corr-4a action	UBOX	1	Training data	H.sapiens
2562	CHIP_HUMAN	SODC_HUMAN	Q9UNE7	P00441	STUB1	SOD1	MEDLINE	17157513	One of the Dorfin-<span class="match term0">CHIP</span> chimeric proteins, Dorfin-<span class="match term0">CHIP</span>(L), ubiquitylated mutant <span class="match term1">SOD1</span> more effectively than did Dorfin(WT) and <span class="match term0">CHIP</span> in vivo, and degraded mutant <span class="match term1">SOD1</span> protein more rapidly than Dorfin(WT) does	UBOX	1	Training data	H.sapiens
2563	CHIP_HUMAN	P53_HUMAN	Q9UNE7	P04637	STUB1	TP53	MEDLINE	20618441	Polyubiquitination of heat-denatured luciferase and the native substrate <span class="match term1">p53</span> was much more efficient in the presence of Hsc70 and Hdj1 than in the presence of Hsp90, indicating that <span class="match term0">CHIP</span> preferentially ubiquitinates Hsp70-bound substrates	UBOX	1	Training data	H.sapiens
2564	CHIP_HUMAN	KAPCA_HUMAN	Q9UNE7	P17612	STUB1	PRKACA	MEDLINE	31189917	UbiNet 2.0	UBOX	1	Other	H.sapiens
2565	CHIP_HUMAN	FOXO1_HUMAN	Q9UNE7	Q12778	STUB1	FOXO1	MEDLINE	19483080	C terminus of Hsc70-interacting protein promotes smooth muscle cell proliferation and survival through ubiquitin-mediated degradation of <span class="match term1">FoxO1</span>	UBOX	1	Training data	H.sapiens
2566	CHIP_HUMAN	AKT1_HUMAN	Q9UNE7	P31749	STUB1	AKT1	MEDLINE	18292230	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2567	CHIP_HUMAN	SYUA_HUMAN	Q9UNE7	P37840	STUB1	SNCA	MEDLINE	18436529	<span class="match term0">CHIP</span> targets toxic alpha-Synuclein oligomers for degradation	UBOX	1	Training data	H.sapiens
2568	CHIP_HUMAN	A6MI22_9HIV1	Q9UNE7	A6MI22	STUB1	tat	MEDLINE	30885946	UbiNet 2.0	UBOX	1	Other	H.sapiens
2569	CHIP_HUMAN	BACE1_HUMAN	Q9UNE7	P56817	STUB1	BACE1	MEDLINE	25773675	UbiNet 2.0	UBOX	1	Other	H.sapiens
2570	CHIP_HUMAN	SMAD1_HUMAN	Q9UNE7	Q15797	STUB1	SMAD1	MEDLINE	14701756	Consistent with the observation that <span class="match term0">CHIP</span> induces <span class="match term1">Smad1</span> degradation, we further show that the expression of <span class="match term0">CHIP</span> can inhibit the transcriptional activities of the <span class="match term1">Smad1</span>/Smad4 complex induced by BMP signals	UBOX	1	Training data	H.sapiens
2571	CHIP_HUMAN	ESR2_HUMAN	Q9UNE7	Q92731	STUB1	ESR2	MEDLINE	16940184	The N-terminal 37-amino acid-region is necessary for the recruitment of the ubiquitin ligase, i.e., the carboxyl terminus of HSC70-interacting protein (<span class="match term0">CHIP</span>), to degrade ERbeta	UBOX	1	Training data	H.sapiens
2572	CHIP_HUMAN	SGK1_HUMAN	Q9UNE7	O00141	STUB1	SGK1	MEDLINE	16895519	In the present study we report that <span class="match term1">SGK</span>-1 forms a complex with the stress-associated E3 ligase <span class="match term0">CHIP</span> [C-terminus of Hsc (heat-shock cognate protein) 70-interacting protein]; <span class="match term0">CHIP</span> is required for both the ubiquitin modification and rapid proteasomal degradation of <span class="match term1">SGK</span>-1	UBOX	1	Training data	H.sapiens
2573	CHIP_HUMAN	ATX1_HUMAN	Q9UNE7	P54253	STUB1	ATXN1	MEDLINE	16831871	Interestingly, <span class="match term0">CHIP</span> also interacts with and ubiquitinates unexpanded ataxin-1	UBOX	1	Training data	H.sapiens
2574	CHIP_HUMAN	M3K5_HUMAN	Q9UNE7	Q99683	STUB1	MAP3K5	MEDLINE	16038411	<span class="match term0">CHIP</span> interacted with <span class="match term1">ASK1</span> in a TPR-dependent fashion and induced ubiquitylation and proteasome-dependent degradation of <span class="match term1">ASK1</span>	UBOX	1	Training data	H.sapiens
2575	CHIP_HUMAN	BMAL1_HUMAN	Q9UNE7	O00327	STUB1	ARNTL	MEDLINE	32041778	The E3 ubiquitin ligase <span class="match term0">STUB1</span> attenuates cell senescence by promoting the ubiquitination and degradation of the core circadian regulator <span class="match term1">BMAL1</span>	UBOX	1	Other	H.sapiens
2576	CHIP_HUMAN	SIR6_HUMAN	Q9UNE7	Q8N6T7	STUB1	SIRT6	MEDLINE	24043303	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2577	CHIP_HUMAN	NFS1_HUMAN	Q9UNE7	Q9Y697	STUB1	NFS1	MEDLINE	21219885	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2578	CHIP_HUMAN	GCR_HUMAN	Q9UNE7	P04150	STUB1	NR3C1	MEDLINE	11676916	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2579	CHIP_HUMAN	TRAF6_HUMAN	Q9UNE7	Q9Y4K3	STUB1	TRAF6	MEDLINE	24578159	UbiNet 2.0	UBOX	1	Other	H.sapiens
2580	CHIP_HUMAN	HS90A_HUMAN	Q9UNE7	P07900	STUB1	HSP90AA1	MEDLINE	19913553	UbiNet 2.0	UBOX	1	Other	H.sapiens
2581	CHIP_HUMAN	CTBP2_HUMAN	Q9UNE7	P56545	STUB1	CTBP2	MEDLINE	23410750	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2582	CHIP_HUMAN	DPM1_HUMAN	Q9UNE7	O60762	STUB1	DPM1	MEDLINE	16280320	Free <span class="match term1">DPM1</span> was strongly associated with the C terminus of Hsc70-interacting protein (<span class="match term0">CHIP</span>), a chaperone-dependent E3 ubiquitin ligase, suggesting that <span class="match term1">DPM1</span> is ubiquitinated, at least in part, by <span class="match term0">CHIP</span>	UBOX	1	Training data	H.sapiens
2583	CHIP_HUMAN	RON_HUMAN	Q9UNE7	Q04912	STUB1	MST1R	MEDLINE	16740632	UbiNet 2.0	UBOX	1	Other	H.sapiens
2584	CHIP_HUMAN	KPCZ_HUMAN	Q9UNE7	Q05513	STUB1	PRKCZ	MEDLINE	21911421	UbiNet 2.0	UBOX	1	Other	H.sapiens
2585	CHIP_HUMAN	SMAD3_HUMAN	Q9UNE7	P84022	STUB1	SMAD3	MEDLINE	15781469	Finally, we demonstrated that <span class="match term0">CHIP</span> served as a U-box dependent E3 ligase that can directly mediate ubiquitination and degradation of <span class="match term1">Smad3</span> and that this action of <span class="match term0">CHIP</span> was independent of TGF-beta signaling	UBOX	1	Training data	H.sapiens
2586	CHIP_HUMAN	NOX5_HUMAN	Q9UNE7	Q96PH1	STUB1	NOX5	MEDLINE	23023377	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2587	CHIP_HUMAN	STK4_HUMAN	Q9UNE7	Q13043	STUB1	STK4	MEDLINE	18381433	Overexpression of Hsp70 mediates proteasomal degradation of <span class="match term1">Mst1</span> in a Hsp70 interacting protein (<span class="match term0">CHIP</span>)-dependent manner	UBOX	1	Training data	H.sapiens
2588	CHIP_HUMAN	NEK10_HUMAN	Q9UNE7	Q6ZWH5	STUB1	NEK10	MEDLINE	29581457	29581457	UBOX	1	Other	H.sapiens
2589	CHIP_HUMAN	MAVS_HUMAN	Q9UNE7	Q7Z434	STUB1	MAVS	MEDLINE	33940459	RACK1 degrades <span class="match term1">MAVS</span> to promote bovine ephemeral fever virus replication via upregulating E3 ubiquitin ligase <span class="match term0">STUB1</span>	UBOX	1	Other	H.sapiens
2590	CHIP_HUMAN	S10A2_HUMAN	Q9UNE7	P29034	STUB1	S100A2	MEDLINE	23344957	UbiNet 2.0	UBOX	1	Other	H.sapiens
2591	CHIP_HUMAN	ALK_HUMAN	Q9UNE7	Q9UM73	STUB1	ALK	MEDLINE	15126367	In line with these observations, the carboxyl hsp70-interacting ubiquitin ligase (<span class="match term0">CHIP</span>), was shown to increase basal ubiquitination and turnover of NPM-<span class="match term1">ALK</span> kinase, supporting a mechanism whereby NPM-<span class="match term1">ALK</span> proceeds rapidly toward hsp70-assisted ubiquitin-dependent proteasomal degradation, when chaperoning activity of hsp90 is prohibited by 17-AAG	UBOX	1	Training data	H.sapiens
2592	CHIP_HUMAN	S12A3_HUMAN	Q9UNE7	P55017	STUB1	SLC12A3	MEDLINE	23482560	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2593	CHIP_HUMAN	MCF2_HUMAN	Q9UNE7	P10911	STUB1	MCF2	MEDLINE	17178836	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2594	CHIP_HUMAN	YAP1_HUMAN	Q9UNE7	P46937	STUB1	YAP1	MEDLINE	31393050	Moreover, we revealed that <span class="match term0">STUB1</span> ubiquitinates <span class="match term1">YAP1</span> at the K280 site by K48-linked polyubiquitination, which in turn increases <span class="match term1">YAP1</span> turnover and promotes cellular chemosensitivity	UBOX	1	Other	H.sapiens
2595	CHIP_HUMAN	SMAD4_HUMAN	Q9UNE7	Q13485	STUB1	SMAD4	MEDLINE	14701756	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2596	CHIP_HUMAN	NQO1_HUMAN	Q9UNE7	P15559	STUB1	NQO1	MEDLINE	21220432	<span class="match term1">NQO1</span> binds <span class="match term0">STUB1</span> via the Hsc70-interacting domain (tetratricopeptide repeat domain) and undergoes ubiquitination and degradation	UBOX	1	Other	H.sapiens
2597	CHIP_HUMAN	MYC_HUMAN	Q9UNE7	P01106	STUB1	MYC	MEDLINE	22543587	The ubiquitin ligase <span class="match term0">CHIP</span> regulates c-<span class="match term1">Myc</span> stability and transcriptional activity.	UBOX	1	Other	H.sapiens
2598	CHIP_HUMAN	TRAF3_HUMAN	Q9UNE7	Q13114	STUB1	TRAF3	MEDLINE	18922468	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2599	CHIP_HUMAN	NFM_HUMAN	Q9UNE7	P07197	STUB1	NEFM	MEDLINE	21219885	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2600	CHIP_HUMAN	IF5A1_HUMAN	Q9UNE7	P63241	STUB1	EIF5A	MEDLINE	24509416	CHIP/<span class="match term0">Stub1</span> interacts with <span class="match term1">eIF5A</span> and mediates its degradation.	UBOX	1	Other	H.sapiens
2601	CHIP_HUMAN	PGK1_HUMAN	Q9UNE7	P00558	STUB1	PGK1	MEDLINE	33940159	LINC00926 downregulates <span class="match term1">PGK1</span> expression by enhancing the ubiquitination of <span class="match term1">PGK1</span> mediated by E3 ligase <span class="match term0">STUB1</span>	UBOX	1	Other	H.sapiens
2602	CHIP_HUMAN	LRRK2_HUMAN	Q9UNE7	Q5S007	STUB1	LRRK2	MEDLINE	19196961	Here we show that the carboxyl terminus of HSP70-interacting protein (<span class="match term0">CHIP</span>) binds, ubiquitinates, and promotes the ubiquitin proteasomal degradation of <span class="match term1">LRRK2</span>	UBOX	1	Training data	H.sapiens
2603	CHIP_HUMAN	SRC_HUMAN	Q9UNE7	P12931	STUB1	SRC	MEDLINE	21911421	E3 ubiquitin ligase <span class="match term0">CHIP</span> facilitates Toll-like receptor signaling by recruiting and polyubiquitinating <span class="match term1">Src</span> and atypical PKC{zeta}.	UBOX	1	Other	H.sapiens
2604	CHIP_HUMAN	STK11_HUMAN	Q9UNE7	Q15831	STUB1	STK11	MEDLINE	21860411	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2605	CHIP_HUMAN	MKKS_HUMAN	Q9UNE7	Q9NPJ1	STUB1	MKKS	MEDLINE	22199232	E3Net	UBOX	1	Other	H.sapiens
2606	CHIP_HUMAN	CY24B_HUMAN	Q9UNE7	P04839	STUB1	CYBB	MEDLINE	23023377	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2607	CHIP_HUMAN	HSP74_HUMAN	Q9UNE7	P34932	STUB1	HSPA4	MEDLINE	19648119	UbiNet 2.0	UBOX	1	Other	H.sapiens
2608	CHIP_HUMAN	MYCD_HUMAN	Q9UNE7	Q8IZQ8	STUB1	MYOCD	MEDLINE	19237536	UbiNet 2.0	UBOX	1	Other	H.sapiens
2609	CHIP_HUMAN	KAPCB_HUMAN	Q9UNE7	P22694	STUB1	PRKACB	MEDLINE	31189917	UbiNet 2.0	UBOX	1	Other	H.sapiens
2610	CHIP_HUMAN	RUNX2_HUMAN	Q9UNE7	Q13950	STUB1	RUNX2	MEDLINE	18541707	<span class="match term0">CHIP</span> promotes <span class="match term1">Runx2</span> degradation and negatively regulates osteoblast differentiation	UBOX	1	Training data	H.sapiens
2611	CHIP_HUMAN	M3K2_HUMAN	Q9UNE7	Q9Y2U5	STUB1	MAP3K2	MEDLINE	20588253	UbiNet 2.0	UBOX	1	Other	H.sapiens
2612	CHIP_HUMAN	PTEN_HUMAN	Q9UNE7	P60484	STUB1	PTEN	MEDLINE	26280536	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2613	CHIP_HUMAN	HSF1_HUMAN	Q9UNE7	Q00613	STUB1	HSF1	MEDLINE	23344957	UbiNet 2.0	UBOX	1	Other	H.sapiens
2614	CHIP_HUMAN	NANO1_HUMAN	Q9UNE7	Q8WY41	STUB1	NANOS1	MEDLINE	22199232	E3Net	UBOX	1	Other	H.sapiens
2615	SYVN1_HUMAN	BMAL1_HUMAN	Q86TM6	O00327	SYVN1	ARNTL	MEDLINE	32765757	In addition, the results of western blotting and reverse transcription-quantitative PCR suggested that <span class="match term0">HRD1</span> promoted K48-associated polyubiquitination of <span class="match term1">BMAL1</span> and thus mediated its degradation via the ubiquitin-proteasome system	RING	1	Other	H.sapiens
2616	SYVN1_HUMAN	CLUS_HUMAN	Q86TM6	P10909	SYVN1	CLU	MEDLINE	17451556	We also report that the ER-associated ubiquitin ligase <span class="match term0">Hrd1</span>/synoviolin can interact with, and ubiquitinate clusterin	RING	1	Training data	H.sapiens
2617	SYVN1_HUMAN	TITIN_HUMAN	Q86TM6	Q8WZ42	SYVN1	TTN	MEDLINE	17141218	Consistent with its role as an E3 for httN, we demonstrate that <span class="match term0">Hrd1</span> interacts with and ubiquitinates httN	RING	1	Training data	H.sapiens
2618	SYVN1_HUMAN	SC6A4_HUMAN	Q86TM6	P31645	SYVN1	SLC6A4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2619	SYVN1_HUMAN	HMDH_HUMAN	Q86TM6	P04035	SYVN1	HMGCR	UniProt	SYVN1_HUMAN	<span class="match term0">SYVN1</span>_HUMAN	RING	1	Training data	H.sapiens
2620	SYVN1_HUMAN	STXB5_HUMAN	Q86TM6	Q5T5C0	SYVN1	STXBP5	MEDLINE	29269412	29269412	RING	1	Other	H.sapiens
2621	SYVN1_HUMAN	GPR37_HUMAN	Q86TM6	O15354	SYVN1	GPR37	UniProt	SYVN1_HUMAN	The unfolded form is specifically ubiquitinated by <span class="match term0">SYVN1</span>, which promotes its proteasomal degradation and prevents neuronal cell death	RING	1	Training data	H.sapiens
2622	SYVN1_HUMAN	HD_HUMAN	Q86TM6	P42858	SYVN1	HTT	MEDLINE	17141218	Consistent with its role as an E3 for httN, we demonstrate that <span class="match term0">Hrd1</span> interacts with and ubiquitinates httN	RING	1	Training data	H.sapiens
2623	SYVN1_HUMAN	A4_HUMAN	Q86TM6	P05067	SYVN1	APP	MEDLINE	20237263	<span class="match term0">HRD1</span> promoted <span class="match term1">APP</span> ubiquitination and degradation, resulting in decreased generation of Abeta	RING	1	Other	H.sapiens
2624	SYVN1_HUMAN	A1AT_HUMAN	Q86TM6	P01009	SYVN1	SERPINA1	MEDLINE	21199683	UbiNet 2.0	RING	1	Training data	H.sapiens
2625	SYVN1_HUMAN	P53_HUMAN	Q86TM6	P04637	SYVN1	TP53	MEDLINE	17828301	Regulation of the synthesis, function and degradation of HDM2 (Mdm2 in mouse) plays a key role in controlling the abundance and activity of the transcription factor <span class="match term1">p53</span>, with consequent implications for the proliferation and survival of normal and cancer cells	RING	1	Training data	H.sapiens
2626	SYVN1_HUMAN	TAU_HUMAN	Q86TM6	P10636	SYVN1	MAPT	MEDLINE	18301957	Concomitantly, expression of exogenous CHIP could promote the degradation of the hyperphosphorylated <span class="match term1">tau</span> induced by overactivation of glycogen synthase kinase-3 (GSK-3) or inhibition of protein phosphatase-2A (PP-2A) in the rat brains and N2A cells	RING	1	Training data	H.sapiens
2627	SYVN1_HUMAN	IDS_HUMAN	Q86TM6	P22304	SYVN1	IDS	MEDLINE	30042467	Accumulated <span class="match term1">IDS</span> mutants in the ER were ubiquitinated by ERAD-related ubiquitin E3 ligase <span class="match term0">HRD1</span> followed by degradation via ERAD	RING	1	Other	H.sapiens
2628	SYVN1_HUMAN	PACRG_HUMAN	Q86TM6	Q96M98	SYVN1	PACRG	MEDLINE	15572843	UbiNet 2.0	RING	1	Training data	H.sapiens
2629	SYVN1_HUMAN	TRAC_HUMAN	Q86TM6	P01848	SYVN1	TRAC	MEDLINE	29655804	WDR20 expression increases TCRalpha ubiquitination, and <span class="match term0">HRD1</span> E3 ligase is essential for the process	RING	1	Other	H.sapiens
2630	SYVN1_HUMAN	SGK1_HUMAN	Q86TM6	O00141	SYVN1	SGK1	MEDLINE	16847254	We determined that the Ub-conjugating UBC6 and UBC7 and the Ub ligase <span class="match term0">HRD1</span> are the ER-associated Ub enzymes that mediate degradation of <span class="match term1">Sgk1</span>; thus, <span class="match term1">Sgk1</span> has been identified as a cytosolic substrate for mammalian <span class="match term0">HRD1</span>	RING	1	Training data	H.sapiens
2631	SYVN1_HUMAN	ATLA1_HUMAN	Q86TM6	Q8WXF7	SYVN1	ATL1	MEDLINE	32916628	The E3 Ubiquitin Ligase <span class="match term0">SYVN1</span> Ubiquitinates Atlastins to Remodel the Endoplasmic Reticulum Network.	RING	1	Other	H.sapiens
2632	SYVN1_HUMAN	CD3D_HUMAN	Q86TM6	P04234	SYVN1	CD3D	MEDLINE	21199683	UbiNet 2.0	RING	1	Training data	H.sapiens
2633	SYVN1_HUMAN	ERN1_HUMAN	Q86TM6	O75460	SYVN1	ERN1	MEDLINE	18369366	<span class="match term0">SYVN1</span> interacts with and catalyses <span class="match term1">IRE1</span> ubiquitination and consequently promotes <span class="match term1">IRE1</span> degradation	RING	1	Training data	H.sapiens
2634	SYVN1_HUMAN	CLUA1_HUMAN	Q86TM6	Q96AJ1	SYVN1	CLUAP1	MEDLINE	17451556	UbiNet 2.0	RING	1	Training data	H.sapiens
2635	SYVN1_HUMAN	NICA_HUMAN	Q86TM6	Q92542	SYVN1	NCSTN	MEDLINE	19725872	An E3 ubiquitin ligase, Synoviolin, is involved in the degradation of immature nicastrin, and regulates the production of amyloid beta-protein	RING	1	Training data	H.sapiens
2636	SYVN1_HUMAN	AMFR_HUMAN	Q86TM6	Q9UKV5	SYVN1	AMFR	MEDLINE	18216283	UbiNet 2.0	RING	1	Training data	H.sapiens
2637	SYVN1_HUMAN	SYVN1_HUMAN	Q86TM6	Q86TM6	SYVN1	SYVN1	MEDLINE	12459480	UbiNet 2.0	RING	1	Training data	H.sapiens
2638	SYVN1_HUMAN	OLR1_HUMAN	Q86TM6	P78380	SYVN1	OLR1	MEDLINE	32308114	Further analysis showed that <span class="match term0">HRD1</span> interacted with <span class="match term1">LOX-1</span> and promoted ubiquitination and degradation of <span class="match term1">LOX-1</span> by the proteasome	RING	1	Other	H.sapiens
2639	TANK_HUMAN	IKKE_HUMAN	Q92844	Q14164	TANK	IKBKE	MEDLINE	23453969	UbiNet 2.0	Other	1	Other	H.sapiens
2640	TANK_HUMAN	KRR1_HUMAN	Q92844	Q13601	TANK	KRR1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2641	TANK_HUMAN	LST8_HUMAN	Q92844	Q9BVC4	TANK	MLST8	MEDLINE	28489822	UbiNet 2.0	Other	1	Other	H.sapiens
2642	TANK_HUMAN	MK11_HUMAN	Q92844	Q15759	TANK	MAPK11	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2643	TANK_HUMAN	DUS14_HUMAN	Q92844	O95147	TANK	DUSP14	MEDLINE	26521044	UbiNet 2.0	Other	1	Other	H.sapiens
2644	TANK_HUMAN	TCAM1_HUMAN	Q92844	Q8IUC6	TANK	TICAM1	MEDLINE	20047764	UbiNet 2.0	Other	1	Other	H.sapiens
2645	TANK_HUMAN	RIPK1_HUMAN	Q92844	Q13546	TANK	RIPK1	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2646	TANK_HUMAN	TRAF3_HUMAN	Q92844	Q13114	TANK	TRAF3	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2647	TANK_HUMAN	BIRC3_HUMAN	Q92844	Q13489	TANK	BIRC3	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2648	TBL1X_HUMAN	CTNB1_HUMAN	O60907	P35222	TBL1X	CTNNB1	MEDLINE	20181957	Direct ubiquitination of <span class="match term1">beta-catenin</span> by Siah-1 and regulation by the exchange factor <span class="match term0">TBL1</span>	F-box	1	Training data	H.sapiens
2649	BACD2_HUMAN	RHOA_HUMAN	Q13829	P61586	TNFAIP1	RHOA	UniProt	BACD2_HUMAN	The BCR(BACURD2) E3 ubiquitin ligase complex mediates the ubiquitination of <span class="match term1">RHOA</span>, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration	BTB_OTHER	1	Training data	H.sapiens
2650	BACD2_HUMAN	CSK2B_HUMAN	Q13829	P67870	TNFAIP1	CSNK2B	MEDLINE	31901862	Taken together, these data indicate that <span class="match term0">TNFAIP1</span> induced degradation of <span class="match term1">CSNK2B</span> via the Cul3/<span class="match term0">TNFAIP1</span> ubiquitin ligase complex.	BTB_OTHER	1	Other	H.sapiens
2651	TNAP3_HUMAN	RNF41_HUMAN	P21580	Q9H4P4	TNFAIP3	RNF41	MEDLINE	34023381	Through this approach, E3 ubiquitin-protein ligase neuregulin receptor degradation protein-1 (<span class="match term1">Nrdp1</span>) was discovered to be a new ubiquitination substrate of <span class="match term0">A20</span>	HECT	1	Other	H.sapiens
2652	TNAP3_HUMAN	RIPK1_HUMAN	P21580	Q13546	TNFAIP3	RIPK1	UniProt	TNAP3_HUMAN	<span class="match term0">TNFAIP3</span> deubiquitinates 'Lys-63' polyubiquitin chains on <span class="match term1">RIPK1</span> and catalyzes the formation of 'Lys-48'-polyubiquitin chains	HECT	1	Training data	H.sapiens
2653	TNAP3_HUMAN	TLR9_HUMAN	P21580	Q9NR96	TNFAIP3	TLR9	MEDLINE	30277474	E-cadherin, expressed on both myeloma cells and pDCs, mediated these effects via a homophilic interaction - activation of E-cadherin signaling upregulated and activated <span class="match term0">TNFAIP3</span> to interact with <span class="match term1">TLR9</span>, resulting in <span class="match term1">TLR9</span> ubiquitination and degradation, and inhibition of IFN-alpha production in pDCs	HECT	1	Other	H.sapiens
2654	TNAP3_HUMAN	TNAP3_HUMAN	P21580	P21580	TNFAIP3	TNFAIP3	MEDLINE	21095585	Full-length <span class="match term0">A20</span> protein wild-type (WT), the single point mutants Y614A or L626R or F615A, and the double mutants Y614A, L626R and Y614A, F615A were expressed in 293T cells and assayed with UbcH7 for the ability to auto-ubiquitinate <span class="match term0">A20</span>. Only <span class="match term0">A20</span> with an intact Ub-binding site II on <span class="match term0">A20</span> ZnF4 was able to promote effective auto-ubiquitination.	HECT	1	Training data	H.sapiens
2655	TOM1_HUMAN	NAB2_HUMAN	O60784	Q15742	TOM1	NAB2	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2656	TOM1_HUMAN	CDC6_HUMAN	O60784	Q99741	TOM1	CDC6	MEDLINE	23129771	UbiNet 2.0	Other	1	Training data	H.sapiens
2657	TOPRS_HUMAN	NKX31_HUMAN	Q9NS56	Q99801	TOPORS	NKX3-1	MEDLINE	18077445	<span class="match term1">NKX3</span>.1 can be ubiquitinated by <span class="match term0">TOPORS</span> in vitro and in vivo, and overexpression of <span class="match term0">TOPORS</span> leads to <span class="match term1">NKX3</span>.1 proteasomal degradation in prostate cancer cells	RING	1	Training data	H.sapiens
2658	TOPRS_HUMAN	H2AX_HUMAN	Q9NS56	P16104	TOPORS	H2AX	MEDLINE	22972498	In vitro assays for ubiquitination revealed that <span class="match term0">TOPORS</span> functions as a novel E3 ligase for <span class="match term1">H2AX</span> ubiquitination	RING	1	Other	H.sapiens
2659	TOPRS_HUMAN	P53_HUMAN	Q9NS56	P04637	TOPORS	TP53	MEDLINE	19895323	It has been suggested that measles virus phosphoprotein may inhibit ubiquitination of Pirh2, which has been reported to be overexpressed in lung carcinoma and is responsible for degrading the cell cycle regulator <span class="match term1">p53</span>	RING	1	Training data	H.sapiens
2660	TRAF1_HUMAN	M3K14_HUMAN	Q13077	Q99558	TRAF1	MAP3K14	MEDLINE	22199232	E3Net	Other	1	Other	H.sapiens
2661	TRAF2_HUMAN	TRAF2_HUMAN	Q12933	Q12933	TRAF2	TRAF2	MEDLINE	20876871	UbiNet 2.0	RING	1	Training data	H.sapiens
2662	TRAF2_HUMAN	MOAP1_HUMAN	Q12933	Q96BY2	TRAF2	MOAP1	MEDLINE	29470995	Furthermore, we can demonstrate that RACK1 functions to bring the E3 ligase, <span class="match term0">TRAF2</span>, to <span class="match term1">MOAP-1</span> in order to undergo a K63-dependent ubiquitination	RING	1	Other	H.sapiens
2663	TRAF2_HUMAN	IKKE_HUMAN	Q12933	Q14164	TRAF2	IKBKE	MEDLINE	23453969	23453969	RING	1	Other	H.sapiens
2664	TRAF2_HUMAN	KRR1_HUMAN	Q12933	Q13601	TRAF2	KRR1	MEDLINE	19810754	It has been assumed that <span class="match term0">TRAF2</span> is a ubiquitin ligase like TRAF6 and mediates K63-linked polyubiquitination of RIP1, a kinase pivotal in TNFalpha-induced NF-kappaB activation	RING	1	Training data	H.sapiens
2665	TRAF2_HUMAN	M3K14_HUMAN	Q12933	Q99558	TRAF2	MAP3K14	UniProt	TRAF2_HUMAN	The heterotrimer formed by TRAF1 and <span class="match term0">TRAF2</span> is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as <span class="match term1">MAP3K14</span>	RING	1	Training data	H.sapiens
2666	TRAF2_HUMAN	BIRC3_HUMAN	Q12933	Q13489	TRAF2	BIRC3	MEDLINE	11907583	UbiNet 2.0	RING	1	Training data	H.sapiens
2667	TRAF2_HUMAN	ASSY_HUMAN	Q12933	P00966	TRAF2	ASS1	MEDLINE	34184805	Mechanistically, LOC113230 acts as a scaffold to facilitate recruiting LRPPRC and the <span class="match term0">TRAF2</span> E3 ubiquitin ligase to <span class="match term1">ASS1</span>, resulting in enhanced ubiquitination and degradation of <span class="match term1">ASS1</span> and decreased arginine synthesis	RING	1	Other	H.sapiens
2668	TRAF2_HUMAN	RIPK1_HUMAN	Q12933	Q13546	TRAF2	RIPK1	MEDLINE	18641654	UbiNet 2.0	RING	1	Training data	H.sapiens
2669	TRAF2_HUMAN	TCAM1_HUMAN	Q12933	Q8IUC6	TRAF2	TICAM1	MEDLINE	20047764	UbiNet 2.0	RING	1	Training data	H.sapiens
2670	TRAF2_HUMAN	ZBT17_HUMAN	Q12933	Q13105	TRAF2	ZBTB17	MEDLINE	20577214	UbiNet 2.0	RING	1	Training data	H.sapiens
2671	TRAF2_HUMAN	DUS14_HUMAN	Q12933	O95147	TRAF2	DUSP14	MEDLINE	26521044	<span class="match term0">TRAF2</span>-mediated Lys63-linked ubiquitination of?<span class="match term1">DUSP14</span>/MKP6?is essential for its phosphatase activity.	RING	1	Other	H.sapiens
2672	TRAF2_HUMAN	MK11_HUMAN	Q12933	Q15759	TRAF2	MAPK11	MEDLINE	19584093	hUbiquitome	RING	1	Other	H.sapiens
2673	TRAF3_HUMAN	UBC9_HUMAN	Q13114	P63279	TRAF3	UBE2I	MEDLINE	34372697	In addition, our results further revealed that viral protein VP3 inhibited the SUMOylation of API5 by targeting API5 and promoting <span class="match term1">UBC9</span> proteasome-dependent degradation through binding to the ubiquitin E3 ligase <span class="match term0">TRAF3</span>	RING	1	Other	H.sapiens
2674	TRAF3_HUMAN	M3K14_HUMAN	Q13114	Q99558	TRAF3	MAP3K14	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2675	TRAF3_HUMAN	M3K7_HUMAN	Q13114	O43318	TRAF3	MAP3K7	MEDLINE	26882989	UbiNet 2.0	RING	1	Other	H.sapiens
2676	TRAF3_HUMAN	IKKE_HUMAN	Q13114	Q14164	TRAF3	IKBKE	MEDLINE	23308279	UbiNet 2.0	RING	1	Training data	H.sapiens
2677	TRAF3_HUMAN	ULK1_HUMAN	Q13114	O75385	TRAF3	ULK1	MEDLINE	32275117	Co-IP assays confirmed that <span class="match term0">TRAF3</span> forms a complex with TRAF2 and cIAP1 and mediates ubiquitin and degradation of Unc-51 like autophagy activating kinase 1 (<span class="match term1">ULK1</span>).	RING	1	Other	H.sapiens
2678	TRAF3_HUMAN	TBK1_HUMAN	Q13114	Q9UHD2	TRAF3	TBK1	MEDLINE	23308279	UbiNet 2.0	RING	1	Training data	H.sapiens
2679	CIKS_HUMAN	TRAF6_HUMAN	O43734	Q9Y4K3	TRAF3IP2	TRAF6	MEDLINE	19825828	Deletion and point mutations of the <span class="match term0">Act1</span> U-box abolished <span class="match term0">Act1</span>-mediated ubiquitination of <span class="match term1">TRAF6</span> and impaired the ability of <span class="match term0">Act1</span> to restore IL-17-dependent signaling and expression of target genes in <span class="match term0">Act1</span>(-/-) mouse embryonic fibroblasts	UBOX	1	Training data	H.sapiens
2680	TRAF4_HUMAN	NTRK1_HUMAN	Q9BUZ4	P04629	TRAF4	NTRK1	MEDLINE	29715200	<span class="match term0">TRAF4</span> promoted K27- and K29-linked ubiquitination at the <span class="match term1">TrkA</span> kinase domain and increased its kinase activity	RING	1	Other	H.sapiens
2681	TRAF4_HUMAN	AKT1_HUMAN	Q9BUZ4	P31749	TRAF4	AKT1	MEDLINE	33152664	Besides, si-COX-2 prevented TGF-beta-induced K63-ubiquitination of <span class="match term1">AKT</span> by blocking the interaction between <span class="match term1">AKT</span> and E3 ubiquitin ligase <span class="match term0">TRAF4</span>	RING	1	Other	H.sapiens
2682	TRAF4_HUMAN	CHK1_HUMAN	Q9BUZ4	O14757	TRAF4	CHEK1	MEDLINE	32357935	RESULTS: <span class="match term0">TRAF4</span> catalyzed the ubiquitination of <span class="match term1">CHK1</span> in multiple CRC cell lines	RING	1	Other	H.sapiens
2683	TRAF4_HUMAN	IRS1_HUMAN	Q9BUZ4	P35568	TRAF4	IRS1	MEDLINE	33991522	The E3 ligase <span class="match term0">TRAF4</span> Promotes IGF Signaling by Mediating Atypical Ubiquitination of <span class="match term1">IRS-1</span>	RING	1	Other	H.sapiens
2684	TRAF4_HUMAN	SMUF2_HUMAN	Q9BUZ4	Q9HAU4	TRAF4	SMURF2	MEDLINE	23973329	UbiNet 2.0	RING	1	Other	H.sapiens
2685	TRAF6_HUMAN	NEMO_HUMAN	Q9Y4K3	Q9Y6K9	TRAF6	IKBKG	MEDLINE	20529958	One of the E3 ligase responsible for K63-linked <span class="match term1">NEMO</span> polyubiquitination is <span class="match term0">TRAF6</span>, which participates in several signaling pathways controlling immunity, osteoclastogenesis, skin development and brain functions	RING	1	Training data	H.sapiens
2686	TRAF6_HUMAN	TRAF6_HUMAN	Q9Y4K3	Q9Y4K3	TRAF6	TRAF6	UniProt	TRAF6_HUMAN	Mediates auto-ubiquitination of CHIP, <span class="match term0">TRAF6</span> and TRIM63/MURF1	RING	1	Training data	H.sapiens
2687	TRAF6_HUMAN	PARK7_HUMAN	Q9Y4K3	Q99497	TRAF6	PARK7	MEDLINE	20634198	Importantly, <span class="match term0">TRAF6</span> stimulates the accumulation of insoluble and polyubiquitinated mutant <span class="match term1">DJ-1</span> into cytoplasmic aggregates	RING	1	Training data	H.sapiens
2688	TRAF6_HUMAN	M3K11_HUMAN	Q9Y4K3	Q16584	TRAF6	MAP3K11	MEDLINE	23172226	<span class="match term0">TRAF6</span>-mediated ubiquitination was required for dissociation of inactive monomeric <span class="match term1">MLK3</span> from the scaffold protein IB1/JIP1, facilitating the subsequent dimerization, autophosphorylation, and catalytic activation of <span class="match term1">MLK3</span>	RING	1	Other	H.sapiens
2689	TRAF6_HUMAN	DNA2_HUMAN	Q9Y4K3	P51530	TRAF6	DNA2	MEDLINE	31216032	Here, we report that the E3 ligase <span class="match term0">TRAF6</span> binds to and mediates the K63-linked polyubiquitination of <span class="match term1">hDNA2</span>, increasing the stability of <span class="match term1">hDNA2</span> and promoting its nuclear localization	RING	1	Other	H.sapiens
2690	TRAF6_HUMAN	M3K7_HUMAN	Q9Y4K3	O43318	TRAF6	MAP3K7	MEDLINE	19043203	We found that expression of the ISGylation system suppresses NF-kappaB activation via <span class="match term0">TRAF6</span> and <span class="match term1">TAK1</span> and that the level of polyubiquitinated <span class="match term0">TRAF6</span> is reduced by expression of the ISGylation system	RING	1	Training data	H.sapiens
2691	TRAF6_HUMAN	ECSIT_HUMAN	Q9Y4K3	Q9BQ95	TRAF6	ECSIT	MEDLINE	32296023	UbiNet 2.0	RING	1	Other	H.sapiens
2692	TRAF6_HUMAN	MALT1_HUMAN	Q9Y4K3	Q9UDY8	TRAF6	MALT1	MEDLINE	15125833	The <span class="match term1">MALT1</span> oligomers bind to <span class="match term0">TRAF6</span>, induce <span class="match term0">TRAF6</span> oligomerization, and activate the ligase activity of <span class="match term0">TRAF6</span> to polyubiquitinate NEMO	RING	1	Training data	H.sapiens
2693	TRAF6_HUMAN	NTRK1_HUMAN	Q9Y4K3	P04629	TRAF6	NTRK1	UniProt	TRAF6_HUMAN	<span class="match term0">TRAF6</span>_HUMAN	RING	1	Training data	H.sapiens
2694	TRAF6_HUMAN	RIPK2_HUMAN	Q9Y4K3	O43353	TRAF6	RIPK2	MEDLINE	17947236	MDP-induced <span class="match term1">Rip2</span> polyubiquitination and NF- B activation require the E2-conjugating enzyme Ubc13, the E3 ubiquitin ligase <span class="match term0">Traf6</span>, and the ubiquitin-activated kinase Tak1.	RING	1	Training data	H.sapiens
2695	TRAF6_HUMAN	CTNB1_HUMAN	Q9Y4K3	P35222	TRAF6	CTNNB1	MEDLINE	30806153	UbiNet 2.0	RING	1	Other	H.sapiens
2696	TRAF6_HUMAN	BECN1_HUMAN	Q9Y4K3	Q14457	TRAF6	BECN1	MEDLINE	20501938	UbiNet 2.0	RING	1	Other	H.sapiens
2697	TRAF6_HUMAN	SYUA_HUMAN	Q9Y4K3	P37840	TRAF6	SNCA	MEDLINE	20634198	<span class="match term0">TRAF6</span> promotes atypical ubiquitination of mutant DJ-1 and alpha-synuclein and is localized to Lewy bodies in sporadic Parkinson's disease brains	RING	1	Training data	H.sapiens
2698	TRAF6_HUMAN	NR2C2_HUMAN	Q9Y4K3	P49116	TRAF6	NR2C2	MEDLINE	18758450	Intriguingly, TGF-beta-induced <span class="match term0">TRAF6</span>-mediated Lys 63-linked polyubiquitylation of <span class="match term1">TAK1</span> Lys 34 correlates with <span class="match term1">TAK1</span> activation	RING	1	Training data	H.sapiens
2699	TRAF6_HUMAN	LGMN_HUMAN	Q9Y4K3	Q99538	TRAF6	LGMN	MEDLINE	24610907	Functional role of asparaginyl endopeptidase ubiquitination by <span class="match term0">TRAF6</span> in tumor invasion and metastasis.	RING	1	Other	H.sapiens
2700	TRAF6_HUMAN	TNR16_HUMAN	Q9Y4K3	P08138	TRAF6	NGFR	MEDLINE	19012753	Finally, we also show that p75(NTR) is a substrate for <span class="match term0">TRAF6</span>-mediated ubiquitination and that <span class="match term0">TRAF6</span> E3 ligase activity is required for regulated intramembrane proteolysis of p75(NTR)	RING	1	Training data	H.sapiens
2701	TRAF6_HUMAN	CENPR_HUMAN	Q9Y4K3	Q13352	TRAF6	ITGB3BP	MEDLINE	16252010	UbiNet 2.0	RING	1	Training data	H.sapiens
2702	TRAF6_HUMAN	TGFR1_HUMAN	Q9Y4K3	P36897	TRAF6	TGFBR1	MEDLINE	25622187	We recently identified a novel TGFbeta-regulated signaling cascade in which TGFbeta type I receptor (TbetaRI) is activated by the E3 ligase TNF-receptor-associated factor 6 (<span class="match term0">TRAF6</span>) via the Lys63-linked polyubiquitination of TbetaRI	RING	1	Other	H.sapiens
2703	TRAF6_HUMAN	MTOR_HUMAN	Q9Y4K3	P42345	TRAF6	MTOR	MEDLINE	23911927	UbiNet 2.0	RING	1	Other	H.sapiens
2704	TRAF6_HUMAN	MLP3B_HUMAN	Q9Y4K3	Q9GZQ8	TRAF6	MAP1LC3B	MEDLINE	30806153	Mechanistically, <span class="match term0">TRAF6</span> interacted with <span class="match term1">MAP1LC3B</span>/LC3B through its LC3-interacting region 'YxxL' and catalyzed K63-linked polyubiquitination of LC3B	RING	1	Other	H.sapiens
2705	TRAF6_HUMAN	IRF7_HUMAN	Q9Y4K3	Q92985	TRAF6	IRF7	MEDLINE	21183682	FADD and TRIM21 can directly ubiquitinate <span class="match term1">IRF7</span>, affect its phosphorylation status, and interfere with the ubiquitin ligase activity of <span class="match term0">TRAF6</span>	RING	1	Training data	H.sapiens
2706	TRAF6_HUMAN	PK3CA_HUMAN	Q9Y4K3	P42336	TRAF6	PIK3CA	MEDLINE	29729098	Here, we identify <span class="match term0">TRAF6</span> as a potent E3 ubiquitin ligase for the PI3K catalytic subunit <span class="match term1">PIK3CA</span> (p110alpha)	RING	1	Other	H.sapiens
2707	TRAF6_HUMAN	HGFL_HUMAN	Q9Y4K3	P26927	TRAF6	MST1	MEDLINE	30673917	Our results reveal that <span class="match term0">TRAF6</span> regulates YAP signaling by promoting the ubiquitination and degradation of <span class="match term1">MST1</span> in pancreatic cancer, suggesting that <span class="match term0">TRAF6</span> could be a possible E3 ligase of <span class="match term1">MST1</span> and a potential therapeutic target.	RING	1	Other	H.sapiens
2708	TRAF6_HUMAN	LG3BP_HUMAN	Q9Y4K3	Q08380	TRAF6	LGALS3BP	MEDLINE	31404116	Furthermore, <span class="match term1">90K</span> enhanced <span class="match term0">TRAF6</span> and TRAF3 ubiquitination and served as a specific ubiquitination substrate of <span class="match term0">TRAF6</span>, leading to transcription factor NF-kappaB, IRF3 and IRF7 translocation from the cytoplasm to the nucleus	RING	1	Other	H.sapiens
2709	TRAF6_HUMAN	HSP74_HUMAN	Q9Y4K3	P34932	TRAF6	HSPA4	MEDLINE	14702098	UbiNet 2.0	RING	1	Other	H.sapiens
2710	TRAF6_HUMAN	AKT2_HUMAN	Q9Y4K3	P31751	TRAF6	AKT2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2711	TRAF6_HUMAN	FHL2_HUMAN	Q9Y4K3	Q14192	TRAF6	FHL2	MEDLINE	18768464	Finally, <span class="match term0">TRAF6</span> and its proximal activator, RANKL, polyubiquitinate <span class="match term1">FHL2</span>, prompting its proteasomal degradation	RING	1	Other	H.sapiens
2712	TRAF6_HUMAN	HXK2_HUMAN	Q9Y4K3	P52789	TRAF6	HK2	MEDLINE	28980855	The Lys63-linked ubiquitination of <span class="match term1">HK2</span> catalyzed by the E3 ligase <span class="match term0">TRAF6</span> was critical for the subsequent recognition of <span class="match term1">HK2</span> by the autophagy receptor protein SQSTM1/p62 for the process of selective autophagic degradation	RING	1	Other	H.sapiens
2713	TRAF6_HUMAN	STAT6_HUMAN	Q9Y4K3	P42226	TRAF6	STAT6	MEDLINE	33017719	Further study showed that <span class="match term0">TRAF6</span> bound <span class="match term1">STAT6</span> by <span class="match term0">TRAF6</span> C domain and reduced K48-ubiquitination of <span class="match term1">STAT6</span> which could induce degradation of <span class="match term1">STAT6</span>, explaining why <span class="match term0">TRAF6</span> could conduct <span class="match term1">STAT6</span> stability	RING	1	Other	H.sapiens
2714	TRAF6_HUMAN	PINK1_HUMAN	Q9Y4K3	Q9BXM7	TRAF6	PINK1	MEDLINE	23885119	SARM1, which is known to be an adaptor protein for Toll-like receptor, binds to <span class="match term1">PINK1</span> and promotes <span class="match term0">TRAF6</span>-mediated lysine 63 chain ubiquitination of <span class="match term1">PINK1</span> at lysine 433	RING	1	Other	H.sapiens
2715	TRAF6_HUMAN	LAT_HUMAN	Q9Y4K3	O43561	TRAF6	LAT	MEDLINE	23514740	UbiNet 2.0	RING	1	Training data	H.sapiens
2716	TRAF6_HUMAN	AKT1_HUMAN	Q9Y4K3	P31749	TRAF6	AKT1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2717	TRAF6_HUMAN	PSN1_HUMAN	Q9Y4K3	P49768	TRAF6	PSEN1	MEDLINE	23707529	UbiNet 2.0	RING	1	Training data	H.sapiens
2718	TRAF6_HUMAN	TCAM1_HUMAN	Q9Y4K3	Q8IUC6	TRAF6	TICAM1	MEDLINE	20047764	UbiNet 2.0	RING	1	Training data	H.sapiens
2719	TRAF6_HUMAN	RUSC1_HUMAN	Q9Y4K3	Q9BVN2	TRAF6	RUSC1	MEDLINE	19365808	Beside to NEMO, we revealed that <span class="match term1">NESCA</span> directly associates to the E3 ubiquitin ligase <span class="match term0">TRAF6</span>, which in turn catalyzes <span class="match term1">NESCA</span> polyubiquitination	RING	1	Training data	H.sapiens
2720	TRAF6_HUMAN	IRF5_HUMAN	Q9Y4K3	Q13568	TRAF6	IRF5	MEDLINE	18824541	UbiNet 2.0	RING	1	Training data	H.sapiens
2721	TRAF6_HUMAN	IRAK1_HUMAN	Q9Y4K3	P51617	TRAF6	IRAK1	MEDLINE	18347055	Stimulation through the interleukin-1 receptor (IL-1R) and some Toll-like receptors (TLRs) induces ubiquitination of <span class="match term0">TRAF6</span> and <span class="match term1">IRAK</span>-1, signaling components required for NF-kappaB and mitogen-activated protein kinase activation	RING	1	Other	H.sapiens
2722	TRAF7_HUMAN	P53_HUMAN	Q6Q0C0	P04637	TRAF7	TP53	MEDLINE	23128672	UbiNet 2.0	DWD	1	Training data	H.sapiens
2723	TRAF7_HUMAN	KLF4_HUMAN	Q6Q0C0	O43474	TRAF7	KLF4	MEDLINE	31730901	<span class="match term0">TRAF7</span> could degrade <span class="match term1">KLF4</span> protein through ubiquitin by interacting with its N-terminus	DWD	1	Other	H.sapiens
2724	TRAF7_HUMAN	TRAF7_HUMAN	Q6Q0C0	Q6Q0C0	TRAF7	TRAF7	MEDLINE	14743216	hUbiquitome	DWD	1	Training data	H.sapiens
2725	TRAIP_HUMAN	KANK1_HUMAN	Q9BWF2	Q14678	TRAIP	KANK1	MEDLINE	34349117	In addition, we found that <span class="match term0">TRAIP</span> promoted <span class="match term1">KANK1</span> polyubiquitination and subsequent degradation, downregulating IGFBP3 and activating the AKT pathway in osteosarcoma cells	RING	1	Other	H.sapiens
2726	TRIB3_HUMAN	PPARA_HUMAN	Q96RU7	Q07869	TRIB3	PPARA	MEDLINE	32621919	Mechanistically, <span class="match term0">TRIB3</span> interacted with <span class="match term1">PPARalpha</span> and contributed to its destabilization by promoting its ubiquitination	Other	1	Other	H.sapiens
2727	TRI11_HUMAN	DUS6_HUMAN	Q96F44	Q16828	TRIM11	DUSP6	MEDLINE	31950060	Therefore, <span class="match term0">TRIM11</span> might suppress the translation of <span class="match term1">DUSP6</span> via improving its ubiquitination	RING	1	Other	H.sapiens
2728	TRI11_HUMAN	SC6A4_HUMAN	Q96F44	P31645	TRIM11	SLC6A4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2729	TRI11_HUMAN	MED15_HUMAN	Q96F44	Q96RN5	TRIM11	MED15	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2730	TRI11_HUMAN	ESR1_HUMAN	Q96F44	P03372	TRIM11	ESR1	MEDLINE	32599554	Further mechanistic analysis indicates that the RING domain of <span class="match term0">TRIM11</span> interacted with the N terminal of <span class="match term1">ERalpha</span> in the cytoplasm and promotes its mono-ubiquitination, thus enhances <span class="match term1">ERalpha</span> protein stability	RING	1	Other	H.sapiens
2731	TRI11_HUMAN	ARX_HUMAN	Q96F44	Q96QS3	TRIM11	ARX	MEDLINE	18248090	UbiNet 2.0	RING	1	Training data	H.sapiens
2732	TRI11_HUMAN	DAPLE_HUMAN	Q96F44	Q9P219	TRIM11	CCDC88C	MEDLINE	32382014	<span class="match term0">TRIM11</span> associated with <span class="match term1">Daple</span> and promoted <span class="match term1">Daple</span> ubiquitin-mediated degradation in a p62-selective autophagic manner, further upregulating beta-catenin expression to induce ABCC9 expression by directly binding to the ABCC9 promoter	RING	1	Other	H.sapiens
2733	TRI11_HUMAN	AXIN1_HUMAN	Q96F44	O15169	TRIM11	AXIN1	MEDLINE	31786079	ONCLUSIONS: Together all, the results suggested that <span class="match term0">TRIM11</span> may be an oncogene in lymphomas, which involving the activation of the beta-catenin signaling and the ubiquitination degradation of <span class="match term1">Axin1</span>.	RING	1	Other	H.sapiens
2734	TRI11_HUMAN	PAX6_HUMAN	Q96F44	P26367	TRIM11	PAX6	MEDLINE	18628401	Here, we report that <span class="match term0">Trim11</span>, a member of the TRIM/RBCC protein family of E3 ubiquitin ligases, interacts with <span class="match term1">Pax6</span> and mediates <span class="match term1">Pax6</span> degradation via the ubiquitin-proteasome system	RING	1	Training data	H.sapiens
2735	TRI11_HUMAN	HD_HUMAN	Q96F44	P42858	TRIM11	HTT	MEDLINE	18248090	UbiNet 2.0	RING	1	Training data	H.sapiens
2736	TRI11_HUMAN	PHLP1_HUMAN	Q96F44	O60346	TRIM11	PHLPP1	MEDLINE	31719797	Results that obtained from co-immunoprecipitation (Co-IP) and ubiquitination assay demonstrated <span class="match term0">TRIM11</span> interacted with <span class="match term1">PHLPP1</span> and promoted its ubiquitination in chordoma cells	RING	1	Other	H.sapiens
2737	TRI11_HUMAN	HMN1_HUMAN	Q96F44	P0CJ68	TRIM11	MTRNR2L1	MEDLINE	12670303	hUbiquitome	RING	1	Other	H.sapiens
2738	TRI13_HUMAN	NR4A1_HUMAN	O60858	P22736	TRIM13	NR4A1	MEDLINE	30224829	The E3 ubiquitin ligase <span class="match term0">Trim13</span> regulates <span class="match term1">Nur77</span> stability via casein kinase 2alpha	RING	1	Other	H.sapiens
2739	TRI13_HUMAN	CD3D_HUMAN	O60858	P04234	TRIM13	CD3D	MEDLINE	17314412	UbiNet 2.0	RING	1	Training data	H.sapiens
2740	TRI13_HUMAN	TRI13_HUMAN	O60858	O60858	TRIM13	TRIM13	MEDLINE	31744379	UbiNet 2.0	RING	1	Other	H.sapiens
2741	TRI13_HUMAN	AKT2_HUMAN	O60858	P31751	TRIM13	AKT2	MEDLINE	21333377	UbiNet 2.0	RING	1	Training data	H.sapiens
2742	TRI13_HUMAN	TERA_HUMAN	O60858	P55072	TRIM13	VCP	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2743	TRI13_HUMAN	MDM2_HUMAN	O60858	Q00987	TRIM13	MDM2	MEDLINE	21333377	UbiNet 2.0	RING	1	Training data	H.sapiens
2744	TRI13_HUMAN	AKT1_HUMAN	O60858	P31749	TRIM13	AKT1	MEDLINE	21333377	Additionally, we found that the interaction of <span class="match term0">RFP2</span> with MDM2 and <span class="match term1">AKT</span> resulted in ubiquitination and proteasomal degradation of MDM2 and <span class="match term1">AKT</span> in vivo and in vitro	RING	1	Other	H.sapiens
2745	TRI15_HUMAN	APOA1_HUMAN	Q9C019	P02647	TRIM15	APOA1	MEDLINE	34311082	<span class="match term0">TRIM15</span> promotes the invasion and metastasis of pancreatic cancer cells by mediating <span class="match term1">APOA1</span> ubiquitination and degradation	RING	1	Other	H.sapiens
2746	TRI17_HUMAN	IRF3_HUMAN	Q9Y577	Q14653	TRIM17	IRF3	MEDLINE	18711448	Here we show that the E3 ubiquitin ligase <span class="match term0">RBCC</span> protein interacting with PKC1 (RBCK1) catalyzes the ubiquitination and degradation of <span class="match term1">IRF3</span>	RING	1	Training data	H.sapiens
2747	TRI17_HUMAN	ZSC21_HUMAN	Q9Y577	Q9Y5A6	TRIM17	ZSCAN21	MEDLINE	30485814	The E3 Ubiquitin Ligases <span class="match term0">TRIM17</span> and TRIM41 Modulate alpha-Synuclein Expression by Regulating <span class="match term1">ZSCAN21</span>	RING	1	Other	H.sapiens
2748	TRI17_HUMAN	MCL1_HUMAN	Q9Y577	Q07820	TRIM17	MCL1	MEDLINE	22976837	UbiNet 2.0	RING	1	Training data	H.sapiens
2749	TRI17_HUMAN	TRI17_HUMAN	Q9Y577	Q9Y577	TRIM17	TRIM17	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2750	TRIM2_HUMAN	NFL_HUMAN	Q9C040	P07196	TRIM2	NEFL	MEDLINE	18687884	UbiNet 2.0	RING	1	Training data	H.sapiens
2751	TRIM2_HUMAN	B2L11_HUMAN	Q9C040	O43521	TRIM2	BCL2L11	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2752	RO52_HUMAN	CDN1B_HUMAN	P19474	P46527	TRIM21	CDKN1B	UniProt	RO52_HUMAN	A <span class="match term0">TRIM21</span>-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of <span class="match term1">CDKN1B</span> ('Thr-187	RING	1	Training data	H.sapiens
2753	RO52_HUMAN	TF65_HUMAN	P19474	Q04206	TRIM21	RELA	MEDLINE	32232831	<span class="match term0">Trim21</span> colocalized with <span class="match term1">p65</span>/Nuclear factor-kappaB (NF-kappaB) in the cytosol and physically bound and ubiquitinated <span class="match term1">p65</span> via a lysine 63 (K63) linkage	RING	1	Other	H.sapiens
2754	RO52_HUMAN	IKKB_HUMAN	P19474	O14920	TRIM21	IKBKB	MEDLINE	19675099	These results suggest that <span class="match term0">Ro52</span> down-regulates Tax-induced NF-kappaB signalling by monoubiquitinating <span class="match term1">IKKbeta</span> and by reducing the level of Tax	RING	1	Training data	H.sapiens
2755	RO52_HUMAN	UBP4_HUMAN	P19474	Q13107	TRIM21	USP4	MEDLINE	16472766	Here, we showed that UnpEL is ubiquitinated by <span class="match term0">Ro52</span> in cooperation with UbcH5B in vitro	RING	1	Training data	H.sapiens
2756	RO52_HUMAN	PHB_HUMAN	P19474	P35232	TRIM21	PHB	MEDLINE	30886235	Here, we found that LPLUNC1 stabilised <span class="match term1">PHB1</span> by inhibiting <span class="match term1">PHB1</span> ubiquitination, which is mediated by E3 ligase <span class="match term0">TRIM21</span>	RING	1	Other	H.sapiens
2757	RO52_HUMAN	GUAA_HUMAN	P19474	P49915	TRIM21	GMPS	MEDLINE	33742136	Mechanistically, SNORD50A/B clearly enhances the interaction between E3 ubiquitin ligase <span class="match term0">TRIM21</span> and its substrate <span class="match term1">GMPS</span> by forming a complex among them, thereby promoting GMPS ubiquitination and its subsequent cytoplasmic sequestration	RING	1	Other	H.sapiens
2758	RO52_HUMAN	IRF8_HUMAN	P19474	Q02556	TRIM21	IRF8	MEDLINE	19494276	In contrast, functional analyses of immune cells from <span class="match term0">Trim21</span>(-/-) mice revealed no abnormalities in their composition or function, even though ubiquitylation of IRF3 and <span class="match term1">IRF8</span> was impaired	RING	1	Training data	H.sapiens
2759	RO52_HUMAN	IRF3_HUMAN	P19474	Q14653	TRIM21	IRF3	MEDLINE	19494276	In contrast, functional analyses of immune cells from <span class="match term0">Trim21</span>(-/-) mice revealed no abnormalities in their composition or function, even though ubiquitylation of <span class="match term1">IRF3</span> and IRF8 was impaired	RING	1	Training data	H.sapiens
2760	RO52_HUMAN	RO52_HUMAN	P19474	P19474	TRIM21	TRIM21	MEDLINE	16472766	Recently, we showed that UnpEL/Usp4 is an isopeptidase that can deconjugate ubiquitin from self-ubiquitinated <span class="match term0">Ro52</span>	RING	1	Training data	H.sapiens
2761	RO52_HUMAN	TRIM5_HUMAN	P19474	Q9C035	TRIM21	TRIM5	MEDLINE	18312418	In addition to the self-ubiquitination, we show that <span class="match term1">TRIM5alpha</span> is ubiquitinated by another E3 ubiquitin ligase, <span class="match term0">Ro52</span>, and deubiquitinated by YopJ, one of the pathogenic proteins derived from Yersinia species	RING	1	Training data	H.sapiens
2762	RO52_HUMAN	NUP62_HUMAN	P19474	P37198	TRIM21	NUP62	MEDLINE	34257278	Induced <span class="match term0">TRIM21</span> ISGylation by IFN-beta enhances <span class="match term1">p62</span> ubiquitination to prevent its autophagosome targeting	RING	1	Other	H.sapiens
2763	RO52_HUMAN	SNAI1_HUMAN	P19474	O95863	TRIM21	SNAI1	MEDLINE	30502437	Overexpression of <span class="match term0">TRIM21</span> leads to increased ubiquitination and proteosomal degradation of <span class="match term1">Snail</span>, while depletion of <span class="match term0">TRIM21</span> decreases the ubiquitination of <span class="match term1">Snail</span>	RING	1	Other	H.sapiens
2764	RO52_HUMAN	IF16_HUMAN	P19474	Q16666	TRIM21	IFI16	MEDLINE	33061806	We also discovered that HPV E7 recruited the E3 ligase <span class="match term0">TRIM21</span> to ubiquitinate and degrade the <span class="match term1">IFI16</span> inflammasome, leading to the inhibition of cell pyroptosis and self-escape from immune surveillance	RING	1	Other	H.sapiens
2765	RO52_HUMAN	Q2F514_HBV	P19474	Q2F514	TRIM21	X	MEDLINE	34097931	<span class="match term0">TRIM21</span> interacts with HBx protein and targets HBx for ubiquitination and proteasomal degradation, leading to impaired HBx-mediated degradation of Smc6 and suppression of HBV replication	RING	1	Other	H.sapiens
2766	RO52_HUMAN	CDN1A_HUMAN	P19474	P38936	TRIM21	CDKN1A	MEDLINE	33900537	Ubiquitination of <span class="match term1">p21</span> by E3 Ligase <span class="match term0">TRIM21</span> Promotes the Proliferation of Human Neuroblastoma Cells	RING	1	Other	H.sapiens
2767	RO52_HUMAN	IRF7_HUMAN	P19474	Q92985	TRIM21	IRF7	MEDLINE	21183682	UbiNet 2.0	RING	1	Training data	H.sapiens
2768	RO52_HUMAN	GLYM_HUMAN	P19474	P34897	TRIM21	SHMT2	MEDLINE	30367038	<span class="match term0">TRIM21</span> acts as an E3 ubiquitin ligase for <span class="match term1">SHMT2</span>	RING	1	Other	H.sapiens
2769	RO52_HUMAN	CDT1_HUMAN	P19474	Q9H211	TRIM21	CDT1	MEDLINE	16407252	UbiNet 2.0	RING	1	Training data	H.sapiens
2770	RO52_HUMAN	IGHG1_HUMAN	P19474	P01857	TRIM21	IGHG1	MEDLINE	18641315	hUbiquitome	RING	1	Other	H.sapiens
2771	TRI22_HUMAN	IRF3_HUMAN	Q8IYM9	Q14653	TRIM22	IRF3	MEDLINE	33187908	In addition, FoxO1 destabilized <span class="match term1">IRF3</span> by facilitating E3 ligase <span class="match term0">TRIM22</span>- or TRIM21-mediated K48-linked ubiquitination of <span class="match term1">IRF3</span>.	RING	1	Other	H.sapiens
2772	TRI22_HUMAN	NFKB1_HUMAN	Q8IYM9	P19838	TRIM22	NFKB1	MEDLINE	32814880	Co-immunoprecipitations demonstrated that <span class="match term0">TRIM22</span> bound a negative regulator of <span class="match term1">NF-kappaB</span>, <span class="match term1">NF-kappaB</span> inhibitor alpha (IkappaBalpha), and accelerated its degradation by inducing K48-linked ubiquitination	RING	1	Other	H.sapiens
2773	TRI22_HUMAN	TRI22_HUMAN	Q8IYM9	Q8IYM9	TRIM22	TRIM22	MEDLINE	18656448	It was found that <span class="match term0">TRIM22</span> underwent self-ubiquitylation in vitro in combination with the E2 enzyme UbcH5B and the ubiquitylation was dependent on its RING finger domain	RING	1	Training data	H.sapiens
2774	TRI23_HUMAN	NEMO_HUMAN	P36406	Q9Y6K9	TRIM23	IKBKG	MEDLINE	32296023	UbiNet 2.0	RING	1	Other	H.sapiens
2775	TRI23_HUMAN	TRAF6_HUMAN	P36406	Q9Y4K3	TRIM23	TRAF6	UniProt	TRI23_HUMAN	In the presence of the human cytomegalovirus (HCMV) protein UL144, participates in 'Lys-63'-linked auto-ubiquitination of <span class="match term1">TRAF6</span> resulting in the virally controlled activation of NF-kappa-B at early time of infection	RING	1	Training data	H.sapiens
2776	TRI23_HUMAN	P53_HUMAN	P36406	P04637	TRIM23	TP53	MEDLINE	32227572	We show in this study that <span class="match term0">TRIM23</span> physically binds to <span class="match term1">P53</span> and enhances the ubiquitination of <span class="match term1">P53</span>, thereby promoting tumour proliferation	RING	1	Other	H.sapiens
2777	TRI23_HUMAN	TRI23_HUMAN	P36406	P36406	TRIM23	TRIM23	MEDLINE	15684077	hUbiquitome	RING	1	Other	H.sapiens
2778	TIF1A_HUMAN	TRAF3_HUMAN	O15164	Q13114	TRIM24	TRAF3	MEDLINE	32324863	<span class="match term0">TRIM24</span> facilitates antiviral immunity through mediating K63-linked <span class="match term1">TRAF3</span> ubiquitination	RING	1	Other	H.sapiens
2779	TIF1A_HUMAN	P53_HUMAN	O15164	P04637	TRIM24	TP53	MEDLINE	19844164	UbiNet 2.0	RING	1	Training data	H.sapiens
2780	TRI25_HUMAN	TRI25_HUMAN	Q14258	Q14258	TRIM25	TRIM25	UniProt	TRI25_HUMAN	Auto-ubiquitinated (in vitro)	RING	1	Training data	H.sapiens
2781	TRI25_HUMAN	MAVS_HUMAN	Q14258	Q7Z434	TRIM25	MAVS	MEDLINE	22626058	UbiNet 2.0	RING	1	Training data	H.sapiens
2782	TRI25_HUMAN	1433S_HUMAN	Q14258	P31947	TRIM25	SFN	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2783	TRI25_HUMAN	RIPK3_HUMAN	Q14258	Q9Y572	TRIM25	RIPK3	MEDLINE	33953350	E3 ligase <span class="match term0">TRIM25</span> ubiquitinates <span class="match term1">RIP3</span> to inhibit TNF induced cell necrosis	RING	1	Other	H.sapiens
2784	TRI25_HUMAN	CIC_HUMAN	Q14258	Q96RK0	TRIM25	CIC	MEDLINE	33115448	Degradation of <span class="match term1">CIC</span> protein following loss of ATXN1L was instead observed to be mediated by the E3 ubiquitin ligase <span class="match term0">TRIM25</span> which was further validated using glioma-derived cell lines and the TCGA breast carcinoma and liver hepatocellular carcinoma cohorts	RING	1	Other	H.sapiens
2785	TRI25_HUMAN	DDX58_HUMAN	Q14258	O95786	TRIM25	DDX58	MEDLINE	20485506	These cells depend on ectopic expression of the <span class="match term1">RIG-I</span> ubiquitinating enzyme <span class="match term0">TRIM25</span> to induce IFN through the <span class="match term1">RIG-I</span>/MAVS pathway	RING	1	Training data	H.sapiens
2786	TRI25_HUMAN	AMFR_HUMAN	Q14258	Q9UKV5	TRIM25	AMFR	MEDLINE	24810856	We show that polyubiquitylation of AMF requires cooperative interaction between <span class="match term1">gp78</span> and the ubiquitin ligase <span class="match term0">TRIM25</span> (tripartite motif-containing protein 25)	RING	1	Other	H.sapiens
2787	TRI25_HUMAN	PTEN_HUMAN	Q14258	P60484	TRIM25	PTEN	MEDLINE	32196840	Knockdown of <span class="match term0">TRIM25</span> resulted in reduced ubiquitination of <span class="match term1">PTEN</span> protein	RING	1	Other	H.sapiens
2788	TRI25_HUMAN	KEAP1_HUMAN	Q14258	Q14145	TRIM25	KEAP1	MEDLINE	31953436	Mechanistically, <span class="match term0">TRIM25</span> directly targets <span class="match term1">Keap1</span> by ubiquitination and degradation	RING	1	Other	H.sapiens
2789	TRI25_HUMAN	MTA1_HUMAN	Q14258	Q13330	TRIM25	MTA1	MEDLINE	30118695	In vitro ubiquitination assay using recombinant wild-type and K98R mutant <span class="match term1">MTA-1</span> confirmed that <span class="match term1">MTA-1</span> is poly-ubiquitinated at K98 residue by <span class="match term0">TRIM25</span>	RING	1	Other	H.sapiens
2790	TRI25_HUMAN	ZFHX3_HUMAN	Q14258	Q15911	TRIM25	ZFHX3	MEDLINE	22452784	UbiNet 2.0	RING	1	Training data	H.sapiens
2791	TRI25_HUMAN	TRAF2_HUMAN	Q14258	Q12933	TRIM25	TRAF2	MEDLINE	32024699	<span class="match term0">TRIM25</span> Promotes TNF-alpha-induced NF-kappaB Activation through Potentiating the K63-Linked Ubiquitination of <span class="match term1">TRAF2</span>	RING	1	Other	H.sapiens
2792	TRI25_HUMAN	KLF5_HUMAN	Q14258	Q13887	TRIM25	KLF5	MEDLINE	21542805	UbiNet 2.0	RING	1	Training data	H.sapiens
2793	TRI25_HUMAN	ESR1_HUMAN	Q14258	P03372	TRIM25	ESR1	MEDLINE	17418098	<span class="match term0">EFP</span> promoted the ubiquitylation of ERalphain vitro and in vivo and consequently promoted the degradation of <span class="match term1">ERalpha</span>	RING	1	Training data	H.sapiens
2794	TRI26_HUMAN	ZEB1_HUMAN	Q12899	P37275	TRIM26	ZEB1	MEDLINE	33649471	<span class="match term0">TRIM26</span> promotes the degradation of <span class="match term1">ZEB1</span> protein by ubiquitination in HCC	RING	1	Other	H.sapiens
2795	TRI26_HUMAN	IRF3_HUMAN	Q12899	Q14653	TRIM26	IRF3	MEDLINE	25763818	<span class="match term0">TRIM26</span> negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear <span class="match term1">IRF3</span>.	RING	1	Other	H.sapiens
2796	TRI27_HUMAN	TEAD4_HUMAN	P14373	Q15561	TRIM27	TEAD4	MEDLINE	33993634	<span class="match term0">TRIM27</span> is a novel E3 ubiquitin ligase that induces K27/48-linked ubiquitination of unpalmitoylated <span class="match term1">TEAD4</span> at Lys278	RING	1	Other	H.sapiens
2797	TRI27_HUMAN	CDN1A_HUMAN	P14373	P38936	TRIM27	CDKN1A	MEDLINE	33251042	<span class="match term0">TRIM27</span> Functions as a Novel Oncogene in Non-Triple-Negative Breast Cancer by Blocking Cellular Senescence through <span class="match term1">p21</span> Ubiquitination	RING	1	Other	H.sapiens
2798	TRI27_HUMAN	PIAS3_HUMAN	P14373	Q9Y6X2	TRIM27	PIAS3	MEDLINE	31747314	More importantly, <span class="match term0">TRIM27</span> interacted with <span class="match term1">PIAS3</span>, and its overexpression promoted <span class="match term1">PIAS3</span> ubiquitination in HaCaT cells	RING	1	Other	H.sapiens
2799	TRI27_HUMAN	TBK1_HUMAN	P14373	Q9UHD2	TRIM27	TBK1	MEDLINE	29688809	Knockout of endogenous USP7 led to enhanced <span class="match term0">TRIM27</span> degradation and reduced <span class="match term1">TBK1</span> ubiquitination and degradation, resulting in enhanced type I IFN signaling	RING	1	Other	H.sapiens
2800	TRI27_HUMAN	P3C2B_HUMAN	P14373	O00750	TRIM27	PIK3C2B	MEDLINE	22128329	UbiNet 2.0	RING	1	Training data	H.sapiens
2801	TRI27_HUMAN	PTEN_HUMAN	P14373	P60484	TRIM27	PTEN	MEDLINE	31719796	Moreover, <span class="match term0">TRIM27</span> interacted with <span class="match term1">PTEN</span> and mediated its poly-ubiquitination in ESCC cells	RING	1	Other	H.sapiens
2802	TIF1B_HUMAN	P53_HUMAN	Q13263	P04637	TRIM28	TP53	MEDLINE	20864041	For example, MAGE-C2-<span class="match term0">TRIM28</span> is shown to target <span class="match term1">p53</span> for degradation in a proteasome-dependent manner, consistent with its tumorigenic functions.	RING	1	Training data	H.sapiens
2803	TIF1B_HUMAN	GPX1_HUMAN	Q13263	P07203	TRIM28	GPX1	MEDLINE	33398366	Co-immunoprecipitation and ubiquitination assays demonstrated that <span class="match term0">TRIM28</span> negatively regulated <span class="match term1">GPX1</span> via ubiquitination	RING	1	Other	H.sapiens
2804	TIF1B_HUMAN	F16P1_HUMAN	Q13263	P09467	TRIM28	FBP1	MEDLINE	28394358	MAGE-A3 and MAGE-C2, which are known to be overexpressed in HCC, can enhance <span class="match term0">TRIM28</span>-dependent degradation of <span class="match term1">FBP1</span> by forming ubiquitin ligase complexes with <span class="match term0">TRIM28</span>.	RING	1	Other	H.sapiens
2805	TIF1B_HUMAN	AAPK1_HUMAN	Q13263	Q13131	TRIM28	PRKAA1	MEDLINE	25945414	Here we discuss our recent work detailing the function of the MAGEA-<span class="match term0">TRIM28</span> ubiquitin ligase as an oncogene product that targets <span class="match term1">PRKAA1</span>/AMPKalpha1 for ubiquitination and proteasome-mediated degradation	RING	1	Other	H.sapiens
2806	TIF1B_HUMAN	IRF7_HUMAN	Q13263	Q92985	TRIM28	IRF7	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2807	TRIM3_HUMAN	BECN1_HUMAN	O75382	Q14457	TRIM3	BECN1	MEDLINE	32021240	Finally, we found in ES cells, <span class="match term0">TRIM3</span> could directly interact with <span class="match term1">Beclin1</span>, and improved its K48-linked polyubiquitinaion, leading to the degradation of <span class="match term1">Beclin1</span> and then regulated autophagy	RING	1	Other	H.sapiens
2808	TRIM3_HUMAN	P53_HUMAN	O75382	P04637	TRIM3	TP53	MEDLINE	33292295	Further investigation showed that <span class="match term0">TRIM3</span> could associate with <span class="match term1">P53</span> and promote <span class="match term1">P53</span> K48-linked ubiquitination and degradation	RING	1	Other	H.sapiens
2809	TRIM3_HUMAN	GKAP1_HUMAN	O75382	Q5VSY0	TRIM3	GKAP1	MEDLINE	20352094	UbiNet 2.0	RING	1	Training data	H.sapiens
2810	TRI31_HUMAN	M3K7_HUMAN	Q9BZY9	O43318	TRIM31	MAP3K7	MEDLINE	33016203	Furthermore, <span class="match term0">TRIM31</span> interacted with and ubiquitinated transforming growth factor-beta-activated kinase-1 (<span class="match term1">TAK1</span>), resulting in <span class="match term1">TAK1</span> activation and subsequent induction of NF-kappaB signaling	RING	1	Other	H.sapiens
2811	TRI31_HUMAN	NLRP3_HUMAN	Q9BZY9	Q96P20	TRIM31	NLRP3	MEDLINE	32716108	<span class="match term0">TRIM31</span> inhibits <span class="match term1">NLRP3</span> inflammasome and pyroptosis of retinal pigment epithelial cells through ubiquitination of <span class="match term1">NLRP3</span>	RING	1	Other	H.sapiens
2812	TRI31_HUMAN	TRI31_HUMAN	Q9BZY9	Q9BZY9	TRIM31	TRIM31	UniProt	TRI31_HUMAN	Auto-ubiquitinated (in vitro)	RING	1	Training data	H.sapiens
2813	TRI31_HUMAN	TIGAR_HUMAN	Q9BZY9	Q9NQ88	TRIM31	TIGAR	MEDLINE	34218200	<span class="match term0">TRIM31</span> interacted with <span class="match term1">TIGAR</span> and promoted the polyubiquitination of <span class="match term1">TIGAR</span>, consequently facilitated its degradation in a proteasome-dependent pathway	RING	1	Other	H.sapiens
2814	TRI32_HUMAN	DTBP1_HUMAN	Q13049	Q96EV8	TRIM32	DTNBP1	MEDLINE	19349376	Using the yeast two-hybrid system, we found that <span class="match term0">TRIM32</span> binds and ubiquitinates dysbindin, a protein implicated in the genetic aetiology of schizophrenia, augmenting its degradation	RING	1	Training data	H.sapiens
2815	TRI32_HUMAN	BBS2_HUMAN	Q13049	Q9BXC9	TRIM32	BBS2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2816	TRI32_HUMAN	TRI32_HUMAN	Q13049	Q13049	TRIM32	TRIM32	MEDLINE	17987106	On the other hand, NO enhanced the stimulatory effect of Pias3 on <span class="match term0">Trim32</span> autoubiquitination	RING	1	Training data	H.sapiens
2817	TRI32_HUMAN	XIAP_HUMAN	Q13049	P98170	TRIM32	XIAP	MEDLINE	21628460	UbiNet 2.0	RING	1	Training data	H.sapiens
2818	TRI32_HUMAN	PIAS3_HUMAN	Q13049	Q9Y6X2	TRIM32	PIAS3	MEDLINE	17987106	On the one hand, NO promoted <span class="match term0">Trim32</span>-mediated <span class="match term1">Pias3</span> ubiquitination	RING	1	Training data	H.sapiens
2819	TRI32_HUMAN	ABI2_HUMAN	Q13049	Q9NYB9	TRIM32	ABI2	MEDLINE	20009572	<span class="match term0">TRIM32</span> promotes cell migration through ubiquitination of Abl interactor 2 (<span class="match term1">Abi2</span>), a tumor suppressor	RING	1	Training data	H.sapiens
2820	TRI32_HUMAN	KPCZ_HUMAN	Q13049	Q05513	TRIM32	PRKCZ	MEDLINE	33096083	We demonstrated that <span class="match term1">PKCzeta</span> was specifically ubiquitinated by <span class="match term0">TRIM32</span>, and further, that <span class="match term1">PKCzeta</span> stability tended to be increased in Th2 cells with a <span class="match term0">Trim32</span> null background	RING	1	Other	H.sapiens
2821	TRI32_HUMAN	PIAS4_HUMAN	Q13049	Q8N2W9	TRIM32	PIAS4	MEDLINE	17626251	<span class="match term0">Trim32</span> binds and ubiquitylates <span class="match term1">Piasy</span>, controlling its stability and accumulation	RING	1	Training data	H.sapiens
2822	TRI32_HUMAN	MYC_HUMAN	Q13049	P01106	TRIM32	MYC	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2823	TRI32_HUMAN	TBK1_HUMAN	Q13049	Q9UHD2	TRIM32	TBK1	MEDLINE	33269343	The ubiquitin ligase <span class="match term0">TRIM32</span> associates with <span class="match term1">TBK1</span> upon EGFR inhibition, and is required for K63-linked ubiquitination and <span class="match term1">TBK1</span> activation	RING	1	Other	H.sapiens
2824	TRI32_HUMAN	OTUL_HUMAN	Q13049	Q96BN8	TRIM32	OTULIN	MEDLINE	31504727	Further experiments found that <span class="match term0">TRIM32</span> conjugates polyubiquitin onto <span class="match term1">OTULIN</span> and the polyubiquitin blocks the interaction between HOIP and <span class="match term1">OTULIN</span>, thereby activating NF-kappaB signaling	RING	1	Other	H.sapiens
2825	TRI32_HUMAN	MYCN_HUMAN	Q13049	P04198	TRIM32	MYCN	MEDLINE	25100564	<span class="match term0">Trim32</span> facilitates degradation of <span class="match term1">MYCN</span> on spindle poles and induces asymmetric cell division in human neuroblastoma cells.	RING	1	Other	H.sapiens
2826	TRI32_HUMAN	STING_HUMAN	Q13049	Q86WV6	TRIM32	STING1	MEDLINE	22745133	<span class="match term0">TRIM32</span> protein modulates type I interferon induction and cellular antiviral response by targeting MITA/<span class="match term1">STING</span> protein for K63-linked ubiquitination.	RING	1	Other	H.sapiens
2827	TRI32_HUMAN	DBND1_HUMAN	Q13049	Q9H9R9	TRIM32	DBNDD1	MEDLINE	19349376	UbiNet 2.0	RING	1	Training data	H.sapiens
2828	TRI32_HUMAN	DESM_HUMAN	Q13049	P17661	TRIM32	DES	MEDLINE	22908310	UbiNet 2.0	RING	1	Training data	H.sapiens
2829	TRI32_HUMAN	TRAF2_HUMAN	Q13049	Q12933	TRIM32	TRAF2	MEDLINE	32145086	In addition, <span class="match term0">TRIM32</span> was found to activate nuclear factor kappaB (NF-kappaB) signalling pathway, and <span class="match term0">TRIM32</span> could interact with TNF receptor-associated factor 2 (<span class="match term1">TRAF2</span>) to promote the K63-linked polyubiquitination of <span class="match term1">TRAF2</span> in RA-FLS	RING	1	Other	H.sapiens
2830	TRI32_HUMAN	SQSTM_HUMAN	Q13049	Q13501	TRIM32	SQSTM1	MEDLINE	31685529	UbiNet 2.0	RING	1	Other	H.sapiens
2831	TRI32_HUMAN	ACTS_HUMAN	Q13049	P68133	TRIM32	ACTA1	MEDLINE	16243356	hUbiquitome	RING	1	Other	H.sapiens
2832	TRI33_HUMAN	SMAD4_HUMAN	Q9UPN9	Q13485	TRIM33	SMAD4	UniProt	TRI33_HUMAN	Deubiquitinates monoubiquitinated <span class="match term1">SMAD4</span>, opposing the activity of E3 ubiquitin-protein ligase <span class="match term0">TRIM33</span>	RING	1	Training data	H.sapiens
2833	TRI33_HUMAN	CTNB1_HUMAN	Q9UPN9	P35222	TRIM33	CTNNB1	MEDLINE	25639486	Here we demonstrate that the tripartite motif-containing protein 33 (<span class="match term0">TRIM33</span>), acting as an E3 ubiquitin ligase, reduces the abundance of nuclear <span class="match term1">beta-catenin</span> protein	RING	1	Other	H.sapiens
2834	TRI33_HUMAN	DHX33_HUMAN	Q9UPN9	Q9H6R0	TRIM33	DHX33	MEDLINE	25172487	The ubiquitination of <span class="match term1">DHX33</span> by <span class="match term0">TRIM33</span> is lysine 63 specific and is required for the formation of the <span class="match term1">DHX33</span>-NLRP3 inflammasome complex.	RING	1	Other	H.sapiens
2835	TRI35_HUMAN	TRAF3_HUMAN	Q9UPQ4	Q13114	TRIM35	TRAF3	MEDLINE	32562145	<span class="match term0">TRIM35</span> promoted the RIG-I-mediated signaling by catalyzing Lys63-linked polyubiquitination of <span class="match term1">TRAF3</span> and the subsequent formation of a signaling complex with VISA and TBK1	RING	1	Other	H.sapiens
2836	TRI36_HUMAN	IRF3_HUMAN	Q9NQ86	Q14653	TRIM36	IRF3	MEDLINE	18711448	UbiNet 2.0	RING	1	Training data	H.sapiens
2837	TRI37_HUMAN	TRAF2_HUMAN	O94972	Q12933	TRIM37	TRAF2	MEDLINE	30043491	Furthermore, we found that <span class="match term0">TRIM37</span> bound to <span class="match term1">TRAF2</span> and promoted K63-linked ubiquitination of <span class="match term1">TRAF2</span>, sustaining the eventual activation of the NF-kappaB pathway	RING	1	Other	H.sapiens
2838	TRI37_HUMAN	SMAD7_HUMAN	O94972	O15105	TRIM37	SMAD7	MEDLINE	32916597	Mechanistically, we showed that <span class="match term0">TRIM37</span> physically interacts with <span class="match term1">SMAD7</span> and promotes ubiquitination-mediated degradation of <span class="match term1">SMAD7</span>, and that <span class="match term1">SMAD7</span> is a key mediator of TRM37-induced hepatic fibrosis	RING	1	Other	H.sapiens
2839	TRI37_HUMAN	TRAF6_HUMAN	O94972	Q9Y4K3	TRIM37	TRAF6	MEDLINE	33839419	Mechanically, <span class="match term0">TRIM37</span> promoted the K63-linked ubiquitination of <span class="match term1">TRAF6</span>	RING	1	Other	H.sapiens
2840	TRI37_HUMAN	TRI37_HUMAN	O94972	O94972	TRIM37	TRIM37	UniProt	TRI37_HUMAN	Auto-ubiquitinated	RING	1	Training data	H.sapiens
2841	TRI38_HUMAN	TRI38_HUMAN	O00635	O00635	TRIM38	TRIM38	MEDLINE	21306652	UbiNet 2.0	RING	1	Training data	H.sapiens
2842	TRI38_HUMAN	TRAF6_HUMAN	O00635	Q9Y4K3	TRIM38	TRAF6	MEDLINE	22323536	As an E3 ligase, <span class="match term0">TRIM38</span> bound to <span class="match term1">TRAF6</span> and promoted K48-linked polyubiquitination, which led to the proteasomal degradation of <span class="match term1">TRAF6</span>	RING	1	Other	H.sapiens
2843	TRI39_HUMAN	MOAP1_HUMAN	Q9HCM9	Q96BY2	TRIM39	MOAP1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2844	TRI39_HUMAN	P53_HUMAN	Q9HCM9	P04637	TRIM39	TP53	MEDLINE	23213260	UbiNet 2.0	RING	1	Training data	H.sapiens
2845	TRIM4_HUMAN	DDX58_HUMAN	Q9C037	O95786	TRIM4	DDX58	MEDLINE	29354136	However, subsequent studies have reported that Riplet, MEX3C, and <span class="match term0">TRIM4</span> ubiquitin ligases are also involved in K63-linked polyubiquitination and the activation of <span class="match term1">RIG-I</span>	RING	1	Other	H.sapiens
2846	TRIM4_HUMAN	TRPM8_HUMAN	Q9C037	Q7Z2W7	TRIM4	TRPM8	MEDLINE	33037615	<span class="match term0">TRIM4</span> interacts with <span class="match term1">TRPM8</span> and regulates its channel function through K423-mediated ubiquitination	RING	1	Other	H.sapiens
2847	TRI41_HUMAN	ZSC21_HUMAN	Q8WV44	Q9Y5A6	TRIM41	ZSCAN21	MEDLINE	30485814	Our data show that <span class="match term1">ZSCAN21</span> stimulates SNCA transcription in neuronal cells and that <span class="match term0">TRIM41</span> is an E3 ubiquitin ligase for <span class="match term1">ZSCAN21</span>	RING	1	Other	H.sapiens
2848	TRI41_HUMAN	KPCB_HUMAN	Q8WV44	P05771	TRIM41	PRKCB	MEDLINE	17893151	<span class="match term0">RINCK</span> induces the ubiquitination of PKC both in vitro and in cells	RING	1	Training data	H.sapiens
2849	TRI41_HUMAN	CGAS_HUMAN	Q8WV44	Q8N884	TRIM41	CGAS	MEDLINE	29760876	We report that an E3 ubiquitin ligase, RING finger protein that interacts with C kinase (RINCK, also known as tripartite motif protein 41, <span class="match term0">TRIM41</span>), is critical for <span class="match term1">cGAS</span> activation by mediating the monoubiquitination of <span class="match term1">cGAS</span>.	RING	1	Other	H.sapiens
2850	TRI41_HUMAN	KPCE_HUMAN	Q8WV44	Q02156	TRIM41	PRKCE	MEDLINE	17893151	UbiNet 2.0	RING	1	Training data	H.sapiens
2851	TRI41_HUMAN	BCL10_HUMAN	Q8WV44	O95999	TRIM41	BCL10	MEDLINE	33640899	<span class="match term0">TRIM41</span> is required to innate antiviral response by polyubiquitinating <span class="match term1">BCL10</span> and recruiting NEMO	RING	1	Other	H.sapiens
2852	TRI46_HUMAN	PPARA_HUMAN	Q7Z4K8	Q07869	TRIM46	PPARA	MEDLINE	32295675	<span class="match term0">TRIM46</span> acts as an oncogene in OS by interactingwith and ubiquitinating <span class="match term1">PPAR</span> alpha, resulting in the activation of NF-kappa B signaling pathway	RING	1	Other	H.sapiens
2853	TRI47_HUMAN	SMAD4_HUMAN	Q96LD4	Q13485	TRIM47	SMAD4	MEDLINE	30979374	<span class="match term0">TRIM47</span> is up-regulated in colorectal cancer, promoting ubiquitination and degradation of <span class="match term1">SMAD4</span>	RING	1	Other	H.sapiens
2854	TRI47_HUMAN	ILF3_HUMAN	Q96LD4	Q12906	TRIM47	ILF3	MEDLINE	34110282	Vesicular Stomatitis Virus (VSV) infection induces the up-regulation and activation of Tim-3 in macrophages which in turn recruited the E3 ubiquitin ligase <span class="match term0">TRIM47</span> to the zinc finger domain of <span class="match term1">NF90</span> and initiated a proteasome-dependent degradation via K48-linked ubiquitination at Lys297	RING	1	Other	H.sapiens
2855	TRI47_HUMAN	P53_HUMAN	Q96LD4	P04637	TRIM47	TP53	MEDLINE	33622324	<span class="match term0">TRIM47</span> promotes malignant progression of renal cell carcinoma by degrading <span class="match term1">P53</span> through ubiquitination	RING	1	Other	H.sapiens
2856	TRI49_HUMAN	BLM_HUMAN	P0CI25	P54132	TRIM49	BLM	MEDLINE	23708797	UbiNet 2.0	RING	1	Other	H.sapiens
2857	TRIM5_HUMAN	TRIM5_HUMAN	Q9C035	Q9C035	TRIM5	TRIM5	MEDLINE	18312418	In addition to the self-ubiquitination, we show that <span class="match term0">TRIM5alpha</span> is ubiquitinated by another E3 ubiquitin ligase, Ro52, and deubiquitinated by YopJ, one of the pathogenic proteins derived from Yersinia species	RING	1	Training data	H.sapiens
2858	TRI50_HUMAN	TRI50_HUMAN	Q86XT4	Q86XT4	TRIM50	TRIM50	MEDLINE	18398435	hUbiquitome	RING	1	Other	H.sapiens
2859	TRI52_HUMAN	TRAF2_HUMAN	Q96A61	Q12933	TRIM52	TRAF2	MEDLINE	32898524	SIGNIFICANCE: <span class="match term0">TRIM52</span> accelerated the growth of BPH-1 cells by upregulating NF-kappaB, and <span class="match term0">TRIM52</span> could promote <span class="match term1">TRAF2</span> ubiquitination	RING	1	Other	H.sapiens
2860	TRI52_HUMAN	PTN11_HUMAN	Q96A61	Q06124	TRIM52	PTPN11	MEDLINE	30918473	Second, we overexpressed SW480 cells with <span class="match term0">TRIM52</span> and observed that <span class="match term0">TRIM52</span> overexpression obviously enhanced the polyubiquitination of <span class="match term1">SHP2</span> (Fig. 5d), suggesting that <span class="match term0">TRIM52</span> may serve as an E3 ligase for <span class="match term1">SHP2</span>	RING	1	Other	H.sapiens
2861	TRI52_HUMAN	PPM1A_HUMAN	Q96A61	P35813	TRIM52	PPM1A	MEDLINE	29898761	<span class="match term0">TRIM52</span> was found interacted with <span class="match term1">PPM1A</span> and <span class="match term0">TRIM52</span> down-regulation inhibited the ubiquitination of <span class="match term1">PPM1A</span>.	RING	1	Other	H.sapiens
2862	TRI56_HUMAN	SAP18_HUMAN	Q9BRZ2	O00422	TRIM56	SAP18	MEDLINE	30670829	vFLIP degrades <span class="match term1">SAP18</span> through a ubiquitin-proteasome pathway by recruiting E3 ubiquitin ligase <span class="match term0">TRIM56</span>	RING	1	Other	H.sapiens
2863	TRI56_HUMAN	VIME_HUMAN	Q9BRZ2	P08670	TRIM56	VIM	MEDLINE	28771721	RNAi mediated silencing of the candidate ubiquitin in Moody cells and concurrent overexpression of the candidate ubiquitin ligases in SKOV-3 confirmed that <span class="match term0">TRIM56</span> is the ubiquitin ligase that is degrading <span class="match term1">vimentin</span> in Moody cells	RING	1	Other	H.sapiens
2864	TRI56_HUMAN	STING_HUMAN	Q9BRZ2	Q86WV6	TRIM56	STING1	MEDLINE	23189823	UbiNet 2.0	RING	1	Training data	H.sapiens
2865	TRI58_HUMAN	DC1I1_HUMAN	Q8NG06	O14576	TRIM58	DYNC1I1	MEDLINE	25241935	UbiNet 2.0	RING	1	Other	H.sapiens
2866	TRI58_HUMAN	DC1L2_HUMAN	Q8NG06	O43237	TRIM58	DYNC1LI2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2867	TRI59_HUMAN	PTEN_HUMAN	Q8IWR1	P60484	TRIM59	PTEN	MEDLINE	32165307	Immunoprecipiation experiments showed the interaction between <span class="match term0">TRIM59</span> and <span class="match term1">PTEN</span> in A549/DDP cells, and that <span class="match term0">TRIM59</span> knockdown suppressed the ubiquitination of <span class="match term1">PTEN</span>	RING	1	Other	H.sapiens
2868	TRI59_HUMAN	P53_HUMAN	Q8IWR1	P04637	TRIM59	TP53	MEDLINE	33240412	At the molecular level, <span class="match term0">TRIM59</span> was indicated to be an E3 putative ubiquitin ligase that targeted the <span class="match term1">p53</span> protein, leading to increased degradation of <span class="match term1">p53</span>, which resulted in decreased chemosensitivity to cisplatin	RING	1	Other	H.sapiens
2869	TRI59_HUMAN	PPM1A_HUMAN	Q8IWR1	P35813	TRIM59	PPM1A	MEDLINE	32348176	Overexpression of <span class="match term0">TRIM59</span> significantly promoted the ubiquitination of <span class="match term1">PPM1A</span>	RING	1	Other	H.sapiens
2870	TRI59_HUMAN	H2AY_HUMAN	Q8IWR1	O75367	TRIM59	MACROH2A1	MEDLINE	31488827	UbiNet 2.0	RING	1	Other	H.sapiens
2871	TRIM6_HUMAN	BTG2_HUMAN	Q9C030	P78543	TRIM6	BTG2	MEDLINE	31992359	Further, Lys5 was essential for <span class="match term0">TRIM6</span> mediated <span class="match term1">TIS21</span> ubiquitination	RING	1	Other	H.sapiens
2872	TRI62_HUMAN	CARD9_HUMAN	Q9BVG3	Q9H257	TRIM62	CARD9	MEDLINE	26488816	Ubiquitin Ligase <span class="match term0">TRIM62</span> Regulates <span class="match term1">CARD9</span>-Mediated Anti-fungal Immunity and Intestinal Inflammation.	RING	1	Other	H.sapiens
2873	TRI62_HUMAN	TRI62_HUMAN	Q9BVG3	Q9BVG3	TRIM62	TRIM62	MEDLINE	23402750	UbiNet 2.0	RING	1	Training data	H.sapiens
2874	TRI63_HUMAN	3HIDH_HUMAN	Q969Q1	P31937	TRIM63	HIBADH	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2875	TRI63_HUMAN	KCRM_HUMAN	Q969Q1	P06732	TRIM63	CKM	MEDLINE	18222470	UbiNet 2.0	RING	1	Training data	H.sapiens
2876	TRI63_HUMAN	TNNC1_HUMAN	Q969Q1	P63316	TRIM63	TNNC1	MEDLINE	15601779	15601779	RING	1	Other	H.sapiens
2877	TRI63_HUMAN	MYPC2_HUMAN	Q969Q1	Q14324	TRIM63	MYBPC2	MEDLINE	17314137	UbiNet 2.0	RING	1	Training data	H.sapiens
2878	TRI63_HUMAN	ATPB_HUMAN	Q969Q1	P06576	TRIM63	ATP5F1B	MEDLINE	23695782	UbiNet 2.0	RING	1	Other	H.sapiens
2879	TRI63_HUMAN	PSMD4_HUMAN	Q969Q1	P55036	TRIM63	PSMD4	MEDLINE	19240029	Furthermore, if the <span class="match term1">S5a</span> UIM domains were fused to GST, the protein was rapidly ubiquitinated by <span class="match term0">MuRF1</span> and CHIP	RING	1	Training data	H.sapiens
2880	TRI63_HUMAN	TNNI3_HUMAN	Q969Q1	P19429	TRIM63	TNNI3	MEDLINE	15601779	In vitro, <span class="match term0">MuRF1</span> functioned as a ubiquitin ligase to catalyze ubiquitylation of troponin I through a RING finger-dependent mechanism	RING	1	Training data	H.sapiens
2881	TRI63_HUMAN	TNNI1_HUMAN	Q969Q1	P19237	TRIM63	TNNI1	MEDLINE	19240029	UbiNet 2.0	RING	1	Other	H.sapiens
2882	TRI63_HUMAN	THA_HUMAN	Q969Q1	P10827	TRIM63	THRA	MEDLINE	26862156	<span class="match term0">MuRF1</span> mono-ubiquitinates <span class="match term1">TRalpha</span> to inhibit T3-induced cardiac hypertrophy in vivo.	RING	1	Other	H.sapiens
2883	TRI63_HUMAN	GMEB1_HUMAN	Q969Q1	Q9Y692	TRIM63	GMEB1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2884	TRI63_HUMAN	MLRS_HUMAN	Q969Q1	Q96A32	TRIM63	MYLPF	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2885	TRI63_HUMAN	MYPC3_HUMAN	Q969Q1	Q14896	TRIM63	MYBPC3	MEDLINE	19506036	UbiNet 2.0	RING	1	Training data	H.sapiens
2886	TRI63_HUMAN	IKBA_HUMAN	Q969Q1	P25963	TRIM63	NFKBIA	MEDLINE	23535871	UbiNet 2.0	RING	1	Training data	H.sapiens
2887	TRI63_HUMAN	MYL1_HUMAN	Q969Q1	P05976	TRIM63	MYL1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2888	TRI63_HUMAN	ACTS_HUMAN	Q969Q1	P68133	TRIM63	ACTA1	MEDLINE	21764995	Muscle actin is polyubiquitinylated in vitro and in vivo and targeted for breakdown by the E3 ligase <span class="match term0">MuRF1</span>.	RING	1	Other	H.sapiens
2889	TRI63_HUMAN	MLRV_HUMAN	Q969Q1	P10916	TRIM63	MYL2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2890	TRI65_HUMAN	TNR6A_HUMAN	Q6PJ69	Q8NDV7	TRIM65	TNRC6A	MEDLINE	24778252	Ubiquitination assays demonstrate that <span class="match term0">TRIM65</span> is an ubiquitin E3 ligase for <span class="match term1">TNRC6</span> proteins	RING	1	Other	H.sapiens
2891	TRI65_HUMAN	ANXA2_HUMAN	Q6PJ69	P07355	TRIM65	ANXA2	MEDLINE	30075204	Collectively, our results suggest that the overexpression of <span class="match term0">TRIM65</span> has an essential oncogenic role via ubiquitination of <span class="match term1">ANXA2</span> in UCB pathogenesis, and that such could be used as a novel prognostic marker and/or therapeutic target for UCB.	RING	1	Other	H.sapiens
2892	TRI65_HUMAN	RHG35_HUMAN	Q6PJ69	Q9NRY4	TRIM65	ARHGAP35	MEDLINE	31332286	Ubiquitin ligase <span class="match term0">TRIM65</span> promotes colorectal cancer metastasis by targeting <span class="match term1">ARHGAP35</span> for protein degradation.	RING	1	Other	H.sapiens
2893	TRI65_HUMAN	VCAM1_HUMAN	Q6PJ69	P19320	TRIM65	VCAM1	MEDLINE	31310649	Expression of wild-type <span class="match term0">TRIM65</span>, but not expression of a <span class="match term0">TRIM65</span> mutant that lacks E3 ubiquitin ligase function in endothelial cells, promotes <span class="match term1">VCAM-1</span> ubiquitination and degradation, whereas small interference RNA-mediated knocking down of <span class="match term0">TRIM65</span> attenuates <span class="match term1">VCAM-1</span> protein degradation	RING	1	Other	H.sapiens
2894	TRI69_HUMAN	P53_HUMAN	Q86WT6	P04637	TRIM69	TP53	MEDLINE	30844644	In conclusion, we provide the first demonstration that Foxo3a is a potential transcription factor for <span class="match term0">TRIM69</span>, and <span class="match term0">TRIM69</span> induces <span class="match term1">p53</span> ubiquitination	RING	1	Other	H.sapiens
2895	TRIM7_HUMAN	BRMS1_HUMAN	Q9C029	Q9HCU9	TRIM7	BRMS1	MEDLINE	32853985	In summary, we have identified an E3 ubiquitin ligase <span class="match term0">TRIM7</span> that regulates osteosarcoma cell invasion, migration and chemoresistance through ubiquitination of <span class="match term1">BRMS1</span>.	RING	1	Other	H.sapiens
2896	TRIM7_HUMAN	TF65_HUMAN	Q9C029	Q04206	TRIM7	RELA	MEDLINE	31958511	E3 ubiquitin ligase <span class="match term0">TRIM7</span> negatively regulates NF-kappa B signaling pathway by degrading <span class="match term1">p65</span> in lung cancer	RING	1	Other	H.sapiens
2897	LIN41_HUMAN	LN28B_HUMAN	Q2Q1W2	Q6ZN17	TRIM71	LIN28B	MEDLINE	24602972	Consistent with the let-7 stimulatory role of <span class="match term0">TRIM71</span> via <span class="match term1">Lin28B</span> polyubiquitination, specific knockdown of <span class="match term0">TRIM71</span> led to downregulation of let-7 expression	RING	1	Other	H.sapiens
2898	TRIM8_HUMAN	ESR1_HUMAN	Q9BZR9	P03372	TRIM8	ESR1	MEDLINE	33163282	Further mechanistic studies showed that <span class="match term0">TRIM8</span> interacts with AF1 domain of <span class="match term1">ERalpha</span> via its RING domain in the cytoplasm and increases poly-ubiquitination of the <span class="match term1">ERalpha</span> protein	RING	1	Other	H.sapiens
2899	TRIM8_HUMAN	SOCS1_HUMAN	Q9BZR9	O15524	TRIM8	SOCS1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
2900	TRIM8_HUMAN	M3K7_HUMAN	Q9BZR9	O43318	TRIM8	MAP3K7	MEDLINE	22084099	UbiNet 2.0	RING	1	Other	H.sapiens
2901	TRIM9_HUMAN	VASP_HUMAN	Q9C026	P50552	TRIM9	VASP	MEDLINE	31820781	Here we show that the <span class="match term0">TRIM9</span>-related protein TRIM67 outcompetes <span class="match term0">TRIM9</span> for interacting with <span class="match term1">VASP</span> and antagonizes <span class="match term0">TRIM9</span>-dependent <span class="match term1">VASP</span> ubiquitination	RING	1	Other	H.sapiens
2902	TRIM9_HUMAN	TRIM9_HUMAN	Q9C026	Q9C026	TRIM9	TRIM9	MEDLINE	20085810	UbiNet 2.0	RING	1	Training data	H.sapiens
2903	TRIPC_HUMAN	ARF_HUMAN	Q14669	Q8N726	TRIP12	CDKN2A	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	H.sapiens
2904	TRIPC_HUMAN	ULA1_HUMAN	Q14669	Q13564	TRIP12	NAE1	MEDLINE	18627766	Our data suggest that that <span class="match term0">TRIP12</span> promotes degradation of APP-BP1 by catalyzing its ubiquitination, which in turn modulates the neddylation pathway	SINGLE_OTHER	1	Training data	H.sapiens
2905	TRIPC_HUMAN	SOX6_HUMAN	Q14669	P35712	TRIP12	SOX6	MEDLINE	23663701	RESULTS: We found that the E3 ligase <span class="match term0">Trip12</span>, a HECT domain E3 ubiquitin ligase, recognizes and polyubiquitinates <span class="match term1">Sox6</span>	SINGLE_OTHER	1	Other	H.sapiens
2906	TRIPC_HUMAN	ARFG1_HUMAN	Q14669	Q8N6T3	TRIP12	ARFGAP1	MEDLINE	22028794	UbiNet 2.0	SINGLE_OTHER	1	Training data	H.sapiens
2907	TRIPC_HUMAN	SMCE1_HUMAN	Q14669	Q969G3	TRIP12	SMARCE1	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	H.sapiens
2908	TP4AP_HUMAN	MYC_HUMAN	Q8TEL6	P01106	TRPC4AP	MYC	UniProt	TP4AP_HUMAN	The DCX(<span class="match term0">TRUSS</span>) complex specifically mediates the polyubiquitination and subsequent degradation of <span class="match term1">MYC</span>	RING	1	Training data	H.sapiens
2909	TP4AP_HUMAN	NFKB1_HUMAN	Q8TEL6	P19838	TRPC4AP	NFKB1	MEDLINE	32889079	<span class="match term0">TRUSS</span> facilitated the ubiquitination of NF-kappaB1/<span class="match term1">p105</span> and promoted its proteolytic processing to generate excess of p50.	RING	1	Other	H.sapiens
2910	TTC3_HUMAN	AKT3_HUMAN	P53804	Q9Y243	TTC3	AKT3	UniProt	TTC3_HUMAN	E3 ubiquitin-protein ligase that mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and <span class="match term1">AKT3</span>) in the nucleus	RING	1	Training data	H.sapiens
2911	TTC3_HUMAN	AKT1_HUMAN	P53804	P31749	TTC3	AKT1	UniProt	TTC3_HUMAN	E3 ubiquitin-protein ligase that mediates the ubiquitination and subsequent degradation of phosphorylated Akt (<span class="match term1">AKT1</span>, AKT2 and AKT3) in the nucleus	RING	1	Training data	H.sapiens
2912	TTC3_HUMAN	AKT2_HUMAN	P53804	P31751	TTC3	AKT2	UniProt	TTC3_HUMAN	E3 ubiquitin-protein ligase that mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, <span class="match term1">AKT2</span> and AKT3) in the nucleus	RING	1	Training data	H.sapiens
2913	UB2G1_HUMAN	MARH6_HUMAN	P62253	O60337	UBE2G1	MARCHF6	MEDLINE	31445887	<span class="match term1">Doa10</span> in the ER membrane then ubiquitinates them with Ubc6 and <span class="match term0">Ubc7</span>	Other	1	Other	H.sapiens
2914	UBE2O_HUMAN	MXI1_HUMAN	Q9C0C9	P50539	UBE2O	MXI1	MEDLINE	32901121	Here, we uncover that <span class="match term0">UBE2O</span> interacts and targets <span class="match term1">Mxi1</span> for ubiquitination and degradation at the K46 residue	Other	1	Other	H.sapiens
2915	UBE2O_HUMAN	HEXI1_HUMAN	Q9C0C9	O94992	UBE2O	HEXIM1	MEDLINE	29845934	Tat hijacks <span class="match term0">UBE2O</span> to ubiquitinate the P-TEFb kinase inhibitor <span class="match term1">HEXIM1</span> of the 7SK snRNP, a fraction of which also resides in the cytoplasm bound to P-TEFb	Other	1	Other	H.sapiens
2916	UBE3A_HUMAN	SCRIB_HUMAN	Q05086	Q14160	UBE3A	SCRIB	MEDLINE	11027293	Human scribble (<span class="match term1">Vartul</span>) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the <span class="match term0">E6AP</span> ubiquitin-protein ligase	SINGLE_OTHER	1	Training data	H.sapiens
2917	UBE3A_HUMAN	PTN3_HUMAN	Q05086	P26045	UBE3A	PTPN3	MEDLINE	17947517	We show here that HPV16 E6 accelerated the proteasome-mediated degradation of <span class="match term1">PTPH1</span>, which required the binding of E6 to the cellular ubiquitin ligase <span class="match term0">E6-AP</span> and to <span class="match term1">PTPH1</span>	SINGLE_OTHER	1	Training data	H.sapiens
2918	UBE3A_HUMAN	MCM7_HUMAN	Q05086	P33993	UBE3A	MCM7	MEDLINE	9852095	<span class="match term1">Mcm7</span> is ubiquitinated in vivo in both an <span class="match term0">E6-AP</span>-dependent and -independent manner	SINGLE_OTHER	1	Training data	H.sapiens
2919	UBE3A_HUMAN	UBE3A_HUMAN	Q05086	Q05086	UBE3A	UBE3A	MEDLINE	10864652	E6-mediated degradation of <span class="match term0">E6AP</span> requires (i) the binding of E6 to <span class="match term0">E6AP</span>, (ii) the catalytic activity of <span class="match term0">E6AP</span>, and (iii) activity of the 26S proteasome, suggesting that E6-<span class="match term0">E6AP</span> interaction results in <span class="match term0">E6AP</span> self-ubiquitination and degradation	SINGLE_OTHER	1	Training data	H.sapiens
2920	UBE3A_HUMAN	CDN1B_HUMAN	Q05086	P46527	UBE3A	CDKN1B	MEDLINE	19591933	<span class="match term0">UBE3A</span>/E6-AP regulates cell proliferation by promoting proteasomal degradation of p27.	SINGLE_OTHER	1	Other	H.sapiens
2921	UBE3A_HUMAN	PSMD4_HUMAN	Q05086	P55036	UBE3A	PSMD4	MEDLINE	19240029	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
2922	UBE3A_HUMAN	PTPA_HUMAN	Q05086	Q15257	UBE3A	PTPA	MEDLINE	31160454	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
2923	UBE3A_HUMAN	RB_HUMAN	Q05086	P06400	UBE3A	RB1	MEDLINE	17907805	The NS5B-dependent ubiquitination of <span class="match term1">pRb</span> requires the ubiquitin ligase activity of E6-associated protein (E6AP), <span class="match term0">as</span> <span class="match term1">pRb</span> abundance was restored by siRNA knockdown of E6AP or overexpression of a dominant-negative E6AP mutant in cells containing HCV RNA replicons	SINGLE_OTHER	1	Training data	H.sapiens
2924	UBE3A_HUMAN	UCHL5_HUMAN	Q05086	Q9Y5K5	UBE3A	UCHL5	MEDLINE	24743594	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
2925	UBE3A_HUMAN	ANXA1_HUMAN	Q05086	P04083	UBE3A	ANXA1	MEDLINE	19204938	Ectopic expression of <span class="match term0">E6AP</span> enhanced the degradation of annexin A1 in vivo	SINGLE_OTHER	1	Training data	H.sapiens
2926	UBE3A_HUMAN	ENOA_HUMAN	Q05086	P06733	UBE3A	ENO1	MEDLINE	31329371	We further confirmed that <span class="match term0">E6AP</span> and Enolase1 interacted and colocalized more in the cytoplasmic periphery in breast cancer cells and further demonstrated that <span class="match term0">E6AP</span> also targeted <span class="match term1">ENO1</span> for ubiquitin-mediated degradation in these cells.	SINGLE_OTHER	1	Other	H.sapiens
2927	UBE3A_HUMAN	TSC2_HUMAN	Q05086	P49815	UBE3A	TSC2	MEDLINE	18298802	An in vivo ubiquitination assay was done to reveal that <span class="match term0">E6AP</span> promoted the ubiquitination of <span class="match term1">TSC2</span> independent of HPV16 E6	SINGLE_OTHER	1	Training data	H.sapiens
2928	UBE3A_HUMAN	P53_HUMAN	Q05086	P04637	UBE3A	TP53	MEDLINE	7800044	We show here that formation of a ubiquitin thioester on <span class="match term0">E6-AP</span>, an E3 involved in the human papillomavirus E6-induced ubiquitination of <span class="match term1">p53</span> (refs 6-10), is an intermediate step in <span class="match term0">E6-AP</span>-dependent ubiquitination	SINGLE_OTHER	1	Training data	H.sapiens
2929	UBE3A_HUMAN	L2GL1_HUMAN	Q05086	Q15334	UBE3A	LLGL1	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	H.sapiens
2930	UBE3A_HUMAN	BLK_HUMAN	Q05086	P51451	UBE3A	BLK	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	H.sapiens
2931	UBE3A_HUMAN	SI1L1_HUMAN	Q05086	O43166	UBE3A	SIPA1L1	MEDLINE	12036950	Additionally, the expression of a dominant-negative <span class="match term0">E6AP</span> mutant (C833A) in cells inhibited the E6-induced degradation of <span class="match term1">E6TP1</span>	SINGLE_OTHER	1	Training data	H.sapiens
2932	UBE3A_HUMAN	PML_HUMAN	Q05086	P29590	UBE3A	PML	MEDLINE	25231954	UbiNet 2.0	SINGLE_OTHER	1	Training data	H.sapiens
2933	UBE3A_HUMAN	DLG1_HUMAN	Q05086	Q12959	UBE3A	DLG1	MEDLINE	17023019	<span class="match term0">E6AP</span> was required for the in vivo degradation of <span class="match term1">DLG1</span> by both HVP-18 E6 and a chimeric HPV-11E6	SINGLE_OTHER	1	Training data	H.sapiens
2934	UBE3A_HUMAN	S100B_HUMAN	Q05086	P04271	UBE3A	S100B	MEDLINE	31783587	Mechanistic study showed that <span class="match term1">Nef</span> and <span class="match term0">UBE3A</span> were specific and antagonistic to each other in regulating proteasome activity and ubiquitination of cellular proteins in general, wherein specific domains of <span class="match term1">Nef</span> overlapping with the long terminal repeat (LTR) were essential for the observed actions	SINGLE_OTHER	1	Other	H.sapiens
2935	UBE3A_HUMAN	ARPC3_HUMAN	Q05086	O15145	UBE3A	ARPC3	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	H.sapiens
2936	UBE3A_HUMAN	RD23A_HUMAN	Q05086	P54725	UBE3A	RAD23A	MEDLINE	10373495	Although the precise role of HHR23 proteins in DNA repair and cell cycle progression remains to be elucidated, our data suggest that <span class="match term0">E6AP</span>-mediated ubiquitination of <span class="match term1">HHR23A</span> may have important implications in DNA repair and cell cycle progression	SINGLE_OTHER	1	Training data	H.sapiens
2937	UBE3A_HUMAN	RD23B_HUMAN	Q05086	P54727	UBE3A	RAD23B	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	H.sapiens
2938	UBE3A_HUMAN	DDI1_HUMAN	Q05086	Q8WTU0	UBE3A	DDI1	MEDLINE	31130875	Here, we further characterize this regulation, by identifying the <span class="match term0">UBE3A</span>-dependent ubiquitination sites and ubiquitin chains formed on <span class="match term1">DDI1</span>	SINGLE_OTHER	1	Other	H.sapiens
2939	UBE3A_HUMAN	BAK_HUMAN	Q05086	Q16611	UBE3A	BAK1	MEDLINE	18715924	In addition, when tested using HPV16 E6 (16E6) and 8E6 <span class="match term0">as</span> representative E6 proteins from the alpha and beta genera, respectively, <span class="match term1">Bak</span> degradation was dependent on the E3 ubiquitin ligase, E6AP	SINGLE_OTHER	1	Training data	H.sapiens
2940	UBE3A_HUMAN	CEBPA_HUMAN	Q05086	P49715	UBE3A	CEBPA	MEDLINE	23598402	Here, for the first time we demonstrate that E6-associated protein (<span class="match term0">E6AP</span>), an E3 ubiquitin ligase targets <span class="match term1">C/EBPalpha</span> for ubiquitin-mediated proteasome degradation and thereby negatively modulates its functions	SINGLE_OTHER	1	Other	H.sapiens
2941	UBE3A_HUMAN	ESR1_HUMAN	Q05086	P03372	UBE3A	ESR1	MEDLINE	23542176	UbiNet 2.0	SINGLE_OTHER	1	Training data	H.sapiens
2942	UBE3A_HUMAN	PRRX1_HUMAN	Q05086	P54821	UBE3A	PRRX1	MEDLINE	20589759	UbiNet 2.0	SINGLE_OTHER	1	Training data	H.sapiens
2943	UBE3A_HUMAN	DLG4_HUMAN	Q05086	P78352	UBE3A	DLG4	MEDLINE	17121805	<span class="match term0">E6AP</span>-dependent degradation of <span class="match term1">DLG4</span>/PSD95 by high-risk human papillomavirus type 18 E6 protein	SINGLE_OTHER	1	Training data	H.sapiens
2944	UBE3A_HUMAN	PRDX1_HUMAN	Q05086	Q06830	UBE3A	PRDX1	MEDLINE	20589759	UbiNet 2.0	SINGLE_OTHER	1	Other	H.sapiens
2945	UBE3A_HUMAN	GOPC_HUMAN	Q05086	Q9HD26	UBE3A	GOPC	MEDLINE	16878151	<span class="match term1">CAL</span> is ubiquitinated by the E6/E6-associated protein (<span class="match term0">E6AP</span>) complex or by <span class="match term0">E6AP</span> alone, albeit less efficiently, which indicates that it could be a normal target of <span class="match term0">E6AP</span>	SINGLE_OTHER	1	Training data	H.sapiens
2946	UBE3A_HUMAN	NELFD_HUMAN	Q05086	Q8IXH7	UBE3A	NELFCD	MEDLINE	17131388	Furthermore, in vitro ubiquitination assay also demonstrates that <span class="match term1">TH1</span> can be ubiquitinated by <span class="match term0">E6-AP</span>	SINGLE_OTHER	1	Training data	H.sapiens
2947	UBE3A_HUMAN	SYUA_HUMAN	Q05086	P37840	UBE3A	SNCA	MEDLINE	19645749	The ubiquitin ligase <span class="match term0">E6-AP</span> promotes degradation of alpha-synuclein	SINGLE_OTHER	1	Training data	H.sapiens
2948	UBE3A_HUMAN	NCOA3_HUMAN	Q05086	Q9Y6Q9	UBE3A	NCOA3	MEDLINE	16951183	<span class="match term1">AIB1</span>/<span class="match term0">E6AP</span> complexes were detected in cellular extracts, and reduction of cellular <span class="match term0">E6AP</span> levels with <span class="match term0">E6AP</span> short interfering RNA prevented proteasomal degradation of <span class="match term1">AIB1</span>	SINGLE_OTHER	1	Training data	H.sapiens
2949	UBE3A_HUMAN	BMAL1_HUMAN	Q05086	O00327	UBE3A	ARNTL	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	H.sapiens
2950	UBE3C_HUMAN	AXIN1_HUMAN	Q15386	O15169	UBE3C	AXIN1	MEDLINE	32930707	In contrast, in vitro overexpression of <span class="match term0">UBE3C</span> promotes GC cell proliferation and inhibits apoptosis through the upregulation of beta-catenin signaling by promoting ubiquitination of <span class="match term1">AXIN1</span>	SINGLE_OTHER	1	Other	H.sapiens
2951	UBE3C_HUMAN	AHNK_HUMAN	Q15386	Q09666	UBE3C	AHNAK	MEDLINE	30503554	We further identified <span class="match term1">AHNAK</span> as a novel <span class="match term0">UBE3C</span> substrate, finding that <span class="match term0">UBE3C</span> maintained stemness by ubiquitinating and promoting <span class="match term1">AHNAK</span> degradation	SINGLE_OTHER	1	Other	H.sapiens
2952	UBE3C_HUMAN	UBE3C_HUMAN	Q15386	Q15386	UBE3C	UBE3C	MEDLINE	11278995	UbiNet 2.0	SINGLE_OTHER	1	Training data	H.sapiens
2953	UBE3C_HUMAN	PK3C3_HUMAN	Q15386	Q8NEB9	UBE3C	PIK3C3	MEDLINE	33637724	Here, we show that ubiquitin ligase <span class="match term0">UBE3C</span> and deubiquitinating enzyme TRABID reciprocally regulate K29/K48-branched ubiquitination of <span class="match term1">VPS34</span>	SINGLE_OTHER	1	Other	H.sapiens
2954	UBE3C_HUMAN	CAND2_HUMAN	Q15386	O75155	UBE3C	CAND2	MEDLINE	12692129	Biochemical and co-transfection studies revealed that <span class="match term1">TIP120B</span>, but not the closely related protein TIP120A, is a specific substrate of KIAA10 in vitro and within C2C12 myoblasts but not in Cos-1 cells	SINGLE_OTHER	1	Training data	H.sapiens
2955	UBE4A_HUMAN	UBE4A_HUMAN	Q14139	Q14139	UBE4A	UBE4A	MEDLINE	11435423	hUbiquitome	UBOX	1	Other	H.sapiens
2956	UBE4B_HUMAN	UN45B_HUMAN	O95155	Q8IWX7	UBE4B	UNC45B	MEDLINE	15294159	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2957	UBE4B_HUMAN	PTTG1_HUMAN	O95155	O95997	UBE4B	PTTG1	MEDLINE	15611659	We further demonstrate that <span class="match term0">Ufd2</span> directly and efficiently ubiquitylates securin in vitro and is required for securin polyubiquitylation in vivo	UBOX	1	Training data	H.sapiens
2958	UBE4B_HUMAN	P53_HUMAN	O95155	P04637	UBE4B	TP53	MEDLINE	21317885	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2959	UBE4B_HUMAN	ATX3_HUMAN	O95155	P54252	UBE4B	ATXN3	MEDLINE	15152500	Furthermore, <span class="match term0">UFD2a</span>, a mammalian ubiquitin-chain assembly factor (E4), associated with VCP and induced polyubiquitylation of <span class="match term1">MJD1</span>	UBOX	1	Training data	H.sapiens
2960	UBE4B_HUMAN	FEZ1_HUMAN	O95155	Q99689	UBE4B	FEZ1	MEDLINE	15466860	E4B mediated the polyubiquitylation of <span class="match term1">FEZ1</span> but did not affect its intracellular stability, suggesting that such modification of <span class="match term1">FEZ1</span> is not a signal for its proteolysis	UBOX	1	Training data	H.sapiens
2961	UBL4A_HUMAN	TRAF6_HUMAN	P11441	Q9Y4K3	UBL4A	TRAF6	MEDLINE	31451677	Ubiquitination assays showed that <span class="match term0">UBL4A</span> promoted the K63-linked ubiquitination of <span class="match term1">TRAF6</span>	Other	1	Other	H.sapiens
2962	UBR1_HUMAN	OPSD_HUMAN	Q8IWV7	P08100	UBR1	RHO	MEDLINE	22199232	E3Net	UBOX	1	Other	H.sapiens
2963	UBR2_HUMAN	H2A1_HUMAN	Q8IWV8	P0C0S8	UBR2	H2AC11	MEDLINE	20080676	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2964	UBR2_HUMAN	H2A2C_HUMAN	Q8IWV8	Q16777	UBR2	H2AC20	MEDLINE	22616001	UbiNet 2.0	UBOX	1	Other	H.sapiens
2965	UBR4_HUMAN	TRPV5_HUMAN	Q5T4S7	Q9NQA5	UBR4	TRPV5	MEDLINE	23747339	UbiNet 2.0	UBOX	1	Training data	H.sapiens
2966	UBR4_HUMAN	PTN14_HUMAN	Q5T4S7	Q15678	UBR4	PTPN14	MEDLINE	32581101	HPV E7 binds the putative tumor suppressor <span class="match term1">PTPN14</span> and targets it for degradation using the ubiquitin ligase <span class="match term0">UBR4</span>	UBOX	1	Other	H.sapiens
2967	UBR5_HUMAN	MYC_HUMAN	O95071	P01106	UBR5	MYC	MEDLINE	32029551	<span class="match term0">UBR5</span> ubiquitinates <span class="match term1">MYC</span> and its effects on <span class="match term1">MYC</span> protein stability are independent of FBXW7.	HECT	1	Other	H.sapiens
2968	UBR5_HUMAN	AGR2_HUMAN	O95071	O95994	UBR5	AGR2	MEDLINE	30647455	We also provided evidence identifying the K48-linked polyubiquitin chains conjugating onto K89 of <span class="match term1">AGR2</span> by an E3 ligase <span class="match term0">UBR5</span>	HECT	1	Other	H.sapiens
2969	UBR5_HUMAN	SOX2_HUMAN	O95071	P48431	UBR5	SOX2	MEDLINE	30894683	We identified <span class="match term0">UBR5</span> as a major ubiquitin E3 ligase that induces <span class="match term1">SOX2</span> degradation through ubiquitinating <span class="match term1">SOX2</span> at lysine 115	HECT	1	Other	H.sapiens
2970	UBR5_HUMAN	ATMIN_HUMAN	O95071	O43313	UBR5	ATMIN	MEDLINE	34321465	<span class="match term0">UBR5</span> can ubiquitinate <span class="match term1">ATMIN</span>	HECT	1	Other	H.sapiens
2971	UBR5_HUMAN	CAZA1_HUMAN	O95071	P52907	UBR5	CAPZA1	MEDLINE	33777788	E3 Ubiquitin Ligase <span class="match term0">UBR5</span> Promotes the Metastasis of Pancreatic Cancer via Destabilizing F-Actin Capping Protein <span class="match term1">CAPZA1</span>	HECT	1	Other	H.sapiens
2972	UBR5_HUMAN	NR1I2_HUMAN	O95071	O75469	UBR5	NR1I2	MEDLINE	24438055	hPXR was shown to be a substrate for DYRK2, and DYRK2-dependent phosphorylation of hPXR facilitated its subsequent ubiquitination by <span class="match term0">UBR5</span>	HECT	1	Other	H.sapiens
2973	UBR5_HUMAN	PCKGC_HUMAN	O95071	P35558	UBR5	PCK1	MEDLINE	21726808	UbiNet 2.0	HECT	1	Training data	H.sapiens
2974	UBR5_HUMAN	PAIP2_HUMAN	O95071	Q9BPZ3	UBR5	PAIP2	MEDLINE	16601676	Supporting a critical role for <span class="match term0">EDD</span> in <span class="match term1">Paip2</span> degradation, knockdown of <span class="match term0">EDD</span> expression by siRNA leads to an increase in <span class="match term1">Paip2</span> protein stability	HECT	1	Training data	H.sapiens
2975	UBR5_HUMAN	CDK9_HUMAN	O95071	P50750	UBR5	CDK9	MEDLINE	21127351	UbiNet 2.0	HECT	1	Training data	H.sapiens
2976	UBR5_HUMAN	TOPB1_HUMAN	O95071	Q92547	UBR5	TOPBP1	MEDLINE	11714696	Using an in vitro reconstitution, specific E2 (ubiquitin-conjugating) enzymes (human UbcH4, UbcH5B, and UbcH5C) transferred ubiquitin molecules to hHYD, leading to the ubiquitination of <span class="match term1">TopBP1</span>	HECT	1	Training data	H.sapiens
2977	UBR5_HUMAN	CEBPA_HUMAN	O95071	P49715	UBR5	CEBPA	MEDLINE	33122826	E3 ubiquitin ligase <span class="match term0">UBR5</span> promotes pancreatic cancer growth and aerobic glycolysis by downregulating FBP1 via destabilization of <span class="match term1">C/EBPalpha</span>	HECT	1	Other	H.sapiens
2978	UBR5_HUMAN	PP2AA_HUMAN	O95071	P67775	UBR5	PPP2CA	MEDLINE	31392083	UbiNet 2.0	HECT	1	Other	H.sapiens
2979	UBR5_HUMAN	HD_HUMAN	O95071	P42858	UBR5	HTT	MEDLINE	30038412	Notably, <span class="match term0">UBR5</span> overexpression induces polyubiquitination and degradation of mutant <span class="match term1">HTT</span>, reducing polyQ-expanded aggregates in HD-cell models	HECT	1	Other	H.sapiens
2980	UBR5_HUMAN	UBR5_HUMAN	O95071	O95071	UBR5	UBR5	MEDLINE	11714696	hUbiquitome	HECT	1	Other	H.sapiens
2981	UBR7_HUMAN	KPRA_HUMAN	Q8N806	Q14558	UBR7	PRPSAP1	MEDLINE	33571115	<span class="match term1">PRPSAP1</span> polyubiquitination-mediated degradation by <span class="match term0">UBR7</span> and inhibition of PRPS activity are also depicted.	UBOX	1	Other	H.sapiens
2982	UCHL1_HUMAN	BIP_HUMAN	P09936	P11021	UCHL1	HSPA5	MEDLINE	32606430	We determined that <span class="match term0">UCHL1</span> interacted with glucose-regulated protein of 78 kDa (<span class="match term1">GRP78</span>) and prompted <span class="match term1">GRP78</span> degradation via ubiquitination	SINGLE_OTHER	1	Other	H.sapiens
2983	UCHL1_HUMAN	SRC8_HUMAN	P09936	Q14247	UCHL1	CTTN	MEDLINE	32120844	Importantly, we found that <span class="match term0">UCHL1</span> interacts with <span class="match term1">CTTN</span>, and may function as a ligase promoting <span class="match term1">CTTN</span> degradation by increasing K48-linked ubiquitination of <span class="match term1">CTTN</span>	SINGLE_OTHER	1	Other	H.sapiens
2984	UCHL1_HUMAN	SMN_HUMAN	P09936	Q16637	UCHL1	SMN1	MEDLINE	20713032	Ubiquitin carboxyl-terminal hydrolase L1 (<span class="match term0">UCHL1</span>) regulates the level of <span class="match term1">SMN</span> expression through ubiquitination in primary spinal muscular atrophy fibroblasts.	SINGLE_OTHER	1	Other	H.sapiens
2985	UHRF1_HUMAN	DNMT1_HUMAN	Q96T88	P26358	UHRF1	DNMT1	MEDLINE	21268065	UbiNet 2.0	RING	1	Training data	H.sapiens
2986	UHRF1_HUMAN	H2B2E_HUMAN	Q96T88	Q16778	UHRF1	H2BC21	MEDLINE	32884836	Here we present evidence that <span class="match term0">UHRF1</span> and USP7 oppositely control ubiquitination of histones H3 and <span class="match term1">H2B</span> in S phase of the cell cycle and that DNMT1 binds both ubiquitinated H3 and <span class="match term1">H2B</span>	RING	1	Other	H.sapiens
2987	UHRF1_HUMAN	H31_HUMAN	Q96T88	P68431	UHRF1	H3C1	MEDLINE	17967883	UbiNet 2.0	RING	1	Other	H.sapiens
2988	UHRF1_HUMAN	PML_HUMAN	Q96T88	P29590	UHRF1	PML	MEDLINE	22945642	UbiNet 2.0	RING	1	Training data	H.sapiens
2989	UHRF1_HUMAN	P53_HUMAN	Q96T88	P04637	UHRF1	TP53	MEDLINE	26102039	Ubiquitin E3 ligase <span class="match term0">UHRF1</span> regulates <span class="match term1">p53</span> ubiquitination and <span class="match term1">p53</span>-dependent cell apoptosis in clear cell Renal Cell Carcinoma	RING	1	Other	H.sapiens
2990	UHRF2_HUMAN	CCND1_HUMAN	Q96PU4	P24385	UHRF2	CCND1	MEDLINE	21952639	UbiNet 2.0	RING	1	Training data	H.sapiens
2991	UHRF2_HUMAN	PCNP_HUMAN	Q96PU4	Q8WW12	UHRF2	PCNP	MEDLINE	14741369	<span class="match term0">NIRF</span> is a ubiquitin ligase that is capable of ubiquitinating <span class="match term1">PCNP</span>, a PEST-containing nuclear protein	RING	1	Training data	H.sapiens
2992	UHRF2_HUMAN	CDN1A_HUMAN	Q96PU4	P38936	UHRF2	CDKN1A	MEDLINE	29923055	In addition, <span class="match term0">UHRF2</span> degraded <span class="match term1">p21</span> through ubiquitination and shortened the half-life of <span class="match term1">p21</span>	RING	1	Other	H.sapiens
2993	UHRF2_HUMAN	CCNE1_HUMAN	Q96PU4	P24864	UHRF2	CCNE1	MEDLINE	21952639	UbiNet 2.0	RING	1	Training data	H.sapiens
2994	UHRF2_HUMAN	H32_HUMAN	Q96PU4	Q71DI3	UHRF2	H3C14	MEDLINE	29506131	While UHRF1 and UHRF2 diverge in their affinities toward hemi-methylated DNA, we surprisingly show that both hemi-methylated and hemi-hydroxymethylated DNA oligonucleotides stimulate <span class="match term0">UHRF2</span> ubiquitin ligase activity toward histone <span class="match term1">H3</span> peptide substrates	Other	1	Other	H.sapiens
2995	VHL_HUMAN	HIF1A_HUMAN	P40337	Q16665	VHL	HIF1A	MEDLINE	20078552	Cullin 2 (CUL2) interacts with the trimeric <span class="match term0">VHL</span>-elongin B-elongin C complex and plays an essential role in the ubiquitinated degradation of <span class="match term1">HIF1alpha</span>	SOCS_VHL_BC-box	1	Training data	H.sapiens
2996	VHL_HUMAN	DVL2_HUMAN	P40337	O14641	VHL	DVL2	MEDLINE	20639871	UbiNet 2.0	SOCS_VHL_BC-box	1	Other	H.sapiens
2997	VHL_HUMAN	HIF3A_HUMAN	P40337	Q9Y2N7	VHL	HIF3A	MEDLINE	19243301	Subcellular dynamics of the <span class="match term0">VHL</span> tumor suppressor: on the move for HIF degradation	SOCS_VHL_BC-box	1	Training data	H.sapiens
2998	VHL_HUMAN	HNRPD_HUMAN	P40337	Q14103	VHL	HNRNPD	MEDLINE	22086907	UbiNet 2.0	SOCS_VHL_BC-box	1	Training data	H.sapiens
2999	VHL_HUMAN	EPAS1_HUMAN	P40337	Q99814	VHL	EPAS1	MEDLINE	15574766	We first examined the ability of mutant <span class="match term0">pVHL</span> to direct degradation of the hypoxia inducible factor (HIF) subunits HIF1alpha and <span class="match term1">HIF2alpha</span>	SOCS_VHL_BC-box	1	Training data	H.sapiens
3000	VHL_HUMAN	UBP33_HUMAN	P40337	Q8TEY7	VHL	USP33	MEDLINE	12056827	In our previous studies, we have shown that <span class="match term1">VDU1</span> (<span class="match term0">pVHL</span>-interacting deubiquitinating enzyme-1) can be ubiquitinated for rapid degradation in a <span class="match term0">pVHL</span>-dependent manner	SOCS_VHL_BC-box	1	Training data	H.sapiens
3001	VHL_HUMAN	CLUS_HUMAN	P40337	P10909	VHL	CLU	MEDLINE	22532874	<span class="match term0">pVHL</span> mediates K63-linked ubiquitination of nCLU.	SOCS_VHL_BC-box	1	Other	H.sapiens
3002	VHL_HUMAN	FINC_HUMAN	P40337	P02751	VHL	FN1	MEDLINE	15262424	They also suggest that some C-terminal mutations may not interfere with <span class="match term1">Fn</span> assembly and that a 3p TSG in addition to <span class="match term0">VHL</span> influences HIF-1alpha degradation	SOCS_VHL_BC-box	1	Training data	H.sapiens
3003	VHL_HUMAN	PPARG_HUMAN	P40337	P37231	VHL	PPARG	MEDLINE	32589900	Ubiquitination of <span class="match term1">PPAR-gamma</span> by <span class="match term0">pVHL</span> inhibits ACLY expression and lipid metabolism, is implicated in tumor progression	SOCS_VHL_BC-box	1	Other	H.sapiens
3004	VHL_HUMAN	UBP20_HUMAN	P40337	Q9Y2K6	VHL	USP20	MEDLINE	15776016	Although <span class="match term0">pVHL</span> functions as a master control for HIF-1alpha stabilization, as <span class="match term0">pVHL</span>-E3 ligase mediates the ubiquitination of both HIF-1alpha and <span class="match term1">VDU2</span>, the balance between the <span class="match term0">pVHL</span>-mediated ubiquitination and <span class="match term1">VDU2</span>-mediated deubiquitination of HIF-1alpha provides another level of control for HIF-1alpha stabilization	SOCS_VHL_BC-box	1	Training data	H.sapiens
3005	VHL_HUMAN	IREB2_HUMAN	P40337	P48200	VHL	IREB2	MEDLINE	15777842	The pathway for <span class="match term1">IRP2</span> degradation involving 2-oxoglutarate-dependent oxygenase(s) does not require the E3 ubiquitin ligase activity of <span class="match term0">pVHL</span>	SOCS_VHL_BC-box	1	Training data	H.sapiens
3006	VHL_HUMAN	BHE40_HUMAN	P40337	O14503	VHL	BHLHE40	MEDLINE	11278694	In this study, we focus on different modes of regulation of <span class="match term1">STRA13</span>, a human ortholog of the mouse basic helix-loop-helix transcriptional factor, previously identified by us as a new von Hippel-Lindau tumor suppressor gene (<span class="match term0">VHL</span>) target.	SOCS_VHL_BC-box	1	Training data	H.sapiens
3007	VHL_HUMAN	RPB7_HUMAN	P40337	P62487	VHL	POLR2G	MEDLINE	12912922	Introducing wild-type <span class="match term0">pVHL</span> into human kidney tumor cell lines carrying endogenous mutant non-functional <span class="match term0">pVHL</span> facilitates ubiquitylation and proteasomal degradation of <span class="match term1">hsRPB7</span>, and decreases its nuclear accumulation	SOCS_VHL_BC-box	1	Training data	H.sapiens
3008	VHL_HUMAN	ADRB2_HUMAN	P40337	P07550	VHL	ADRB2	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	H.sapiens
3009	VHL_HUMAN	RPTOR_HUMAN	P40337	Q8N122	VHL	RPTOR	MEDLINE	34290272	<span class="match term0">VHL</span> interacts with <span class="match term1">RAPTOR</span> and increases <span class="match term1">RAPTOR</span> degradation by ubiquitination, thereby inhibiting mTORC1 signaling	SOCS_VHL_BC-box	1	Other	H.sapiens
3010	VHL_HUMAN	AURKA_HUMAN	P40337	O14965	VHL	AURKA	MEDLINE	34002003	<span class="match term0">VHL</span> in its role as an E3 ubiquitin ligase targets <span class="match term1">AURKA</span> for degradation and in the absence of <span class="match term0">VHL</span>, high levels of <span class="match term1">AURKA</span> result in destabilization of the primary cilium	SOCS_VHL_BC-box	1	Other	H.sapiens
3011	VHL_HUMAN	MLP3B_HUMAN	P40337	Q9GZQ8	VHL	MAP1LC3B	MEDLINE	30902965	In conclusion, our results showed that <span class="match term0">pVHL</span> interacts with MAPL1LC3B and inhibits LC3B-mediated autophagy via <span class="match term1">MAP1LC3B</span> ubiquitination	SOCS_VHL_BC-box	1	Other	H.sapiens
3012	VHL_HUMAN	HIF1N_HUMAN	P40337	Q9NWT6	VHL	HIF1AN	MEDLINE	17132228	UbiNet 2.0	SOCS_VHL_BC-box	1	Training data	H.sapiens
3013	VHL_HUMAN	KPCI_HUMAN	P40337	P41743	VHL	PRKCI	MEDLINE	11574546	An active PKClambda mutant is ubiquitinated more extensively than wild-type PKClambda in HEK293 cells, and the ubiquitination is further enhanced by the overexpression of <span class="match term0">pVHL</span>	SOCS_VHL_BC-box	1	Training data	H.sapiens
3014	VHL_HUMAN	TGFR1_HUMAN	P40337	P36897	VHL	TGFBR1	MEDLINE	29662646	In-vitro studies revealed that <span class="match term0">pVHL</span> interacted with <span class="match term1">ALK5</span> to downregulate its expression through K48-linked poly-ubiquitination and proteasomal degradation, thus negatively controlling TGF-beta induced cancer cell invasiveness	SOCS_VHL_BC-box	1	Other	H.sapiens
3015	VHL_HUMAN	SKP2_HUMAN	P40337	Q13309	VHL	SKP2	MEDLINE	21358672	UbiNet 2.0	SOCS_VHL_BC-box	1	Training data	H.sapiens
3016	DCAF1_HUMAN	CDN1B_HUMAN	Q9Y4B6	Q8IXI2	VPRBP	PPP2R1A	MEDLINE	25720411	25720411	DWD	1	Other	H.sapiens
3017	VPRBP_HUMAN	MERL_HUMAN	Q9Y4B6	P35240	VPRBP	NF2	UniProt	VPRBP_HUMAN	Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/<span class="match term0">VprBP</span> E3 ubiquitin-protein ligase complex for ubiquitination and subsequent proteasome-dependent degradation	DWD	1	Training data	H.sapiens
3018	VPS18_HUMAN	PLK2_HUMAN	Q9P253	Q9NYY3	VPS18	PLK2	MEDLINE	16203730	Ubiquitylation and degradation of serum-inducible kinase by hVPS18, a RING-H2 type ubiquitin ligase	RING	1	Training data	H.sapiens
3019	VPS18_HUMAN	GGA3_HUMAN	Q9P253	Q9NZ52	VPS18	GGA3	MEDLINE	16996030	Here, we show that <span class="match term1">GGA3</span> is monoubiquitylated by a RING-H2 type-ubiquitin ligase hVPS18 (human homologue of vacuolar protein sorting 18)	RING	1	Training data	H.sapiens
3020	WDHD1_HUMAN	MARE2_HUMAN	O75717	Q15555	WDHD1	MAPRE2	MEDLINE	32426268	Thus, the ubiquitin ligase <span class="match term0">WDHD1</span> induces cisplatin resistance in LUAD by promoting <span class="match term1">MAPRE2</span> ubiquitination.	DWD	1	Other	H.sapiens
3021	WSB1_HUMAN	HIPK2_HUMAN	Q9Y6I7	Q9H2X6	WSB1	HIPK2	MEDLINE	18093972	Domain analysis of <span class="match term0">WSB-1</span> showed that WD40-repeats and the SOCS box were required for its interaction with and degradation of <span class="match term1">HIPK2</span>, respectively	DWD	1	Training data	H.sapiens
3022	WSB1_HUMAN	IOD2_HUMAN	Q9Y6I7	Q92813	WSB1	DIO2	UniProt	WSB1_HUMAN	<span class="match term0">WSB1</span>_HUMAN	DWD	1	Training data	H.sapiens
3023	WWP1_HUMAN	RUNX2_HUMAN	Q9H0M0	Q13950	WWP1	RUNX2	MEDLINE	18083927	In the absence of Shn3, <span class="match term1">Runx2</span> degradation by <span class="match term0">WWP1</span> is inhibited resulting in increased levels of <span class="match term1">Runx2</span> protein and enhanced expression of <span class="match term1">Runx2</span> target genes leading to increased osteoblast synthetic activity	HECT	1	Training data	H.sapiens
3024	WWP1_HUMAN	SMAD2_HUMAN	Q9H0M0	Q15796	WWP1	SMAD2	MEDLINE	15359284	UbiNet 2.0	HECT	1	Training data	H.sapiens
3025	WWP1_HUMAN	GAG_HTL1A	Q9H0M0	P03345	WWP1	gag	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
3026	WWP1_HUMAN	GAG_HTL1C	Q9H0M0	P14076	WWP1	gag	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
3027	WWP1_HUMAN	GAG_HTL1L	Q9H0M0	P0C209	WWP1	gag	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
3028	WWP1_HUMAN	SMAD6_HUMAN	Q9H0M0	O43541	WWP1	SMAD6	UniProt	WWP1_HUMAN	Ubiquitinated by <span class="match term0">WWP1</span> (By similarity)	HECT	1	Training data	H.sapiens
3029	WWP1_HUMAN	P53_HUMAN	Q9H0M0	P04637	WWP1	TP53	MEDLINE	16924229	Here, we demonstrate the role of HECT domain E3 ligase, <span class="match term0">WWP1</span>, in regulating <span class="match term1">p53</span> localization and activity	HECT	1	Training data	H.sapiens
3030	WWP1_HUMAN	KLF2_HUMAN	Q9H0M0	Q9Y5W3	WWP1	KLF2	MEDLINE	15003522	UbiNet 2.0	HECT	1	Training data	H.sapiens
3031	WWP1_HUMAN	MUC1_HUMAN	Q9H0M0	P15941	WWP1	MUC1	MEDLINE	34404764	<span class="match term0">WWP1</span> targeting <span class="match term1">MUC1</span> for ubiquitin-mediated lysosomal degradation to suppress carcinogenesis.	HECT	1	Other	H.sapiens
3032	WWP1_HUMAN	CXCR4_HUMAN	Q9H0M0	P61073	WWP1	CXCR4	MEDLINE	22266093	UbiNet 2.0	HECT	1	Training data	H.sapiens
3033	WWP1_HUMAN	SMAD4_HUMAN	Q9H0M0	Q13485	WWP1	SMAD4	MEDLINE	15817471	UbiNet 2.0	HECT	1	Other	H.sapiens
3034	WWP1_HUMAN	AMOL2_HUMAN	Q9H0M0	Q9Y2J4	WWP1	AMOTL2	MEDLINE	34404733	Here, we provide evidence that the E3 ligase <span class="match term0">WWP1</span> (WW-domain containing protein 1) mono-ubiquitinates <span class="match term1">AMOTL2</span> (angiomotin-like 2) at K347 and K408	HECT	1	Other	H.sapiens
3035	WWP1_HUMAN	EI24_HUMAN	Q9H0M0	O14681	WWP1	EI24	MEDLINE	32252198	Results: <span class="match term0">WWP1</span> can interact with <span class="match term1">EI24</span> and ubiquitin-degrade <span class="match term1">EI24</span> protein	HECT	1	Other	H.sapiens
3036	WWP1_HUMAN	CDN1B_HUMAN	Q9H0M0	P46527	WWP1	CDKN1B	MEDLINE	21795702	Additionally, <span class="match term0">WWP1</span> had a strong preference for catalyzing the Lys-48-linked polyubiquitination of p27(<span class="match term1">Kip1</span>) in vitro	HECT	1	Other	H.sapiens
3037	WWP1_HUMAN	GAG_HTL1M	Q9H0M0	P14077	WWP1	gag	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
3038	WWP1_HUMAN	SPART_HUMAN	Q9H0M0	Q8N0X7	WWP1	SPART	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
3039	WWP1_HUMAN	ERBB4_HUMAN	Q9H0M0	Q15303	WWP1	ERBB4	MEDLINE	19047365	Deletion of the C2 membrane association domain of <span class="match term0">WWP1</span> allowed more efficient s80(<span class="match term1">HER4</span>) degradation, suggesting that <span class="match term0">WWP1</span> is normally part of a membrane complex that regulates <span class="match term1">HER4</span> membrane species levels, with a predilection for the growth-inhibitory Cyt1 isoform	HECT	1	Training data	H.sapiens
3040	WWP1_HUMAN	LATS1_HUMAN	Q9H0M0	O95835	WWP1	LATS1	MEDLINE	23573293	UbiNet 2.0	HECT	1	Training data	H.sapiens
3041	WWP1_HUMAN	P63_HUMAN	Q9H0M0	Q9H3D4	WWP1	TP63	MEDLINE	18806757	These data suggest that <span class="match term0">WWP1</span> may have a context-dependent role in regulating cell survival through targeting different <span class="match term1">p63</span> proteins for degradation	HECT	1	Training data	H.sapiens
3042	WWP1_HUMAN	DVL2_HUMAN	Q9H0M0	O14641	WWP1	DVL2	MEDLINE	31340145	Here, we report that USP9X, a deubiquitylase, and <span class="match term0">WWP1</span>, an E3 ubiquitin ligase, regulate a ubiquitin rheostat on <span class="match term1">DVL2</span>, a WNT signaling protein	HECT	1	Other	H.sapiens
3043	WWP1_HUMAN	TGFR1_HUMAN	Q9H0M0	P36897	WWP1	TGFBR1	MEDLINE	15817471	Alternatively, I-Smads elicit degradation of the TGF-beta receptor by recruiting the WW and HECT domain E3 ligases, Smurfs, <span class="match term0">WWP1</span>, or NEDD4-2	HECT	1	Training data	H.sapiens
3044	WWP1_HUMAN	EPS15_HUMAN	Q9H0M0	P42566	WWP1	EPS15	MEDLINE	22051607	UbiNet 2.0	HECT	1	Other	H.sapiens
3045	WWP1_HUMAN	WWP1_HUMAN	Q9H0M0	Q9H0M0	WWP1	WWP1	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
3046	WWP1_HUMAN	TRAF6_HUMAN	Q9H0M0	Q9Y4K3	WWP1	TRAF6	MEDLINE	23799152	UbiNet 2.0	HECT	1	Training data	H.sapiens
3047	WWP1_HUMAN	PTEN_HUMAN	Q9H0M0	P60484	WWP1	PTEN	MEDLINE	31097636	Polyubiquitination by the ubiquitin E3 ligase <span class="match term0">WWP1</span> (WW domain-containing ubiquitin E3 ligase 1) suppressed the dimerization, membrane recruitment, and function of <span class="match term1">PTEN</span>	HECT	1	Other	H.sapiens
3048	WWP1_HUMAN	KLF5_HUMAN	Q9H0M0	Q13887	WWP1	KLF5	MEDLINE	16223724	Furthermore, <span class="match term0">WWP1</span> mediated the ubiquitination and degradation of <span class="match term1">KLF5</span>, and the catalytic cysteine residue of <span class="match term0">WWP1</span> is essential for its function	HECT	1	Training data	H.sapiens
3049	WWP1_HUMAN	SMAD7_HUMAN	Q9H0M0	O15105	WWP1	SMAD7	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
3050	WWP1_HUMAN	RNF11_HUMAN	Q9H0M0	Q9Y3C5	WWP1	RNF11	MEDLINE	18724389	Although <span class="match term0">WWP1</span> is able to ubiquitinate <span class="match term1">RNF11</span> in vitro and in vivo, <span class="match term0">WWP1</span> neither targets <span class="match term1">RNF11</span> for degradation nor changes <span class="match term1">RNF11</span>'s cellular localization	HECT	1	Training data	H.sapiens
3051	WWP1_HUMAN	TGFR2_HUMAN	Q9H0M0	P37173	WWP1	TGFBR2	MEDLINE	15817471	UbiNet 2.0	HECT	1	Training data	H.sapiens
3052	WWP1_HUMAN	EGFR_HUAMN	Q9H0M0	P00533	WWP1	EGFR	MEDLINE	32694521	TRIB3 interacts with EGFR and recruits PKCalpha to induce a Thr654 phosphorylation and <span class="match term0">WWP1</span>-induced Lys689 ubiquitination in the  <span class="match term1">EGFR</span> juxtamembrane region, which enhances EGFR recycling, stability, downstream activity, and NSCLC stemness.	HECT	1	Other	H.sapiens
3053	WWP1_HUMAN#WWP2_HUMAN	P73_HUMAN	Q9H0M0#O00308	O15350	WWP1#WWP2	TP73	MEDLINE	25071155	WWP2-WWP1 ubiquitin ligase complex coordinated by PPM1G maintains the balance between cellular <span class="match term1">p73</span> and DeltaNp73 levels	HECT	1	Other	H.sapiens
3054	WWP2_HUMAN	SMAD7_HUMAN	O00308	O15105	WWP2	SMAD7	MEDLINE	21258410	UbiNet 2.0	HECT	1	Other	H.sapiens
3055	WWP2_HUMAN	DMRT1_HUMAN	O00308	Q9Y5R6	WWP2	DMT1	MEDLINE	18776082	18776082	HECT	1	Other	H.sapiens
3056	WWP2_HUMAN	NRAM2_HUMAN	O00308	P49281	WWP2	SLC11A2	MEDLINE	18776082	This promotes <span class="match term1">DMT1</span> ubiquitination and degradation by <span class="match term0">WWP2</span>	HECT	1	Training data	H.sapiens
3057	WWP2_HUMAN	EGR2_HUMAN	O00308	P11161	WWP2	EGR2	MEDLINE	19651900	<span class="match term0">AIP2</span> interacts with and promotes ubiquitin-mediated degradation of <span class="match term1">EGR2</span>, a zinc finger transcription factor that has been found to regulate Fas ligand (FasL) expression during activation-induced T-cell death	HECT	1	Training data	H.sapiens
3058	WWP2_HUMAN	RPB1_HUMAN	O00308	P24928	WWP2	POLR2A	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
3059	WWP2_HUMAN	PO5F1_HUMAN	O00308	Q01860	WWP2	POU5F1	MEDLINE	15047715	Moreover, <span class="match term0">Wwp2</span> promotes <span class="match term1">Oct-4</span> degradation in the presence of overexpressed ubiquitin	HECT	1	Training data	H.sapiens
3060	WWP2_HUMAN	P73_HUMAN	O00308	O15350	WWP2	TP73	MEDLINE	25071155	<span class="match term0">WWP2</span>-WWP1 ubiquitin ligase complex coordinated by PPM1G maintains the balance between cellular <span class="match term1">p73</span> and DeltaNp73 levels	HECT	1	Other	H.sapiens
3061	WWP2_HUMAN	PAIP1_HUMAN	O00308	Q9H074	WWP2	PAIP1	MEDLINE	25266661	Here, we show that the E6AP carboxyl terminus (HECT)-type ubiquitin ligase WW domain-containing protein 2 (<span class="match term0">WWP2</span>), a homolog of the HECT-type ubiquitin ligase WWP1, interacts with and targets <span class="match term1">Paip1</span> for ubiquitination and proteasomal degradation	HECT	1	Other	H.sapiens
3062	WWP2_HUMAN	ABI3_HUMAN	O00308	Q9P2A4	WWP2	ABI3	MEDLINE	15998807	UbiNet 2.0	HECT	1	Training data	H.sapiens
3063	WWP2_HUMAN	PTEN_HUMAN	O00308	P60484	WWP2	PTEN	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
3064	WWP2_HUMAN	RUNX2_HUMAN	O00308	Q13950	WWP2	RUNX2	MEDLINE	28500134	Co-immunoprecipitation experiments showed the interaction of <span class="match term0">WWP2</span> with <span class="match term1">RUNX2</span> in vitro and in vivo Mono-ubiquitination by <span class="match term0">WWP2</span> leads to <span class="match term1">RUNX2</span> transactivation, as evidenced by the wild type of <span class="match term0">WWP2</span>, but not its ubiquitin ligase-dead mutant, augmenting <span class="match term1">RUNX2</span>-reponsive reporter activity	HECT	1	Other	H.sapiens
3065	WWP2_HUMAN	TCAM1_HUMAN	O00308	Q8IUC6	WWP2	TICAM1	MEDLINE	23479606	E3 ligase <span class="match term0">WWP2</span> negatively regulates TLR3-mediated innate immune response by targeting <span class="match term1">TRIF</span> for ubiquitination and degradation.	HECT	1	Other	H.sapiens
3066	WWP2_HUMAN	NOTC3_HUMAN	O00308	Q9UM47	WWP2	NOTCH3	MEDLINE	25356737	Wild-type <span class="match term0">WWP2</span> but not ligase-deficient mutant <span class="match term0">WWP2</span> increases mono-ubiquitination of the membrane-tethered <span class="match term1">Notch3</span> fragment, therefore attenuating <span class="match term1">Notch3</span> pathway activity in cancer cells and leading to cell cycle arrest	HECT	1	Other	H.sapiens
3067	WWP2_HUMAN	SMAD3_HUMAN	O00308	P84022	WWP2	SMAD3	MEDLINE	21258410	Unexpectedly, we also find that <span class="match term0">WWP2</span>-N, which lacks the HECT ubiquitin ligase domain, can also interact with <span class="match term0">WWP2</span>-FL in a TGFbeta-regulated manner and activate endogenous <span class="match term0">WWP2</span> ubiquitin ligase activity causing degradation of unstimulated Smad2 and <span class="match term1">Smad3</span>	HECT	1	Other	H.sapiens
3068	WWP2_HUMAN	WWP2_HUMAN	O00308	O00308	WWP2	WWP2	MEDLINE	22199232	E3Net	HECT	1	Other	H.sapiens
3069	XIAP_HUMAN	DBLOH_HUMAN	P98170	Q9NR28	XIAP	DIABLO	MEDLINE	15749826	Here we show that X-linked IAP (<span class="match term0">XIAP</span>) mediates the polyubiquitination of caspase-9 and <span class="match term1">Smac</span>	RING	1	Training data	H.sapiens
3070	XIAP_HUMAN	M3K3_HUMAN	P98170	Q99759	XIAP	MAP3K3	MEDLINE	24975362	UbiNet 2.0	RING	1	Other	H.sapiens
3071	XIAP_HUMAN	COMD1_HUMAN	P98170	Q8N668	XIAP	COMMD1	UniProt	XIAP_HUMAN	Ubiquitinated by <span class="match term0">XIAP</span>, leading to its proteasomal degradation	RING	1	Training data	H.sapiens
3072	XIAP_HUMAN	RIPK2_HUMAN	P98170	O43353	XIAP	RIPK2	MEDLINE	23818254	UbiNet 2.0	RING	1	Training data	H.sapiens
3073	XIAP_HUMAN	CASP7_HUMAN	P98170	P55210	XIAP	CASP7	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
3074	XIAP_HUMAN	M3K7_HUMAN	P98170	O43318	XIAP	MAP3K7	UniProt	XIAP_HUMAN	<span class="match term0">XIAP</span>_HUMAN	RING	1	Training data	H.sapiens
3075	XIAP_HUMAN	AIFM1_HUMAN	P98170	O95831	XIAP	AIFM1	MEDLINE	22103349	These <span class="match term0">XIAP</span> binds and ubiquitinates <span class="match term1">AIF</span>, and in this study, we determined the functional consequences of <span class="match term0">XIAP</span>-mediated <span class="match term1">AIF</span> ubiquitination	RING	1	Other	H.sapiens
3076	XIAP_HUMAN	XIAP_HUMAN	P98170	P98170	XIAP	XIAP	MEDLINE	14960576	Here we show that Smac/DIABLO, a mammalian functional homolog of Reaper/Hid/Grim, selectively causes the rapid degradation of c-IAP1 and c-IAP2 but not <span class="match term0">XIAP</span> and Livin in HeLa cells, although it efficiently promotes the auto-ubiquitination of them all	RING	1	Training data	H.sapiens
3077	XIAP_HUMAN	NUP62_HUMAN	P98170	P37198	XIAP	NUP62	MEDLINE	30275562	<span class="match term0">XIAP</span> facilitates breast and colon carcinoma growth via promotion of <span class="match term1">p62</span> depletion through ubiquitination-dependent proteasomal degradation	RING	1	Other	H.sapiens
3078	XIAP_HUMAN	TLE5_HUMAN	P98170	Q08117	XIAP	TLE5	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
3079	XIAP_HUMAN	AIF1_HUMAN	P98170	P55008	XIAP	AIF1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
3080	XIAP_HUMAN	XAF1_HUMAN	P98170	Q6GPH4	XIAP	XAF1	MEDLINE	22811387	By applying in vitro ubiquitination assay, we observed that <span class="match term1">XAF1</span>(RBD) /<span class="match term0">XIAP</span> interaction is essential for the ubiquitination of GST-<span class="match term1">XAF1</span>(RBD) fusion protein	RING	1	Other	H.sapiens
3081	XIAP_HUMAN	PGAM5_HUMAN	P98170	Q96HS1	XIAP	PGAM5	MEDLINE	23201124	UbiNet 2.0	RING	1	Other	H.sapiens
3082	XIAP_HUMAN	CASP3_HUMAN	P98170	P42574	XIAP	CASP3	MEDLINE	11447297	A proteasome inhibitor suppressed the degradation of caspase-3 by <span class="match term0">XIAP</span>, suggesting the involvement of a ubiquitin-proteasome pathway in the degradation	RING	1	Training data	H.sapiens
3083	XIAP_HUMAN	TLE3_HUMAN	P98170	Q04726	XIAP	TLE3	MEDLINE	22304967	<span class="match term0">XIAP</span> monoubiquitylates Groucho/TLE to promote canonical Wnt signaling.	RING	1	Other	H.sapiens
3084	XIAP_HUMAN	M3K2_HUMAN	P98170	Q9Y2U5	XIAP	MAP3K2	MEDLINE	18761086	We conclude that, through interaction with <span class="match term1">MEKK2</span>, <span class="match term0">XIAP</span> functions in an ubiquitin ligase dependent manner to evoke a second wave of NF-kappaB activation, resulting in the modulation of NF-kappaB target gene expression	RING	1	Training data	H.sapiens
3085	XIAP_HUMAN	CASP9_HUMAN	P98170	P55211	XIAP	CASP9	MEDLINE	15749826	Here we show that X-linked IAP (<span class="match term0">XIAP</span>) mediates the polyubiquitination of caspase-9 and Smac	RING	1	Training data	H.sapiens
3086	XIAP_HUMAN	PTEN_HUMAN	P98170	P60484	XIAP	PTEN	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
3087	XIAP_HUMAN	RIPK4_HUMAN	P98170	P57078	XIAP	RIPK4	MEDLINE	21931591	cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).	RING	1	Other	H.sapiens
3088	XIAP_HUMAN	TLE1_HUMAN	P98170	Q04724	XIAP	TLE1	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
3089	XIAP_HUMAN	RAF1_HUMAN	P98170	P04049	XIAP	RAF1	MEDLINE	19011619	<span class="match term0">XIAP</span> binds strongly to <span class="match term1">C-RAF</span> and promotes the ubiquitylation of <span class="match term1">C-RAF</span> in vivo through the Hsp90-mediated quality control system, independently of its E3 ligase activity	RING	1	Training data	H.sapiens
3090	XIAP_HUMAN	CCS_HUMAN	P98170	O14618	XIAP	CCS	MEDLINE	19948006	UbiNet 2.0	RING	1	Training data	H.sapiens
3091	XIAP_HUMAN	BIRC5_HUMAN	P98170	O15392	XIAP	BIRC5	MEDLINE	17613533	UbiNet 2.0	RING	1	Training data	H.sapiens
3092	XIAP_HUMAN	TLE2_HUMAN	P98170	Q04725	XIAP	TLE2	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
3093	XIAP_HUMAN	CASP8_HUMAN	P98170	Q14790	XIAP	CASP8	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
3094	XIAP_HUMAN	SEPT4_HUMAN	P98170	O43236	XIAP	SEPTIN4	MEDLINE	22185822	UbiNet 2.0	RING	1	Training data	H.sapiens
3095	XIAP_HUMAN	TLE4_HUMAN	P98170	Q04727	XIAP	TLE4	MEDLINE	22199232	E3Net	RING	1	Other	H.sapiens
3096	XIAP_HUMAN	HSP71_HUMAN	P98170	P08107	XIAP	HSPA1A	MEDLINE	15756021	hUbiquitome	RING	1	Other	H.sapiens
3097	NIPA_HUMAN	CCNB1_HUMAN	Q86WB0	P14635	ZC3HC1	CCNB1	UniProt	NIPA_HUMAN	Probable component of an SCF-type E3 ligase complex, SCF(<span class="match term0">NIPA</span>), a complex that controls mitotic entry by mediating ubiquitination and subsequent degradation of cyclin B1 (<span class="match term1">CCNB1</span>) (By similarity)	F-box	1	Training data	H.sapiens
3098	ZFP91_HUMAN	M3K14_HUMAN	Q96JP5	Q99558	ZFP91	MAP3K14	MEDLINE	20682767	We show that <span class="match term0">ZFP91</span> interacts with and promotes the Lys(63)-linked ubiquitination of <span class="match term1">NIK</span> and subsequent processing of p100 to p52	HECT	1	Training data	H.sapiens
3099	ZFP91_HUMAN	BECN1_HUMAN	Q96JP5	Q14457	ZFP91	BECN1	MEDLINE	33355624	Mechanistically, <span class="match term0">ZFP91</span> rapidly translocated from the nucleus to the cytoplasm in response to TCR stimulation and then mediated <span class="match term1">BECN1</span> ubiquitination to promote <span class="match term1">BECN1</span>-PIK3C3 complex formation	HECT	1	Other	H.sapiens
3100	ZFP91_HUMAN	HNRPF_HUMAN	Q96JP5	P52597	ZFP91	HNRNPF	MEDLINE	29706618	We identified <span class="match term0">ZFP91</span> as the E3 ubiquitin ligase that is responsible for hnRNP F ubiquitination at Lys 185 and proteasomal degradation	HECT	1	Other	H.sapiens
3101	ZNRF1_HUMAN	AKT1_HUMAN	Q8ND25	P31749	ZNRF1	AKT1	MEDLINE	14561866	UbiNet 2.0	RING	1	Training data	H.sapiens
3102	ZNRF1_HUMAN	GLNA_HUMAN	Q8ND25	P15104	ZNRF1	GLUL	MEDLINE	14561866	UbiNet 2.0	RING	1	Training data	H.sapiens
3103	ZNRF1_HUMAN	CAV1_HUMAN	Q8ND25	Q03135	ZNRF1	CAV1	MEDLINE	28593998	The ubiquitin ligase <span class="match term0">ZNRF1</span> promotes caveolin-1 ubiquitination and degradation to modulate inflammation.	RING	1	Other	H.sapiens
3104	ZNRF1_HUMAN	EGFR_HUMAN	Q8ND25	P00533	ZNRF1	EGFR	MEDLINE	33996800	We further demonstrate that <span class="match term0">ZNRF1</span> and Casitas B-lineage lymphoma (CBL), another E3 ubiquitin ligase responsible for <span class="match term1">EGFR</span> ubiquitination, mediate ubiquitination at distinct lysine residues on <span class="match term1">EGFR</span>	RING	1	Other	H.sapiens
3105	ZNRF1_HUMAN	ZNRF1_HUMAN	Q8ND25	Q8ND25	ZNRF1	ZNRF1	MEDLINE	14561866	hUbiquitome	RING	1	Other	H.sapiens
3106	ZNRF2_HUMAN	ZNRF2_HUMAN	Q8NHG8	Q8NHG8	ZNRF2	ZNRF2	MEDLINE	14561866	hUbiquitome	RING	1	Other	H.sapiens
3107	ZSWM2_HUMAN	ZSWM2_HUMAN	Q8NEG5	Q8NEG5	ZSWIM2	ZSWIM2	MEDLINE	16522193	UbiNet 2.0	RING	1	Training data	H.sapiens
3108	NEDD4_HUMAN	RAP2A_HUMAN	P46934	P10114	NEDD4	RAP2A	MEDLINE	28405688	Moreover, <span class="match term0">Nedd4-1</span> selectively ubiquitinated its specific substrates, the wild-type Rap2a (WT-<span class="match term1">Rap2a</span>) and dominant-active Rap2a (DA-<span class="match term1">Rap2a</span>) rather than the dominant-negative Rap2a (DN-Rap2a) in the U251 cells	HECT	1	Other	H.sapiens
3109	MARH8_HUMAN	PD1L1_HUMAN	Q5T0T0	Q9NZQ7	MARCHF8	CD274	MEDLINE	34183449	Membrane-associated <span class="match term0">RING-CH 8</span> functions as a novel <span class="match term1">PD-L1</span> E3 ligase to mediate <span class="match term1">PD-L1</span> degradation induced by EGFR inhibitors	RING	1	Other	H.sapiens
3110	TRAF2_HUMAN	DYR1A_HUMAN	Q12933	Q13627	TRAF2	DYRK1A	MEDLINE	34117217	K63-linked ubiquitination of <span class="match term1">DYRK1A</span> by <span class="match term0">TRAF2</span> alleviates Sprouty 2-mediated degradation of EGFR	RING	1	Other	H.sapiens
3111	RNF12_HUMAN	P53_HUMAN	Q9NVW2	P04637	RLIM	TP53	MEDLINE	33328571	We further observed that TRIM28 regulates the ubiquitin ligases <span class="match term1">RLIM</span> and MDM2 to target the <span class="match term1">p53</span> levels during lung tumorigenesis	RING	1	Other	H.sapiens
3112	RN123_HUMAN	CCNG2_HUMAN	Q5XPI4	Q16589	RNF123	CCNG2	MEDLINE	33205477	We also discovered that the E3 ligase Ring finger protein 123 (<span class="match term0">RNF123</span>), as a novel <span class="match term1">CCNG2</span> target among HTR8/SVneo cells, interacted with Dvl2 and participated in CCNG2-induced polyubiquitination degradation of Dvl2	RING	1	Other	H.sapiens
3113	MDM2_HUMAN	SUV91_HUMAN	Q00987	O43463	MDM2	SUV39H1	MEDLINE	33691908	In addition, we showed that EBP1 directly interacts with Suv39H1, and this interaction is required for recruiting the E3 ligase <span class="match term0">MDM2</span> for <span class="match term1">Suv39H1</span> degradation	RING	1	Other	H.sapiens
3114	HACE1_HUMAN	SPIN1_HUMAN	Q8IYU2	Q9Y657	HACE1	SPIN1	MEDLINE	33421097	Ubiquitin-independent proteasomal degradation of <span class="match term1">Spindlin-1</span> by the E3 ligase <span class="match term0">HACE1</span> contributes to cell-cell adhesion	HECT	1	Other	H.sapiens
3115	RN123_HUMAN	DVL2_HUMAN	Q5XPI4	O14641	RNF123	DVL2	MEDLINE	33205477	We also discovered that the E3 ligase Ring finger protein 123 (<span class="match term1">RNF123</span>), as a novel CCNG2 target among HTR8/SVneo cells, interacted with <span class="match term1">Dvl2</span> and participated in CCNG2-induced polyubiquitination degradation of <span class="match term1">Dvl2</span>	RING	1	Other	H.sapiens
3116	X_HBVD3	SMC6_HUMAN	P03165	Q96SB8	X	SMC6	MEDLINE	32235678	UbiNet 2.0	Other	1	Other	Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
3117	X_HBVD3	SMC5_HUMAN	P03165	Q8IY18	X	SMC5	MEDLINE	31167910	UbiNet 2.0	Other	1	Other	Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
3118	X_HBVD3	PSME4_HUMAN	P03165	Q14997	X	PSME4	MEDLINE	32235678	UbiNet 2.0	Other	1	Other	Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
3119	X_HBVD3	ZEB2_HUMAN	P03165	O60315	X	ZEB2	MEDLINE	32235678	UbiNet 2.0	Other	1	Other	Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
3120	X_HBVD3	STIM1_HUMAN	P03165	Q13586	X	STIM1	MEDLINE	32235678	UbiNet 2.0	Other	1	Other	Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
3121	E1B55_ADE05#Q6VGT3_ADE05	DNLI4_HUMAN	P03243#Q6VGT3	P49917	E4	LIG4	MEDLINE	22199232	E3Net	Other	1	Other	Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
3122	E1B55_ADE05#Q6VGT3_ADE05	ITA3_HUMAN	P03243#Q6VGT3	P26006	E4	ITGA3	MEDLINE	22199232	E3Net	Other	1	Other	Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
3123	E1B55_ADE05#Q6VGT3_ADE05	MRE11_HUMAN	P03243#Q6VGT3	P49959	E4	MRE11	MEDLINE	22199232	E3Net	Other	1	Other	Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
3124	E1B55_ADE05#Q6VGT3_ADE05	P53_HUMAN	P03243#Q6VGT3	P04637	E4	TP53	MEDLINE	22199232	E3Net	Other	1	Other	Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
3125	ICP0_HHV11	ZBT10_HUMAN	P08393	Q96DT7	ICP0	ZBTB10	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3126	ICP0_HHV11	ICP0_HHV11	P08393	P08393	ICP0	ICP0	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3127	ICP0_HHV11	MORC3_HUMAN	P08393	Q14149	ICP0	MORC3	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3128	ICP0_HHV11	RNF8_HUMAN	P08393	O76064	ICP0	RNF8	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3129	ICP0_HHV11	CENPC_HUMAN	P08393	Q03188	ICP0	CENPC	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3130	ICP0_HHV11	RN168_HUMAN	P08393	Q8IYW5	ICP0	RNF168	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3131	ICP0_HHV11	PRKDC_HUMAN	P08393	P78527	ICP0	PRKDC	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3132	ICP0_HHV11	IF16_HUMAN	P08393	Q16666	ICP0	IFI16	MEDLINE	23427152	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3133	ICP0_HHV11	NACC2_HUMAN	P08393	Q96BF6	ICP0	NACC2	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3134	ICP0_HHV11	UBP7_HUMAN	P08393	Q93009	ICP0	USP7	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3135	ICP0_HHV11	ARI3A_HUMAN	P08393	Q99856	ICP0	ARID3A	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3136	ICP0_HHV11	ZBTB4_HUMAN	P08393	Q9P1Z0	ICP0	ZBTB4	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3137	ICP0_HHV11	ZBT38_HUMAN	P08393	Q8NAP3	ICP0	ZBTB38	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3138	ICP0_HHV11	ETV6_HUMAN	P08393	P41212	ICP0	ETV6	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3139	ICP0_HHV11	MBD1_HUMAN	P08393	Q9UIS9	ICP0	MBD1	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3140	ICP0_HHV11	NACC1_HUMAN	P08393	Q96RE7	ICP0	NACC1	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3141	ICP0_HHV11	SP100_HUMAN	P08393	P23497	ICP0	SP100	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3142	ICP0_HHV11	BEND3_HUMAN	P08393	Q5T5X7	ICP0	BEND3	MEDLINE	32416261	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3143	ICP0_HHV11	CENPB_HUMAN	P08393	P07199	ICP0	CENPB	MEDLINE	22199232	E3Net	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3144	ICP0_HHV11	PML_HUMAN	P08393	P29590	ICP0	PML	MEDLINE	22199232	E3Net	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3145	ICP0_HHV11	ATRX_HUMAN	P08393	P46100	ICP0	ATRX	MEDLINE	22787211	UbiNet 2.0	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3146	ICP0_HHV11	CENPA_HUMAN	P08393	P49450	ICP0	CENPA	MEDLINE	22199232	E3Net	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3147	ICP0_HHV11	P53_HUMAN	P08393	P04637	ICP0	TP53	MEDLINE	22199232	E3Net	RING	1	Other	Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
3148	O92608_HHV8	HEY1_HUMAN	O92608	Q9Y5J3	ORF50	HEY1	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3149	MIR1_HHV8P	CD1D_HUMAN	P90495	P15813	K3	CD1D	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3150	MIR1_HHV8P	HLAA_HUMAN	P90495	P04439	K3	HLA-A	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3151	MIR1_HHV8P	INGR1_HUMAN	P90495	P15260	K3	IFNGR1	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3152	MIR2_HHV8P	CD86_HUMAN	P90489	P42081	K5	CD86	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3153	MIR2_HHV8P	ICAM1_HUMAN	P90489	P05362	K5	ICAM1	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3154	MIR2_HHV8P	INGR1_HUMAN	P90489	P15260	K5	IFNGR1	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3155	MIR2_HHV8P	BST2_HUMAN	P90489	Q10589	K5	BST2	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3156	MIR2_HHV8P	CD166_HUMAN	P90489	Q13740	K5	ALCAM	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3157	MIR2_HHV8P	HLAB_HUMAN	P90489	P01889	K5	HLA-B	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3158	MIR2_HHV8P	CD1D_HUMAN	P90489	P15813	K5	CD1D	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3159	MIR2_HHV8P	PECA1_HUMAN	P90489	P16284	K5	PECAM1	MEDLINE	22199232	E3Net	Other	1	Other	Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
3160	VIF_HV1B1	ABC3F_HUMAN	P69720	Q8IUX4	vif	APOBEC3F	MEDLINE	22199232	E3Net	Other	1	Other	Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1)
3161	VIF_HV1B1	ABC3G_HUMAN	P69720	Q9HC16	vif	APOBEC3G	MEDLINE	22199232	E3Net	Other	1	Other	Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1)
3162	VIF_HV1B1	ABC3C_HUMAN	P69720	Q9NRW3	vif	APOBEC3C	MEDLINE	22199232	E3Net	Other	1	Other	Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1)
3163	VE6_HPV16	P53_HUMAN	P03126	P04637	E6	TP53	MEDLINE	22199232	E3Net	Other	1	Other	Human papillomavirus type 16
3164	VE6_HPV16	DLG1_HUMAN	P03126	Q12959	E6	DLG1	MEDLINE	22199232	E3Net	Other	1	Other	Human papillomavirus type 16
3165	VE6_HPV16	SI1L1_HUMAN	P03126	O43166	E6	SIPA1L1	MEDLINE	22199232	E3Net	Other	1	Other	Human papillomavirus type 16
3166	VE6_HPV16	KDM5C_HUMAN	P03126	P41229	E6	KDM5C	MEDLINE	25231954	UbiNet 2.0	Other	1	Other	Human papillomavirus type 16
3167	VE6_HPV18	KDM5C_HUMAN	P06463	P41229	E6	KDM5C	MEDLINE	25231954	UbiNet 2.0	Other	1	Other	Human papillomavirus type 18
3168	AHR_MOUSE	PPARG_MOUSE	P30561	P37238	Ahr	Pparg	MEDLINE	31653699	UbiNet 2.0	Other	1	Other	M.musculus
3169	AHR_MOUSE	RIPK1_MOUSE	P30561	Q60855	Ahr	Ripk1	MEDLINE	34015312	<span class="match term0">AHR</span> could ubiquitinate <span class="match term1">RIPK1</span>, promote IAPs expression and inhibit NF-kappaB activation in NCM460 cells.	Other	1	Other	M.musculus
3170	AMFR_MOUSE	CD82_MOUSE	Q9R049	P40237	Amfr	Cd82	MEDLINE	32555380	Meanwhile, vIRF1 degrades metastasis suppressor <span class="match term1">CD82</span> through an ubiquitin-proteasome pathway by recruiting E3 ubiquitin ligase <span class="match term0">AMFR</span> to <span class="match term1">CD82</span>, which protects CDCP1 from <span class="match term1">CD82</span>-mediated, palmitoylation-dependent degradation	RING	1	Other	M.musculus
3171	ARI1_MOUSE	PD1L1_MOUSE	Q9Z1K5	Q9EP73	Arih1	Cd274	MEDLINE	33879767	We identify <span class="match term0">ARIH1</span> as the E3 ubiquitin ligase responsible for targeting <span class="match term1">PD-L1</span> to degradation	RING	1	Other	M.musculus
3172	ASB17_MOUSE	MCL1_MOUSE	Q8VHP9	P97287	Asb17	Mcl1	MEDLINE	33803505	E3 Ubiquitin Ligase <span class="match term0">ASB17</span> Promotes Apoptosis by Ubiquitylating and Degrading BCLW and <span class="match term1">MCL1</span>	SOCS_VHL_BC-box	1	Other	M.musculus
3173	ASB9_MOUSE	KCRB_MOUSE	Q91ZT8	Q04447	Asb9	Ckb	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	M.musculus
3174	FBW1A_MOUSE	ATF4_MOUSE	Q3ULA2	Q06507	Btrc	Atf4	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3175	FBW1A_MOUSE	PLK4_MOUSE	Q3ULA2	Q64702	Btrc	Plk4	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3176	FBW1A_MOUSE	DLG1_MOUSE	Q3ULA2	Q811D0	Btrc	Dlg1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3177	FBW1A_MOUSE	IKBE_MOUSE	Q3ULA2	O54910	Btrc	Nfkbie	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3178	FBW1A_MOUSE	PCAT1_MOUSE	Q3ULA2	Q3TFD2	Btrc	Lpcat1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3179	FBW1A_MOUSE	SMAD4_MOUSE	Q3ULA2	P97471	Btrc	Smad4	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3180	FBW1A_MOUSE	MPIP1_MOUSE	Q3ULA2	P48964	Btrc	Cdc25a	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3181	FBW1A_MOUSE	SMAD3_MOUSE	Q3ULA2	Q8BUN5	Btrc	Smad3	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3182	FBW1A_MOUSE	SNAI1_MOUSE	Q3ULA2	Q02085	Btrc	Snai1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3183	FBW1A_MOUSE	IKBB_MOUSE	Q3ULA2	Q60778	Btrc	Nfkbib	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3184	FBW1A_MOUSE	IKBA_MOUSE	Q3ULA2	Q9Z1E3	Btrc	Nfkbia	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3185	FBW1A_MOUSE	FBX5_MOUSE	Q3ULA2	Q7TSG3	Btrc	Fbxo5	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3186	FBW1A_MOUSE	CD4_MOUSE	Q3ULA2	P06332	Btrc	Cd4	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3187	FBW1A_MOUSE	MDM2_MOUSE	Q3ULA2	P23804	Btrc	Mdm2	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3188	FBW1A_MOUSE	NFKB2_MOUSE	Q3ULA2	Q9WTK5	Btrc	Nfkb2	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3189	FBW1A_MOUSE	NFKB1_MOUSE	Q3ULA2	P25799	Btrc	Nfkb1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3190	FBW1A_MOUSE	CTNB1_MOUSE	Q3ULA2	Q02248	Btrc	Ctnnb1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3191	CBL_MOUSE	VGFR2_MOUSE	P22682	P35918	Cbl	Kdr	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3192	CBL_MOUSE	VAV_MOUSE	P22682	P27870	Cbl	Vav1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3193	CBL_MOUSE	IRF8_MOUSE	P22682	P23611	Cbl	Irf8	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3194	CBL_MOUSE	SRBS2_MOUSE	P22682	Q3UTJ2	Cbl	Sorbs2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3195	CBL_MOUSE	EGFR_MOUSE	P22682	Q01279	Cbl	Egfr	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3196	CBL_MOUSE	STA5A_MOUSE	P22682	P42230	Cbl	Stat5a	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3197	CBL_MOUSE	STA5B_MOUSE	P22682	P42232	Cbl	Stat5b	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3198	CBL_MOUSE	CSF1R_MOUSE	P22682	P09581	Cbl	Csf1r	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3199	CBL_MOUSE	FGFR4_MOUSE	P22682	Q03142	Cbl	Fgfr4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3200	CBL_MOUSE	KIT_MOUSE	P22682	P05532	Cbl	Kit	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3201	CBL_MOUSE	CRKL_MOUSE	P22682	P47941	Cbl	Crkl	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3202	CBL_MOUSE	IL6RB_MOUSE	P22682	Q00560	Cbl	Il6st	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3203	CBL_MOUSE	B2L11_MOUSE	P22682	O54918	Cbl	Bcl2l11	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3204	CBL_MOUSE	FGFR1_MOUSE	P22682	P16092	Cbl	Fgfr1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3205	CBL_MOUSE	MET_MOUSE	P22682	P16056	Cbl	Met	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3206	CBL_MOUSE	RELB_MOUSE	P22682	Q04863	Cbl	Relb	MEDLINE	33962939	Mechanistically, we identify that c-<span class="match term0">Cbl</span> functions downstream of Dectin-2 and Dectin-3 to mediate the ubiquitination and degradation of noncanonical nuclear factor kappaB subunit <span class="match term1">RelB</span>	RING	1	Other	M.musculus
3207	CBL_MOUSE	SH3K1_MOUSE	P22682	Q8R550	Cbl	Sh3kbp1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3208	CBL_MOUSE	FRS2_MOUSE	P22682	Q8C180	Cbl	Frs2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3209	CBL_MOUSE	HGS_MOUSE	P22682	Q99LI8	Cbl	Hgs	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3210	CBL_MOUSE	FGFR2_MOUSE	P22682	P21803	Cbl	Fgfr2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3211	CBL_MOUSE	PGFRB_MOUSE	P22682	P05622	Cbl	Pdgfrb	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3212	CBL_MOUSE	FGFR3_MOUSE	P22682	Q61851	Cbl	Fgfr3	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3213	CBL_MOUSE	DDX58_MOUSE	P22682	Q6Q899	Cbl	Ddx58	MEDLINE	23374343	UbiNet 2.0	RING	1	Other	M.musculus
3214	CBL_MOUSE	LYN_MOUSE	P22682	P25911	Cbl	Lyn	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3215	CBL_MOUSE	KSYK_MOUSE	P22682	P48025	Cbl	Syk	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3216	CBL_MOUSE	PGFRA_MOUSE	P22682	P26618	Cbl	Pdgfra	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3217	CBLB_MOUSE	IRF4_MOUSE	Q3TTA7	Q64287	Cblb	Irf4	MEDLINE	30446383	RASA3 promoted proteasome-mediated <span class="match term1">IRF4</span> protein degradation by facilitating interaction of <span class="match term1">IRF4</span> with E3-ubiquitin ligase <span class="match term0">Cbl-b</span>	RING	1	Other	M.musculus
3218	CBLB_MOUSE	KSYK_MOUSE	Q3TTA7	P48025	Cblb	Syk	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3219	CBLB_MOUSE	SH3K1_MOUSE	Q3TTA7	Q8R550	Cblb	Sh3kbp1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3220	CBLB_MOUSE	NMDE2_MOUSE	Q3TTA7	Q01097	Cblb	Grin2b	MEDLINE	32606037	Ubiquitination of <span class="match term1">GluN2B</span> by <span class="match term0">Cbl-b</span> decreased the synaptic transmission mediated by <span class="match term1">GluN2B</span>-containing NMDARs	RING	1	Other	M.musculus
3221	CBLB_MOUSE	PLCG1_MOUSE	Q3TTA7	Q62077	Cblb	Plcg1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3222	CBLB_MOUSE	CBLB_MOUSE	Q3TTA7	Q3TTA7	Cblb	Cblb	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3223	HAKAI_MOUSE	CADH1_MOUSE	Q9JIY2	P09803	Cbll1	Cdh1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3224	CDC16_MOUSE	YDJC_MOUSE	Q8R349	Q14BV6	Cdc16	Ydjc	MEDLINE	31485224	<span class="match term0">CDC16</span> might promote ubiquitination of <span class="match term1">YDJC</span> since <span class="match term0">CDC16</span> comprises a ubiquitin ligase in the APC/C complex	Other	1	Other	M.musculus
3225	CDC20_MOUSE	CDN1A_MOUSE	Q9JJ66	P39689	Cdc20	Cdkn1a	MEDLINE	29719258	PPM1K Regulates Hematopoiesis and Leukemogenesis through <span class="match term0">CDC20</span>-Mediated Ubiquitination of MEIS1 and <span class="match term1">p21</span>	CDC20	1	Other	M.musculus
3226	CDC20_MOUSE	MEIS1_MOUSE	Q9JJ66	Q60954	Cdc20	Meis1	MEDLINE	29719258	A mitochondrial-targeted 2C-type Ser/Thr protein phosphatase (PPM1K) promotes the catabolism of BCAAs to maintain <span class="match term1">MEIS1</span> and p21 levels by decreasing the ubiquitination-mediated degradation controlled by the E3 ubiquitin ligase <span class="match term0">CDC20</span>	CDC20	1	Other	M.musculus
3227	CDC20_MOUSE	CCNB1_MOUSE	Q9JJ66	P24860	Cdc20	Ccnb1	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3228	CDC20_MOUSE	RUNX1_MOUSE	Q9JJ66	Q03347	Cdc20	Runx1	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3229	CDC20_MOUSE	PTTG1_MOUSE	Q9JJ66	Q9CQJ7	Cdc20	Pttg1	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3230	CHFR_MOUSE	CHFR_MOUSE	Q810L3	Q810L3	Chfr	Chfr	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3231	CHFR_MOUSE	HDAC1_MOUSE	Q810L3	O09106	Chfr	Hdac1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3232	CHFR_MOUSE	PLK1_MOUSE	Q810L3	Q07832	Chfr	Plk1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3233	CHFR_MOUSE	AURKA_MOUSE	Q810L3	P97477	Chfr	Aurka	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3234	CNOT4_MOUSE	CNOT4_MOUSE	Q8BT14	Q8BT14	Cnot4	Cnot4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3235	COP1_MOUSE	CEBPA_MOUSE	Q9R1A8	P53566	Cop1	Cebpa	MEDLINE	23884858	<span class="match term0">COP1</span> targets <span class="match term1">C/EBPalpha</span> for degradation and induces acute myeloid leukemia via Trib1.	DWD	1	Other	M.musculus
3236	COP1_MOUSE	JUN_MOUSE	Q9R1A8	P05627	Cop1	Jun	MEDLINE	21403399	Biochemical studies have suggested conflicting roles for the E3 ubiquitin ligase constitutive photomorphogenesis protein 1 (<span class="match term0">Cop1</span>; also known as Rfwd2) in tumorigenesis, providing evidence for both the oncoprotein c-<span class="match term1">Jun</span> and the tumor suppressor p53 as its targets	DWD	1	Other	M.musculus
3237	CRBN_MOUSE	G5E8H3_MOUSE	Q8C7D2	G5E8H3	Crbn	Ikzf1	MEDLINE	29496670	Here we found that IMiD compounds cause selective ubiquitination and degradation of the transcription factor <span class="match term1">IKZF1</span> in CD34+ cells by the Cereblon (<span class="match term0">CRBN</span>) E3 ubiquitin ligase.	SINGLE_OTHER	1	Other	M.musculus
3238	CRBN_MOUSE	-	Q8C7D2	-	Crbn	AMPK GAMMA	MEDLINE	32333926	UbiNet 2.0	SINGLE_OTHER	1	Other	M.musculus
3239	CYLD_MOUSE	M3K7_MOUSE	Q80TQ2	Q62073	Cyld	Map3k7	MEDLINE	29291351	Mechanistically, <span class="match term0">CYLD</span> interacts directly with the kinase <span class="match term1">TAK1</span> and removes its K63-linked polyubiquitin chain, which blocks downstream activation of the JNK-p38 cascades	Other	1	Other	M.musculus
3240	CYLD_MOUSE	SMAD7_MOUSE	Q80TQ2	O35253	Cyld	Smad7	MEDLINE	30315770	We found that sCYLD mediated lysine 63-linked ubiquitination of <span class="match term1">SMAD7</span>.	Other	1	Other	M.musculus
3241	DCAF1_MOUSE	MERL_MOUSE	Q80TR8	P46662	Dcaf1	Nf2	MEDLINE	22199232	E3Net	DWD	1	Other	M.musculus
3242	DDB2_MOUSE	XPC_MOUSE	Q99J79	P51612	Ddb2	Xpc	MEDLINE	22199232	E3Net	DWD	1	Other	M.musculus
3243	DET1_MOUSE#COP1_MOUSE	CRTC2_MOUSE	Q9D0A0#Q9R1A8	Q3U182	Det1#Cop1	Crtc2	MEDLINE	22199232	E3Net	Other	1	Other	M.musculus
3244	DTL_MOUSE	CRY1_MOUSE	Q3TLR7	P97784	Dtl	Cry1	MEDLINE	26431207	CUL4-DDB1-<span class="match term0">CDT2</span> E3 Ligase Regulates the Molecular Clock Activity by Promoting Ubiquitination-Dependent Degradation of the Mammalian <span class="match term1">CRY1</span>.	DWD	1	Other	M.musculus
3245	E4F1_MOUSE	P53_MOUSE	Q8CCE9	P02340	E4f1	Tp53	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3246	FANCL_MOUSE	FACD2_MOUSE	Q9CR14	Q80V62	Fancl	Fancd2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3247	FBRS_MOUSE	ITB1_MOUSE	Q8R089	P09055	Fbrs	Itgb1	MEDLINE	15723043	UbiNet 2.0	Other	1	Other	M.musculus
3248	FXL12_MOUSE	CDN1C_MOUSE	Q9EPX5	P49919	Fbxl12	Cdkn1c	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3249	FXL17_MOUSE	ANM1_MOUSE	Q9QZN1	Q9JIF0	Fbxl17	Prmt1	MEDLINE	28883095	UbiNet 2.0	F-box	1	Other	M.musculus
3250	FBXL5_MOUSE	DCTN1_MOUSE	Q8C2S5	O08788	Fbxl5	Dctn1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3251	FBXL5_MOUSE	IREB2_MOUSE	Q8C2S5	Q811J3	Fbxl5	Ireb2	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3252	FBXL6_MOUSE	HS90A_MOUSE	Q9QXW0	P07901	Fbxl6	Hsp90aa1	MEDLINE	32576198	<span class="match term0">FBXL6</span> promoted K63-dependent ubiquitination of <span class="match term1">HSP90AA1</span> to stabilize it	F-box	1	Other	M.musculus
3253	FBXL7_MOUSE	AURKA_MOUSE	Q5BJ29	P97477	Fbxl7	Aurka	MEDLINE	22306998	Novel E3 ligase component <span class="match term0">FBXL7</span> ubiquitinates and degrades Aurora A, causing mitotic arrest.	F-box	1	Other	M.musculus
3254	FBX11_MOUSE	P53_MOUSE	Q7TPD1	P02340	Fbxo11	Tp53	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3255	FBX2_MOUSE	NMDE1_MOUSE	Q80UW2	P35436	Fbxo2	Grin2a	MEDLINE	25878288	Using cell-based models and F-box Only Protein 2 (<span class="match term0">Fbxo2</span>) knock-out mice, we found that the ubiquitin ligase substrate adaptor protein <span class="match term0">Fbxo2</span>, previously reported to facilitate the degradation of the NMDAR subunit GluN1 in vitro, also functions to regulate GluN1 and <span class="match term1">GluN2A</span> subunit levels in the adult mouse brain	Other	1	Other	M.musculus
3256	FBX2_MOUSE	BACE1_MOUSE	Q80UW2	P56818	Fbxo2	Bace1	MEDLINE	20854419	UbiNet 2.0	Other	1	Other	M.musculus
3257	FBX2_MOUSE	NMDZ1_MOUSE	Q80UW2	P35438	Fbxo2	Grin1	MEDLINE	25878288	Using cell-based models and F-box Only Protein 2 (<span class="match term0">Fbxo2</span>) knock-out mice, we found that the ubiquitin ligase substrate adaptor protein <span class="match term0">Fbxo2</span>, previously reported to facilitate the degradation of the NMDAR subunit <span class="match term1">GluN1</span> in vitro, also functions to regulate <span class="match term1">GluN1</span> and GluN2A subunit levels in the adult mouse brain	Other	1	Other	M.musculus
3258	FBX2_MOUSE	INSR_MOUSE	Q80UW2	P15208	Fbxo2	Insr	MEDLINE	27932386	UbiNet 2.0	Other	1	Other	M.musculus
3259	FBX2_MOUSE	A4_MOUSE	Q80UW2	P12023	Fbxo2	App	MEDLINE	24469452	UbiNet 2.0	Other	1	Other	M.musculus
3260	FBX31_MOUSE	CCND1_MOUSE	Q3TQF0	P25322	Fbxo31	Ccnd1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3261	FBX32_MOUSE	EIF3F_MOUSE	Q9CPU7	Q9DCH4	Fbxo32	Eif3f	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3262	FBX32_MOUSE	MYOG_MOUSE	Q9CPU7	P12979	Fbxo32	Myog	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3263	FBX32_MOUSE	MYOD1_MOUSE	Q9CPU7	P10085	Fbxo32	Myod1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3264	FBX32_MOUSE	FOXO1_MOUSE	Q9CPU7	Q9R1E0	Fbxo32	Foxo1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3265	FBX33_MOUSE	YBOX1_MOUSE	Q8VE08	P62960	Fbxo33	Ybx1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3266	FBX4_MOUSE	CCND1_MOUSE	Q8CHQ0	P25322	Fbxo4	Ccnd1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3267	FBX5_MOUSE	RAD51_MOUSE	Q7TSG3	Q08297	Fbxo5	Rad51	MEDLINE	30554948	UbiNet 2.0	F-box	1	Other	M.musculus
3268	FBX6_MOUSE	CHK1_MOUSE	Q9QZN4	O35280	Fbxo6	Chek1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3269	FBW1B_MOUSE	INAR1_MOUSE	Q5SRY7	P33896	Fbxw11	Ifnar1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3270	FBW1B_MOUSE	IKBA_MOUSE	Q5SRY7	Q9Z1E3	Fbxw11	Nfkbia	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3271	FBW1B_MOUSE	CTNB1_MOUSE	Q5SRY7	Q02248	Fbxw11	Ctnnb1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3272	Q8CFE8_MOUSE	FXL19_HUMAN	Q8CFE8	Q6PCT2	Fbxw17	FBXL19	MEDLINE	33053230	In the study, we discovered that a new ubiquitin E3 ligase, SCFFBXW17 , ubiquitinates and induces <span class="match term1">FBXL19</span> degradation.	Other	1	Other	M.musculus
3273	FBXW5_MOUSE	M3K5_MOUSE	Q9QXW2	O35099	Fbxw5	Map3k5	MEDLINE	30703849	<span class="match term0">FBXW5</span> is the central component of the SCF complex (SCFFbxw5 ) that directly interacts with and ubiquitinates <span class="match term1">ASK1</span> in hepatocytes during NASH development	F-box	1	Other	M.musculus
3274	FBXW7_MOUSE	IKBA_MOUSE	Q8VBV4	Q9Z1E3	Fbxw7	Nfkbia	MEDLINE	31945730	In conclusion, <span class="match term0">FBW7</span> is a novel E3 ubiquitin ligase for <span class="match term1">IkappaBalpha</span> and thereby leads to NF-kappaB activation and inflammation	F-box	1	Other	M.musculus
3275	FBXW7_MOUSE	KLF7_MOUSE	Q8VBV4	Q99JB0	Fbxw7	Klf7	MEDLINE	30838725	We have now applied DiPIUS to the F-box protein <span class="match term0">Fbxw7</span> in three cell lines (mHepa, Neuro2A and C2C12) and thereby identified Kruppel-like factor 7 (<span class="match term1">KLF7</span>) as a candidate substrate of the SCFFbxw7 ubiquitin ligase complex	F-box	1	Other	M.musculus
3276	FBXW7_MOUSE	JUN_MOUSE	Q8VBV4	P05627	Fbxw7	Jun	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3277	FBXW7_MOUSE	MYB_MOUSE	Q8VBV4	P06876	Fbxw7	Myb	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3278	FBXW7_MOUSE	TPP1_MOUSE	Q8VBV4	O89023	Fbxw7	Tpp1	MEDLINE	33086033	<span class="match term0">FBW7</span> binding to telomere protection protein 1 (<span class="match term1">TPP1</span>) facilitates <span class="match term1">TPP1</span> multisite polyubiquitination and accelerates degradation, triggering telomere uncapping and DNA damage response	F-box	1	Other	M.musculus
3279	FBXW7_MOUSE	NOTC1_MOUSE	Q8VBV4	Q01705	Fbxw7	Notch1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3280	FBXW7_MOUSE	MCL1_MOUSE	Q8VBV4	P97287	Fbxw7	Mcl1	MEDLINE	30275535	Mechanistically, we clarified that <span class="match term0">FBXW7</span> promoted TMPD-induced cell apoptosis by catalyzing <span class="match term1">MCL1</span> degradation through K48-linked ubiquitination	F-box	1	Other	M.musculus
3281	FBXW7_MOUSE	NOX1_MOUSE	Q8VBV4	Q8CIZ9	Fbxw7	Nox1	MEDLINE	31445163	<span class="match term0">FBW7</span> knockout increased <span class="match term1">Nox1</span> protein stability by inhibiting ubiquitin-mediated degradation	F-box	1	Other	M.musculus
3282	FBXW7_MOUSE	CCNE1_MOUSE	Q8VBV4	Q61457	Fbxw7	Ccne1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3283	FBXW7_MOUSE	MYC_MOUSE	Q8VBV4	P01108	Fbxw7	Myc	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3284	FBXW7_MOUSE	SHOC2_MOUSE	Q8VBV4	O88520	Fbxw7	Shoc2	MEDLINE	30865892	UbiNet 2.0	F-box	1	Other	M.musculus
3285	FBXW7_MOUSE	MTOR_MOUSE	Q8VBV4	Q9JLN9	Fbxw7	Mtor	MEDLINE	31119177	<span class="match term0">FBW7</span> constitutes the SCF (Skp1-Cullin1-F-box protein) recognition subunit of E3 ubiquitin ligase, and <span class="match term0">mTOR</span> is a substrate of FBW7 that can be modified by ubiquitination and be degraded via proteasomes	F-box	1	Other	M.musculus
3286	FZR1_MOUSE	SKIL_MOUSE	Q9R1K5	Q60665	Fzr1	Skil	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3287	FZR1_MOUSE	KITH_MOUSE	Q9R1K5	P04184	Fzr1	Tk1	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3288	FZR1_MOUSE	DNMT1_MOUSE	Q9R1K5	P13864	Fzr1	Dnmt1	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3289	FZR1_MOUSE	RUNX1_MOUSE	Q9R1K5	Q03347	Fzr1	Runx1	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3290	FZR1_MOUSE	CDC20_MOUSE	Q9R1K5	Q9JJ66	Fzr1	Cdc20	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3291	FZR1_MOUSE	Q60979_MOUSE	Q9R1K5	Q60979	Fzr1	Skil	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3292	FZR1_MOUSE	PTTG1_MOUSE	Q9R1K5	Q9CQJ7	Fzr1	Pttg1	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3293	FZR1_MOUSE	MYF5_MOUSE	Q9R1K5	P24699	Fzr1	Myf5	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3294	FZR1_MOUSE	CCNB1_MOUSE	Q9R1K5	P24860	Fzr1	Ccnb1	MEDLINE	22199232	E3Net	CDC20	1	Other	M.musculus
3295	GAN_MOUSE	MAP1B_MOUSE	Q8CA72	P14873	Gan	Map1b	MEDLINE	22199232	E3Net	BTB_3	1	Other	M.musculus
3296	GAN_MOUSE	-	Q8CA72	-	Gan	IF	MEDLINE	23585478	UbiNet 2.0	BTB_3	1	Other	M.musculus
3297	GAN_MOUSE	MAP1S_MOUSE	Q8CA72	Q8C052	Gan	Map1s	MEDLINE	22199232	E3Net	BTB_3	1	Other	M.musculus
3298	HACE1_MOUSE	FINC_MOUSE	Q3U0D9	P11276	Hace1	Fn1	MEDLINE	29515254	We revealed that <span class="match term0">HACE1</span> promoted the K27 ubiquitination of fibronectin and regulated its secretion	HECT	1	Other	M.musculus
3299	F8WIE5_MOUSE	CLD5_MOUSE	F8WIE5	O54942	Hectd1	Cldn5	MEDLINE	29797543	Together, the results suggested that STK may affect the expression of E3 ubiquitin ligase <span class="match term0">HECTD1</span> and subsequently increase the degradation of claudin-5, thus enabling SS2 to traverse the BBB.	Other	1	Other	M.musculus
3300	F8WIE5_MOUSE	IKBA_MOUSE	F8WIE5	Q9Z1E3	Hectd1	Nfkbia	MEDLINE	32555320	Using a proteomics approach, we demonstrate that LXN interacts and forms a functional complex with <span class="match term0">HECTD1</span> (an E3 ubiquitin ligase) and ribosomal protein subunit3 (Rps3). IkappaBalppa is one of the substrates of <span class="match term0">HECTD1</span>. Ectopic expression of LXN leads to IkappaBalppa accumulation in intestinal epithelial cells, however, LXN knockdown enhances the interaction of <span class="match term0">HECTD1</span> and Rps3, contributing to the ubiquitination degradation of IkappaBalppa, and subsequently enhances inflammatory response.	HECT	1	Other	M.musculus
3301	HECD3_MOUSE	TARA_MOUSE	Q3U487	Q99KW3	Hectd3	Triobp	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3302	HECD3_MOUSE	MALT1_MOUSE	Q3U487	Q2TBA3	Hectd3	Malt1	MEDLINE	30741923	UbiNet 2.0	HECT	1	Other	M.musculus
3303	HECD3_MOUSE	STAT3_MOUSE	Q3U487	P42227	Hectd3	Stat3	MEDLINE	30741923	Moreover, <span class="match term1">Stat3</span> K180 and Malt1 K648 are targeted by <span class="match term0">Hectd3</span> for non-degradative polyubiquitination to mediate robust generation of RORgammat+IL-17Ahi effector CD4+ T cells	HECT	1	Other	M.musculus
3304	HECD3_MOUSE	STX8_MOUSE	Q3U487	O88983	Hectd3	Stx8	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3305	HECD3_MOUSE	TRAF3_MOUSE	Q3U487	Q60803	Hectd3	Traf3	MEDLINE	29920190	<span class="match term0">HECTD3</span> regulated type I IFN production by mediating K63-linked polyubiquitination of <span class="match term1">TRAF3</span> at residue K138	HECT	1	Other	M.musculus
3306	HERC2_MOUSE	NLRC4_MOUSE	Q4U2R1	Q3UP24	Herc2	Nlrc4	MEDLINE	33858325	CONCLUSION: Fendrr can protect against the ubiquitination and degradation of <span class="match term1">NLRC4</span> protein through E3 ubiquitin ligase <span class="match term0">HERC2</span>, thereby accelerating the pyroptosis of microglia.	Other	1	Other	M.musculus
3307	HERC2_MOUSE	XPA_MOUSE	Q4U2R1	Q64267	Herc2	Xpa	MEDLINE	22199232	E3Net	Other	1	Other	M.musculus
3308	HUWE1_MOUSE	P53_MOUSE	Q7TMY8	P02340	Huwe1	Tp53	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3309	HUWE1_MOUSE	WIPI2_MOUSE	Q7TMY8	Q80W47	Huwe1	Wipi2	MEDLINE	30340022	mTORC1 phosphorylates Ser395 of <span class="match term1">WIPI2</span>, directing <span class="match term1">WIPI2</span> to interact specifically with the E3 ubiquitin ligase <span class="match term0">HUWE1</span> for ubiquitination and proteasomal degradation	HECT	1	Other	M.musculus
3310	HUWE1_MOUSE	MYCN_MOUSE	Q7TMY8	P03966	Huwe1	Mycn	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3311	HUWE1_MOUSE	ATOH1_MOUSE	Q7TMY8	P48985	Huwe1	Atoh1	MEDLINE	31959916	Mechanistically, PHD3 bounds the E3 ubiquitin ligase <span class="match term0">HUWE1</span> and prevented <span class="match term0">HUWE1</span> from mediating ubiquitination and degradation of <span class="match term1">ATOH1</span>, an essential driver for goblet cell differentiation	HECT	1	Other	M.musculus
3312	HUWE1_MOUSE	EGFR_MOUSE	Q7TMY8	Q01279	Huwe1	Egfr	MEDLINE	32017279	Further analysis indicated that <span class="match term0">HUWE1</span> physically interacted with <span class="match term1">EGFR</span> and promoted its ubiquitination and degradation	HECT	1	Other	M.musculus
3313	Q4JG03_MOUSE	Q9Z197_MOUSE	Q4JG03	Q9Z197	Huwe1	c-myc	MEDLINE	23699408	Mule/<span class="match term0">Huwe1</span>/Arf-BP1 suppresses Ras-driven tumorigenesis by preventing <span class="match term1">c-Myc</span>/Miz1-mediated down-regulation of p21 and p15.	HECT	1	Other	M.musculus
3314	Q4JG03_MOUSE	PIAS2_MOUSE	Q4JG03	Q8C5D8	Huwe1	Pias2	MEDLINE	23699408	UbiNet 2.0	HECT	1	Other	M.musculus
3315	HUWE1_MOUSE	KAT7_MOUSE	Q7TMY8	Q5SVQ0	Huwe1	Kat7	MEDLINE	32555450	In this study, we find out that Brpf3 protein level is critical for <span class="match term1">Myst2</span> stability and E3 ligase <span class="match term0">Huwe1</span> functions as a novel negative regulator of <span class="match term1">Myst2</span> via ubiquitin-mediated degradation	HECT	1	Other	M.musculus
3316	IRAK1_MOUSE	PELI1_MOUSE	Q62406	Q8C669	Irak1	Peli1	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	M.musculus
3317	IRAK4_MOUSE	PELI1_MOUSE	Q8R4K2	Q8C669	Irak4	Peli1	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	M.musculus
3318	ITCH_MOUSE	NR0B2_MOUSE	Q8C863	Q62227	Itch	Nr0b2	MEDLINE	29925997	<span class="match term0">Itch</span> and WWP2 formed a complex and cooperated to enhance TCR-proximal signaling by catalyzing the conjugation of atypical ubiquitin chains to the phosphatase <span class="match term1">SHP</span>-1 and reducing the association of <span class="match term1">SHP</span>-1 with the tyrosine kinase Lck	HECT	1	Other	M.musculus
3319	ITCH_MOUSE	JUNB_MOUSE	Q8C863	P09450	Itch	Junb	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3320	ITCH_MOUSE	P73_MOUSE	Q8C863	Q9JJP2	Itch	Tp73	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3321	ITCH_MOUSE	SRBP2_MOUSE	Q8C863	Q3U1N2	Itch	Srebf2	MEDLINE	25777360	The E3 Ubiquitin Ligase <span class="match term0">ITCH</span> modulates lipid metabolism impacting on atherosclerosis progression independently from effects on myeloid cells polarization through control of SIRT6 and <span class="match term1">SREBP2</span> ubiquitination	HECT	1	Other	M.musculus
3322	ITCH_MOUSE	CXCR4_MOUSE	Q8C863	P70658	Itch	Cxcr4	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3323	ITCH_MOUSE	ERBB4_MOUSE	Q8C863	Q61527	Itch	Erbb4	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3324	ITCH_MOUSE	BID_MOUSE	Q8C863	P70444	Itch	Bid	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3325	ITCH_MOUSE	SNX9_MOUSE	Q8C863	Q91VH2	Itch	Snx9	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3326	ITCH_MOUSE	OCLN_MOUSE	Q8C863	Q61146	Itch	Ocln	MEDLINE	33636390	Our mechanistic studies revealed that abnormal reactive oxygen species (ROS) in mutant SOD1-expressing cells induced occludin phosphorylation, which facilitated the subsequent occludin ubiquitination mediated by the E3 ligase <span class="match term0">ITCH</span>	HECT	1	Other	M.musculus
3327	ITCH_MOUSE	NOTC1_MOUSE	Q8C863	Q01705	Itch	Notch1	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3328	ITCH_MOUSE	NR2C2_MOUSE	Q8C863	P49117	Itch	Nr2c2	MEDLINE	22057290	The E3 ligase <span class="match term0">Itch</span> and deubiquitinase Cyld act together to regulate <span class="match term1">Tak1</span> and inflammation.	HECT	1	Other	M.musculus
3329	ITCH_MOUSE	FOXO1_MOUSE	Q8C863	Q9R1E0	Itch	Foxo1	MEDLINE	24859451	The E3 ubiquitin ligase <span class="match term0">Itch</span> is required for the differentiation of follicular helper T cells.	HECT	1	Other	M.musculus
3330	ITCH_MOUSE	RORG_MOUSE	Q8C863	P51450	Itch	Rorc	MEDLINE	27322655	UbiNet 2.0	HECT	1	Other	M.musculus
3331	ITCH_MOUSE	SIR6_MOUSE	Q8C863	P59941	Itch	Sirt6	MEDLINE	25777360	The E3 Ubiquitin Ligase <span class="match term0">ITCH</span> modulates lipid metabolism impacting on atherosclerosis progression independently from effects on myeloid cells polarization through control of <span class="match term1">SIRT6</span> and SREBP2 ubiquitination	HECT	1	Other	M.musculus
3332	ITCH_MOUSE	ITCH_MOUSE	Q8C863	Q8C863	Itch	Itch	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3333	ITCH_MOUSE	BCL10_MOUSE	Q8C863	Q9Z0H7	Itch	Bcl10	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3334	ITCH_MOUSE	P63_MOUSE	Q8C863	O88898	Itch	Tp63	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3335	ITCH_MOUSE	JUN_MOUSE	Q8C863	P05627	Itch	Jun	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3336	ITCH_MOUSE	CFLAR_MOUSE	Q8C863	O35732	Itch	Cflar	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3337	ITCH_MOUSE	SMAD2_MOUSE	Q8C863	Q62432	Itch	Smad2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3338	ITCH_MOUSE	KLF10_MOUSE	Q8C863	O89091	Itch	Klf10	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3339	ITCH_MOUSE#WWP2_MOUSE	PTN6_MOUSE	Q8C863#Q9DBH0	P29351	Itch#Wwp2	Ptpn6	MEDLINE	29925997	UbiNet 2.0	Other	1	Other	M.musculus
3340	KAT2B_MOUSE	MDM2_MOUSE	Q9JHD1	P23804	Kat2b	Mdm2	MEDLINE	32404984	Interestingly, <span class="match term0">PCAF</span> also possesses E3 ubiquitin ligase activity for <span class="match term1">MDM2</span> and can stabilize p53 protein levels	SINGLE_OTHER	1	Other	M.musculus
3341	BACD1_MOUSE	RHOA_MOUSE	Q8BGV7	Q9QUI0	Kctd13	Rhoa	MEDLINE	22199232	E3Net	BTB_OTHER	1	Other	M.musculus
3342	KEAP1_MOUSE	PGAM5_MOUSE	Q9Z2X8	Q8BX10	Keap1	Pgam5	MEDLINE	22199232	E3Net	BTB_3	1	Other	M.musculus
3343	KEAP1_MOUSE	NF2L2_MOUSE	Q9Z2X8	Q60795	Keap1	Nfe2l2	MEDLINE	22199232	E3Net	BTB_3	1	Other	M.musculus
3344	KLH17_MOUSE	GRIK2_MOUSE	Q6TDP3	P39087	Klhl17	Grik2	MEDLINE	22199232	E3Net	BTB_3	1	Other	M.musculus
3345	KLHL2_MOUSE	Q6TKP2_MOUSE	Q8JZP3	Q6TKP2	Klhl2	Npcd	MEDLINE	21549840	UbiNet 2.0	Other	1	Other	M.musculus
3346	KLH21_MOUSE	AURKB_MOUSE	Q3U410	O70126	Klhl21	Aurkb	MEDLINE	22199232	E3Net	BTB_3	1	Other	M.musculus
3347	KLHL3_MOUSE	CLD8_MOUSE	E0CZ16	Q9Z260	Klhl3	Cldn8	MEDLINE	25831548	<span class="match term0">KLHL3</span> regulates paracellular chloride transport in the kidney by ubiquitination of claudin-8.	BTB_3	1	Other	M.musculus
3348	KLH31_MOUSE	FLNC_MOUSE	Q8BWA5	Q8VHX6	Klhl31	Flnc	MEDLINE	28872460	In the <span class="match term0">Klhl31</span>-knockout mice, <span class="match term1">FlnC</span> protein levels were highly upregulated with no change in transcription, and we further demonstrated that <span class="match term0">Klhl31</span> targets <span class="match term1">FlnC</span> for ubiquitination and degradation	BTB_OTHER	1	Other	M.musculus
3349	KLH41_MOUSE	NRAP_MOUSE	A2AUC9	Q80XB4	Klhl41	Nrap	MEDLINE	30986853	Dysregulation of <span class="match term1">NRAP</span> degradation by <span class="match term0">KLHL41</span> contributes to pathophysiology in nemaline myopathy.	BTB_3	1	Other	M.musculus
3350	LNX1_MOUSE	NUMB_MOUSE	O70263	Q9QZS3	Lnx1	Numb	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3351	LNX1_MOUSE	CXD2_MOUSE	O70263	O54851	Lnx1	Gjd2	MEDLINE	30295974	Our results suggest that a <span class="match term0">LNX</span> protein mediates ubiquitination of <span class="match term1">Cx36</span> at neuronal gap junctions, with consequent <span class="match term1">Cx36</span> internalization, and may thereby contribute to intracellular mechanisms that govern the recently identified modifiability of synaptic transmission at electrical synapses.	RING	1	Other	M.musculus
3352	LRSM1_MOUSE	TS101_MOUSE	Q80ZI6	Q61187	Lrsam1	Tsg101	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3353	MALT1_MOUSE	NEMO_MOUSE	Q2TBA3	O88522	Malt1	Ikbkg	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3354	M3K1_MOUSE	MK03_MOUSE	P53349	Q63844	Map3k1	Mapk3	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3355	M3K1_MOUSE	MK01_MOUSE	P53349	P63085	Map3k1	Mapk1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3356	M3K1_MOUSE	JUN_MOUSE	P53349	P05627	Map3k1	Jun	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3357	M3K1_MOUSE	DTX1_MOUSE	P53349	Q61010	Map3k1	Dtx1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3358	M3K1_MOUSE	FOSL2_MOUSE	P53349	P47930	Map3k1	Fosl2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3359	MARH1_MOUSE	HB2A_MOUSE	Q6NZQ8	P14483	Marchf1	H2-Ab1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3360	MARH1_MOUSE	CD86_MOUSE	Q6NZQ8	P42082	Marchf1	Cd86	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3361	MARH1_MOUSE	TNR6_MOUSE	Q6NZQ8	P25446	Marchf1	Fas	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3362	MARH1_MOUSE	TFR1_MOUSE	Q6NZQ8	Q62351	Marchf1	Tfrc	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3363	MARHB_MOUSE	CD4_MOUSE	Q8CBH7	P06332	Marchf11	Cd4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3364	MARH2_MOUSE	TFR1_MOUSE	Q99M02	Q62351	MARCHF2	Tfrc	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3365	MARH2_MOUSE	CD86_MOUSE	Q99M02	P42082	MARCHF2	Cd86	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3366	MARH4_MOUSE	CD4_MOUSE	Q80TE3	P06332	Marchf4	Cd4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3367	MARH5_MOUSE	FIS1_MOUSE	Q3KNM2	Q9CQ92	Marchf5	Fis1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3368	MARH5_MOUSE	DNM1L_MOUSE	Q3KNM2	Q8K1M6	Marchf5	Dnm1l	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3369	MARH5_MOUSE	MFN1_MOUSE	Q3KNM2	Q811U4	Marchf5	Mfn1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3370	MARH7_MOUSE	MARH7_MOUSE	Q9WV66	Q9WV66	Marchf7	Marchf7	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3371	MARH8_MOUSE	HB2A_MOUSE	Q9DBD2	P14483	Marchf8	H2-Ab1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3372	MARH8_MOUSE	CD86_MOUSE	Q9DBD2	P42082	Marchf8	Cd86	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3373	MARH9_MOUSE	ICAM1_MOUSE	Q3TZ87	P13597	Marchf9	Icam1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3374	MARH9_MOUSE	CD4_MOUSE	Q3TZ87	P06332	Marchf9	Cd4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3375	MDM2_MOUSE	MDM2_MOUSE	P23804	P23804	Mdm2	Mdm2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3376	MDM2_MOUSE	DLG4_MOUSE	P23804	Q62108	Mdm2	Dlg4	MEDLINE	32561413	In addition, <span class="match term0">Mdm2</span> knockdown abolished <span class="match term1">PSD95</span> ubiquitination and increased KA-induced seizure activity in PLPP/CIN-/- mice without affecting AKT activity and protein levels of p53 and neural precursor cell expressed developmentally down-regulated gene 4-like (NEDD4-2)	RING	1	Other	M.musculus
3377	MDM2_MOUSE	ARC_MOUSE	P23804	Q9WV31	Mdm2	Arc	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3378	MDM2_MOUSE	PPARG_MOUSE	P23804	P37238	Mdm2	Pparg	MEDLINE	33617858	MicroRNA-498 disturbs the occurrence and aggression of colon cancer through targeting <span class="match term0">MDM2</span> to mediate <span class="match term1">PPARgamma</span> ubiquitination	RING	1	Other	M.musculus
3379	MDM2_MOUSE	P53_MOUSE	P23804	P02340	Mdm2	Tp53	MEDLINE	31847675	<span class="match term0">Mdm2</span> Promotes Odontoblast-like Differentiation by Ubiquitinating Dlx3 and <span class="match term1">p53</span>.	RING	1	Other	M.musculus
3380	MDM2_MOUSE	TELT_MOUSE	P23804	O70548	Mdm2	Tcap	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3381	MDM2_MOUSE	JMY_MOUSE	P23804	Q9QXM1	Mdm2	Jmy	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3382	MDM2_MOUSE	ANDR_MOUSE	P23804	P19091	Mdm2	Ar	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3383	MDM2_MOUSE	KAT5_MOUSE	P23804	Q8CHK4	Mdm2	Kat5	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3384	MDM2_MOUSE	SIR6_MOUSE	P23804	P59941	Mdm2	Sirt6	MEDLINE	33042992	Mechanistically, <span class="match term0">MDM2</span> ubiquitination degraded <span class="match term1">SIRT6</span> in RA	RING	1	Other	M.musculus
3385	MDM2_MOUSE	KAT2B_MOUSE	P23804	Q9JHD1	Mdm2	Kat2b	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3386	MDM2_MOUSE	E2F1_MOUSE	P23804	Q61501	Mdm2	E2f1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3387	MDM2_MOUSE	MDM4_MOUSE	P23804	O35618	Mdm2	Mdm4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3388	MDM2_MOUSE	ARRB2_MOUSE	P23804	Q91YI4	Mdm2	Arrb2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3389	MDM2_MOUSE	ARRB1_MOUSE	P23804	Q8BWG8	Mdm2	Arrb1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3390	MDM2_MOUSE	APEX1_MOUSE	P23804	P28352	Mdm2	Apex1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3391	MDM2_MOUSE	DLX3_MOUSE	P23804	Q64205	Mdm2	Dlx3	MEDLINE	31847675	Taken together, our study revealed that <span class="match term0">Mdm2</span> promoted the odontoblast-like differentiation of mDPCs by ubiquitinating both <span class="match term1">Dlx3</span> and p53 <span class="match term1">Dlx3</span> and p53.	RING	1	Other	M.musculus
3392	MDM2_MOUSE	HIPK2_MOUSE	P23804	Q9QZR5	Mdm2	Hipk2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3393	MDM2_MOUSE	ACE2_MOUSE	P23804	Q8R0I0	Mdm2	Ace2	MEDLINE	32755395	In this study, we investigated whether <span class="match term0">MDM2</span> is involved in the PTM of <span class="match term1">ACE2</span> via its ubiquitination of <span class="match term1">ACE2</span>, and whether an AMPK and <span class="match term0">MDM2</span> crosstalk regulates the pathogenesis of PH	RING	1	Other	M.musculus
3394	MGRN1_MOUSE	TS101_MOUSE	Q9D074	Q61187	Mgrn1	Tsg101	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3395	MIB1_MOUSE	MIB1_MOUSE	Q80SY4	Q80SY4	Mib1	Mib1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3396	MIB1_MOUSE	DLL3_MOUSE	Q80SY4	O88516	Mib1	Dll3	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3397	MIB1_MOUSE	DAPK1_MOUSE	Q80SY4	Q80YE7	Mib1	Dapk1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3398	MIB1_MOUSE	DLL4_MOUSE	Q80SY4	Q9JI71	Mib1	Dll4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3399	MIB1_MOUSE	DLL1_MOUSE	Q80SY4	Q61483	Mib1	Dll1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3400	MIB2_MOUSE	DLL1_MOUSE	Q8R516	Q61483	Mib2	Dll1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3401	MIB2_MOUSE	DLL4_MOUSE	Q8R516	Q9JI71	Mib2	Dll4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3402	MIB2_MOUSE	CYLD_MOUSE	Q8R516	Q80TQ2	Mib2	Cyld	MEDLINE	31366726	However, whether <span class="match term0">MIB2</span> is an E3 ubiquitin ligase that acts on <span class="match term1">CYLD</span> is unknown	RING	1	Other	M.musculus
3403	MIB2_MOUSE	GPX4_MOUSE	Q8R516	O70325	Mib2	Gpx4	MEDLINE	34121396	Downregulated <span class="match term0">MIB2</span> enhanced <span class="match term1">GPX4</span> stability and reduced its ubiquitination	RING	1	Other	M.musculus
3404	MIB2_MOUSE	DLL3_MOUSE	Q8R516	O88516	Mib2	Dll3	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3405	TRI18_MOUSE	PRM2_MOUSE	O70583	P07978	Mid1	Prm2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3406	MKRN1_MOUSE	P53_MOUSE	Q9QXP6	P02340	Mkrn1	Tp53	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3407	MKRN1_MOUSE	CDN1A_MOUSE	Q9QXP6	P39689	Mkrn1	Cdkn1a	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3408	MUL1_MOUSE	AKT1_MOUSE	Q8VCM5	P31750	Mul1	Akt1	MEDLINE	32164484	<span class="match term0">MUL1</span> (mitochondrial ubiquitin ligase activator of NFKB 1) also played a vital role in the lysosomal degradation of <span class="match term1">AKT</span> by sequentially ubiquitinating <span class="match term1">AKT</span> residues K284 to K214 for R-HSPA5-mediated autophagy	RING	1	Other	M.musculus
3409	MUL1_MOUSE	AKT2_MOUSE	Q8VCM5	Q60823	Mul1	Akt2	MEDLINE	32184272	Moreover, the E3 ligase <span class="match term0">Mul1</span> played an essential role in BCAAs/BCKAs-mTORC2-induced <span class="match term1">Akt2</span> ubiquitin-dependent degradation	RING	1	Other	M.musculus
3410	MYCB2_MOUSE	Q3UGI8_MOUSE	Q7TPH6	Q3UGI8	Mycbp2	Tsc2	MEDLINE	32965772	Meanwhile, E3 ubiquitin ligase <span class="match term0">Mycbp2</span> could ubiquitinate <span class="match term1">TSC2</span> protein	RING	1	Other	M.musculus
3411	MYCB2_MOUSE	NMNA2_MOUSE	Q7TPH6	Q8BNJ3	Mycbp2	Nmnat2	MEDLINE	29997255	<span class="match term0">PAM</span> forms an atypical SCF ubiquitin ligase complex that ubiquitinates and degrades <span class="match term1">NMNAT2</span>.	RING	1	Other	M.musculus
3412	MYLIP_MOUSE	LRP8_MOUSE	Q8BM54	Q924X6	Mylip	Lrp8	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3413	MYLIP_MOUSE	LDLR_MOUSE	Q8BM54	P35951	Mylip	Ldlr	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3414	MYLIP_MOUSE	MYLIP_MOUSE	Q8BM54	Q8BM54	Mylip	Mylip	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3415	NEDD4_MOUSE	NFIP2_MOUSE	P46935	Q91ZP6	Nedd4	Ndfip2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3416	NEDD4_MOUSE	CBLB_MOUSE	P46935	Q3TTA7	Nedd4	Cblb	MEDLINE	18931680	<span class="match term0">Nedd4</span> augments the adaptive immune response by promoting ubiquitin-mediated degradation of <span class="match term1">Cbl-b</span> in activated T cells.	HECT	1	Other	M.musculus
3417	NEDD4_MOUSE	BCL10_MOUSE	P46935	Q9Z0H7	Nedd4	Bcl10	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3418	NEDD4_MOUSE	KSYK_MOUSE	P46935	P48025	Nedd4	Syk	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3419	NEDD4_MOUSE	GGA3_MOUSE	P46935	Q8BMI3	Nedd4	Gga3	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3420	NEDD4_MOUSE	TRPA1_MOUSE	P46935	Q8BLA8	Nedd4	Trpa1	MEDLINE	32679097	Mechanistically, O2 suppresses <span class="match term1">TRPA1</span> channel activity by protein internalization via O2-dependent proline hydroxylation and subsequent ubiquitination by an E3 ubiquitin ligase, <span class="match term0">NEDD4</span>-1 (neural precursor cell-expressed developmentally down-regulated protein 4)	HECT	1	Other	M.musculus
3421	NEDD4_MOUSE	SYUA_MOUSE	P46935	O55042	Nedd4	Snca	MEDLINE	32703111	Parkinson's disease-causing protein alpha-Synuclein (alpha-Syn) is ubiquitinated by the <span class="match term0">Nedd4</span> family and degraded by endosomes	HECT	1	Other	M.musculus
3422	NEDD4_MOUSE	VHL_MOUSE	P46935	P40338	Nedd4	Vhl	MEDLINE	32792353	Using proteomic analysis of the Daam2-<span class="match term1">VHL</span> complex coupled with conditional genetic knockout mouse models, we further discovered that the E3 ubiquitin ligase <span class="match term0">Nedd4</span> is required for developmental myelination through stabilization of <span class="match term1">VHL</span> via K63-linked ubiquitination	HECT	1	Other	M.musculus
3423	NEDD4_MOUSE	LYN_MOUSE	P46935	P25911	Nedd4	Lyn	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3424	NEDD4_MOUSE	FOXA1_MOUSE	P46935	P35582	Nedd4	Foxa1	MEDLINE	33530829	The binding relationships between <span class="match term0">NEDD4</span> and <span class="match term1">FOXA1</span>, <span class="match term1">FOXA1</span> and microRNA (miRNA)-340-5p, and miR-340-5p and ATF1 were validated by Co-immunoprecipitation, chromatin immunoprecipitation and luciferase assays, and <span class="match term0">NEDD4</span> was demonstrated to trigger <span class="match term1">FOXA1</span> ubiquitination and degradation	HECT	1	Other	M.musculus
3425	NEDD4_MOUSE	PTEN_MOUSE	P46935	O08586	Nedd4	Pten	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3426	NEDD4_MOUSE	NEDD4_MOUSE	P46935	P46935	Nedd4	Nedd4	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3427	NEDD4_MOUSE	NFIP1_MOUSE	P46935	Q8R0W6	Nedd4	Ndfip1	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3428	NED4L_MOUSE	PP2BA_MOUSE	Q8CFI0	P63328	Nedd4l	Ppp3ca	MEDLINE	31357244	UbiNet 2.0	HECT	1	Other	M.musculus
3429	NED4L_MOUSE	SCN5A_MOUSE	Q8CFI0	Q9JJV9	Nedd4l	Scn5a	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3430	E9PXB7_MOUSE	CTNB1_MOUSE	E9PXB7	Q02248	Nedd4l	Ctnnb1	MEDLINE	34330894	ALCAP2 inhibits lung adenocarcinoma cell proliferation, migration and invasion via the ubiquitination of <span class="match term1">beta-catenin</span> by upregulating the E3 ligase <span class="match term0">NEDD4L</span>	HECT	1	Other	M.musculus
3431	NED4L_MOUSE	SCN8A_MOUSE	Q8CFI0	Q9WTU3	Nedd4l	Scn8a	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3432	NED4L_MOUSE	S38A2_MOUSE	Q8CFI0	Q8CFE6	Nedd4l	Slc38a2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3433	NED4L_MOUSE	SCNNA_MOUSE	Q8CFI0	Q61180	Nedd4l	Scnn1a	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3434	E9PXB7_MOUSE	SYUA_MOUSE	E9PXB7	O55042	Nedd4l	Snca	MEDLINE	32703111	Focal ischemia significantly increased <span class="match term0">Nedd4l</span> expression and poly-ubiquitinated alpha-Syn levels, and knockout of <span class="match term0">Nedd4l</span> reduced post-ischemic poly-ubiquitinated alpha-Syn that is majorly located in the peri-infarct neurons	HECT	1	Other	M.musculus
3435	NED4L_MOUSE	GRIA1_MOUSE	Q8CFI0	P23818	Nedd4l	Gria1	MEDLINE	28212375	UbiNet 2.0	HECT	1	Other	M.musculus
3436	NED4L_MOUSE	SCNNG_MOUSE	Q8CFI0	Q9WU39	Nedd4l	Scnn1g	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3437	NED4L_MOUSE	SCN9A_MOUSE	Q8CFI0	Q62205	Nedd4l	Scn9a	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3438	E9PXB7_MOUSE	ULK1_MOUSE	E9PXB7	O70405	Nedd4l	Ulk1	MEDLINE	31959741	<span class="match term1">ULK1</span> expression was stabilized in <span class="match term0">NEDD4L</span> knockdown cells compared to that in control cells, suggesting that <span class="match term0">NEDD4L</span> is involved in <span class="match term1">ULK1</span> ubiquitination and its subsequent degradation	HECT	1	Other	M.musculus
3439	NED4L_MOUSE	SMAD2_MOUSE	Q8CFI0	Q62432	Nedd4l	Smad2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3440	NED4L_MOUSE	SGK1_MOUSE	Q8CFI0	Q9WVC6	Nedd4l	Sgk1	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3441	E9PXB7_MOUSE	Q6DR99_MOUSE	E9PXB7	Q6DR99	Nedd4l	Nrg1	MEDLINE	32703967	We here assessed the regulation of <span class="match term1">NRG1</span> by the E3 ubiquitin ligase <span class="match term0">Nedd4l</span> (neural precursor cell expressed developmentally downregulated 4-like) and investigated whether <span class="match term1">NRG1</span> changes in the mPFC might lead to vulnerability to depression-like behaviours	HECT	1	Other	M.musculus
3442	NED4L_MOUSE	CLCN5_MOUSE	Q8CFI0	Q9WVD4	Nedd4l	Clcn5	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3443	NED4L_MOUSE	SCNAA_MOUSE	Q8CFI0	Q6QIY3	Nedd4l	Scn10a	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3444	NED4L_MOUSE	NFIP2_MOUSE	Q8CFI0	Q91ZP6	Nedd4l	Ndfip2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3445	E9PXB7_MOUSE	YBOX1_MOUSE	E9PXB7	P62960	Nedd4l	Ybx1	MEDLINE	30947518	Mechanistically, circNfix reinforced the interaction of <span class="match term1">Ybx1</span> (Y-box binding protein 1) with <span class="match term0">Nedd4l</span> (an E3 ubiquitin ligase), and induced <span class="match term1">Ybx1</span> degradation through ubiquitination, repressing cyclin A2 and cyclin B1 expression	HECT	1	Other	M.musculus
3446	NEUL1_MOUSE	PDE9A_MOUSE	Q923S6	O70628	Neurl1	Pde9a	MEDLINE	31068605	Neuralized family member <span class="match term0">NEURL1</span> is a ubiquitin ligase for the cGMP-specific phosphodiesterase 9A.	RING	1	Other	M.musculus
3447	NEUL1_MOUSE	JAG1_MOUSE	Q923S6	Q9QXX0	Neurl1	Jag1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3448	NEU1B_MOUSE	DLL1_MOUSE	Q0MW30	Q61483	Neurl1b	Dll1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3449	NEU1B_MOUSE	DLL3_MOUSE	Q0MW30	O88516	Neurl1b	Dll3	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3450	NEU1B_MOUSE	DLL4_MOUSE	Q0MW30	Q9JI71	Neurl1b	Dll4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3451	NEUL2_MOUSE	CTNB1_MOUSE	Q9D0S4	Q02248	Neurl2	Ctnnb1	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	M.musculus
3452	NHLC1_MOUSE	PPR3C_MOUSE	Q8BR37	Q7TMB3	Nhlrc1	Ppp1r3c	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3453	NHLC1_MOUSE	EPM2A_MOUSE	Q8BR37	Q9WUA5	Nhlrc1	Epm2a	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3454	NOSIP_MOUSE	EPOR_MOUSE	Q9D6T0	P14753	Nosip	Epor	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3455	OTUL_MOUSE	A0A087WSP5_MOUSE	Q3UCV8	A0A087WSP5	Otulin	Stat1	MEDLINE	32123171	Linear ubiquitination of <span class="match term1">STAT1</span> is removed rapidly by <span class="match term0">OTULIN</span> upon type-I interferon stimulation, which facilitates activation of interferon-<span class="match term1">STAT1</span> signaling	Other	1	Other	M.musculus
3456	PAXI1_MOUSE	PCNA_MOUSE	Q6NZQ4	P17918	Paxip1	Pcna	MEDLINE	22199232	E3Net	Other	1	Other	M.musculus
3457	PDLI2_MOUSE	TF65_MOUSE	Q8R1G6	Q04207	Pdlim2	Rela	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	M.musculus
3458	PDLI2_MOUSE	STAT1_MOUSE	Q8R1G6	P42225	Pdlim2	Stat1	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	M.musculus
3459	PZRN3_MOUSE	MUSK_MOUSE	Q69ZS0	Q61006	Pdzrn3	Musk	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3460	PELI1_MOUSE	IRAK1_MOUSE	Q8C669	Q62406	Peli1	Irak1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3461	PELI1_MOUSE	RBP1_MOUSE	Q8C669	Q62172	Peli1	Ralbp1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3462	PJA1_MOUSE	SC6A4_MOUSE	O55176	Q60857	Pja1	Slc6a4	MEDLINE	31891772	Taken together, these results indicate that DGKdelta interacts with <span class="match term1">SERT</span> and induces <span class="match term1">SERT</span> degradation in an activity-dependent manner through the Praja-1 ubiquitin ligase-proteasome system	RING	1	Other	M.musculus
3463	PJA1_MOUSE	MAGD1_MOUSE	O55176	Q9QYH6	Pja1	Maged1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3464	PRKN_MOUSE	PRKN_MOUSE	Q9WVS6	Q9WVS6	Prkn	Prkn	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3465	PRKN_MOUSE	RBP2_MOUSE	Q9WVS6	Q9ERU9	Prkn	Ranbp2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3466	PRKN_MOUSE	AIMP2_MOUSE	Q9WVS6	Q8R010	Prkn	Aimp2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3467	PRKN_MOUSE	VDAC3_MOUSE	Q9WVS6	Q60931	Prkn	Vdac3	MEDLINE	30763678	UbiNet 2.0	RING	1	Other	M.musculus
3468	PRKN_MOUSE	GPR37_MOUSE	Q9WVS6	Q9QY42	Prkn	Gpr37	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3469	PRKN_MOUSE	FIS1_MOUSE	Q9WVS6	Q9CQ92	Prkn	Fis1	MEDLINE	29809156	29809156	RING	1	Other	M.musculus
3470	RAD18_MOUSE	PCNA_MOUSE	Q9QXK2	P17918	Rad18	Pcna	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3471	RAD18_MOUSE	TP53B_MOUSE	Q9QXK2	P70399	Rad18	Tp53bp1	MEDLINE	31506606	Here, we report that betaarr1 directs <span class="match term1">53BP1</span> degradation by acting as a scaffold for the E3-ubiquitin ligase <span class="match term0">Rad18</span>	RING	1	Other	M.musculus
3472	RAG1_MOUSE	RAG1_MOUSE	P15919	P15919	Rag1	Rag1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3473	RAG1_MOUSE	IMA5_MOUSE	P15919	Q60960	Rag1	Kpna1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3474	RC3H1_MOUSE	ICOS_MOUSE	Q4VGL6	Q9WVS0	Rc3h1	Icos	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3475	ZN363_MOUSE	CDN1B_MOUSE	Q9CR50	P46414	Rchy1	Cdkn1b	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3476	RFFL_MOUSE	P53_MOUSE	Q6ZQM0	P02340	Rffl	Tp53	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3477	RFFL_MOUSE	RFFL_MOUSE	Q6ZQM0	Q6ZQM0	Rffl	Rffl	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3478	RFWD3_MOUSE	P53_MOUSE	Q8CIK8	P02340	Rfwd3	Tp53	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3479	RHBT1_MOUSE	PDE5A_MOUSE	Q9DAK3	Q8CG03	Rhobtb1	Pde5a	MEDLINE	30896450	UbiNet 2.0	BTB_OTHER	1	Other	M.musculus
3480	RNF12_MOUSE	LDB1_MOUSE	Q9WTV7	P70662	Rlim	Ldb1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3481	RNF12_MOUSE	LDB2_MOUSE	Q9WTV7	O55203	Rlim	Ldb2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3482	RNF12_MOUSE	LIMK1_MOUSE	Q9WTV7	P53668	Rlim	Limk1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3483	RNF12_MOUSE	TERF1_MOUSE	Q9WTV7	P70371	Rlim	Terf1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3484	RNF12_MOUSE	HDAC2_MOUSE	Q9WTV7	P70288	Rlim	Hdac2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3485	RN123_MOUSE	CDN1B_MOUSE	Q5XPI3	P46414	Rnf123	Cdkn1b	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3486	RN125_MOUSE	DDX58_MOUSE	Q9D9R0	Q6Q899	Rnf125	Ddx58	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3487	RN128_MOUSE	SIR1_MOUSE	Q9D304	Q923E4	Rnf128	Sirt1	MEDLINE	33771967	E3 ubiquitin ligase <span class="match term0">Grail</span> promotes hepatic steatosis through <span class="match term1">Sirt1</span> inhibition	RING	1	Other	M.musculus
3488	RN135_MOUSE	DDX58_MOUSE	Q9CWS1	Q6Q899	Rnf135	Ddx58	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3489	R144A_MOUSE	PRKDC_MOUSE	Q925F3	P97313	Rnf144a	Prkdc	MEDLINE	34400221	<span class="match term0">RNF144A</span> is a DNA damage-induced E3 ubiquitin ligase that targets proteins involved in genome instability for degradation, e.g., <span class="match term1">DNA-PKcs</span> and BMI1	SINGLE_OTHER	1	Other	M.musculus
3490	R144A_MOUSE	PD1L1_MOUSE	Q925F3	Q9EP73	Rnf144a	Cd274	MEDLINE	34400221	<span class="match term0">RNF144A</span> interacts with <span class="match term1">PD-L1</span> in the plasma membrane and intracellular vesicles and promotes poly-ubiquitination and degradation of <span class="match term1">PD-L1</span>	SINGLE_OTHER	1	Other	M.musculus
3491	R144A_MOUSE	LN28B_MOUSE	Q925F3	Q45KJ6	Rnf144a	Lin28b	MEDLINE	33978933	Further analysis revealed that <span class="match term0">RNF144A</span> induced <span class="match term1">LIN28B</span> degradation through ubiquitination in EOC cells	SINGLE_OTHER	1	Other	M.musculus
3492	R144B_MOUSE	TYW4_MOUSE	Q8BKD6	Q8BYR1	Rnf144b	Lcmt2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3493	RN152_MOUSE	RHEB_MOUSE	Q8BG47	Q921J2	Rnf152	Rheb	MEDLINE	30514904	30514904	RING	1	Other	M.musculus
3494	RN170_MOUSE	TLR3_MOUSE	Q8CBG9	Q99MB1	Rnf170	Tlr3	MEDLINE	31076723	E3 ubiquitin ligase <span class="match term0">RNF170</span> inhibits innate immune responses by targeting and degrading <span class="match term1">TLR3</span> in murine cells	RING	1	Other	M.musculus
3495	RN180_MOUSE	ZIC2_MOUSE	Q3U827	Q62520	Rnf180	Zic2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3496	RN182_MOUSE	VATL_MOUSE	Q8C432	P63082	Rnf182	Atp6v0c	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3497	RN183_MOUSE	TR10B_MOUSE	Q8QZS5	Q9QZM4	Rnf183	Tnfrsf10b	MEDLINE	31889078	<span class="match term0">RNF183</span> mediated K63-linked ubiquitination and lysosomal degradation of <span class="match term1">DR5</span>	RING	1	Other	M.musculus
3498	RN186_MOUSE	EPHB2_MOUSE	Q9D241	P54763	Rnf186	Ephb2	MEDLINE	33280498	Upon stimulation by ligand EFNB1 (ephrin B1), <span class="match term1">EPHB2</span> is ubiquitinated by <span class="match term0">RNF186</span> at Lys892, and further recruits MAP1LC3B for autophagy	RING	1	Other	M.musculus
3499	RN19A_MOUSE	CASR_MOUSE	P50636	Q9QY96	Rnf19a	Casr	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3500	RN19A_MOUSE	SODC_MOUSE	P50636	P08228	Rnf19a	Sod1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3501	RN19B_MOUSE	UCKL1_MOUSE	A2A7Q9	Q91YL3	Rnf19b	Uckl1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3502	RING2_MOUSE	H2AB1_MOUSE	Q9CQJ4	Q9CQ70	Rnf2	H2ab1	MEDLINE	31403616	31403616	RING	1	Other	M.musculus
3503	RING2_MOUSE	RING2_MOUSE	Q9CQJ4	Q9CQJ4	Rnf2	Rnf2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3504	RING2_MOUSE	RYBP_MOUSE	Q9CQJ4	Q8CCI5	Rnf2	Rybp	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3505	BRE1A_MOUSE	H2B1A_MOUSE	Q5DTM8	P70696	Rnf20	H2bc1	MEDLINE	30692271	<span class="match term0">RNF20</span>/RNF40-mediated monoubiquitination of histone H2B on lysine 120 (H2Bub) has been suggested as a potential mediator of DSB repair, although the nature and function of this posttranslational modification remain enigmatic.	RING	1	Other	M.musculus
3506	RN216_MOUSE	RN216_MOUSE	P58283	P58283	Rnf216	Rnf216	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3507	RN216_MOUSE	KAPCB_MOUSE	P58283	P68181	Rnf216	Prkacb	MEDLINE	33724554	<span class="match term0">RNF216</span> interacts with <span class="match term1">PRKACB</span> and promotes its degradation through the ubiquitin-lysosome pathway	RING	1	Other	M.musculus
3508	RN220_MOUSE	TADBP_MOUSE	Q6PDX6	Q921F2	Rnf220	Tardbp	MEDLINE	33386850	Haploinsufficiency of the TDP43 ubiquitin E3 ligase <span class="match term0">RNF220</span> leads to ALS-like motor neuron defects in the mouse	RING	1	Other	M.musculus
3509	RN220_MOUSE	SIN3B_MOUSE	Q6PDX6	Q62141	Rnf220	Sin3b	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3510	RN220_MOUSE	A0A087WSP5_MOUSE	Q6PDX6	A0A087WSP5	Rnf220	Stat1	MEDLINE	32814877	<span class="match term0">RNF220</span> mediates K63-linked polyubiquitination of <span class="match term1">STAT1</span> and promotes host defense	RING	1	Other	M.musculus
3511	RN220_MOUSE	RN220_MOUSE	Q6PDX6	Q6PDX6	Rnf220	Rnf220	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3512	RNF31_MOUSE	A0A087WSP5_MOUSE	Q924T7	A0A087WSP5	Rnf31	Stat1	MEDLINE	32123171	Collectively, our findings demonstrated that cellular <span class="match term1">STAT1</span> undergoes <span class="match term0">HOIP</span>-induced linear ubiquitination.	RING	1	Other	M.musculus
3513	RNF31_MOUSE	TNAP3_MOUSE	Q924T7	Q60769	Rnf31	Tnfaip3	MEDLINE	34416243	<span class="match term0">RNF31</span> mediated ubiquitination of <span class="match term1">A20</span> aggravates inflammation and hepatocyte apoptosis through the TLR4/MyD88/NF-kappaB signaling pathway	RING	1	Other	M.musculus
3514	RNF34_MOUSE	CY24A_MOUSE	Q99KR6	Q61462	Rnf34	Cyba	MEDLINE	34015492	<span class="match term0">RNF34</span> deletion increased p22phox protein stability by inhibiting ubiquitin-mediated degradation	RING	1	Other	M.musculus
3515	RNF34_MOUSE	PRGC1_MOUSE	Q99KR6	O70343	Rnf34	Ppargc1a	MEDLINE	31704983	<span class="match term0">RNF34</span> interacted with <span class="match term1">PGC-1alpha</span> and targeted it for ubiquitin-dependent degradation	RING	1	Other	M.musculus
3516	RNF4_MOUSE	RNF4_MOUSE	Q9QZS2	Q9QZS2	Rnf4	Rnf4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3517	RNF4_MOUSE	ETV4_MOUSE	Q9QZS2	P28322	Rnf4	Etv4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3518	RNF4_MOUSE	PARP1_MOUSE	Q9QZS2	P11103	Rnf4	Parp1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3519	BRE1B_MOUSE	H2B1A_MOUSE	Q3U319	P70696	Rnf40	H2bc1	MEDLINE	30692271	E3 Ubiquitin Ligases RNF20 and <span class="match term0">RNF40</span> Are Required for Double-Stranded Break (DSB) Repair: Evidence for Monoubiquitination of Histone H2B Lysine 120 as a Novel Axis of DSB Signaling and Repair. Taken together, these data lead us to hypothesize that RNF20- and <span class="match term0">RNF40</span>-mediated H2B ubiquitination in response to DSBs may represent an independent yet uncharacterized pathway for DSB signaling.	RING	1	Other	M.musculus
3520	RNF41_MOUSE	ERBB3_MOUSE	Q8BH75	Q61526	Rnf41	Erbb3	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3521	RNF41_MOUSE	CLC9A_MOUSE	Q8BH75	Q8BRU4	Rnf41	Clec9a	MEDLINE	33264090	Intriguingly, <span class="match term0">RNF41</span> regulates the downstream fate of <span class="match term1">Clec9A</span> by directly binding and ubiquitinating the extracellular domains of <span class="match term1">Clec9A</span>	RING	1	Other	M.musculus
3522	RNF41_MOUSE	CEBPA_MOUSE	Q8BH75	P53566	Rnf41	Cebpa	MEDLINE	32351331	Upregulation of <span class="match term0">Nrdp1</span> in macrophages significantly promoted M2 macrophage polarization via ubiquitinating and activating C/EBP-beta	RING	1	Other	M.musculus
3523	RNF41_MOUSE	RNF41_MOUSE	Q8BH75	Q8BH75	Rnf41	Rnf41	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3524	RNF43_MOUSE	RNF43_MOUSE	Q5NCP0	Q5NCP0	Rnf43	Rnf43	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3525	RNF5_MOUSE	S10A8_MOUSE	O35445	P27005	Rnf5	S100a8	MEDLINE	30232010	<span class="match term1">S100A8</span> is identified as an <span class="match term0">RNF5</span> substrate, resulting in <span class="match term1">S100A8</span> ubiquitination and proteasomal-dependent degradation that is attenuated upon inflammatory stimuli	RING	1	Other	M.musculus
3526	RNF5_MOUSE	PAXI_MOUSE	O35445	Q8VI36	Rnf5	Pxn	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3527	RNF5_MOUSE	JKAMP_MOUSE	O35445	Q8BI36	Rnf5	Jkamp	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3528	RNF5_MOUSE	STING_MOUSE	O35445	Q3TBT3	Rnf5	Sting1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3529	RNF5_MOUSE	SYVN1_MOUSE	O35445	Q9DBY1	Rnf5	Syvn1	MEDLINE	34272738	<span class="match term0">RNF5</span> directly bound to <span class="match term1">HRD1</span> and promoted its lysine 48 (K48)- and K33-linked ubiquitination and subsequent proteasomal degradation	RING	1	Other	M.musculus
3530	RNF6_MOUSE	ANDR_MOUSE	Q9DBU5	P19091	Rnf6	Ar	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3531	RNF6_MOUSE	LIMK1_MOUSE	Q9DBU5	P53668	Rnf6	Limk1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3532	RNF8_MOUSE	AKT1_MOUSE	Q8VC56	P31750	Rnf8	Akt1	MEDLINE	32597970	Furthermore, <span class="match term0">RNF8</span> bound to <span class="match term1">AKT1</span> and mediated its ubiquitination	RING	1	Other	M.musculus
3533	RNF8_MOUSE	H2AB1_MOUSE	Q8VC56	Q9CQ70	Rnf8	H2ab1	MEDLINE	28825854	28825854	RING	1	Other	M.musculus
3534	RNF8_MOUSE	H2B1F_MOUSE	Q8VC56	P10853	Rnf8	H2bc7	MEDLINE	28825854	28825854	RING	1	Other	M.musculus
3535	SIA1A_MOUSE	EGLN1_MOUSE	P61092	Q91YE3	Siah1a	Egln1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3536	SIA1A_MOUSE	MYB_MOUSE	P61092	P06876	Siah1a	Myb	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3537	SIA1A_MOUSE	CTNB1_MOUSE	P61092	Q02248	Siah1a	Ctnnb1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3538	SIA1A_MOUSE	PML_MOUSE	P61092	Q60953	Siah1a	Pml	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3539	SIA1A_MOUSE	EGLN3_MOUSE	P61092	Q91UZ4	Siah1a	Egln3	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3540	SIA1A_MOUSE	PLCE1_MOUSE	P61092	Q8K4S1	Siah1a	Plce1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3541	SIAH2_MOUSE	DYRK2_MOUSE	Q06986	Q5U4C9	Siah2	Dyrk2	MEDLINE	31515251	In addition to transcriptional regulation, stabilization of <span class="match term1">DYRK2</span> protein by inhibiting ubiquitin E3 ligase <span class="match term0">SIAH2</span> with vitamin K3 promoted apoptosis and abrogated self-renewal in murine and human CML stem/progenitor cells	RING	1	Other	M.musculus
3542	SIAH2_MOUSE	EGLN3_MOUSE	Q06986	Q91UZ4	Siah2	Egln3	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3543	SIAH2_MOUSE	LATS2_MOUSE	Q06986	Q7TSJ6	Siah2	Lats2	MEDLINE	25438054	UbiNet 2.0	RING	1	Other	M.musculus
3544	SIAH2_MOUSE	NCOR1_MOUSE	Q06986	Q60974	Siah2	Ncor1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3545	SIAH2_MOUSE	PML_MOUSE	Q06986	Q60953	Siah2	Pml	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3546	SIAH2_MOUSE	EGLN1_MOUSE	Q06986	Q91YE3	Siah2	Egln1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3547	SIAH2_MOUSE	TRAF2_MOUSE	Q06986	P39429	Siah2	Traf2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3548	SIAH2_MOUSE	NAC3_MOUSE	Q06986	S4R2P9	Siah2	Slc8a3	MEDLINE	32164721	Moreover, activation of the E3 ubiquitin ligase <span class="match term0">SIAH2</span> impaired mitochondrial integrity by promoting proteolytic degradation of <span class="match term1">NCX3</span> and consequent Ca2+ overload into mitochondria during OGD and reoxygenation.	RING	1	Other	M.musculus
3549	SIAH2_MOUSE	AKAP1_MOUSE	Q06986	O08715	Siah2	Akap1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3550	SIAH2_MOUSE	PLCE1_MOUSE	Q06986	Q8K4S1	Siah2	Plce1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3551	SKP2_MOUSE	CCNE1_MOUSE	Q9Z0Z3	Q61457	Skp2	Ccne1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3552	SKP2_MOUSE	CDN1A_MOUSE	Q9Z0Z3	P39689	Skp2	Cdkn1a	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3553	SKP2_MOUSE	CTNB1_MOUSE	Q9Z0Z3	Q02248	Skp2	Ctnnb1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3554	SKP2_MOUSE	MYC_MOUSE	Q9Z0Z3	P01108	Skp2	Myc	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3555	SKP2_MOUSE	IKBE_MOUSE	Q9Z0Z3	O54910	Skp2	Nfkbie	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3556	SKP2_MOUSE	IKBB_MOUSE	Q9Z0Z3	Q60778	Skp2	Nfkbib	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3557	SKP2_MOUSE	UBP18_MOUSE	Q9Z0Z3	Q9WTV6	Skp2	Usp18	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3558	SKP2_MOUSE	CDN1B_MOUSE	Q9Z0Z3	P46414	Skp2	Cdkn1b	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3559	SKP2_MOUSE	BECN1_MOUSE	Q9Z0Z3	O88597	Skp2	Becn1	MEDLINE	34428336	Co-immunoprecipitation and ubiquitination assays suggested that <span class="match term0">SKP2</span> induced K48-linked ubiquitination of <span class="match term1">Beclin1</span>	F-box	1	Other	M.musculus
3560	SKP2_MOUSE	IKBA_MOUSE	Q9Z0Z3	Q9Z1E3	Skp2	Nfkbia	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3561	SKP2_MOUSE	FOXO1_MOUSE	Q9Z0Z3	Q9R1E0	Skp2	Foxo1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3562	SKP2_MOUSE	FGD1_MOUSE	Q9Z0Z3	P52734	Skp2	Fgd1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3563	SKP2_MOUSE	CDN1C_MOUSE	Q9Z0Z3	P49919	Skp2	Cdkn1c	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3564	SMUF1_MOUSE	M3K2_MOUSE	Q9CUN6	Q61083	Smurf1	Map3k2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3565	SMUF1_MOUSE	SMAD5_MOUSE	Q9CUN6	P97454	Smurf1	Smad5	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3566	SMUF1_MOUSE	TRAF3_MOUSE	Q9CUN6	Q60803	Smurf1	Traf3	MEDLINE	29734366	Importantly, RNA virus infection promotes the binding of <span class="match term0">Smurf1</span> to MAVS, <span class="match term1">TRAF3</span> and TRAF6, which leads to ubiquitination-dependent degradation of every component of the MAVS/<span class="match term1">TRAF3</span>/TRAF6 signalosome and subsequent potent inhibition of IFNs production	HECT	1	Other	M.musculus
3567	SMUF1_MOUSE	RHOA_MOUSE	Q9CUN6	Q9QUI0	Smurf1	Rhoa	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3568	SMUF1_MOUSE	RUNX2_MOUSE	Q9CUN6	Q08775	Smurf1	Runx2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3569	SMUF1_MOUSE	CIKS_MOUSE	Q9CUN6	Q8N7N6	Smurf1	Traf3ip2	MEDLINE	34183666	We demonstrate that <span class="match term0">SMURF1</span> ubiquitin ligase activity is essential for <span class="match term1">TRAF3IP2</span> ubiquitination and activation of NF-kappaB-mediate beta-cell apoptosis	HECT	1	Other	M.musculus
3570	SMUF1_MOUSE	SMAD1_MOUSE	Q9CUN6	P70340	Smurf1	Smad1	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3571	SMUF2_MOUSE	SATB1_MOUSE	A2A5Z6	Q60611	Smurf2	Satb1	MEDLINE	30742943	Furthermore, we identified <span class="match term0">SMURF2</span> as an E3 ubiquitin ligase that promotes <span class="match term1">SATB1</span> degradation by upregulating its ubiquitination, and its deficiency promotes colon cancer cell proliferation and <span class="match term1">SATB1</span> target gene transcription	HECT	1	Other	M.musculus
3572	SMUF2_MOUSE	TYY1_MOUSE	A2A5Z6	Q00899	Smurf2	Yy1	MEDLINE	33722608	<span class="match term0">Smurf2</span> elevated <span class="match term1">YY1</span> ubiquitination and degradation, and <span class="match term1">YY1</span> increased HIF1alpha expression to promote DDIT4 in neurons	HECT	1	Other	M.musculus
3573	SMUF2_MOUSE	SMAD7_MOUSE	A2A5Z6	O35253	Smurf2	Smad7	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3574	SMUF2_MOUSE	STABP_MOUSE	A2A5Z6	Q9CQ26	Smurf2	Stambp	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3575	SMUF2_MOUSE	GSK3A_MOUSE	A2A5Z6	Q2NL51	Smurf2	Gsk3a	MEDLINE	33168412	Furthermore, LINC00671 induced GSK-3beta ubiquitination and upregulated beta-catenin expression through <span class="match term0">Smurf2</span>	HECT	1	Other	M.musculus
3576	SMUF2_MOUSE	CTNB1_MOUSE	A2A5Z6	Q02248	Smurf2	Ctnnb1	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3577	SMUF2_MOUSE	BRE1A_MOUSE	A2A5Z6	Q5DTM8	Smurf2	Rnf20	MEDLINE	33097595	These data indicate that <span class="match term0">SMURF2</span>-mediated <span class="match term1">RNF20</span> ubiquitination and degradation controlled by ATM-induced phosphorylation at S384 constitutes a negative feedback loop that regulates DSB repair.	HECT	1	Other	M.musculus
3578	SMUF2_MOUSE	RUNX2_MOUSE	A2A5Z6	Q08775	Smurf2	Runx2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3579	SMUF2_MOUSE	RAP1B_MOUSE	A2A5Z6	Q99JI6	Smurf2	Rap1b	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3580	SOCS1_MOUSE	TF65_MOUSE	O35716	Q04207	Socs1	Rela	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	M.musculus
3581	SOCS1_MOUSE	IRS1_MOUSE	O35716	P35569	Socs1	Irs1	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	M.musculus
3582	SOCS1_MOUSE	IRS2_MOUSE	O35716	P81122	Socs1	Irs2	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	M.musculus
3583	SOCS2_MOUSE	SOCS3_MOUSE	O35717	O35718	Socs2	Socs3	MEDLINE	22199232	E3Net	Other	1	Other	M.musculus
3584	SOCS3_MOUSE	IRS2_MOUSE	O35718	P81122	Socs3	Irs2	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	M.musculus
3585	SOCS3_MOUSE	IRS1_MOUSE	O35718	P35569	Socs3	Irs1	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	M.musculus
3586	SPOP_MOUSE	BMI1_MOUSE	Q6ZWS8	P25916	Spop	Bmi1	MEDLINE	22199232	E3Net	Other	1	Other	M.musculus
3587	SPOP_MOUSE	H2AY_MOUSE	Q6ZWS8	Q9QZQ8	Spop	Macroh2a1	MEDLINE	22199232	E3Net	Other	1	Other	M.musculus
3588	SPOP_MOUSE	MYC_MOUSE	Q6ZWS8	P01108	Spop	Myc	MEDLINE	28414305	<span class="match term0">SPOP</span> regulates prostate epithelial cell proliferation and promotes ubiquitination and turnover of c-<span class="match term1">MYC</span> oncoprotein.	Other	1	Other	M.musculus
3589	SPOP_MOUSE	ODPX_MOUSE	Q6ZWS8	Q8BKZ9	Spop	Pdhx	MEDLINE	20811152	UbiNet 2.0	Other	1	Other	M.musculus
3590	SPOP_MOUSE	DAXX_MOUSE	Q6ZWS8	O35613	Spop	Daxx	MEDLINE	22199232	E3Net	Other	1	Other	M.musculus
3591	SPSB1_MOUSE	CDN1A_MOUSE	Q9D5L7	P39689	Spsb1	Cdkn1a	MEDLINE	30712944	Notably, mechanistic investigations revealed that <span class="match term0">SPSB1</span> accelerated <span class="match term1">p21</span> destabilization by directly interacting with <span class="match term1">p21</span> and promoting its ubiquitin-mediated proteasomal degradation	SOCS_VHL_BC-box	1	Other	M.musculus
3592	CHIP_MOUSE	M3K12_MOUSE	Q9WUD1	Q60700	Stub1	Map3k12	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3593	CHIP_MOUSE	GATA4_MOUSE	Q9WUD1	Q08369	Stub1	Gata4	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3594	CHIP_MOUSE	TAU_MOUSE	Q9WUD1	P10637	Stub1	Mapt	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3595	CHIP_MOUSE	RUNX2_MOUSE	Q9WUD1	Q08775	Stub1	Runx2	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3596	CHIP_MOUSE	HD_MOUSE	Q9WUD1	P42859	Stub1	Htt	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3597	CHIP_MOUSE	AHR_MOUSE	Q9WUD1	P30561	Stub1	Ahr	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3598	CHIP_MOUSE	SODC_MOUSE	Q9WUD1	P08228	Stub1	Sod1	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3599	CHIP_MOUSE	DLK1_MOUSE	Q9WUD1	Q09163	Stub1	Dlk1	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3600	CHIP_MOUSE	NOS1_MOUSE	Q9WUD1	Q9Z0J4	Stub1	Nos1	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3601	CHIP_MOUSE	CHIP_MOUSE	Q9WUD1	Q9WUD1	Stub1	Stub1	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3602	CHIP_MOUSE	SGK1_MOUSE	Q9WUD1	Q9WVC6	Stub1	Sgk1	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3603	CHIP_MOUSE	AKT1_MOUSE	Q9WUD1	P31750	Stub1	Akt1	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3604	CHIP_MOUSE	RAF1_MOUSE	Q9WUD1	Q99N57	Stub1	Raf1	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3605	CHIP_MOUSE	HSP7C_MOUSE	Q9WUD1	P63017	Stub1	Hspa8	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3606	CHIP_MOUSE	ESR1_MOUSE	Q9WUD1	P19785	Stub1	Esr1	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3607	CHIP_MOUSE	MKKS_MOUSE	Q9WUD1	Q9JI70	Stub1	Mkks	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3608	CHIP_MOUSE	SMAD3_MOUSE	Q9WUD1	Q8BUN5	Stub1	Smad3	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3609	SYVN1_MOUSE	P53_MOUSE	Q9DBY1	P02340	Syvn1	Tp53	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3610	SYVN1_MOUSE	SGK1_MOUSE	Q9DBY1	Q9WVC6	Syvn1	Sgk1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3611	SYVN1_MOUSE	MAFA_MOUSE	Q9DBY1	Q8CF90	Syvn1	Mafa	MEDLINE	32086291	Furthermore, mechanistic assay results indicate that <span class="match term0">HRD1</span> is a novel E3 ubiquitin ligase that targets <span class="match term1">MafA</span> for ubiquitination and degradation in diabetic beta-cells, resulting in cytoplasmic accumulation of <span class="match term1">MafA</span> and in the reduction of its biological function in the nucleus	RING	1	Other	M.musculus
3612	SYVN1_MOUSE	ERN1_MOUSE	Q9DBY1	Q9EQY0	Syvn1	Ern1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3613	SYVN1_MOUSE	PFKAP_MOUSE	Q9DBY1	Q9WUA3	Syvn1	Pfkp	MEDLINE	33588886	Mechanistically, <span class="match term0">HRD1</span> interacted and colocalized with <span class="match term1">PFKP</span> in the cytoplasm, targeted <span class="match term1">PFKP</span> for ubiquitination and degradation, and ultimately reduced <span class="match term1">PFKP</span> expression and activity in breast cancer cells	RING	1	Other	M.musculus
3614	SYVN1_MOUSE	NICA_MOUSE	Q9DBY1	P57716	Syvn1	Ncstn	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3615	SYVN1_MOUSE	NF2L2_MOUSE	Q9DBY1	Q60795	Syvn1	Nfe2l2	MEDLINE	33654072	Furthermore, <span class="match term0">HRD1</span> served as an E3-ligase to facilitate the downregulation of <span class="match term1">NRF2</span> through ubiquitination-degradation pathway, and the QSLVPDI motif on <span class="match term1">NRF2</span> constituted an active site for its interaction with <span class="match term0">HRD1</span>	RING	1	Other	M.musculus
3616	SYVN1_MOUSE	MAVS_MOUSE	Q9DBY1	Q8VCF0	Syvn1	Mavs	MEDLINE	32943610	Gain- and loss-of-function experiments indicated that Mfn2 interacted with <span class="match term1">MAVS</span> and recruited E3 ligase <span class="match term0">SYVN1</span> to promote the polyubiquitination of <span class="match term1">MAVS</span>	RING	1	Other	M.musculus
3617	TBL1X_MOUSE	CTNB1_MOUSE	Q9QXE7	Q02248	Tbl1x	Ctnnb1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3618	BACD2_MOUSE	RHOA_MOUSE	O70479	Q9QUI0	Tnfaip1	Rhoa	MEDLINE	22199232	E3Net	BTB_OTHER	1	Other	M.musculus
3619	TOPRS_MOUSE	NKX31_MOUSE	Q80Z37	P97436	Topors	Nkx3-1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3620	TRAF2_MOUSE	TRAF3_MOUSE	P39429	Q60803	Traf2	Traf3	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3621	TRAF2_MOUSE	SRC_MOUSE	P39429	P05480	Traf2	Src	MEDLINE	31619538	<span class="match term1">Src</span> undergoes polyinosinic:polycytidylic acid-dependent lysine 63 chain ubiquitination, and <span class="match term0">TRAF2</span> is a direct E3 ligase for <span class="match term1">Src</span>	RING	1	Other	M.musculus
3622	TRAF2_MOUSE	LST8_MOUSE	P39429	Q9DCJ1	Traf2	Mlst8	MEDLINE	28489822	UbiNet 2.0	RING	1	Other	M.musculus
3623	TRAF2_MOUSE	M3K14_MOUSE	P39429	Q9WUL6	Traf2	Map3k14	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3624	TRAF3_MOUSE	TNAP3_MOUSE	Q60803	Q60769	Traf3	Tnfaip3	MEDLINE	29720226	29720226	RING	1	Other	M.musculus
3625	TRAF3_MOUSE	M3K14_MOUSE	Q60803	Q9WUL6	Traf3	Map3k14	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3626	TRAF6_MOUSE	M3K5_MOUSE	P70196	O35099	Traf6	Map3k5	MEDLINE	31222801	Conclusion: These results suggest that Lys6-linked polyubiquitination of <span class="match term1">ASK1</span> by <span class="match term0">TRAF6</span> represents a mechanism underlying <span class="match term1">ASK1</span> activation in hepatocytes and a key driving force of proinflammatory and profibrogenic responses in NASH	RING	1	Other	M.musculus
3627	TRAF6_MOUSE	BIRC3_MOUSE	P70196	O08863	Traf6	Birc3	MEDLINE	19898473	UbiNet 2.0	RING	1	Other	M.musculus
3628	TRAF6_MOUSE	TRAF6_MOUSE	P70196	P70196	Traf6	Traf6	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3629	TRAF6_MOUSE	EZH2_MOUSE	P70196	Q61188	Traf6	Ezh2	MEDLINE	33996254	<span class="match term0">TRAF6</span> mediated the ubiquitination of <span class="match term1">EZH2</span> and increased miR-429 expression, and miR-429 targeted PPARalpha	RING	1	Other	M.musculus
3630	TRAF6_MOUSE	NR2C2_MOUSE	P70196	P49117	Traf6	Nr2c2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3631	TRAF6_MOUSE	AKT1_MOUSE	P70196	P31750	Traf6	Akt1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3632	TRAF6_MOUSE	BIRC2_MOUSE	P70196	Q62210	Traf6	Birc2	MEDLINE	19898473	UbiNet 2.0	RING	1	Other	M.musculus
3633	TRAF6_MOUSE	FOXP3_MOUSE	P70196	Q99JB6	Traf6	Foxp3	MEDLINE	30886050	We further determined that <span class="match term1">FOXP3</span> undergoes K63-linked ubiquitination at lysine 262 mediated by the E3 ligase <span class="match term0">TRAF6</span>	RING	1	Other	M.musculus
3634	TRAF6_MOUSE	CASP8_MOUSE	P70196	O89110	Traf6	Casp8	MEDLINE	30979779	TP53INP2 binds caspase-8 and the ubiquitin ligase <span class="match term0">TRAF6</span>, thereby promoting the ubiquitination and activation of caspase-8 by <span class="match term0">TRAF6</span>	RING	1	Other	M.musculus
3635	TRAF6_MOUSE	M3K7_MOUSE	P70196	Q62073	Traf6	Map3k7	MEDLINE	33987665	From a mechanistic perspective, MTDH recruited <span class="match term0">TRAF6</span> to <span class="match term1">TAK1</span>, leading to <span class="match term0">TRAF6</span>-mediated <span class="match term1">TAK1</span> K63 ubiquitination and phosphorylation, ultimately facilitating TLR-induced NF-kappaB and MAPK signaling	RING	1	Other	M.musculus
3636	TRAF6_MOUSE	ECSIT_MOUSE	P70196	Q9QZH6	Traf6	Ecsit	MEDLINE	31281713	Interestingly, p62-<span class="match term1">ECSIT</span> interaction inhibited the interaction between <span class="match term0">TRAF6</span> and <span class="match term1">ECSIT</span> and attenuated the ubiquitination of <span class="match term1">ECSIT</span>	RING	1	Other	M.musculus
3637	TRAF6_MOUSE	TNAP3_MOUSE	P70196	Q60769	Traf6	Tnfaip3	MEDLINE	29720226	29720226	RING	1	Other	M.musculus
3638	TRAF6_MOUSE	RAB7A_MOUSE	P70196	P51150	Traf6	Rab7a	MEDLINE	31932498	In mature endosomes, <span class="match term1">RAB7</span> directly interacts with <span class="match term0">TRAF6</span> E3 ubiquitin ligase, which catalyzes K63 polyubiquitination for NF-kappaB activation	RING	1	Other	M.musculus
3639	TRAF6_MOUSE	NEMO_MOUSE	P70196	O88522	Traf6	Ikbkg	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3640	TRAF6_MOUSE	RIPK2_MOUSE	P70196	P58801	Traf6	Ripk2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3641	TRI10_MOUSE	PTEN_MOUSE	Q9WUH5	O08586	Trim10	Pten	MEDLINE	32343488	The results of this study reveal the involvement of <span class="match term0">TRIM10</span> in pathological cardiac hypertrophy, which may occur by prompting of <span class="match term1">PTEN</span> ubiquitination and subsequent activation of AKT signalling	RING	1	Other	M.musculus
3642	TRI11_MOUSE	PAX6_MOUSE	Q99PQ2	P63015	Trim11	Pax6	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3643	TRI11_MOUSE	MED15_MOUSE	Q99PQ2	Q924H2	Trim11	Med15	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3644	TRI13_MOUSE	DDIT3_MOUSE	Q9CYB0	P35639	Trim13	Ddit3	MEDLINE	31901873	These data suggested that <span class="match term0">TRIM13</span> targeted <span class="match term1">CHOP</span> for ubiquitination	RING	1	Other	M.musculus
3645	TRI17_MOUSE	TRI17_MOUSE	Q7TPM3	Q7TPM3	Trim17	Trim17	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3646	TRIM2_MOUSE	NFL_MOUSE	Q9ESN6	P08551	Trim2	Nefl	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3647	RO52_MOUSE	IKKB_MOUSE	Q62191	O88351	Trim21	Ikbkb	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3648	RO52_MOUSE	IRF8_MOUSE	Q62191	P23611	Trim21	Irf8	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3649	Q3U7K7_MOUSE	DDX41_MOUSE	Q3U7K7	Q91VN6	Trim21	Ddx41	MEDLINE	31755557	<span class="match term0">TRIM21</span> is an IFN-stimulated E3 ligase that controls the activity of pattern-recognition signaling via ubiquitination of IFN-regulatory factors (IRF) and <span class="match term1">DDX41</span>	Other	1	Other	M.musculus
3650	Q3U7K7_MOUSE	NUP62_MOUSE	Q3U7K7	Q63850	Trim21	Nup62	MEDLINE	34233258	We recently reported that the ubiquitin E3 ligase <span class="match term0">TRIM21</span> interacts and ubiquitylates <span class="match term1">p62</span> and negatively regulates the <span class="match term1">p62</span>-Keap1-Nrf2 antioxidant pathway	Other	1	Other	M.musculus
3651	Q3U7K7_MOUSE	PD1L1_MOUSE	Q3U7K7	Q9EP73	Trim21	Cd274	MEDLINE	34130052	The <span class="match term1">PD-L1</span> protein degradation is mediated by E3 ligase <span class="match term0">TRIM21</span> via ubiquitination-proteasome pathway	Other	1	Other	M.musculus
3652	Q3U7K7_MOUSE	SOCS3_MOUSE	Q3U7K7	O35718	Trim21	Socs3	MEDLINE	33815395	We found that <span class="match term1">SOCS3</span> in thymic epithelial cells (TECs) binds to the E3 ubiquitin ligase TRIM 21 and that <span class="match term0">Trim21</span> -/- mice showed increased thymic cellularity	Other	1	Other	M.musculus
3653	Q3U7K7_MOUSE	ANO1_MOUSE	Q3U7K7	Q8BHY3	Trim21	Ano1	MEDLINE	33957127	In vitro and in vivo assays demonstrated that whereas TRIM23 ubiquitinated <span class="match term1">ANO1</span> leading to its stabilization, <span class="match term0">TRIM21</span> ubiquitinated <span class="match term1">ANO1</span> and induced its degradation	Other	1	Other	M.musculus
3654	RO52_MOUSE	UBP4_MOUSE	Q62191	P35123	Trim21	Usp4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3655	TRI23_MOUSE	ANO1_MOUSE	Q8BGX0	Q8BHY3	Trim23	Ano1	MEDLINE	33957127	In vitro and in vivo assays demonstrated that whereas <span class="match term0">TRIM23</span> ubiquitinated <span class="match term1">ANO1</span> leading to its stabilization, TRIM21 ubiquitinated <span class="match term1">ANO1</span> and induced its degradation	RING	1	Other	M.musculus
3656	TRI25_MOUSE	DDX58_MOUSE	Q61510	Q6Q899	Trim25	Ddx58	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3657	TRI25_MOUSE	IFIH1_MOUSE	Q61510	Q8R5F7	Trim25	Ifih1	MEDLINE	30193849	ZCCHC3 also recruited the E3 ubiquitin ligase <span class="match term0">TRIM25</span> to the RIG-I and <span class="match term1">MDA5</span> complexes to facilitate its K63-linked polyubiquitination and activation	RING	1	Other	M.musculus
3658	TRI25_MOUSE	PPARG_MOUSE	Q61510	P37238	Trim25	Pparg	MEDLINE	30323259	Taken together, these data indicate that <span class="match term0">TRIM25</span> is a novel E3 ubiquitin ligase of <span class="match term1">PPARgamma</span> and that <span class="match term0">TRIM25</span> is a novel target for <span class="match term1">PPARgamma</span>-associated metabolic diseases.	RING	1	Other	M.musculus
3659	TRI26_MOUSE	XCT_MOUSE	Q99PN3	Q9WTR6	Trim26	Slc7a11	MEDLINE	33869196	In conclusion, <span class="match term0">TRIM26</span> promotes HSCs ferroptosis to suppress liver fibrosis through mediating the ubiquitination of <span class="match term1">SLC7A11</span>	RING	1	Other	M.musculus
3660	TIF1B_MOUSE	B2LA1_MOUSE	Q62318	Q07440	Trim28	Bcl2a1	MEDLINE	30042493	Indeed, endogenous <span class="match term0">TRIM28</span> and <span class="match term1">BCL2A1</span> bind to each other at the mitochondria and <span class="match term0">TRIM28</span> knock-down decreases <span class="match term1">BCL2A1</span> ubiquitination	RING	1	Other	M.musculus
3661	TRIM3_MOUSE	TLR3_MOUSE	Q9R1R2	Q99MB1	Trim3	Tlr3	MEDLINE	32878999	<span class="match term0">TRIM3</span> mediates K63-linked polyubiquitination of <span class="match term1">TLR3</span> at K831, which is enhanced following poly(I:C) stimulation	RING	1	Other	M.musculus
3662	TRI31_MOUSE	MAVS_MOUSE	Q8R0K2	Q8VCF0	Trim31	Mavs	MEDLINE	31149635	MAM-localized Rac1 limits <span class="match term1">MAVS</span>' interaction with E3 ligase <span class="match term0">Trim31</span> and hence inhibits <span class="match term1">MAVS</span> ubiquitination, aggregation, and activation	RING	1	Other	M.musculus
3663	TRI31_MOUSE	TRI31_MOUSE	Q8R0K2	Q8R0K2	Trim31	Trim31	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3664	TRI32_MOUSE	MYC_MOUSE	Q8CH72	P01108	Trim32	Myc	MEDLINE	29899379	A complex of the ubiquitin ligase <span class="match term0">TRIM32</span> and the deubiquitinase USP7 balances the level of c-<span class="match term1">Myc</span> ubiquitination and thereby determines neural stem cell fate specification.	RING	1	Other	M.musculus
3665	TRI32_MOUSE	PIAS4_MOUSE	Q8CH72	Q9JM05	Trim32	Pias4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3666	TRI32_MOUSE	TRI32_MOUSE	Q8CH72	Q8CH72	Trim32	Trim32	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3667	TRI32_MOUSE	DTBP1_MOUSE	Q8CH72	Q91WZ8	Trim32	Dtnbp1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3668	TRI32_MOUSE	ABI2_MOUSE	Q8CH72	P62484	Trim32	Abi2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3669	TRI33_MOUSE	SMAD4_MOUSE	Q99PP7	P97471	Trim33	Smad4	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3670	TRI37_MOUSE	TRI37_MOUSE	Q6PCX9	Q6PCX9	Trim37	Trim37	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3671	Q5SZ99_MOUSE	TRAF6_MOUSE	Q5SZ99	P70196	Trim38	Traf6	MEDLINE	22323536	E3 ubiquitin ligase tripartite motif 38 negatively regulates TLR-mediated immune responses by proteasomal degradation of TNF receptor-associated factor 6 in macrophages.	RING	1	Other	M.musculus
3672	TRI47_MOUSE	FOXO1_MOUSE	Q8C0E3	Q9R1E0	Trim47	Foxo1	MEDLINE	33408486	<span class="match term0">TRIM47</span> Promotes the Development of Glioma by Ubiquitination and Degradation of <span class="match term1">FOXO1</span>	RING	1	Other	M.musculus
3673	TRI56_MOUSE	STING_MOUSE	Q80VI1	Q3TBT3	Trim56	Sting1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3674	TRI59_MOUSE	ABHD5_MOUSE	Q922Y2	Q9DBL9	Trim59	Abhd5	MEDLINE	32867817	Mechanistic investigations revealed that <span class="match term0">TRIM59</span> physically interacts with abhydrolase domain containing 5 (<span class="match term1">ABHD5</span>) and directly induced the ubiquitination of <span class="match term1">ABHD5</span> and led to its proteasome-dependent degradation	RING	1	Other	M.musculus
3675	TRI63_MOUSE	MLRV_MOUSE	Q38HM4	P51667	Trim63	Myl2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3676	TRI63_MOUSE	MYPC2_MOUSE	Q38HM4	Q5XKE0	Trim63	Mybpc2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3677	TRI63_MOUSE	TNNI3_MOUSE	Q38HM4	P48787	Trim63	Tnni3	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3678	TRI63_MOUSE	KCRM_MOUSE	Q38HM4	P07310	Trim63	Ckm	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3679	TRI63_MOUSE	MLRS_MOUSE	Q38HM4	P97457	Trim63	Mylpf	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3680	TRI63_MOUSE	MYL1_MOUSE	Q38HM4	P05977	Trim63	Myl1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3681	TRI65_MOUSE	DUS6_MOUSE	Q8BFW4	Q9DBB1	Trim65	Dusp6	MEDLINE	33146694	<span class="match term0">TRIM65</span> promoted the cell proliferation and invasion of EMS cells via the ERK1/2/C-myc pathway through ubiquitination of <span class="match term1">DUSP6</span>	RING	1	Other	M.musculus
3682	TRI65_MOUSE	RHG35_MOUSE	Q8BFW4	Q91YM2	Trim65	Arhgap35	MEDLINE	31332286	Ubiquitin ligase <span class="match term0">TRIM65</span> promotes colorectal cancer metastasis by targeting <span class="match term1">ARHGAP35</span> for protein degradation	RING	1	Other	M.musculus
3683	TRI72_MOUSE	IRS1_MOUSE	Q1XH17	P35569	Trim72	Irs1	MEDLINE	29884820	Mitsugumin 53 (<span class="match term0">MG53</span>) is an E3 ligase that induces insulin receptor substrate-1 (<span class="match term1">IRS-1</span>) ubiquitination and degradation in skeletal muscle.	RING	1	Other	M.musculus
3684	TRIM8_MOUSE	M3K7_MOUSE	Q99PJ2	Q62073	Trim8	Map3k7	MEDLINE	31167620	At last, we found Nespas-inhibited <span class="match term0">TRIM8</span> (tripartite motif 8)-induced K63-linked polyubiquitination of <span class="match term1">TAK1</span>	RING	1	Other	M.musculus
3685	TP4AP_MOUSE	IKBA_MOUSE	Q9JLV2	Q9Z1E3	Trpc4ap	Nfkbia	MEDLINE	29704259	Conclusion: Hepatocyte <span class="match term0">TRUSS</span> promotes pathological stimuli-induced NAFLD and metabolic disorders, through activation of NF-kappaB by promoting ubiquitination and degradation of <span class="match term1">IkappaBalpha</span>	RING	1	Other	M.musculus
3686	TTC3_MOUSE	AKT1_MOUSE	O88196	P31750	Ttc3	Akt1	MEDLINE	22199232	E3Net	Other	1	Other	M.musculus
3687	TTC3_MOUSE	AKT2_MOUSE	O88196	Q60823	Ttc3	Akt2	MEDLINE	22199232	E3Net	Other	1	Other	M.musculus
3688	TTC3_MOUSE	AKT3_MOUSE	O88196	Q9WUA6	Ttc3	Akt3	MEDLINE	22199232	E3Net	Other	1	Other	M.musculus
3689	UBE2O_MOUSE	AAPK2_MOUSE	Q6ZPJ3	Q8BRK8	Ube2o	Prkaa2	MEDLINE	31292296	Mechanistically, <span class="match term0">UBE2O</span> acted as a ubiquitin ligase and targeted AMPKalpha2 for ubiquitin-dependent degradation in skeletal muscle; further, muscle-specific heterozygous knockout of <span class="match term1">Prkaa2</span> ablated <span class="match term0">UBE2O</span>-controlled metabolic processes	Other	1	Other	M.musculus
3690	UBE3A_MOUSE	SYUA_MOUSE	O08759	O55042	Ube3a	Snca	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	M.musculus
3691	UBE3A_MOUSE	P53_MOUSE	O08759	P02340	Ube3a	Tp53	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	M.musculus
3692	UBE3A_MOUSE	A0A0A0MQ73_MOUSE	O08759	A0A0A0MQ73	Ube3a	Kmt2d	MEDLINE	30230575	Here we show that the E3 ubiquitin ligase <span class="match term0">UBE3A</span> targets <span class="match term1">MLL4</span> for degradation, thereby suppressing high-fat diet (HFD)-induced expression of the hepatic steatosis target genes of <span class="match term1">MLL4</span>	SINGLE_OTHER	1	Other	M.musculus
3693	UBE3A_MOUSE	RAB3A_MOUSE	O08759	P63011	Ube3a	Rab3a	MEDLINE	33542309	Here we identified the synaptic protein Rabphilin-3a (RPH3A), an effector of the <span class="match term1">RAB3A</span> small GTPase involved in axonal vesicle priming and docking, as a ubiquitination target of <span class="match term0">UBE3A</span>	SINGLE_OTHER	1	Other	M.musculus
3694	UBE3A_MOUSE	RP3A_MOUSE	O08759	P47708	Ube3a	Rph3a	MEDLINE	33542309	In conclusion, our results identify <span class="match term1">RPH3A</span> as a novel target of <span class="match term0">UBE3A</span> and suggest that <span class="match term0">UBE3A</span>-dependent ubiquitination of <span class="match term1">RPH3A</span> serves a non-degradative function.	SINGLE_OTHER	1	Other	M.musculus
3695	UBR1_MOUSE	OPSD_MOUSE	O70481	P15409	Ubr1	Rho	MEDLINE	22199232	E3Net	UBOX	1	Other	M.musculus
3696	UBR4_MOUSE	HAT1_MOUSE	A2AN08	Q8BY71	Ubr4	Hat1	MEDLINE	31365869	In Drosophila and mouse myofibers, loss of <span class="match term0">UBR4</span> induces hypertrophy via decreased ubiquitination and degradation of a core set of target proteins, including the <span class="match term1">HAT1</span>/RBBP4/RBBP7 histone-binding complex	Other	1	Other	M.musculus
3697	VHL_MOUSE	HIF1A_MOUSE	P40338	Q61221	Vhl	Hif1a	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	M.musculus
3698	VHL_MOUSE	EPAS1_MOUSE	P40338	P97481	Vhl	Epas1	MEDLINE	22199232	E3Net	SOCS_VHL_BC-box	1	Other	M.musculus
3699	WWP1_MOUSE	ERBB4_MOUSE	Q8BZZ3	Q61527	Wwp1	Erbb4	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3700	WWP1_MOUSE	KLF15_MOUSE	Q8BZZ3	Q9EPW2	Wwp1	Klf15	MEDLINE	30830866	Hyperglycemia was found to upregulate the <span class="match term1">KLF15</span> protein in skeletal muscle of diabetic animals, which is achieved via downregulation of the E3 ubiquitin ligase <span class="match term0">WWP1</span> and consequent suppression of the ubiquitin-dependent degradation of <span class="match term1">KLF15</span>	HECT	1	Other	M.musculus
3701	WWP1_MOUSE	WWP1_MOUSE	Q8BZZ3	Q8BZZ3	Wwp1	Wwp1	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3702	WWP1_MOUSE	DVL2_MOUSE	Q8BZZ3	Q60838	Wwp1	Dvl2	MEDLINE	34139860	<span class="match term1">DVL2</span> was stabilized by <span class="match term0">WWP1</span> mediated K27-linked polyubiquitination	HECT	1	Other	M.musculus
3703	WWP1_MOUSE	JUNB_MOUSE	Q8BZZ3	P09450	Wwp1	Junb	MEDLINE	21809421	<span class="match term0">Wwp1</span> promotes ubiquitination and degradation of <span class="match term1">JunB</span>, an AP-1 transcription factor that positively regulates osteoblast differentiation	HECT	1	Other	M.musculus
3704	WWP1_MOUSE	RUNX2_MOUSE	Q8BZZ3	Q08775	Wwp1	Runx2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3705	WWP1_MOUSE	SMAD6_MOUSE	Q8BZZ3	O35182	Wwp1	Smad6	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3706	WWP1_MOUSE	P53_MOUSE	Q8BZZ3	P02340	Wwp1	Tp53	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3707	WWP2_MOUSE	EGR2_MOUSE	Q9DBH0	P08152	Wwp2	Egr2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3708	WWP2_MOUSE	WWP2_MOUSE	Q9DBH0	Q9DBH0	Wwp2	Wwp2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3709	WWP2_MOUSE	DCTN6_MOUSE	Q9DBH0	Q9WUB4	Wwp2	Dctn6	MEDLINE	31430374	Our Co-IP and ubiquitination analysis demonstrated that <span class="match term0">WWP2</span> interacted with <span class="match term1">p27</span>, and <span class="match term0">WWP2</span> overexpression significantly promoted the ubiquitination of <span class="match term1">p27</span>. These data suggested that the cell cycle transition from the G0/G1 phase to the S phase in lung cancer cells might be regulated by <span class="match term0">WWP2</span> through ubiquitination of <span class="match term1">P27</span>.	HECT	1	Other	M.musculus
3710	WWP2_MOUSE	SMAD2_MOUSE	Q9DBH0	Q62432	Wwp2	Smad2	MEDLINE	31399586	UbiNet 2.0	HECT	1	Other	M.musculus
3711	WWP2_MOUSE	RUNX2_MOUSE	Q9DBH0	Q08775	Wwp2	Runx2	MEDLINE	31160553	UbiNet 2.0	HECT	1	Other	M.musculus
3712	WWP2_MOUSE	PTEN_MOUSE	Q9DBH0	O08586	Wwp2	Pten	MEDLINE	29685889	Our results demonstrate that <span class="match term0">WWP2</span>, rather than CHIP, is an ubiquitin ligase that promotes <span class="match term1">PTEN</span> degradation in vivo Considering <span class="match term1">PTEN</span>'s significant role in tumor development, we propose that <span class="match term0">WWP2</span> may be a potential target for fine-tuning <span class="match term1">PTEN</span> levels in anticancer therapies.	HECT	1	Other	M.musculus
3713	WWP2_MOUSE	NRAM2_MOUSE	Q9DBH0	P49282	Wwp2	Slc11a2	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3714	WWP2_MOUSE	RPB1_MOUSE	Q9DBH0	P08775	Wwp2	Polr2a	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3715	WWP2_MOUSE	NR0B2_MOUSE	Q9DBH0	Q62227	Wwp2	Nr0b2	MEDLINE	29925997	Thus, <span class="match term1">SHP</span>-1 was a substrate for Itch- and <span class="match term0">WWP2</span>-mediated ubiquitination in T cells.	HECT	1	Other	M.musculus
3716	WWP2_MOUSE	PO5F1_MOUSE	Q9DBH0	P20263	Wwp2	Pou5f1	MEDLINE	22199232	E3Net	HECT	1	Other	M.musculus
3717	WWP2_MOUSE	SOX2_MOUSE	Q9DBH0	P48432	Wwp2	Sox2	MEDLINE	25042802	The E3 ligase <span class="match term0">WWP2</span> specifically interacts with K119-methylated <span class="match term1">Sox2</span> through its HECT domain to promote <span class="match term1">Sox2</span> ubiquitination	HECT	1	Other	M.musculus
3718	WWP2_MOUSE	KLF5_MOUSE	Q9DBH0	Q9Z0Z7	Wwp2	Klf5	MEDLINE	33164644	Further investigation found that <span class="match term0">WWP2</span> was coexpressed and interacted with <span class="match term1">KLF5</span> in the nuclei, leading to ubiquitination of <span class="match term1">KLF5</span>	HECT	1	Other	M.musculus
3719	WWP2_MOUSE	SEPT4_MOUSE	Q9DBH0	P28661	Wwp2	Septin4	MEDLINE	31924572	In addition, <span class="match term0">WWP2</span> interacted with the GTPase domain of <span class="match term1">Septin4</span>, ubiquitinating <span class="match term1">Septin4</span>-K174 to degrade <span class="match term1">Septin4</span> through the ubiquitin-proteasome system, which inhibited the <span class="match term1">Septin4</span>-PARP1 endothelial damage complex	HECT	1	Other	M.musculus
3720	XIAP_MOUSE	M3K2_MOUSE	Q60989	Q61083	Xiap	Map3k2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3721	XIAP_MOUSE	PTEN_MOUSE	Q60989	O08586	Xiap	Pten	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3722	XIAP_MOUSE	COMD1_MOUSE	Q60989	Q8K4M5	Xiap	Commd1	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3723	NIPA_MOUSE	CCNB1_MOUSE	Q80YV2	P24860	Zc3hc1	Ccnb1	MEDLINE	22199232	E3Net	F-box	1	Other	M.musculus
3724	ZNRF1_MOUSE	CAV1_MOUSE	Q91V17	P49817	Znrf1	Cav1	MEDLINE	28593998	We demonstrate that <span class="match term0">ZNRF1</span> physically interacts with <span class="match term1">CAV1</span> in response to lipopolysaccharide and mediates ubiquitination and degradation of <span class="match term1">CAV1</span>	RING	1	Other	M.musculus
3725	ZSWM2_MOUSE	ZSWM2_MOUSE	Q9D9X6	Q9D9X6	Zswim2	Zswim2	MEDLINE	22199232	E3Net	RING	1	Other	M.musculus
3726	Q5DTH1_MOUSE	ARHGF_MOUSE	Q5DTH1	Q5FWH6	Ube3a	Arhgef15	MEDLINE	31114479	As an E3 ligase, many functional target proteins of <span class="match term0">E6AP</span> have been discovered, including p53, Arc, <span class="match term1">Ephexin5</span>, and SK2.	HECT	1	Other	M.musculus
3727	DDB1_MOUSE	CRY1_MOUSE	Q3U1J4	P97784	Ddb1	Cry1	MEDLINE	32246987	Mechanistically, DDB1 stabilizes ChREBPalpha through CRY1, a known ubiquitination target of DDB1 E3 ligase. 	RING	1	Other	M.musculus
3728	RN220_MACFA	RN220_MACFA	Q8HXD5	Q8HXD5	RNF220	RNF220	MEDLINE	22199232	E3Net	RING	1	Other	Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
3729	MDM2_MESAU	MDM2_MESAU	Q60524	Q60524	MDM2	MDM2	MEDLINE	22199232	E3Net	RING	1	Other	Mesocricetus auratus (Golden hamster)
3730	MIR1_MHV68	HA11_MOUSE	O41933	P01899	K3	H2-D1	MEDLINE	22199232	E3Net	Other	1	Other	Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
3731	MIR1_MHV68	HA1B_MOUSE	O41933	P01901	K3	H2-K1	MEDLINE	22199232	E3Net	Other	1	Other	Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
3732	MIR1_MHV68	Q95457_MOUSE	O41933	Q95457	K3	H2-D1	MEDLINE	22199232	E3Net	Other	1	Other	Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
3733	LAP_MYXVL	CD4_RABIT	Q997C2	P46630	LAP	CD4	MEDLINE	22199232	E3Net	RING	1	Other	Myxoma virus (strain Lausanne) (MYXV)
3734	RAG1_RABIT	RAG1_RABIT	P34088	P34088	RAG1	RAG1	MEDLINE	22199232	E3Net	RING	1	Other	O.cuniculus
3735	RAG1_ONCMY	H32_ONCMY	Q91187	P84234	rag1	-	MEDLINE	22199232	E3Net	Other	1	Other	Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
3736	SPL11_ORYSJ	SPIN1_ORYSJ	Q653Z5	Q75GR5	SPL11	SPIN1	MEDLINE	22199232	E3Net	Other	1	Other	Oryza sativa subsp. japonica (Rice)
3737	XB3_ORYSJ	Q40640_ORYSA	Q65XV2	Q40640	XB3	Xa21	MEDLINE	22199232	E3Net	RING	1	Other	Oryza sativa subsp. japonica (Rice)
3738	CHFR_PONAB	HDAC1_PONAB	Q5RF77	Q5RAG0	CHFR	HDAC1	MEDLINE	22199232	E3Net	RING	1	Other	P.abelii
3739	NED4L_PONAB	SMAD2_PONAB	Q5RBF2	Q5R7C0	NEDD4L	SMAD2	MEDLINE	22199232	E3Net	HECT	1	Other	P.abelii
3740	NED4L_PONAB	CLCN5_PONAB	Q5RBF2	Q5RBK4	NEDD4L	CLCN5	MEDLINE	22199232	E3Net	HECT	1	Other	P.abelii
3741	SPOP_PONAB	BMI1_PONAB	Q5NVK7	Q5R8L2	SPOP	BMI1	MEDLINE	22199232	E3Net	Other	1	Other	P.abelii
3742	BACD2_PONAB	RHOA_PONAB	Q5RBH4	Q5REY6	TNFAIP1	RHOA	MEDLINE	22199232	E3Net	BTB_OTHER	1	Other	P.abelii
3743	HPAB2_PSESM	P93216_SOLLC	Q8RSY1	P93216	hopAB2	fen	MEDLINE	22199232	E3Net	Other	1	Other	Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
3744	D3ZV15_RAT	SRBS2_RAT	D3ZV15	O35413	Cbl	Sorbs2	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3745	D3ZV15_RAT	FGFR1_RAT	D3ZV15	Q04589	Cbl	Fgfr1	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3746	D3ZV15_RAT	PGFRB_RAT	D3ZV15	Q05030	Cbl	Pdgfrb	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3747	D3ZV15_RAT	IL2_RAT	D3ZV15	P17108	Cbl	Il2	MEDLINE	30021515	Increased expression of the <span class="match term0">Cbl</span> family of E3 ubiquitin ligases decreases Interleukin-2 production in a rat model of peripheral neuropathy	RING	1	Other	R.norvegicus
3748	D3ZV15_RAT	FGFR4_RAT	D3ZV15	Q498D6	Cbl	Fgfr4	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3749	D3ZV15_RAT	PGFRA_RAT	D3ZV15	P20786	Cbl	Pdgfra	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3750	CBLB_RAT	PLCG1_RAT	Q8K4S7	P10686	Cblb	Plcg1	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3751	CBLB_RAT	SH3K1_RAT	Q8K4S7	Q925Q9	Cblb	Sh3kbp1	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3752	CBLB_RAT	KSYK_RAT	Q8K4S7	Q64725	Cblb	Syk	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3753	CBLB_RAT	CBLB_RAT	Q8K4S7	Q8K4S7	Cblb	Cblb	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3754	Q5BJY0_RAT	P53_RAT	Q5BJY0	P10361	Cop1	Tp53	MEDLINE	32537758	CONCLUSIONS: Fendrr can inhibit H/R-induced cardiomyocyte apoptosis, which is partly through promoting the ubiquitination and degradation of <span class="match term1">p53</span> by increasing the binding of <span class="match term0">Cop1</span> and <span class="match term1">p53</span>.	DWD	1	Other	R.norvegicus
3755	D4A722_RAT	TSC2_RAT	D4A722	P49816	Deleted	Tsc2	MEDLINE	22199232	E3Net	Other	1	Other	R.norvegicus
3756	FBX11_RAT	P53_RAT	Q7TSL3	P10361	Fbxo11	Tp53	MEDLINE	22199232	E3Net	F-box	1	Other	R.norvegicus
3757	B0BNL1_RAT	B1WC74_RAT	B0BNL1	B1WC74	Fbxo21	Eid1	MEDLINE	33450132	<span class="match term0">FBXO21</span> is a subunit of ubiquitin E3 ligases that degrades P-glycoprotein and <span class="match term1">EID1</span> by ubiquitination and activates the JNK and p38 pathways; however, its role in OA remains unknown	Other	1	Other	R.norvegicus
3758	B0BNL1_RAT	MDR1_RAT	B0BNL1	P43245	Fbxo21	Abcb1	MEDLINE	33450132	<span class="match term0">FBXO21</span> is a subunit of ubiquitin E3 ligases that degrades P-glycoprotein and EID1 by ubiquitination and activates the JNK and p38 pathways; however, its role in OA remains unknown	Other	1	Other	R.norvegicus
3759	FBX31_RAT	SMAD7_RAT	B2RYN2	O88406	Fbxo31	Smad7	MEDLINE	31680332	Moreover, <span class="match term0">FBXO31</span> enhanced ubiquitination of <span class="match term1">Smad7</span>	F-box	1	Other	R.norvegicus
3760	FBX31_RAT	CCND1_RAT	B2RYN2	P39948	Fbxo31	Ccnd1	MEDLINE	22199232	E3Net	F-box	1	Other	R.norvegicus
3761	FBX32_RAT	TNNI3_RAT	Q91Z62	P23693	Fbxo32	Tnni3	MEDLINE	22199232	E3Net	F-box	1	Other	R.norvegicus
3762	FBX32_RAT	DUS1_RAT	Q91Z62	Q64623	Fbxo32	Dusp1	MEDLINE	22199232	E3Net	F-box	1	Other	R.norvegicus
3763	FBX6_RAT	CHK1_RAT	Q923V4	Q91ZN7	Fbxo6	Chek1	MEDLINE	22199232	E3Net	F-box	1	Other	R.norvegicus
3764	F1LVZ9_RAT	A0A0G2K7X2_RAT	F1LVZ9	A0A0G2K7X2	Hectd3	Traf3	MEDLINE	33627626	Mechanistically, both the DOC and HECT domains of <span class="match term0">HECTD3</span> directly interacted with <span class="match term1">TRAF3</span>, and the catalytic Cys (C832) in the HECT domain promoted the K63-linked polyubiquitination of <span class="match term1">TRAF3</span> at Lys138	HECT	1	Other	R.norvegicus
3765	HUWE1_RAT	P53_RAT	P51593	P10361	Huwe1	Tp53	MEDLINE	22199232	E3Net	HECT	1	Other	R.norvegicus
3766	KEAP1_RAT	PGAM5_RAT	P57790	Q562B5	Keap1	Pgam5	MEDLINE	22199232	E3Net	BTB_3	1	Other	R.norvegicus
3767	KEAP1_RAT	NF2L2_RAT	P57790	O54968	Keap1	Nfe2l2	MEDLINE	22199232	E3Net	BTB_3	1	Other	R.norvegicus
3768	KLH17_RAT	GRIK2_RAT	Q8K430	P42260	Klhl17	Grik2	MEDLINE	22199232	E3Net	BTB_3	1	Other	R.norvegicus
3769	KLH21_RAT	AURKB_RAT	D4A2K4	O55099	Klhl21	Aurkb	MEDLINE	22199232	E3Net	BTB_3	1	Other	R.norvegicus
3770	LHX1_RAT	LIMK1_RAT	P63007	P53669	Lhx1	Limk1	MEDLINE	22199232	E3Net	Other	1	Other	R.norvegicus
3771	M3K1_RAT	MK03_RAT	Q62925	P21708	Map3k1	Mapk3	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3772	M3K1_RAT	JUN_RAT	Q62925	P17325	Map3k1	Jun	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3773	M3K1_RAT	MK01_RAT	Q62925	P63086	Map3k1	Mapk1	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3774	MARHB_RAT	CD4_RAT	A6P320	P05540	Marchf11	Cd4	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3775	MARH2_RAT	TFR1_RAT	Q5I0I2	Q99376	Marchf2	Tfrc	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3776	D3ZVH5_RAT	ARBK1_RAT	D3ZVH5	P26817	Mdm2	Grk2	MEDLINE	30915659	<span class="match term1">GRK2</span> upregulation was associated to calpain-dependent degradation of the <span class="match term1">GRK2</span> ubiquitin ligase <span class="match term0">MDM2</span> and to enhanced NF-kappaB-dependent <span class="match term1">GRK2</span> gene expression in correlation with calpain-mediated IkB proteolysis	RING	1	Other	R.norvegicus
3777	MYLIP_RAT	MYLIP_RAT	D3ZDI6	D3ZDI6	Mylip	Mylip	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3778	MYLIP_RAT	LDLR_RAT	D3ZDI6	P35952	Mylip	Ldlr	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3779	NEDD4_RAT	NOTC1_RAT	Q62940	Q07008	Nedd4	Notch1	MEDLINE	22199232	E3Net	HECT	1	Other	R.norvegicus
3780	NEDD4_RAT	EAA3_RAT	Q62940	P51907	Nedd4	Slc1a1	MEDLINE	22199232	E3Net	HECT	1	Other	R.norvegicus
3781	NEDD4_RAT	NTRK1_RAT	Q62940	P35739	Nedd4	Ntrk1	MEDLINE	22199232	E3Net	HECT	1	Other	R.norvegicus
3782	NEDD4_RAT	NFIP1_RAT	Q62940	Q5U2S1	Nedd4	Ndfip1	MEDLINE	22199232	E3Net	HECT	1	Other	R.norvegicus
3783	NHLC1_RAT	EPM2A_RAT	Q6IMG5	Q91XQ2	Nhlrc1	Epm2a	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3784	NHLC1_RAT	PPR3C_RAT	Q6IMG5	Q5U2R5	Nhlrc1	Ppp1r3c	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3785	PZRN3_RAT	MUSK_RAT	P68907	Q62838	Pdzrn3	Musk	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3786	PRKN_RAT	PRKN_RAT	Q9JK66	Q9JK66	Prkn	Prkn	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3787	PRKN_RAT	GPR37_RAT	Q9JK66	Q9QYC6	Prkn	Gpr37	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3788	PRKN_RAT	SEPT5_RAT	Q9JK66	Q9JJM9	Prkn	Septin5	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3789	PRKN_RAT	AIMP2_RAT	Q9JK66	Q32PX2	Prkn	Aimp2	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3790	RN182_RAT	VATL_RAT	D3ZBM4	P63081	Rnf182	Atp6v0c	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3791	RING2_RAT	H2A2A_RAT	Q4KLY4	P0CC09	Rnf2	H2ac18	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3792	RNF4_RAT	RNF4_RAT	O88846	O88846	Rnf4	Rnf4	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3793	RNF5_RAT	PAXI_RAT	Q5M807	Q66H76	Rnf5	Pxn	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3794	SIAH1_RAT	SYPH_RAT	Q920M9	P07825	Siah1	Syp	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3795	SIAH2_RAT	SYUA_RAT	Q8R4T2	P37377	Siah2	Snca	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3796	SIAH2_RAT	AKAP1_RAT	Q8R4T2	O88884	Siah2	Akap1	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3797	SIAH2_RAT	SYPH_RAT	Q8R4T2	P07825	Siah2	Syp	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3798	B2GUZ0_RAT	PSMD9_RAT	B2GUZ0	Q9WTV5	Skp2	Psmd9	MEDLINE	22199232	E3Net	F-box	1	Other	R.norvegicus
3799	B2GUZ0_RAT	O08769_RAT	B2GUZ0	O08769	Skp2	Cdkn1b	MEDLINE	22199232	E3Net	F-box	1	Other	R.norvegicus
3800	D3ZCF5_RAT	SMAD7_RAT	D3ZCF5	O88406	Smurf1	Smad7	MEDLINE	32871042	<span class="match term0">SMURF1</span> was a target gene of miR-148a-3p, and resulted in ubiquitination and degradation of <span class="match term1">SMAD7</span> to decreased BCL2 expression	HECT	1	Other	R.norvegicus
3801	F1M3F2_RAT	B5DFE2_RAT	F1M3F2	B5DFE2	Smurf2	Ezh2	MEDLINE	30649914	Inhibition of <span class="match term0">Smurf2</span> translation by miR-322/503 protects from ischemia-reperfusion injury by modulating <span class="match term1">EZH2</span>/Akt/GSK3beta signaling.	HECT	1	Other	R.norvegicus
3802	F1M3F2_RAT	D3ZWL1_RAT	F1M3F2	D3ZWL1	Smurf2	Skil	MEDLINE	28447757	UbiNet 2.0	HECT	1	Other	R.norvegicus
3803	D4A4T0_RAT	ARC_RAT	D4A4T0	Q63053	Stub1	Arc	MEDLINE	33431799	<span class="match term0">CHIP</span> promotes Wnt signaling and regulates <span class="match term1">Arc</span> stability by recruiting and polyubiquitinating LEF1 or <span class="match term1">Arc</span>	UBOX	1	Other	R.norvegicus
3804	BACD2_RAT	RHOA_RAT	Q7TNY1	P61589	Tnfaip1	Rhoa	MEDLINE	22199232	E3Net	BTB_OTHER	1	Other	R.norvegicus
3805	TRAF6_RAT	TRAF6_RAT	B5DF45	B5DF45	Traf6	Traf6	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3806	TRAF6_RAT	SODC_RAT	B5DF45	P07632	Traf6	Sod1	MEDLINE	32029478	Functionally, <span class="match term0">TRAF6</span> stimulated polyubiquitination and aggregation of the interacting <span class="match term1">SOD1</span> variants	RING	1	Other	R.norvegicus
3807	TRI17_RAT	TRI17_RAT	Q9WV59	Q9WV59	Trim17	Trim17	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3808	Q6P7B3_RAT	NL1A1_RAT	Q6P7B3	D9I2F9	Trim25	Nlrp1a	MEDLINE	34313957	In summary, <span class="match term0">TRIM25</span> exerts its cardioprotective effects by promoting the ubiquitination of NLRP1 in DOX-induced cardiomyocyte pyroptosis, which provides a novel therapeutic strategy for DOX-induced cardiotoxicity.	Other	1	Other	R.norvegicus
3809	D3ZJ28_RAT	IKBA_RAT	D3ZJ28	Q63746	Trim52	Nfkbia	MEDLINE	33122622	CONCLUSIONS <span class="match term0">TRIM52</span> activated the NF-kappaB signaling pathway by promoting <span class="match term1">IkappaBalpha</span> ubiquitination, thereby regulating LPS-induced microglial cell activation and the inflammatory response.	RING	1	Other	R.norvegicus
3810	TRI55_RAT	DUS1_RAT	Q5PQN5	Q64623	Trim55	Dusp1	MEDLINE	32463795	<span class="match term0">TRIM55</span> inhibited <span class="match term1">DUSP1</span> protein expression through ubiquitination of <span class="match term1">DUSP1</span>	RING	1	Other	R.norvegicus
3811	TRI63_RAT	TNNI3_RAT	Q91Z63	P23693	Trim63	Tnni3	MEDLINE	22199232	E3Net	RING	1	Other	R.norvegicus
3812	D3ZQE3_RAT	IKBA_RAT	D3ZQE3	Q63746	Trim8	Nfkbia	MEDLINE	32463919	Moreover, <span class="match term0">TRIM8</span> interacted with <span class="match term1">IkappaBalpha</span> and promoted its ubiquitination in PC12 cells	RING	1	Other	R.norvegicus
3813	UBE4A_RAT	G3V6W8_RAT	Q6P7A2	G3V6W8	Ube4a	Bmp7	MEDLINE	30663414	Concurrent overexpression experiments confirmed that <span class="match term0">UBE4A</span> is the ubiquitin ligase that degrades <span class="match term1">BMP7</span>	UBOX	1	Other	R.norvegicus
3814	B4F767_RAT	PARP1_RAT	B4F767	P27008	Wwp2	Parp1	MEDLINE	32139900	In addition, lysine 418 (K418) and lysine 249 (K249) were shown to be of critical importance in regulating <span class="match term1">PARP1</span> ubiquitination and degradation by <span class="match term0">WWP2</span>	HECT	1	Other	R.norvegicus
3815	LAP_RFVKA	CD4_RABIT	Q9Q8T2	P46630	s153R	CD4	MEDLINE	22199232	E3Net	Other	1	Other	Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain Kasza))
3816	NSP1_ROTAD	IRF3_HUMAN	B3SRS0	Q14653	-	IRF3	MEDLINE	22199232	E3Net	Other	1	Other	Rotavirus A (strain RVA/Human/United States/D/1974/G1P1A[8]) (RV-A)
3817	AMA1_YEAST	CG21_YEAST	P50082	P24868	AMA1	CLB1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3818	AMA1_YEAST	SECU_YEAST	P50082	P40316	AMA1	PDS1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3819	AMA1_YEAST	CGS5_YEAST	P50082	P30283	AMA1	CLB5	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3820	BRE1_YEAST	H2B1_YEAST	Q07457	P02293	BRE1	HTB1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3821	BRE1_YEAST	H2B2_YEAST	Q07457	P02294	BRE1	HTB2	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3822	BRE1_YEAST	SWD2_YEAST	Q07457	P36104	BRE1	SWD2	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3823	CDC20_YEAST	KIP1_YEAST	P26309	P28742	CDC20	KIP1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3824	CDC20_YEAST	CGS5_YEAST	P26309	P30283	CDC20	CLB5	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3825	CDC20_YEAST	SPO13_YEAST	P26309	P23624	CDC20	SPO13	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3826	CDC20_YEAST	MPS1_YEAST	P26309	P54199	CDC20	MPS1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3827	CDC20_YEAST	CG22_YEAST	P26309	P24869	CDC20	CLB2	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3828	CDC20_YEAST	SECU_YEAST	P26309	P40316	CDC20	PDS1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3829	CDC20_YEAST	HSL1_YEAST	P26309	P34244	CDC20	HSL1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3830	CDC20_YEAST	ACM1_YEAST	P26309	Q08981	CDC20	ACM1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3831	CDC20_YEAST	UME6_YEAST	P26309	P39001	CDC20	UME6	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3832	CDC20_YEAST	CG23_YEAST	P26309	P24870	CDC20	CLB3	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3833	CDC4_YEAST	RCN1_YEAST	P07834	P36054	CDC4	RCN1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3834	CDC4_YEAST	HSL1_YEAST	P07834	P34244	CDC4	HSL1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3835	CDC4_YEAST	CG12_YEAST	P07834	P20438	CDC4	CLN2	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3836	CDC4_YEAST	CDC4_YEAST	P07834	P07834	CDC4	CDC4	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3837	CDC4_YEAST	GCN4_YEAST	P07834	P03069	CDC4	GCN4	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3838	CDC4_YEAST	CBF3C_YEAST	P07834	P35203	CDC4	CTF13	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3839	CDC4_YEAST	CDC6_YEAST	P07834	P09119	CDC4	CDC6	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3840	CDC4_YEAST	STE5_YEAST	P07834	P32917	CDC4	STE5	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3841	CDC4_YEAST	FAR1_YEAST	P07834	P21268	CDC4	FAR1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3842	CDC4_YEAST	CGS6_YEAST	P07834	P32943	CDC4	CLB6	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3843	CDC4_YEAST	HAC1_YEAST	P07834	P41546	CDC4	HAC1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3844	CDC4_YEAST	SWI5_YEAST	P07834	P08153	CDC4	SWI5	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3845	CDC4_YEAST	SIC1_YEAST	P07834	P38634	CDC4	SIC1	MEDLINE	9285816	Ubiquitin chain formation is abrogated in cdc4ts mutant extracts and assembly restored by the addition of exogenous <span class="match term0">CDC4</span>, suggesting a direct role for this protein in <span class="match term1">SIC1</span> multiubiquitination	Other	1	Other	S.cerevisiae
3846	CDC4_YEAST	TEC1_YEAST	P07834	P18412	CDC4	TEC1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3847	CDH1_YEAST	ASE1_YEAST	P53197	P50275	CDH1	ASE1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3848	CDH1_YEAST	ACM1_YEAST	P53197	Q08981	CDH1	ACM1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3849	CDH1_YEAST	CDC20_YEAST	P53197	P26309	CDH1	CDC20	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3850	CDH1_YEAST	HSL1_YEAST	P53197	P34244	CDH1	HSL1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3851	CDH1_YEAST	CGS5_YEAST	P53197	P30283	CDH1	CLB5	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3852	CDH1_YEAST	MPS1_YEAST	P53197	P54199	CDH1	MPS1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3853	CDH1_YEAST	CDC5_YEAST	P53197	P32562	CDH1	CDC5	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3854	CDH1_YEAST	FIN1_YEAST	P53197	Q03898	CDH1	FIN1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3855	CDH1_YEAST	SECU_YEAST	P53197	P40316	CDH1	PDS1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3856	CDH1_YEAST	CIN8_YEAST	P53197	P27895	CDH1	CIN8	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3857	CDH1_YEAST	IQG1_YEAST	P53197	Q12280	CDH1	IQG1	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3858	CDH1_YEAST	CG22_YEAST	P53197	P24869	CDH1	CLB2	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3859	CDH1_YEAST	CG23_YEAST	P53197	P24870	CDH1	CLB3	MEDLINE	22199232	E3Net	CDC20	1	Other	S.cerevisiae
3860	CBF3C_YEAST	CBF3C_YEAST	P35203	P35203	CTF13	CTF13	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3861	DIA2_YEAST	TEC1_YEAST	Q08496	P18412	DIA2	TEC1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3862	ELOA1_YEAST	RPB1_YEAST	P53861	P04050	ELA1	RPO21	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3863	GRR1_YEAST	CG12_YEAST	P24814	P20438	GRR1	CLN2	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3864	GRR1_YEAST	MKS1_YEAST	P24814	P34072	GRR1	MKS1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3865	GRR1_YEAST	GIC2_YEAST	P24814	Q06648	GRR1	GIC2	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3866	GRR1_YEAST	STD1_YEAST	P24814	Q02794	GRR1	STD1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3867	GRR1_YEAST	F16P_YEAST	P24814	P09201	GRR1	FBP1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3868	GRR1_YEAST	IME2_YEAST	P24814	P32581	GRR1	IME2	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3869	GRR1_YEAST	CG11_YEAST	P24814	P20437	GRR1	CLN1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3870	GRR1_YEAST	GRR1_YEAST	P24814	P24814	GRR1	GRR1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3871	GRR1_YEAST	MTH1_YEAST	P24814	P35198	GRR1	MTH1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3872	GRR1_YEAST	GIS4_YEAST	P24814	Q04233	GRR1	GIS4	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3873	GRR1_YEAST	CYK2_YEAST	P24814	Q05080	GRR1	HOF1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3874	GRR1_YEAST	SIC1_YEAST	P24814	P38634	GRR1	SIC1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3875	GRR1_YEAST	GAL2_YEAST	P24814	P13181	GRR1	GAL2	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3876	-	CAN_YEAST	-	P53615	HEYL	NCE103	MEDLINE	31789040	UbiNet 2.0	Other	1	Other	S.cerevisiae
3877	HRD1_YEAST	HRD1_YEAST	Q08109	Q08109	HRD1	HRD1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3878	HRD1_YEAST	PDR5_YEAST	Q08109	P33302	HRD1	PDR5	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3879	HRD1_YEAST	HMDH2_YEAST	Q08109	P12684	HRD1	HMG2	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3880	HRD1_YEAST	CDC48_YEAST	Q08109	P25694	HRD1	CDC48	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3881	HRD1_YEAST	HMDH1_YEAST	Q08109	P12683	HRD1	HMG1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3882	HRD1_YEAST	DER1_YEAST	Q08109	P38307	HRD1	DER1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3883	HRD1_YEAST	CBPY_YEAST	Q08109	P00729	HRD1	PRC1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3884	HRD1_YEAST	SC61A_YEAST	Q08109	P32915	HRD1	SEC61	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3885	HRT3_YEAST	HRT3_YEAST	Q12347	Q12347	HRT3	HRT3	MEDLINE	22199232	E3Net	F-box	1	Other	S.cerevisiae
3886	MDM30_YEAST	MDM34_YEAST	Q05930	P53083	MDM30	MDM34	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3887	MDM30_YEAST	FZO1_YEAST	Q05930	P38297	MDM30	FZO1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3888	MDM30_YEAST	GAL4_YEAST	Q05930	P04386	MDM30	GAL4	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3889	MET30_YEAST	SWE1_YEAST	P39014	P32944	MET30	SWE1	MEDLINE	22199232	E3Net	F-box	1	Other	S.cerevisiae
3890	MET30_YEAST	CG13_YEAST	P39014	P13365	MET30	CLN3	MEDLINE	22199232	E3Net	F-box	1	Other	S.cerevisiae
3891	MET30_YEAST	MET4_YEAST	P39014	P32389	MET30	MET4	MEDLINE	22199232	E3Net	F-box	1	Other	S.cerevisiae
3892	MET30_YEAST	MET30_YEAST	P39014	P39014	MET30	MET30	MEDLINE	22199232	E3Net	F-box	1	Other	S.cerevisiae
3893	MET30_YEAST#CDC4_YEAST	CENPA_YEAST	P39014#P07834	P36012	MET30#CDC4	CSE4	MEDLINE	32032354	We show that two Skp, Cullin, F-box (SCF) ubiquitin ligases with the evolutionarily conserved F-box proteins Met30 and Cdc4 interact and cooperatively regulate proteolysis of endogenous <span class="match term1">Cse4</span> and prevent its mislocalization for faithful chromosome segregation under physiological conditions	Other	1	Other	S.cerevisiae
3894	NOT4_YEAST	NACB1_YEAST	P34909	Q02642	MOT2	EGD1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3895	NOT4_YEAST	NACA_YEAST	P34909	P38879	MOT2	EGD2	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3896	MPE1_YEAST	YSH1_YEAST	P35728	Q06224	MPE1	YSH1	MEDLINE	32009536	<span class="match term1">Ysh1</span> ubiquitination is mediated by the Ubc4 ubiquitin conjugating enzyme and <span class="match term0">Mpe1</span>, which in addition to its function in C/P, is also a RING ubiquitin ligase	Other	1	Other	S.cerevisiae
3897	NAM7_YEAST	NAM7_YEAST	P30771	P30771	NAM7	NAM7	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
3898	SIZ2_YEAST	SIZ2_YEAST	Q12216	Q12216	NFI1	NFI1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3899	PIB1_YEAST	RDS2_YEAST	Q06651	P19541	PIB1	RDS2	MEDLINE	31604822	Through in vivo and in vitro experiments, we establish <span class="match term0">Pib1</span> as the ubiquitin E3 ligase that regulates <span class="match term1">Rds2</span> ubiquitination and stability	RING	1	Other	S.cerevisiae
3900	PSH1_YEAST	CENPA_YEAST	Q12161	P36012	PSH1	CSE4	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3901	RAD18_YEAST	HO_YEAST	P10862	P09932	RAD18	HO	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3902	RAD18_YEAST	RAD5_YEAST	P10862	P32849	RAD18	RAD5	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3903	RAD18_YEAST	PCNA_YEAST	P10862	P15873	RAD18	POL30	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3904	RAD5_YEAST	PCNA_YEAST	P32849	P15873	RAD5	POL30	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3905	RAD7_YEAST	RAD4_YEAST	P06779	P14736	RAD7	RAD4	MEDLINE	22199232	E3Net	F-box	1	Other	S.cerevisiae
3906	RMD5_YEAST	F16P_YEAST	Q12508	P09201	RMD5	FBP1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
3907	RSP5_YEAST	SNA4_YEAST	P39940	Q07549	RSP5	SNA4	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3908	RSP5_YEAST	RPC8_YEAST	P39940	P35718	RSP5	RPC25	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3909	RSP5_YEAST	VPS9_YEAST	P39940	P54787	RSP5	VPS9	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3910	RSP5_YEAST	YM46_YEAST	P39940	Q03231	RSP5	YMR181C	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3911	RSP5_YEAST	ZRT1_YEAST	P39940	P32804	RSP5	ZRT1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3912	RSP5_YEAST	TAF3_YEAST	P39940	Q12297	RSP5	TAF3	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3913	RSP5_YEAST	ROG3_YEAST	P39940	P43602	RSP5	ROG3	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3914	RSP5_YEAST	STE2_YEAST	P39940	D6VTK4	RSP5	STE2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3915	RSP5_YEAST	ACK1_YEAST	P39940	Q07622	RSP5	ACK1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3916	RSP5_YEAST	ART10_YEAST	P39940	P18634	RSP5	ART10	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3917	RSP5_YEAST	LSB1_YEAST	P39940	P53281	RSP5	LSB1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3918	RSP5_YEAST	GAL2_YEAST	P39940	P13181	RSP5	GAL2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3919	RSP5_YEAST	HPR1_YEAST	P39940	P17629	RSP5	HPR1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3920	RSP5_YEAST	SNA3_YEAST	P39940	P14359	RSP5	SNA3	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3921	RSP5_YEAST	CUE5_YEAST	P39940	Q08412	RSP5	CUE5	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3922	RSP5_YEAST	ROD1_YEAST	P39940	Q02805	RSP5	ROD1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3923	RSP5_YEAST	BSD2_YEAST	P39940	P38356	RSP5	BSD2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3924	RSP5_YEAST	RSA1_YEAST	P39940	Q08932	RSP5	RSA1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3925	RSP5_YEAST	SRP40_YEAST	P39940	P32583	RSP5	SRP40	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3926	RSP5_YEAST	YIP5_YEAST	P39940	P53108	RSP5	YIP5	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3927	RSP5_YEAST	YKC3_YEAST	P39940	P36103	RSP5	YKL023W	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3928	RSP5_YEAST	RPN10_YEAST	P39940	P38886	RSP5	RPN10	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3929	RSP5_YEAST	ALY1_YEAST	P39940	P36117	RSP5	ALY1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3930	RSP5_YEAST	BXI1_YEAST	P39940	P48558	RSP5	BXI1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3931	RSP5_YEAST	CTR1_YEAST	P39940	P49573	RSP5	CTR1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3932	RSP5_YEAST	MVB12_YEAST	P39940	P42939	RSP5	MVB12	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3933	RSP5_YEAST	NOP53_YEAST	P39940	Q12080	RSP5	NOP53	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3934	RSP5_YEAST	WWM1_YEAST	P39940	P43582	RSP5	WWM1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3935	RSP5_YEAST	SLA1_YEAST	P39940	P32790	RSP5	SLA1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3936	RSP5_YEAST	EAF7_YEAST	P39940	P53911	RSP5	EAF7	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3937	RSP5_YEAST	G6PI_YEAST	P39940	P12709	RSP5	PGI1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3938	RSP5_YEAST	CBPY_YEAST	P39940	P00729	RSP5	PRC1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3939	RSP5_YEAST	SPT23_YEAST	P39940	P35210	RSP5	SPT23	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3940	RSP5_YEAST	RPB7_YEAST	P39940	P34087	RSP5	RPB7	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3941	RSP5_YEAST	YP084_YEAST	P39940	Q06821	RSP5	YPR084W	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3942	RSP5_YEAST	MGA2_YEAST	P39940	P40578	RSP5	MGA2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3943	RSP5_YEAST	ENT2_YEAST	P39940	Q05785	RSP5	ENT2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3944	RSP5_YEAST	MUP1_YEAST	P39940	P50276	RSP5	MUP1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3945	RSP5_YEAST	TRM1_YEAST	P39940	P15565	RSP5	TRM1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3946	RSP5_YEAST	PHO91_YEAST	P39940	P27514	RSP5	PHO91	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3947	RSP5_YEAST	SIT1_YEAST	P39940	P39980	RSP5	SIT1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3948	RSP5_YEAST	ARN1_YEAST	P39940	P38731	RSP5	ARN1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3949	RSP5_YEAST	MAL11_YEAST	P39940	P53048	RSP5	MAL11	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3950	RSP5_YEAST	RIM4_YEAST	P39940	P38741	RSP5	RIM4	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3951	RSP5_YEAST	NKP2_YEAST	P39940	Q06162	RSP5	NKP2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3952	RSP5_YEAST	EAR1_YEAST	P39940	Q03212	RSP5	EAR1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3953	RSP5_YEAST	YL326_YEAST	P39940	Q06170	RSP5	YLR326W	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3954	RSP5_YEAST	RCR2_YEAST	P39940	Q03446	RSP5	RCR2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3955	RSP5_YEAST	CBPS_YEAST	P39940	P27614	RSP5	CPS1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3956	RSP5_YEAST	HXT7_YEAST	P39940	P39004	RSP5	HXT7	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3957	RSP5_YEAST	ALY2_YEAST	P39940	P47029	RSP5	ALY2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3958	RSP5_YEAST	RIR2_YEAST	P39940	P09938	RSP5	RNR2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3959	RSP5_YEAST	YHT1_YEAST	P39940	P38835	RSP5	YHR131C	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3960	RSP5_YEAST	NACA_YEAST	P39940	P38879	RSP5	EGD2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3961	RSP5_YEAST	NSL1_YEAST	P39940	Q12143	RSP5	NSL1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3962	RSP5_YEAST	BUL1_YEAST	P39940	P48524	RSP5	BUL1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3963	RSP5_YEAST	GPA1_YEAST	P39940	P08539	RSP5	GPA1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3964	RSP5_YEAST	ECM21_YEAST	P39940	P38167	RSP5	ECM21	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3965	RSP5_YEAST	TAT1_YEAST	P39940	P38085	RSP5	TAT1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3966	RSP5_YEAST	BSC5_YEAST	P39940	P53755	RSP5	BSC5	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3967	RSP5_YEAST	YLH47_YEAST	P39940	Q06493	RSP5	YLH47	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3968	RSP5_YEAST	RFA1_YEAST	P39940	P22336	RSP5	RFA1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3969	RSP5_YEAST	PPN1_YEAST	P39940	Q04119	RSP5	PPN1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3970	RSP5_YEAST	RV167_YEAST	P39940	P39743	RSP5	RVS167	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3971	RSP5_YEAST	ALG6_YEAST	P39940	Q12001	RSP5	ALG6	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3972	RSP5_YEAST	CSR2_YEAST	P39940	Q12734	RSP5	CSR2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3973	RSP5_YEAST	PUT4_YEAST	P39940	P15380	RSP5	PUT4	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3974	RSP5_YEAST	RCR1_YEAST	P39940	P38212	RSP5	RCR1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3975	RSP5_YEAST	MCA1_YEAST	P39940	Q08601	RSP5	MCA1	MEDLINE	30675380	We noted multiple ubiquitination sites on Yca1 and established <span class="match term0">Rsp5</span> as the candidate E3 ligase involved in this process	HECT	1	Other	S.cerevisiae
3976	RSP5_YEAST	SMF1_YEAST	P39940	P38925	RSP5	SMF1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3977	RSP5_YEAST	PMA1_YEAST	P39940	P05030	RSP5	PMA1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3978	RSP5_YEAST	DIA1_YEAST	P39940	P54005	RSP5	DIA1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3979	RSP5_YEAST	SLA2_YEAST	P39940	P33338	RSP5	SLA2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3980	RSP5_YEAST	NOP3_YEAST	P39940	Q01560	RSP5	NPL3	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3981	RSP5_YEAST	ARR3_YEAST	P39940	Q06598	RSP5	ARR3	MEDLINE	30776335	Endocytic degradation of Acr3 is promoted by the ubiquitin ligase <span class="match term0">Rsp5</span> and requires polyubiquitination of Acr3 at multiple lysine residues via lysine 63-linked ubiquitin chains	HECT	1	Other	S.cerevisiae
3982	RSP5_YEAST	ALR1_YEAST	P39940	Q08269	RSP5	ALR1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3983	RSP5_YEAST	HXT6_YEAST	P39940	P39003	RSP5	HXT6	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3984	RSP5_YEAST	MAL61_YEASX	P39940	P15685	RSP5	MAL61	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3985	RSP5_YEAST	SGT1_YEAST	P39940	Q08446	RSP5	SGT1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3986	RSP5_YEAST	CARP_YEAST	P39940	P07267	RSP5	PEP4	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3987	RSP5_YEAST	GAP1_YEAST	P39940	P19145	RSP5	GAP1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3988	RSP5_YEAST	TAT2_YEAST	P39940	P38967	RSP5	TAT2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3989	RSP5_YEAST	YPQ1_YEAST	P39940	Q12010	RSP5	YPQ1	MEDLINE	33351098	Cell Biol.https://doi.org/10.1083/jcb.202001116) show that in Saccharomyces cerevisiae, the vacuole-associated <span class="match term0">Rsp5</span> ubiquitin ligase uses a TMD in substrate adaptor Ssh4 to recognize membrane helices in <span class="match term1">Ypq1</span>, which targets this lysine transporter for lysosomal degradation during lysine starvation.	HECT	1	Other	S.cerevisiae
3990	RSP5_YEAST	NTH2_YEAST	P39940	Q08214	RSP5	NTG2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3991	RSP5_YEAST	YD012_YEAST	P39940	Q12489	RSP5	YDL012C	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3992	RSP5_YEAST	SNC1_YEAST	P39940	P31109	RSP5	SNC1	MEDLINE	31067149	Degradative sorting requires lysine residues in the juxtamembrane region of <span class="match term1">Snc1</span> and is mediated by the <span class="match term0">Rsp5</span> ubiquitin ligase and its transmembrane adapters, Ear1 and Ssh4, which localize to endosome and vacuole membranes	HECT	1	Other	S.cerevisiae
3993	RSP5_YEAST	FUR4_YEAST	P39940	P05316	RSP5	FUR4	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3994	RSP5_YEAST	ART5_YEAST	P39940	P53244	RSP5	ART5	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3995	RSP5_YEAST	SC61A_YEAST	P39940	P32915	RSP5	SEC61	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3996	RSP5_YEAST	TRE1_YEAST	P39940	Q08919	RSP5	TRE1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3997	RSP5_YEAST	SIP5_YEAST	P39940	P40210	RSP5	SIP5	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3998	RSP5_YEAST	RPB1_YEAST	P39940	P04050	RSP5	RPO21	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
3999	RSP5_YEAST	CDC3_YEAST	P39940	P32457	RSP5	CDC3	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
4000	RSP5_YEAST	PHO87_YEAST	P39940	P25360	RSP5	PHO87	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
4001	SAF1_YEAST	URA7_YEAST	P38352	P28274	SAF1	URA7	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
4002	SAF1_YEAST	ADE_YEAST	P38352	P53909	SAF1	AAH1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
4003	SAN1_YEAST	SIR4_YEAST	P22470	P11978	SAN1	SIR4	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4004	SAN1_YEAST	SPT16_YEAST	P22470	P32558	SAN1	SPT16	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4005	SAN1_YEAST	SAM35_YEAST	P22470	P14693	SAN1	SAM35	MEDLINE	32118579	UbiNet 2.0	RING	1	Other	S.cerevisiae
4006	SAN1_YEAST	SIR3_YEAST	P22470	P06701	SAN1	SIR3	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4007	SAN1_YEAST	CDC13_YEAST	P22470	P32797	SAN1	CDC13	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4008	SAN1_YEAST	MEX67_YEAST	P22470	Q99257	SAN1	MEX67	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4009	SKP2_YEAST	SKP2_YEAST	P42843	P42843	SKP2	SKP2	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
4010	SLX8_YEAST	MOT1_YEAST	P40072	P32333	SLX8	MOT1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4011	DOA10_YEAST	MTAL2_YEAST	P40318	P0CY08	SSM4	MATALPHA2	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4012	DOA10_YEAST	MPS2_YEAS7	P40318	A6ZUA4	SSM4	MPS2	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4013	DOA10_YEAST	STE6_YEAST	P40318	P12866	SSM4	STE6	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4014	DOA10_YEAST	UBC6_YEAST	P40318	P33296	SSM4	UBC6	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4015	DOA10_YEAST	PYRF_YEAST	P40318	P03962	SSM4	URA3	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4016	DOA10_YEAST	CBF3A_YEAST	P40318	P32504	SSM4	CBF2	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4017	DOA10_YEAST	MPS2_YEAST	P40318	P53159	SSM4	MPS2	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4018	DOA10_YEAST	PMA1_YEAST	P40318	P05030	SSM4	PMA1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4019	TOM1_YEAST	NAB2_YEAST	Q03280	P32505	TOM1	NAB2	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
4020	TOM1_YEAST	TRA1_YEAST	Q03280	P38811	TOM1	TRA1	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
4021	TOM1_YEAST	YRA1_YEAST	Q03280	Q12159	TOM1	YRA1	MEDLINE	30951522	Previous work from our laboratory showed that <span class="match term1">Yra1</span> ubiquitination by <span class="match term0">Tom1</span> is important for mRNA export	HECT	1	Other	S.cerevisiae
4022	TOM1_YEAST	SPT7_YEAST	Q03280	P35177	TOM1	SPT7	MEDLINE	22199232	E3Net	HECT	1	Other	S.cerevisiae
4023	TUL1_YEAST	TLG1_YEAST	P36096	Q03322	TUL1	TLG1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4024	TUL1_YEAST	PPN1_YEAST	P36096	Q04119	TUL1	PPN1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4025	TUL1_YEAST	PEP12_YEAST	P36096	P32854	TUL1	PEP12	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4026	TUL1_YEAST	CBPS_YEAST	P36096	P27614	TUL1	CPS1	MEDLINE	22199232	E3Net	RING	1	Other	S.cerevisiae
4027	UBC4_YEAST	YSH1_YEAST	P15731	Q06224	UBC4	YSH1	MEDLINE	32009536	<span class="match term1">Ysh1</span> ubiquitination is mediated by the <span class="match term0">Ubc4</span> ubiquitin conjugating enzyme and Mpe1, which in addition to its function in C/P, is also a RING ubiquitin ligase	Other	1	Other	S.cerevisiae
4028	UBR1_YEAST	SEN2_YEAST	P19812	P16658	UBR1	SEN2	MEDLINE	32118579	UbiNet 2.0	UBOX	1	Other	S.cerevisiae
4029	UBR1_YEAST	CUP9_YEAST	P19812	P41817	UBR1	CUP9	MEDLINE	22199232	E3Net	UBOX	1	Other	S.cerevisiae
4030	UBR2_YEAST	RPN4_YEAST	Q07963	Q03465	UBR2	RPN4	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
4031	UCC1_YEAST	UCC1_YEAST	Q05947	Q05947	UCC1	UCC1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
4032	UFD2_YEAST	SPT23_YEAST	P54860	P35210	UFD2	SPT23	MEDLINE	22199232	E3Net	UBOX	1	Other	S.cerevisiae
4033	UFD4_YEAST	SSK1_YEAST	P33202	Q07084	UFD4	SSK1	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	S.cerevisiae
4034	UFD4_YEAST	CUE1_YEAST	P33202	P38428	UFD4	CUE1	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	S.cerevisiae
4035	UFD4_YEAST	UBC7_YEAST	P33202	Q02159	UFD4	UBC7	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	S.cerevisiae
4036	UFD4_YEAST	RAD4_YEAST	P33202	P14736	UFD4	RAD4	MEDLINE	22199232	E3Net	SINGLE_OTHER	1	Other	S.cerevisiae
4037	UFO1_YEAST	UFO1_YEAST	Q04511	Q04511	UFO1	UFO1	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
4038	UFO1_YEAST	POLH_YEAST	Q04511	Q04049	UFO1	RAD30	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
4039	UFO1_YEAST	HO_YEAST	Q04511	P09932	UFO1	HO	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
4040	YD306_YEAST	YD306_YEAST	Q06640	Q06640	YDR306C	YDR306C	MEDLINE	22199232	E3Net	Other	1	Other	S.cerevisiae
4041	RAG1_PIG	RAG1_PIG	Q867B5	Q867B5	RAG1	RAG1	MEDLINE	22199232	E3Net	Other	1	Other	S.scrofa
4042	RN19A_PIG	CASR_PIG	Q2VJ60	O62714	RNF19A	CASR	MEDLINE	22199232	E3Net	RING	1	Other	S.scrofa
4043	HRD1_SCHPO	SREBP_SCHPO	O74757	Q9UUD1	hrd1	sre1	MEDLINE	22199232	E3Net	RING	1	Other	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
4044	POF1_SCHPO	ZIP1_SCHPO	P87053	Q10424	pof1	zip1	MEDLINE	22199232	E3Net	F-box	1	Other	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
4045	POP2_SCHPO#POP1_SCHPO	CDC18_SCHPO	O14170#P87060	P41411	pop2#pop1	cdc18	MEDLINE	22199232	E3Net	Other	1	Other	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
4046	POP2_SCHPO#POP1_SCHPO	RUM1_SCHPO	O14170#P87060	P40380	pop2#pop1	rum1	MEDLINE	22199232	E3Net	Other	1	Other	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
4047	PUB1_SCHPO	MPIP_SCHPO	Q92462	P06652	pub1	cdc25	MEDLINE	8635463	<span class="match term0">Pub1</span> acts as an E6-AP-like protein ubiquitiin ligase in the degradation of <span class="match term1">cdc25</span>.	HECT	1	Other	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
4048	IPA9_SHIFL	NEMO_HUMAN	Q8VSC3	Q9Y6K9	ipaH9.8	IKBKG	MEDLINE	32296023	UbiNet 2.0	Other	1	Other	Shigella flexneri
4049	IPA9_SHIFL	GBP1_HUMAN	Q8VSC3	P32455	ipaH9.8	GBP1	MEDLINE	31216343	Structural mechanism for guanylate-binding proteins (GBPs) targeting by the Shigella E3 ligase <span class="match term0">IpaH9.8</span>.	Other	1	Other	Shigella flexneri
4050	P0_TYYVF	AGO9_ARATH	P09504	Q84VQ0	ORF0	AGO9	MEDLINE	22199232	E3Net	Other	1	Other	Turnip yellows virus (isolate FL-1) (TuYV) (BWYV-FL1)
4051	HAKAI_XENLA	CADH1_XENLA	Q4V7X9	P30944	cbll1	cdh1	MEDLINE	22199232	E3Net	Other	1	Other	Xenopus laevis (African clawed frog)
4052	DTLA_XENLA	PCNA_XENLA	Q4V837	P18248	dtl-a	pcna	MEDLINE	22199232	E3Net	Other	1	Other	Xenopus laevis (African clawed frog)
4053	DTLB_XENLA	PCNA_XENLA	Q6GPU3	P18248	dtl-b	pcna	MEDLINE	22199232	E3Net	Other	1	Other	Xenopus laevis (African clawed frog)
4054	KLH12_XENLA	-	Q6NRH0	-	klhl12	DSH	MEDLINE	16547521	UbiNet 2.0	Other	1	Other	Xenopus laevis (African clawed frog)
4055	MDM2_XENLA	MDM2_XENLA	P56273	P56273	mdm2	mdm2	MEDLINE	22199232	E3Net	RING	1	Other	Xenopus laevis (African clawed frog)
4056	MIB1_XENLA	Q91902_XENLA	Q6GNY1	Q91902	mib1	dll1.L	MEDLINE	22199232	E3Net	RING	1	Other	Xenopus laevis (African clawed frog)
4057	B1WBC4_XENLA	Q91902_XENLA	B1WBC4	Q91902	mib2.S	dll1.L	MEDLINE	22199232	E3Net	Other	1	Other	Xenopus laevis (African clawed frog)
4058	Q6GMD5_XENLA	Q9PWK7_XENLA	Q6GMD5	Q9PWK7	nedd4l.S	clcn5.L	MEDLINE	22199232	E3Net	Other	1	Other	Xenopus laevis (African clawed frog)
4059	Q8UVQ6_XENLA	Q91902_XENLA	Q8UVQ6	Q91902	neurl1.L	dll1.L	MEDLINE	22199232	E3Net	RING	1	Other	Xenopus laevis (African clawed frog)
4060	PAXI1_XENLA	PCNA_XENLA	Q90WJ3	P18248	paxip1	pcna	MEDLINE	22199232	E3Net	Other	1	Other	Xenopus laevis (African clawed frog)
4061	-	SNAI2_XENLA	-	Q91924	Ppa	snai2	MEDLINE	16887825	UbiNet 2.0	Other	1	Other	Xenopus laevis (African clawed frog)
4062	-	Q5U4S2_XENLA	-	Q5U4S2	Ppa	zeb2.S	MEDLINE	16887825	UbiNet 2.0	Other	1	Other	Xenopus laevis (African clawed frog)
4063	-	-	-	-	Ppa	twist	MEDLINE	16887825	UbiNet 2.0	Other	1	Other	Xenopus laevis (African clawed frog)
4064	RAG1_XENLA	H32_XENLA	Q91829	P84233	rag1	-	MEDLINE	22199232	E3Net	Other	1	Other	Xenopus laevis (African clawed frog)
4065	RAG1_XENLA	H33_XENLA	Q91829	Q6PI79	rag1	-	MEDLINE	22199232	E3Net	Other	1	Other	Xenopus laevis (African clawed frog)
4066	NIPA_XENLA	CCNB1_XENLA	Q6P7H4	P13350	zc3hc1	ccnb1	MEDLINE	22199232	E3Net	Other	1	Other	Xenopus laevis (African clawed frog)
4067	LAP_YMTV5	CD4_ERYPA	Q6TV02	Q08339	LAP	CD4	MEDLINE	22199232	E3Net	Other	1	Other	Yaba monkey tumor virus (strain VR587) (YMTV)
4068	LAP_YLDV	CD4_HUMAN	Q9DHV7	P01730	5L	CD4	MEDLINE	22199232	E3Net	Other	1	Other	Yaba-like disease virus (YLDV)