UBE2C

Details:

UniProt Entry: O00762
Gene: UBE2C
Class: Other E3 Components
Family: E2
Protein length: 179
Database confidence: 0.125
InterPro: InterPro Entry
Mode of Action: unknown
AlphaFold Model: Link

Protein Sequence ▾

>O00762
MASQNRDPAA TSVAAARKGA EPSGGAARGP VGKRLQQELM TLMMSGDKGI SAFPESDNLF
KWVGTIHGAA GTVYEDLRYK LSLEFPSGYP YNAPTVKFLT PCYHPNVDTQ GNICLDILKE
KWSALYDVRT ILLSIQSLLG EPNIDSPLNT HAAELWKNPT AFKKYLQETY SKQVTSQEP

Domain Architecture (From InterPro) ▾

Start	End	Type	Name	InterPro	Source
26	179	Homologous_superfamily	Ubiquitin-conjugating enzyme/RWD-like	IPR016135	G3DSA:3.10.110.10
30	175	Domain	Ubiquitin-conjugating enzyme E2	IPR000608	PS50127
32	172	Homologous_superfamily	Ubiquitin-conjugating enzyme/RWD-like	IPR016135	SSF54495
33	170	Domain	Ubiquitin-conjugating enzyme E2	IPR000608	cd00195
34	168	Domain	Ubiquitin-conjugating enzyme E2	IPR000608	PF00179
103	118	Active_site	Ubiquitin-conjugating enzyme, active site	IPR023313	PS00183

Protein functions ▾

GO term	Name	Ontology	Evidence	Reference
GO:0031146	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	Biological Process	IDA	PMID:22017875
GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	Biological Process	IDA	PMID:27910872
GO:0045842	positive regulation of mitotic metaphase/anaphase transition	Biological Process	IDA	PMID:9637688
GO:0000209	protein polyubiquitination	Biological Process	IBA	GO_REF:0000033
GO:0006511	ubiquitin-dependent protein catabolic process	Biological Process	IDA	PMID:18485873
GO:0010458	exit from mitosis	Biological Process	IMP	PMID:19822757
GO:0010994	free ubiquitin chain polymerization	Biological Process	IDA	PMID:19822757
GO:0016567	protein ubiquitination	Biological Process	IEA	GO_REF:0000041
GO:0030071	regulation of mitotic metaphase/anaphase transition	Biological Process	IBA	GO_REF:0000033
GO:0031145	anaphase-promoting complex-dependent catabolic process	Biological Process	IBA	GO_REF:0000033
GO:0031536	positive regulation of exit from mitosis	Biological Process	IMP	PMID:9122200
GO:0032446	protein modification by small protein conjugation	Biological Process	IEA	GO_REF:0000117
GO:0051301	cell division	Biological Process	IEA	GO_REF:0000043
GO:0070936	protein K48-linked ubiquitination	Biological Process	IDA	PMID:20061386
GO:0070979	protein K11-linked ubiquitination	Biological Process	IDA	PMID:18485873
GO:1904668	positive regulation of ubiquitin protein ligase activity	Biological Process	TAS	PMID:17443180
GO:0005634	nucleus	Cellular Component	IBA	GO_REF:0000033
GO:0005654	nucleoplasm	Cellular Component	TAS	Reactome:R-HSA-174057
GO:0005829	cytosol	Cellular Component	IDA	GO_REF:0000052
GO:0005886	plasma membrane	Cellular Component	IDA	GO_REF:0000052
GO:0000151	ubiquitin ligase complex	Cellular Component	IDA	PMID:15749827
GO:0005680	anaphase-promoting complex	Cellular Component	IDA	PMID:16413484
GO:0004842	ubiquitin-protein transferase activity	Molecular Function	IDA	PMID:18485873
GO:0000166	nucleotide binding	Molecular Function	IEA	GO_REF:0000043
GO:0005515	protein binding	Molecular Function	IPI	PMID:19822757
GO:0005524	ATP binding	Molecular Function	IEA	GO_REF:0000043
GO:0016740	transferase activity	Molecular Function	IEA	GO_REF:0000043
GO:0019787	ubiquitin-like protein transferase activity	Molecular Function	IEA	GO_REF:0000117
GO:0044389	ubiquitin-like protein ligase binding	Molecular Function	IPI	PMID:15749827
GO:0061630	ubiquitin protein ligase activity	Molecular Function	TAS	Reactome:R-HSA-9686969
GO:0061631	ubiquitin conjugating enzyme activity	Molecular Function	IEA	GO_REF:0000003

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The E3 Ligome database, including all associated data, metadata, and documentation, is the intellectual property of Goethe University (PROXIDRUGs consortium) under the InnoDATA project.
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If you use or refer to the Database in your publications, reports, or presentations, you must cite the paper: Dutta, A., Cristiani, A., Nikte, S.V. et al. Multi-scale classification decodes the complexity of the human E3 ligome. Nat Commun 16, 11382 (2025).

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For inquiries, permissions, or support regarding the Database, please contact: Dr. Ramachandra M. Bhaskara, Goethe University Frankfurt.
Email: bhaskara@med.uni-frankfurt.de.
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