ZN363

Details:

UniProt Entry: Q96PM5
Gene: RCHY1
Class: RING
Family: RING4
Protein length: 261
Database confidence: 1.0
InterPro: InterPro Entry
Mode of Action: Complex
AlphaFold Model: Link
PDB Structures: 2jrj, 2k2c, 2k2d, 7ynx

Protein Sequence ▾

>Q96PM5
MAATAREDGA SGQERGQRGC EHYDRGCLLK APCCDKLYTC RLCHDNNEDH QLDRFKVKEV
QCINCEKIQH AQQTCEECST LFGEYYCDIC HLFDKDKKQY HCENCGICRI GPKEDFFHCL
KCNLCLAMNL QGRHKCIENV SRQNCPICLE DIHTSRVVAH VLPCGHLLHR TCYEEMLKEG
YRCPLCMHSA LDMTRYWRQL DDEVAQTPMP SEYQNMTVDI LCNDCNGRST VQFHILGMKC
KICESYNTAQ AGGRRISLDQ Q

Domain Architecture (From InterPro) ▾

Start	End	Type	Name	InterPro	Source
13	80	Domain	Zinc finger, CHY-type	IPR008913	PS51266
16	82	Homologous_superfamily	Zinc finger, CHY-type superfamily	IPR037274	SSF161219
20	92	Domain	Zinc finger, CHY-type	IPR008913	PF05495
82	144	Domain	Zinc finger, CTCHY-type	IPR017921	PS51270
83	138	Homologous_superfamily	Zinc finger, CTCHY-type superfamily	IPR037275	SSF161245
138	188	Homologous_superfamily	Zinc finger, RING/FYVE/PHD-type	IPR013083	G3DSA:3.30.40.10
144	186	Domain	Zinc finger, RING-type	IPR001841	PF13639
145	186	Domain	Zinc finger, RING-type	IPR001841	SM00184
145	186	Domain	Zinc finger, RING-type	IPR001841	PS50089
191	248	Domain	RCHY1, zinc-ribbon	IPR039512	PF14599

Protein functions ▾

GO term	Name	Ontology	Evidence	Reference
GO:0006511	ubiquitin-dependent protein catabolic process	Biological Process	IBA	GO_REF:0000033
GO:0016567	protein ubiquitination	Biological Process	IBA	GO_REF:0000033
GO:0031398	positive regulation of protein ubiquitination	Biological Process	IDA	PMID:19483087
GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	Biological Process	IDA	PMID:19483087
GO:0070987	error-free translesion synthesis	Biological Process	TAS	Reactome:R-HSA-110320
GO:0072344	rescue of stalled ribosome	Biological Process	IDA	PMID:33909987
GO:0005634	nucleus	Cellular Component	IEA	GO_REF:0000120
GO:0005654	nucleoplasm	Cellular Component	IDA	GO_REF:0000052
GO:0005737	cytoplasm	Cellular Component	IEA	GO_REF:0000120
GO:0005829	cytosol	Cellular Component	IDA	GO_REF:0000052
GO:0016607	nuclear speck	Cellular Component	IEA	GO_REF:0000044
GO:0000151	ubiquitin ligase complex	Cellular Component	IDA	PMID:19043414
GO:0008270	zinc ion binding	Molecular Function	IEA	GO_REF:0000120
GO:0046872	metal ion binding	Molecular Function	IEA	GO_REF:0000043
GO:0002039	p53 binding	Molecular Function	IPI	PMID:19043414
GO:0004842	ubiquitin-protein transferase activity	Molecular Function	TAS	Reactome:R-HSA-5655170
GO:0005515	protein binding	Molecular Function	IPI	PMID:15781263
GO:0016740	transferase activity	Molecular Function	IEA	GO_REF:0000043
GO:0042803	protein homodimerization activity	Molecular Function	IPI	PMID:19483087
GO:0061630	ubiquitin protein ligase activity	Molecular Function	IEA	GO_REF:0000003

Enzyme–Substrate Interactions ▾


O14579	COPE	Yes	Yes	No	No	—	No	E3-specific
Q9Y253	POLH	Yes	Yes	No	No	—	No	E3-specific
Q15717	ELAV1	Yes	No	No	No	—	No	E3-specific
Q9Y5M8	SRPRB	Yes	Yes	No	No	—	No	E3-specific
P49458	SRP09	Yes	Yes	No	No	—	No	E3-specific
Q5T7V8	GORAB	Yes	Yes	Yes	No	20452352, 21988832	EBI-7943644	E3-specific

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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.
Website maintained by Alberto Cristiani, Arghya Dutta, and Siddhanta V. Nikte.