Q96PM5 · ZN363_HUMAN
- ProteinRING finger and CHY zinc finger domain-containing protein 1
- GeneRCHY1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids261 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase that mediates ubiquitination of target proteins, including p53/TP53, TP73, HDAC1 and CDKN1B (PubMed:16914734, PubMed:17721809, PubMed:18006823, PubMed:19043414, PubMed:19483087, PubMed:21994467).
Mediates ubiquitination and degradation of p53/TP53; preferentially acts on tetrameric p53/TP53 (PubMed:19043414, PubMed:19483087).
Catalyzes monoubiquitinates the translesion DNA polymerase POLH (PubMed:21791603).
Involved in the ribosome-associated quality control (RQC) pathway, which mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes: RCHY1 acts downstream of NEMF and recognizes CAT tails associated with stalled nascent chains, leading to their ubiquitination and degradation (PubMed:33909987).
Mediates ubiquitination and degradation of p53/TP53; preferentially acts on tetrameric p53/TP53 (PubMed:19043414, PubMed:19483087).
Catalyzes monoubiquitinates the translesion DNA polymerase POLH (PubMed:21791603).
Involved in the ribosome-associated quality control (RQC) pathway, which mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes: RCHY1 acts downstream of NEMF and recognizes CAT tails associated with stalled nascent chains, leading to their ubiquitination and degradation (PubMed:33909987).
Isoform 4
Has no E3 ubiquitin-protein ligase activity.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 20 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 22 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 33 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 34 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 40 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 43 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 44 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 50 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 62 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 65 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 75 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 78 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 87 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 90 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 101 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 102 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 105 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 108 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 118 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 119 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 122 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 125 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 134 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 136 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | p53 binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | error-free translesion synthesis | |
Biological Process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process | |
Biological Process | positive regulation of protein ubiquitination | |
Biological Process | protein autoubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | rescue of stalled ribosome | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRING finger and CHY zinc finger domain-containing protein 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96PM5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 176 | Abolishes E3 ubiquitin-protein ligase activity. | ||||
Sequence: M → E | ||||||
Mutagenesis | 186 | Abolishes E3 ubiquitin-protein ligase activity. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 240 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056312 | 1-261 | RING finger and CHY zinc finger domain-containing protein 1 | |||
Sequence: MAATAREDGASGQERGQRGCEHYDRGCLLKAPCCDKLYTCRLCHDNNEDHQLDRFKVKEVQCINCEKIQHAQQTCEECSTLFGEYYCDICHLFDKDKKQYHCENCGICRIGPKEDFFHCLKCNLCLAMNLQGRHKCIENVSRQNCPICLEDIHTSRVVAHVLPCGHLLHRTCYEEMLKEGYRCPLCMHSALDMTRYWRQLDDEVAQTPMPSEYQNMTVDILCNDCNGRSTVQFHILGMKCKICESYNTAQAGGRRISLDQQ | ||||||
Modified residue | 257 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Subject to ubiquitination and proteasomal degradation. Interaction with PLAGL2 or KAT5 enhances protein stability.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Interaction
Subunit
Monomer and homodimer. Interacts with AR, MDM2, KAT5, PLAG1, PLAGL2, COPE, UBE2D2 and GORAB/NTKLBP1.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 13-80 | CHY-type | ||||
Sequence: QERGQRGCEHYDRGCLLKAPCCDKLYTCRLCHDNNEDHQLDRFKVKEVQCINCEKIQHAQQTCEECST | ||||||
Zinc finger | 82-144 | CTCHY-type | ||||
Sequence: FGEYYCDICHLFDKDKKQYHCENCGICRIGPKEDFFHCLKCNLCLAMNLQGRHKCIENVSRQN | ||||||
Zinc finger | 145-189 | RING-type | ||||
Sequence: CPICLEDIHTSRVVAHVLPCGHLLHRTCYEEMLKEGYRCPLCMHS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 8 isoforms produced by Alternative splicing.
Q96PM5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsA
- Length261
- Mass (Da)30,110
- Last updated2001-12-01 v1
- ChecksumAC03786F6B42A03D
Q96PM5-2
- Name2
- SynonymsB
- Differences from canonical
- 171-179: Missing
Q96PM5-3
- Name3
- SynonymsC
- Differences from canonical
- 180-261: Missing
Q96PM5-4
- Name4
- SynonymsPirh2b
- Differences from canonical
- 180-261: GYRCPLCMHSALDMTRYWRQLDDEVAQTPMPSEYQNMTVDILCNDCNGRSTVQFHILGMKCKICESYNTAQAGGRRISLDQQ → YDQVLETAG
Q96PM5-5
- Name5
- SynonymsPirh2D
Q96PM5-6
- Name6
- Differences from canonical
- 1-30: MAATAREDGASGQERGQRGCEHYDRGCLLK → MAPAVKSE
Q96PM5-7
- Name7
- NoteGene prediction based on partial mRNA data.
- Differences from canonical
- 31-70: Missing
Q96PM5-8
- Name8
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_053787 | 1-30 | in isoform 6 | |||
Sequence: MAATAREDGASGQERGQRGCEHYDRGCLLK → MAPAVKSE | ||||||
Sequence conflict | 11-13 | in Ref. 1; ACT35531/ACT35532/ACT35533 and 3; AAK96896 | ||||
Sequence: SGQ → TGE | ||||||
Alternative sequence | VSP_053788 | 31-70 | in isoform 7 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_053385 | 68-75 | in isoform 5 | |||
Sequence: IQHAQQTC → NSTCPTDL | ||||||
Alternative sequence | VSP_053386 | 76-261 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 142 | in Ref. 11; AAH47393 | ||||
Sequence: R → Q | ||||||
Alternative sequence | VSP_038467 | 171-179 | in isoform 2 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_038468 | 180-261 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_044085 | 180-261 | in isoform 4 | |||
Sequence: GYRCPLCMHSALDMTRYWRQLDDEVAQTPMPSEYQNMTVDILCNDCNGRSTVQFHILGMKCKICESYNTAQAGGRRISLDQQ → YDQVLETAG | ||||||
Sequence conflict | 220 | in Ref. 8; BAD92309 | ||||
Sequence: I → F |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GQ250944 EMBL· GenBank· DDBJ | ACT35531.1 EMBL· GenBank· DDBJ | mRNA | ||
GQ250945 EMBL· GenBank· DDBJ | ACT35532.1 EMBL· GenBank· DDBJ | mRNA | ||
GQ250946 EMBL· GenBank· DDBJ | ACT35533.1 EMBL· GenBank· DDBJ | mRNA | ||
AF247041 EMBL· GenBank· DDBJ | AAL76101.1 EMBL· GenBank· DDBJ | mRNA | ||
AF255666 EMBL· GenBank· DDBJ | AAK96896.1 EMBL· GenBank· DDBJ | mRNA | ||
AF305424 EMBL· GenBank· DDBJ | AAL09356.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209072 EMBL· GenBank· DDBJ | BAD92309.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY888047 EMBL· GenBank· DDBJ | AAX78233.1 EMBL· GenBank· DDBJ | mRNA | ||
GU937000 EMBL· GenBank· DDBJ | ADD21555.1 EMBL· GenBank· DDBJ | mRNA | ||
AK091501 EMBL· GenBank· DDBJ | BAG52375.1 EMBL· GenBank· DDBJ | mRNA | ||
AC096759 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471057 EMBL· GenBank· DDBJ | EAX05725.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC047393 EMBL· GenBank· DDBJ | AAH47393.1 EMBL· GenBank· DDBJ | mRNA |