Tag | Content |
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CPLM ID | CPLM-019526 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | RING finger and CHY zinc finger domain-containing protein 1 |
Protein Synonyms/Alias | Androgen receptor N-terminal-interacting protein; CH-rich-interacting match with PLAG1; E3 ubiquitin-protein ligase Pirh2; RING finger protein 199; Zinc finger protein 363; p53-induced RING-H2 protein; hPirh2 |
Gene Name | RCHY1 |
Gene Synonyms/Alias | ARNIP; CHIMP; PIRH2; RNF199; ZNF363 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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30 | YDRGCLLKAPCCDKL | ubiquitination | [1] | 58 | QLDRFKVKEVQCINC | ubiquitination | [1] | 135 | MNLQGRHKCIENVSR | ubiquitination | [1] | 178 | TCYEEMLKEGYRCPL | ubiquitination | [1] | 241 | HILGMKCKICESYNT | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity. |
Sequence Annotation | ZN_FING 13 80 CHY-type. ZN_FING 82 144 CTCHY-type. ZN_FING 145 189 RING-type. MOD_RES 257 257 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 261 AA |
Protein Sequence | MAATAREDGA SGQERGQRGC EHYDRGCLLK APCCDKLYTC RLCHDNNEDH QLDRFKVKEV 60 QCINCEKIQH AQQTCEECST LFGEYYCDIC HLFDKDKKQY HCENCGICRI GPKEDFFHCL 120 KCNLCLAMNL QGRHKCIENV SRQNCPICLE DIHTSRVVAH VLPCGHLLHR TCYEEMLKEG 180 YRCPLCMHSA LDMTRYWRQL DDEVAQTPMP SEYQNMTVDI LCNDCNGRST VQFHILGMKC 240 KICESYNTAQ AGGRRISLDQ Q 261 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:HGNC. GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IDA:UniProtKB. GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB. GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IDA:UniProtKB. GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB. GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB. GO:0051865; P:protein autoubiquitination; IDA:UniProtKB. GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB. |
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