CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
30YDRGCLLKAPCCDKLubiquitination[1]
58QLDRFKVKEVQCINCubiquitination[1]
135MNLQGRHKCIENVSRubiquitination[1]
178TCYEEMLKEGYRCPLubiquitination[1]
241HILGMKCKICESYNTubiquitination[1]
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. 
Interpro
 IPR004039; Rubredoxin-type_fold.
 IPR008913; Znf_CHY.
 IPR017921; Znf_CTCHY.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF05495; zf-CHY
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS51266; ZF_CHY
 PS51270; ZF_CTCHY
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS