zinc finger protein 363; RING finger & CHY zinc finger domain-containing protein 1; androgen receptor N-terminal-interacting protein; CH-rich-interacting match with PLAG1; E3 ubiquitin-protein ligase Pirh2; RING finger protein 199; p53-induced RING-H2 protein; hPirh2 (RCHY1, ARNIP,CHIMP, PIRH2, RNF199, ZNF363)
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Function
- mediates E3-dependent ubiquitination & proteasomal degradation of target proteins, including p53/TP53, HDAC1 & CDKN1B
- preferentially acts on tetrameric p53/TP53
- role in regulation of CDKN1B & p53/TP53 levels, thus role in regulation of the cell cycle progression
- increases AR transcription factor activity
- protein modification; protein ubiquitination
- subject to ubiquitination & proteasomal degradation
- interaction with PLAGL2 or KAT5 enhances protein stability
- monomer & homodimer
- interacts with AR, p53/TP53, MDM2, HDAC1, KAT5, PLAG1, PLAGL2, CDKN1B, UBE2D2 & GORAB/NTKLBP1
- p53 induced ubiquitin protein ligase; interacts with amino acid residues 82-292 of p53 & promotes ubiquitination independent of mdm2[3]
Structure
- contains 1 CHY-type Zn+2 finger
- contains 1 CTCHY-type Zn+2 finger
- contains 1 RING-type Zn+2 finger
Compartment
nucleus. nucleus speckle. cytoplasm
Alternative splicing
named isoforms=3
Expression
- up-regulated during the S phase of the cell cycle
- expressed at low levels during G phase
More general terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/Q96PM5.html
- ↑ Atlas of Genetics & Cytogenetics in Oncology & Haematology http://atlasgeneticsoncology.org/genes/RCHY1ID43012ch04q21.html
- ↑ 3.0 3.1 Leng RP et al Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell 112:779-791, 2003 PMID: https://www.ncbi.nlm.nih.gov/pubmed/12654245
- ↑ Logan IR et al Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome. J Biol Chem 279(12):11696-11704, 2004 PMID: https://www.ncbi.nlm.nih.gov/pubmed/14701804