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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)

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

Related

pirh2 gene

General

nuclear protein phosphoprotein ring finger protein E3 ubiquitin ligase; ubiquitin-ligating enzyme E3; N end-recognizing protein

Properties

SIZE: entity length = 261 aa MW = 30 kD COMPARTMENT: cytoplasm cell nucleus MOTIF: Zinc finger NAME: Zinc finger SITE: 13-80 EFFECTOR-BOUND: Zn+2 Zinc finger NAME: Zinc finger SITE: 82-144 EFFECTOR-BOUND: Zn+2 RING-finger {145-189} EFFECTOR-BOUND: Zn+2 FOR-BINDING-OF: DNA motif Ser phosphorylation site {S257}

Database Correlations

OMIM 607680 UniProt Q96PM5 Pfam PF05495 Entrez Gene 25898 Kegg hsa:25898

References

  1. UniProt :accession Q96PM5
  2. Atlas of Genetics & Cytogenetics in Oncology & Haematology http://atlasgeneticsoncology.org/genes/RCHY1ID43012ch04q21.html
  3. Leng RP et al Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell 112:779-791, 2003 PMID: 12654245
  4. 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: 14701804