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Protein Page:
RCHY1 (human)

Overview
RCHY1 Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, HDAC1 and p27Kip1. Preferentially acts on tetrameric p53/TP53. Contributes to the regulation of p27Kip1 and p53/TP53 levels, and thereby contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity. Monomer and homodimer. Interacts with AR, p53/TP53, MDM2, HDAC1, KAT5, PLAG1, PLAGL2, p27Kip1, COPE, UBE2D2 and GORAB/NTKLBP1. Up-regulated during the S phase of the cell cycle. Expressed at low levels during G phase. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 6.3.2.-; Ubiquitin conjugating system; EC 6.3.2.19; Nuclear receptor co-regulator; Ubiquitin ligase
Cellular Component: cytoplasm; nucleolus; nuclear speck; nucleus; ubiquitin ligase complex
Molecular Function: protein binding; protein homodimerization activity; zinc ion binding; p53 binding; ubiquitin-protein ligase activity; receptor binding
Biological Process: protein autoubiquitination; positive regulation of protein ubiquitination; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; protein ubiquitination during ubiquitin-dependent protein catabolic process; protein ubiquitination
Reference #:  Q96PM5 (UniProtKB)
Alt. Names/Synonyms: Androgen receptor N-terminal-interacting protein; androgen-receptor N-terminal-interacting protein; ARNIP; CH-rich interacting match with PLAG1; CH-rich-interacting match with PLAG1; CHIMP; DKFZp586C1620; E3 ubiquitin-protein ligase Pirh2; hARNIP; hPirh2; p53-induced RING-H2 protein; PIRH2; PRO1996; RCHY1; ring finger and CHY zinc finger domain containing 1; RING finger and CHY zinc finger domain-containing protein 1; RING finger protein 199; RNF199; Zinc finger protein 363; ZN363; ZNF363
Gene Symbols: RCHY1
Molecular weight: 30,110 Da
Basal Isoelectric point: 6.26  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RCHY1

Protein Structure Not Found.


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Sites Implicated In
cell growth, altered: T154‑p, S155‑p
transcription, inhibited: S211‑p, T217‑p
activity, inhibited: S211‑p, T217‑p
enzymatic activity, inhibited: T154‑p, S155‑p
intracellular localization: T154‑p, S155‑p
ubiquitination: T154‑p, S155‑p, S211‑p, T217‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 1 T154-p ICLEDIHtsRVVAHV
1 1 S155-p CLEDIHtsRVVAHVL
0 2 Y173-p HLLHRTCyEEMLKEG
0 2 Y181-p EEMLKEGyRCPLCMH
1 0 S211-p VAQTPMPsEYQNMtV
1 0 T217-p PsEYQNMtVDILCND
0 6 S257-p QAGGRRIsLDQQ___
  mouse

 
T154 ICLEDIHTSRVVAHV
S155 CLEDIHTSRVVAHVL
Y173 HLLHRTCYEEMLKEG
Y181 EEMLKEGYRCPLCMH
S211 VAQTPMPSEYQNVTV
T217 PSEYQNVTVDILCND
P257 QAGGRRVPVDQQ___
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