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Protein Page:
RCHY1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Ubiquitin ligase; Nuclear receptor co-regulator; Ubiquitin conjugating system; EC 6.3.2.19; EC 6.3.2.-
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; 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 Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

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

 
0 1 K135-ub MNLQGRHkCIENVSR
1 1 T154-p ICLEDIHtsRVVAHV
1 1 S155-p CLEDIHtsRVVAHVL
0 1 T171-p CGHLLHRtCyEEMLK
0 1 Y173-p HLLHRtCyEEMLKEG
0 1 Y181-p EEMLKEGyRCPLCMH
1 0 S211-p VAQTPMPsEYQNMtV
1 0 T217-p PsEYQNMtVDILCND
0 1 K241-ub HILGMKCkICESYNT
0 7 S257-p QAGGRRIsLDQQ___
  mouse

 
K135 TNLRGKHKCIENVSR
T154 ICLEDIHTSRVVAHV
S155 CLEDIHTSRVVAHVL
T171 CGHLLHRTCYEEMLK
Y173 HLLHRTCYEEMLKEG
Y181 EEMLKEGYRCPLCMH
S211 VAQTPMPSEYQNVTV
T217 PSEYQNVTVDILCND
K241 HILGMKCKLCDSYNT
P257 QAGGRRVPVDQQ___
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