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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: Nuclear receptor co-regulator; EC 6.3.2.-; Ubiquitin ligase; Ubiquitin conjugating system; EC 6.3.2.19 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®

Select Structure to View Below RCHY1 2JRJ - A=138-189 (human) 2K2C - A=1-137 (human) 2K2D - A=187-261 (human) 2DKT - A=9-138 (mouse) 2ECM - A=145-186 (mouse)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 2JRJ 2K2C 2K2D  |  Phospho3D  |  DISEASE  |  NURSA  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

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

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-u	MNLQGRHkCIENVSR
1	1		T154-p	ICLEDIHtsRVVAHV
1	1		S155-p	CLEDIHtsRVVAHVL
0	1		T171-p	CGHLLHRtCyEEMLK
0	2		Y173-p	HLLHRtCyEEMLKEG
0	2		Y181-p	EEMLKEGyRCPLCMH
0	1		K241-u	HILGMKCkICESYNT
0	5		S257-p	QAGGRRIsLDQQ___

	mouse
K135	TNLRGKHKCIENVSR
T154	ICLEDIHTSRVVAHV
S155	CLEDIHTSRVVAHVL
T171	CGHLLHRTCYEEMLK
Y173	HLLHRTCYEEMLKEG
Y181	EEMLKEGYRCPLCMH
K241	HILGMKCKLCDSYNT
P257	QAGGRRVPVDQQ___

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