Home

MUTYH (human)

Overview MUTYH Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2- OH-A DNA glycosylase activities. Belongs to the Nth/MutY family. 6 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB. Protein type: Mitochondrial; Hydrolase; EC 3.2.2.-; DNA repair Cellular Component: nucleoplasm; mitochondrion; nucleus Molecular Function: protein binding; 4 iron, 4 sulfur cluster binding; endonuclease activity; metal ion binding; hydrolase activity, acting on glycosyl bonds; MutLalpha complex binding; MutLbeta complex binding; MutSbeta complex binding; MutSalpha complex binding Biological Process: mismatch repair; depurination; base-excision repair, AP site formation; base-excision repair; DNA repair Reference #:  Q9UIF7 (UniProtKB) Alt. Names/Synonyms: A/G-specific adenine DNA glycosylase; CYP2C; hMYH; MGC4416; MutY homolog; mutY homolog (E. coli); MUTYH; MYH Gene Symbols: MUTYH Molecular weight: 60,069 Da Basal Isoelectric point: 8.99  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below MUTYH 1X51 - A=356-497 (human) 3N5N - X/Y=76-362 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1X51 3N5N  |  ENZYME  |  Phospho3D  |  DISEASE 132600 137215 604933 608456  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
enzymatic activity, induced: S535‑p protein stabilization: S535‑p

	Modification Sites and Domains

	Modification Sites in Parent Protein, Orthologs, and Isoforms

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		S6-p	__MTPLVsRLsRLWA
0	1		S9-p	TPLVsRLsRLWAIMR
0	1		S360-p	VNFPRKAsRKPPREE
0	3		Y494-p	MKKVFRVyQGQQPGT
0	1		S505-p	QPGTCMGsKRSQVSs
0	3		S512-p	sKRSQVSsPCSRKKP
1	1		S535-p	NFFRSHIsTDAHSLN

	mouse
S7	_MKKLQASVRSHKKQ
S10	KLQASVRSHKKQPAN
S331	ANFPRKASRRPPREE
Y465	MKKVFRMYEDHRQGT
S476	RQGTRKGSKRSQVCP
P483	SKRSQVCPPSSRKKP
P506	TFFQRHIPTDKPNST

	rat
S7	_MKKLRASVRSHKKQ
S10	KLRASVRSHKKQPAN
S331	VNFPRKASRRPPREE
Y466	MKKVFRVYEEHRRGT
S477	RRGTCKGSKRPQVCT
T484	SKRPQVCTPSSRKKP
P507	RFFQRHIPTHKPNST

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.