Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
MUTYH (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Hydrolase; Tumor suppressor; EC 3.2.2.-; Mitochondrial; DNA repair, damage
Chromosomal Location of Human Ortholog: 1p34.1
Cellular Component: mitochondrion; nucleoplasm; nucleus
Molecular Function: 4 iron, 4 sulfur cluster binding; DNA N-glycosylase activity; metal ion binding; MutLalpha complex binding; MutLbeta complex binding; MutSalpha complex binding; MutSbeta complex binding; protein binding
Biological Process: base-excision repair; base-excision repair, AP site formation; depurination; DNA repair; mismatch repair; response to oxidative stress
Disease: Familial Adenomatous Polyposis, 2; Gastric Cancer; Pilomatrixoma
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® Total Proteins
Select Structure to View Below

MUTYH

Protein Structure Not Found.


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


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

Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

HTP: 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 S24‑p KPRAAVGsGHRKQAA
0 1 K105‑ub LSWYDQEkRDLPWRR
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
- gap
K79 LSWYDQEKRDLPWRN
S331 ANFPRKASRRPPREE
Y465 MKKVFRMYEDHRQGT
S476 RQGTRKGSKRSQVCP
P483 SKRSQVCPPSSRKKP
P506 TFFQRHIPTDKPNST
  rat

 
S7 _MKKLRASVRSHKKQ
S10 KLRASVRSHKKQPAN
- gap
K79 LSWYDQEKRDLPWRK
S331 VNFPRKASRRPPREE
Y466 MKKVFRVYEEHRRGT
S477 RRGTCKGSKRPQVCT
T484 SKRPQVCTPSSRKKP
P507 RFFQRHIPTHKPNST
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.