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Protein Page:
MSH2 (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
MSH2 Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2- MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis. Heterodimer consisting of MSH2-MSH6 (MutS alpha) or MSH2- MSH3 (MutS beta). Both heterodimer form a ternary complex with MutL alpha (MLH1-PMS1). Interacts with EXO1. Part of the BRCA1- associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with ATR. Interacts with SLX4/BTBD12; this interaction is direct and links MutS beta to SLX4, a subunit of different structure-specific endonucleases. Interacts with SMARCAD1. Ubiquitously expressed. Belongs to the DNA mismatch repair MutS family. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein
Cellular Component: nuclear chromosome; membrane; MutSalpha complex; MutSbeta complex
Molecular Function: protein C-terminus binding; DNA-dependent ATPase activity; protein homodimerization activity; double-strand/single-strand DNA junction binding; dinucleotide repeat insertion binding; single thymine insertion binding; ATPase activity; oxidized purine DNA binding; magnesium ion binding; ADP binding; protein kinase binding; mismatched DNA binding; loop DNA binding; Y-form DNA binding; centromeric DNA binding; protein binding; enzyme binding; four-way junction DNA binding; DNA binding; single guanine insertion binding; guanine/thymine mispair binding; double-stranded DNA binding; MutLalpha complex binding; dinucleotide insertion or deletion binding; single-stranded DNA binding; ATP binding
Biological Process: determination of adult life span; maintenance of DNA repeat elements; germ cell development; positive regulation of helicase activity; double-strand break repair; negative regulation of neuron apoptosis; cell cycle arrest; DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; response to X-ray; oxidative phosphorylation; ATP catabolic process; negative regulation of DNA recombination; mismatch repair; postreplication repair; in utero embryonic development; somatic hypermutation of immunoglobulin genes; male gonad development; isotype switching; DNA repair; response to UV-B; meiotic mismatch repair; B cell mediated immunity; intra-S DNA damage checkpoint; B cell differentiation; somatic recombination of immunoglobulin gene segments; meiotic gene conversion; negative regulation of meiotic recombination
Reference #:  P43246 (UniProtKB)
Alt. Names/Synonyms: COCA1; DNA mismatch repair protein Msh2; FCC1; hMSH2; HNPCC; HNPCC1; LCFS2; MSH2; mutS homolog 2, colon cancer, nonpolyposis type 1 (E. coli); MutS protein homolog 2
Gene Symbols: MSH2
Molecular weight: 104,743 Da
Basal Isoelectric point: 5.58  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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MSH2

Protein Structure Not Found.


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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 2 Y66-p KTQGVIKyMGPAGAk
0 3 K73-ac yMGPAGAkNLQsVVL
0 2 K73-ub yMGPAGAkNLQsVVL
0 1 S77-p AGAkNLQsVVLSKMN
0 1 K104-ac QYRVEVYkNRAGNKA
0 4 K104-m3 QYRVEVYkNRAGNKA
0 1 K110 YkNRAGNKASkENDW
0 1 K113-ac RAGNKASkENDWYLA
0 1 K113 RAGNKASKENDWYLA
0 1 K172-ub YVDSIQRkLGLCEFP
0 1 T206-p CVLPGGEtAGDMGKL
0 1 Y238-p DFSTKDIyQDLNRLL
0 22 K249-ub NRLLKGKkGEQMNSA
0 8 K332-ub SLAALLNkCKTPQGQ
0 1 K423 NVIQALEKHEGKHQK
0 1 S479-p PSFDPNLsELREIMN
0 1 K550-ac DIQKNGVkFTNSkLT
0 3 K555-ac GVkFTNSkLTSLNEE
0 1 K555-ub GVkFTNSkLTSLNEE
0 1 K565-ub SLNEEYTkNkTEYEE
0 1 K567-ub NEEYTkNkTEYEEAQ
0 1 K635-ac GQGRIILkASRHACV
0 5 K741-ub SILRSATkDsLIIID
0 1 S743-p LRSATkDsLIIIDEL
0 5 K845-ub KHVIECAkQKALELE
0 7 S860-p EFQYIGEsQGyDIME
0 2 Y863-p YIGEsQGyDIMEPAA
0 4 K871-ub DIMEPAAkkCYLERE
0 1 K872-ub IMEPAAkkCYLEREQ
0 1 K882-ub LEREQGEkIIQEFLS
0 1 T897-p KVKQMPFtEMsEENI
0 1 S900-p QMPFtEMsEENITIK
0 2 K918-ub LKAEVIAkNNsFVNE
0 2 S921-p EVIAkNNsFVNEIIS
  mouse

 
Y66 KTQGVIKYMGPAGSK
K73 YMGPAGSKTLQSVVL
K73 YMGPAGSKTLQSVVL
S77 AGSKTLQSVVLSKMN
K104 QYRVEVYKNKAGNKA
K104 QYRVEVYKNKAGNKA
K110 YKNKAGNKASKENEW
K113 KAGNKASKENEWYLA
K113 KAGNKASKENEWYLA
K172 YVDSTQRKLGLCEFP
T206 CVLPGGETTGDMGKL
Y238 DFSTKDIYQDLNRLL
K249-ub NRLLKGKkGEQINSA
K332-ub SLAALLNkCKTAQGQ
K423-ub SVIQALEkYEGRHQA
S479 PSFDPNLSELREVMD
K550 DIQKNGVKFTNSELS
E555 GVKFTNSELSSLNEE
E555 GVKFTNSELSSLNEE
K565 SLNEEYTKNKGEYEE
K567 NEEYTKNKGEYEEAQ
K635 GKGRIILKASRHACV
K741 SILRSATKDSLIIID
S743 LRSATKDSLIIIDEL
K845 RHVIACAKQKALELE
S860 EFQNIGTSLGCDEAE
C863 NIGTSLGCDEAEPAA
K871 DEAEPAAKRRCLERE
R872 EAEPAAKRRCLEREQ
K882 LEREQGEKIILEFLS
T897 KVKQVPFTAMSEESI
S900 QVPFTAMSEESISAK
K918 LKAEVVAKNNSFVNE
S921 EVVAKNNSFVNEIIS
  rat

 
Y66-p KTQGVIKyMGPAGAK
K73 yMGPAGAKTLQTVVL
K73 yMGPAGAKTLQTVVL
T77 AGAKTLQTVVLSKMN
K104 HYRVEVYKNKAGNkA
K104 HYRVEVYKNKAGNkA
K110-ub YKNKAGNkASkENDW
K113 KAGNkASKENDWYLA
K113-ub KAGNkASkENDWYLA
K172 DVDSTQRKLGLCEFP
T206 CILPGGETAGDMGKL
Y238 DFSTKDIYQDLNRLL
K249 NRLLKGRKGEQMNSA
K332 SLAAFLNKCKTAQGQ
K423 NVIQALEKYQGRHQA
S479 PSFDPNLSELREVMD
K550 DIQKNGVKFTNSELS
E555 GVKFTNSELSSLNEE
E555 GVKFTNSELSSLNEE
K565 SLNEEYTKNKGEYEE
K567 NEEYTKNKGEYEEAQ
K635 GKGRIIVKASRHACV
K741 SILRSATKDSLIIID
S743 LRSATKDSLIIIDEL
K845 RHVIECAKQKALELE
S860 EFQSIGTSQGHDETQ
H863 SIGTSQGHDETQPAA
K871 DETQPAAKRRCLERE
R872 ETQPAAKRRCLEREQ
K882 LEREQGEKIILEFLS
T897 KVKQVPFTDLSEESV
S900 QVPFTDLSEESVSVK
K918 LKAEVLAKNNSFVNE
S921 EVLAKNNSFVNEIIS
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