DNA mismatch repair protein Msh2 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P43246 (MSH2_HUMAN)

Last modified June 16, 2009. Version 109. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
DNA mismatch repair protein Msh2
Alternative name(s):
MutS protein homolog 2

Gene names

Name:

MSH2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	934 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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. Ref.13 Ref.14 Ref.15 Ref.17 Ref.20 Ref.26 Ref.28
Subunit structure	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. Ref.11 Ref.12 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25
Subcellular location	Nucleus Potential.
Tissue specificity	Ubiquitously expressed. Ref.19
Post-translational modification	Phosphorylated by PRKCZ, which may prevent MutS alpha degradation by the ubiquitin-proteasome pathway. Ref.27 Ref.32 Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.27 Ref.32
Involvement in disease	Defects in MSH2 are the cause of hereditary non-polyposis colorectal cancer type 1 (HNPCC1) [MIM:120435]. Mutations in more than one gene locus can be involved alone or in combination in the production of the HNPCC phenotype (also called Lynch syndrome). Most families with clinically recognized HNPCC have mutations in either MLH1 or MSH2 genes. HNPCC is an autosomal, dominantly inherited disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early onset colorectal carcinoma (CRC) and extra-colonic cancers of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Cancers in HNPCC originate within benign neoplastic polyps termed adenomas. Clinically, HNPCC is often divided into two subgroups. Type I: hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II: patients have an increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term "suspected HNPCC" or "incomplete HNPCC" can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. MSH2 mutations may predispose to hematological malignancies and multiple cafe-au-lait spots. Ref.3 Ref.4 Ref.16 Ref.35 Ref.38 Ref.40 Ref.41 Ref.42 Ref.43 Ref.46 Ref.47 Ref.48 Ref.50 Ref.53 Ref.55 Ref.56 Ref.57 Ref.58 Ref.60 Ref.61 Ref.63 Ref.64 Ref.66 Ref.67 Ref.68 Ref.71 Ref.72 Ref.73 Ref.74 Ref.75 Ref.77 Ref.78 Ref.79 Ref.81 Ref.82 Ref.83 Ref.84 Ref.85 Ref.86 Ref.87 Ref.88 Ref.89 Ref.90 Ref.91 Ref.92 Ref.94 Ref.95 Ref.96 Defects in MSH2 are a cause of Muir-Torre syndrome (MTS) [MIM:158320]. MTS is a rare autosomal dominant disorder characterized by sebaceous neoplasms and visceral malignancy. Ref.4 Defects in MSH2 are a cause of susceptibility to endometrial cancer [MIM:608089]. Ref.4
Sequence similarities	Belongs to the DNA mismatch repair mutS family.
Sequence caution	The sequence AAC27930.1 differs from that shown. Reason: Frameshift at position 417. The frameshift is caused by a single nucleotide deletion which is found in a HNPCC kindred.

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Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Hereditary nonpolyposis colorectal cancer
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Anti-oncogene
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	B cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB isotype switching Inferred from sequence or structural similarity. Source: UniProtKB maintenance of DNA repeat elements Inferred from mutant phenotype. Source: HGNC male gonad development Inferred from sequence or structural similarity. Source: UniProtKB mismatch repair Ref.9 Ref.65 Inferred from direct assay. Source: UniProtKB negative regulation of DNA recombination Inferred from direct assay. Source: UniProtKB negative regulation of cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of neuron apoptosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of helicase activity Inferred from direct assay. Source: UniProtKB postreplication repair Ref.9 Inferred from direct assay. Source: UniProtKB response to UV-B Inferred from sequence or structural similarity. Source: UniProtKB response to X-ray Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	MutSalpha complex Ref.11 Inferred from direct assay. Source: HGNC MutSbeta complex Ref.11 Inferred from direct assay. Source: HGNC
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW guanine/thymine mispair binding Ref.11 Inferred from mutant phenotype. Source: MGI protein C-terminus binding Inferred from physical interaction. Source: UniProtKB protein homodimerization activity Ref.11 Inferred from direct assay. Source: HGNC
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-355888,EBI-355888
EXO1	P39875	1	EBI-355888,EBI-6738	From a different organism.
EXO1	Q9UQ84-1	2	EBI-355888,EBI-944694
MSH3	P20585	1	EBI-355888,EBI-1164205
MSH6	P52701	1	EBI-355888,EBI-395529
PTP4A3	O75365	1	EBI-355888,EBI-1043866

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 934

934

DNA mismatch repair protein Msh2

PRO_0000115183

Regions

Nucleotide binding

669 – 676

ATP Potential

Region

601 – 671

Interaction with EXO1

Amino acid modifications

Modified residue

860

Phosphoserine Ref.32

Natural variations

Natural variant

A → T in HNPCC1. Ref.90

VAR_054511

Natural variant

T → M Could be associated with increased colorectal cancer susceptibility. dbSNP rs17217716. Ref.58 Ref.6 Ref.80

VAR_013171

Natural variant

S → I in colorectal cancer. Ref.76

VAR_043736

Natural variant

V → F in gastric cancer; uncertain pathogenicity; cryptic acceptor splice site suppressed on ex vivo splicing assay. Ref.63

VAR_043737

Natural variant

T → P in HNPCC1; shows slightly reduced mismatch binding or release efficiency. Ref.91 Ref.94

VAR_043738

Natural variant

G → S in CRC. Ref.80

VAR_043739

Natural variant

Y → C: dbSNP rs17217723. Ref.6

VAR_019233

Natural variant

T → M in HNPCC1. Ref.71

VAR_043740

Natural variant

A → V in HNPCC1. Ref.71

VAR_043741

Natural variant

H → Q in HNPCC1. dbSNP rs33946261. Ref.40

VAR_004470

Natural variant

Missing in HNPCC1; uncertain pathogenicity; has no effect on ex vivo splicing assay. Ref.74 Ref.90 Ref.95

VAR_043742

Natural variant

L → F in HNPCC1. Ref.86

VAR_043743

Natural variant

R → H Ref.5

VAR_004471

Natural variant

Y → C in HNPCC1; uncertain pathogenicity. Ref.63

VAR_043744

Natural variant

102

V → I in HNPCC1. Ref.72

VAR_043745

Natural variant

106

R → K: dbSNP rs41295286. Ref.93

VAR_038026

Natural variant

110

K → T in HNPCC1; somatic mutation. Ref.43

VAR_043746

Natural variant

127

N → S in HNPCC1; shows no defects. dbSNP rs17217772. Ref.77 Ref.94

VAR_019234

Natural variant

139

N → S in HNPCC1.

VAR_004472

Natural variant

145

I → M in HNPCC1. Ref.90

VAR_004473

Natural variant

161

V → D in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.64 Ref.91 Ref.94

VAR_012936

Natural variant

162

G → A in HNPCC1. Ref.89 Ref.91 Ref.92 Ref.94 Ref.96

VAR_054512

Natural variant

162

G → R in HNPCC1; shows a decreased expression level of the MutS alpha complex and is associated with an abnormal subcellular localization pattern; affects protein stability; associated with an absence of the protein in tumors. Ref.89 Ref.91 Ref.92 Ref.94 Ref.96

VAR_043747

Natural variant

163

V → D in HNPCC1. Ref.72 Ref.79

VAR_043748

Natural variant

163

V → G in HNPCC1. Ref.72 Ref.79

VAR_022670

Natural variant

164

G → R in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.91 Ref.94

VAR_043749

Natural variant

167

D → H in HNPCC1; does not show a decreased expression level of the MutS alpha complex and is not associated with an abnormal subcellular localization pattern; could be a polymorphism. Ref.68 Ref.73 Ref.96

VAR_004474

Natural variant

169

I → V in HNPCC1; uncertain pathogenicity. Ref.87

VAR_043750

Natural variant

173

L → P in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.91 Ref.94

VAR_043751

Natural variant

175

L → P in HNPCC1. Ref.78

VAR_043752

Natural variant

187

L → P in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.91 Ref.94

VAR_043753

Natural variant

198

E → G in HNPCC1.

VAR_054513

Natural variant

199

C → R in glioma; also associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.95 Ref.49

VAR_012937

Natural variant

203

G → R in CRC; uncertain pathogenicity; somatic mutation. Ref.80

VAR_043754

Natural variant

216

I → V in HNPCC1; could be a polymorphism; shows slightly reduced mismatch binding or release efficiency. Ref.64

VAR_012938

Natural variant

246

K → Q in HNPCC1; uncertain pathogenicity. Ref.55

VAR_043755

Natural variant

265 – 314

Missing in HNPCC1. Ref.48

VAR_004475

Natural variant

272

A → V Associated wiht HNPCC1; shows slightly reduced mismatch binding or release efficiency; results in partial exon 5 skipping on ex vivo splicing assay. dbSNP rs34136999. Ref.91 Ref.94 Ref.95

VAR_043756

Natural variant

283

D → Y in HNPCC1. Ref.88

VAR_043757

Natural variant

305

A → T in HNPCC1. Ref.41

VAR_004476

Natural variant

322

G → D Common polymorphism; may be associated with increased colorectal cancer susceptibility; the equivalent substitution in yeast reduces the mismatch repair efficiency in vitro; shows slightly reduced mismatch binding or release efficiency. dbSNP rs4987188. Ref.47 Ref.55 Ref.61 Ref.72 Ref.74 Ref.90 Ref.94 Ref.6 Ref.76 Ref.93 Ref.37 Ref.45 Ref.51 Ref.54 Ref.59 Ref.65 Ref.70

VAR_004477

Natural variant

323

S → C in HNPCC1; uncertain pathogenicity. Ref.42 Ref.63

VAR_012939

Natural variant

323

S → Y in HNPCC1; uncertain pathogenicity. Ref.42 Ref.63

VAR_043758

Natural variant

331

N → D Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.95

VAR_054514

Natural variant

333

C → Y in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.91 Ref.94

VAR_043759

Natural variant

335

T → I in HNPCC1; uncertain pathogenicity. Ref.63

VAR_043760

Natural variant

336

P → S in HNPCC1. Ref.53

VAR_043761

Natural variant

342

V → I in colorectal cancer. Ref.76

VAR_043762

Natural variant

349

P → L in HNPCC1. Ref.85

VAR_043763

Natural variant

359

R → S in HNPCC1; shows a decreased expression level of the MutS alpha comp lex and is associated with an abnormal subcellular localization pattern. Ref.73 Ref.96

VAR_043764

Natural variant

390

L → F in HNPCC1; uncertain pathogenicity; the equivalent substitution in yeast partially affects mismatch repair in vitro. dbSNP rs17224367. Ref.56 Ref.87 Ref.90

VAR_004478

Natural variant

393

K → M in HNPCC1. Ref.68

VAR_043765

Natural variant

419

Q → K in CRC; uncertain pathogenicity; the equivalent substitution in yeast partially affects mismatch repair in vitro. Ref.87 Ref.80

VAR_012940

Natural variant

440

Missing in HNPCC1. Ref.83

VAR_043766

Natural variant

470

V → E Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.95

VAR_054515

Natural variant

492

M → V in HNPCC1.

VAR_043767

Natural variant

506

D → Y in CRC; sporadic; early onset; the equivalent substitution in yeast partially affects mismatch repair in vitro. Ref.50 Ref.39

VAR_012941

Natural variant

524

R → P in HNPCC1; defective in mismatch repair activity. Ref.16 Ref.68

VAR_004479

Natural variant

552

T → P in HNPCC1. Ref.75

VAR_043768

Natural variant

554

S → R in HNPCC1; could be a polymorphism. Ref.64

VAR_012942

Natural variant

562

E → V in HNPCC1. Ref.46

VAR_004480

Natural variant

564

T → A in HNPCC1; uncertain pathogenicity. dbSNP rs55778204. Ref.72 Ref.87

VAR_043769

Natural variant

583

N → S in HNPCC1. Ref.75

VAR_043770

Natural variant

596

N → S in HNPCC1; could be a polymorphism. dbSNP rs41295288. Ref.35 Ref.38 Ref.41 Ref.53 Ref.55 Ref.68 Ref.71 Ref.85

VAR_012943

Natural variant

596

Missing in HNPCC1; has no effect on ex vivo splicing assay. Ref.35 Ref.38 Ref.41 Ref.53 Ref.55 Ref.68 Ref.71 Ref.85

VAR_004481

Natural variant

600

A → V in HNPCC1. Ref.67

VAR_043771

Natural variant

603

D → N in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.61 Ref.91 Ref.94

VAR_043772

Natural variant

610

H → N Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.95

VAR_054516

Natural variant

619

Y → C in CRC. Ref.80

VAR_043773

Natural variant

622

P → L in HNPCC1; the equivalent substitution in yeast causes loss of function in a mismatch repair assay. Ref.3 Ref.68

VAR_004482

Natural variant

629

Q → R in HNPCC1; uncertain pathogenicity. Ref.63 Ref.83 Ref.87

VAR_043774

Natural variant

636

A → P in HNPCC1; partial functional loss; mainly causes defects in mismatch binding or release efficiency. Ref.57 Ref.75 Ref.91 Ref.94

VAR_012944

Natural variant

638

R → G Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.95

VAR_054517

Natural variant

639

H → R in HNPCC1. Ref.3 Ref.43

VAR_043775

Natural variant

639

H → Y in HNPCC1; the equivalent substitution in yeast does not affect mismatch repair efficiency in vitro. Ref.3 Ref.43

VAR_004483

Natural variant

641

C → G Ref.48

VAR_004484

Natural variant

645

Q → E Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.95

VAR_054518

Natural variant

647

E → K in HNPCC1. Ref.43

VAR_043776

Natural variant

656

Y → H in HNPCC1; somatic mutation. Ref.43

VAR_043777

Natural variant

660

D → G in HNPCC1. Ref.79

VAR_022671

Natural variant

670

P → L: dbSNP rs41294982. Ref.93

VAR_038027

Natural variant

671

N → Y in HNPCC1; uncertain pathogenicity. Ref.82

VAR_043778

Natural variant

674

G → S in HNPCC1; somatic mutation. Ref.68

VAR_004485

Natural variant

679

I → T in HNPCC1; somatic mutation. Ref.43

VAR_043779

Natural variant

688

M → I in HNPCC1. Ref.50 Ref.58 Ref.83

VAR_012945

Natural variant

692

G → R in HNPCC1. Ref.60

VAR_009250

Natural variant

696

P → L Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.95

VAR_054519

Natural variant

697

C → F in HNPCC1; the equivalent substitution in yeast causes loss of function in a mismatch repair assay; mainly causes defects in mismatch binding or release efficiency. Ref.47 Ref.60 Ref.91 Ref.94

VAR_004486

Natural variant

697

C → R in HNPCC1; has no effect on ex vivo splicing assay. Ref.47 Ref.60 Ref.91 Ref.94

VAR_009251

Natural variant

714

A → V in HNPCC1; uncertain pathogenicity. Ref.63

VAR_043780

Natural variant

723

S → F in HNPCC1; has no effect on ex vivo splicing assay. Ref.67

VAR_043781

Natural variant

729

M → V in HNPCC1; somatic mutation. Ref.43

VAR_043782

Natural variant

732

T → I in HNPCC1; somatic mutation. Ref.43

VAR_043783

Natural variant

745 – 746

Missing in HNPCC1; mainly causes defects in mismatch binding or release efficiency.

VAR_043784

Natural variant

748

D → Y Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.95

VAR_054520

Natural variant

749

E → K in HNPCC1; mainly causes defects in mismatch binding or release efficiency; the mutant protein is well expressed in tumors. Ref.91 Ref.94

VAR_043785

Natural variant

770

I → V Ref.48

VAR_004487

Natural variant

779

M → I: dbSNP rs41295292. Ref.93

VAR_038028

Natural variant

807

T → S: dbSNP rs41295294. Ref.93

VAR_038029

Natural variant

813

M → V in HNPCC1. Ref.66

VAR_043786

Natural variant

824

Q → E in gastric cancer; uncertain pathogenicity. Ref.63

VAR_043787

Natural variant

834

A → T in HNPCC1; shows no defects; could be a polymorphism. Ref.41 Ref.55 Ref.94

VAR_004488

Natural variant

835

N → H: dbSNP rs41295296. Ref.93

VAR_038030

Natural variant

839

H → Q Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.84 Ref.95

VAR_054521

Natural variant

839

H → R in HNPCC1. Ref.84

VAR_043788

Natural variant

845

K → E in HNPCC1. Ref.58

VAR_013172

Natural variant

853

E → A in HNPCC1; uncertain pathogenicity. Ref.74 Ref.90

VAR_043789

Natural variant

868

P → A in gastric cancer; uncertain pathogenicity. Ref.63

VAR_043790

Natural variant

870

A → G in gastric cancer; uncertain pathogenicity. Ref.63

VAR_043791

Natural variant

873

C → G in gastric cancer; uncertain pathogenicity. Ref.63

VAR_043792

Natural variant

886

E → G in HNPCC1. Ref.71

VAR_043793

Natural variant

905

T → R in HNPCC1; could be a polymorphism. Ref.68

VAR_004489

Natural variant

911

L → R: dbSNP rs41295182. Ref.93

VAR_038031

Natural variant

923

V → E in HNPCC1; could be a polymorphism. Ref.71 Ref.94

VAR_043794

Natural variant

931

K → T in HNPCC1. Ref.81

VAR_043795

Experimental info

Mutagenesis

674

G → A: Mainly causes defects in mismatch binding or release efficiency. Ref.94

Mutagenesis

675

K → R: No effect on mismatch binding, complete loss of DNA repair function when associated with MSH6 mutant R-1140. Ref.15

Secondary structure

934

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P43246-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 664A058C78242E05
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FASTA

934

104,743

        10         20         30         40         50         60 
MAVQPKETLQ LESAAEVGFV RFFQGMPEKP TTTVRLFDRG DFYTAHGEDA LLAAREVFKT 

        70         80         90        100        110        120 
QGVIKYMGPA GAKNLQSVVL SKMNFESFVK DLLLVRQYRV EVYKNRAGNK ASKENDWYLA 

       130        140        150        160        170        180 
YKASPGNLSQ FEDILFGNND MSASIGVVGV KMSAVDGQRQ VGVGYVDSIQ RKLGLCEFPD 

       190        200        210        220        230        240 
NDQFSNLEAL LIQIGPKECV LPGGETAGDM GKLRQIIQRG GILITERKKA DFSTKDIYQD 

       250        260        270        280        290        300 
LNRLLKGKKG EQMNSAVLPE MENQVAVSSL SAVIKFLELL SDDSNFGQFE LTTFDFSQYM 

       310        320        330        340        350        360 
KLDIAAVRAL NLFQGSVEDT TGSQSLAALL NKCKTPQGQR LVNQWIKQPL MDKNRIEERL 

       370        380        390        400        410        420 
NLVEAFVEDA ELRQTLQEDL LRRFPDLNRL AKKFQRQAAN LQDCYRLYQG INQLPNVIQA 

       430        440        450        460        470        480 
LEKHEGKHQK LLLAVFVTPL TDLRSDFSKF QEMIETTLDM DQVENHEFLV KPSFDPNLSE 

       490        500        510        520        530        540 
LREIMNDLEK KMQSTLISAA RDLGLDPGKQ IKLDSSAQFG YYFRVTCKEE KVLRNNKNFS 

       550        560        570        580        590        600 
TVDIQKNGVK FTNSKLTSLN EEYTKNKTEY EEAQDAIVKE IVNISSGYVE PMQTLNDVLA 

       610        620        630        640        650        660 
QLDAVVSFAH VSNGAPVPYV RPAILEKGQG RIILKASRHA CVEVQDEIAF IPNDVYFEKD 

       670        680        690        700        710        720 
KQMFHIITGP NMGGKSTYIR QTGVIVLMAQ IGCFVPCESA EVSIVDCILA RVGAGDSQLK 

       730        740        750        760        770        780 
GVSTFMAEML ETASILRSAT KDSLIIIDEL GRGTSTYDGF GLAWAISEYI ATKIGAFCMF 

       790        800        810        820        830        840 
ATHFHELTAL ANQIPTVNNL HVTALTTEET LTMLYQVKKG VCDQSFGIHV AELANFPKHV 

       850        860        870        880        890        900 
IECAKQKALE LEEFQYIGES QGYDIMEPAA KKCYLEREQG EKIIQEFLSK VKQMPFTEMS 

       910        920        930 
EENITIKLKQ LKAEVIAKNN SFVNEIISRI KVTT

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human mutator gene homolog MSH2 and its association with hereditary nonpolyposis colon cancer." Fishel R., Lescoe M., Rao M., Copeland N.G., Jenkins N.A., Garber J., Kane M.F., Kolodner R.D. Cell 75:1027-1038(1993) [PubMed: 8252616] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Erratum Fishel R., Lescoe M., Rao M., Copeland N.G., Jenkins N.A., Garber J., Kane M.F., Kolodner R.D. Cell 77:167-167(1994) [PubMed: 8156592] [Abstract]
[3]	"Mutations of a mutS homolog in hereditary nonpolyposis colorectal cancer." Leach F.S., Nicolaides N.C., Papadopoulos N., Liu B., Jen J., Parsons R., Peltomaeki P., Sistonen P., Aaltonen L.A., Nystroem-Lahti M., Guan X.-Y., Zhang J., Meltzer P.S., Yu J.-W., Kao F.-T., Chen D.J., Cerosaletti K.M., Fournier R.E.K. Vogelstein B. Cell 75:1215-1225(1993) [PubMed: 8261515] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HNPCC1 LEU-622 AND TYR-639.
[4]	"Structure of the human MSH2 locus and analysis of two Muir-Torre kindreds for msh2 mutations." Kolodner R.D., Hall N.R., Lipford J., Kane M.F., Rao M.R.S., Morrison P., Wirth L., Finan P.J., Burn J., Chapman P., Earabino C., Merchant E., Bishop D.T. Genomics 24:516-526(1994) [PubMed: 7713503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISEASE.
[5]	"Seven new mutations in hMSH2, an HNPCC gene, identified by denaturing gradient-gel electrophoresis." Wijnen J., Vasen H., Khan P.M., Menko F.H., van der Klift H., van Leeuwen C., van den Broek M., van Leeuwen-Cornelisse I., Nagengast F., Meijers-Heijboer A., Lindhout D., Griffioen G., Cats A., Kleibeuker J., Varesco L., Bertario L., Bisgaard M.-L., Mohr J., Fodde R. Am. J. Hum. Genet. 56:1060-1066(1995) [PubMed: 7726159] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-96.
[6]	NIEHS SNPs program Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-8; CYS-43; SER-127; ASP-322 AND PHE-390.
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[8]	"A novel germline mutation at exon 7 of the hMSH2 gene (417 del G) in a large HNPCC Brazilian kindred." Corvello C.M., Bevilacqua R.A.U., Rossi B.M., Simpson A.J.G. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 375-425. Tissue: Blood.
[9]	"Purified human MSH2 protein binds to DNA containing mismatched nucleotides." Fishel R., Ewel A., Lescoe M.K. Cancer Res. 54:5539-5542(1994) [PubMed: 7923193] [Abstract] Cited for: DNA-BINDING.
[10]	"A carboxy terminal domain of the hMSH-2 gene product is sufficient for binding specific mismatched oligonucleotides." Whitehouse A., Taylor G.R., Deeble J., Phillips S.E., Meredith D.M., Markham A.F. Biochem. Biophys. Res. Commun. 225:289-295(1996) [PubMed: 8769132] [Abstract] Cited for: DNA-BINDING.
[11]	"hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6." Acharya S., Wilson T., Gradia S., Kane M.F., Guerrette S., Marsischky G.T., Kolodner R.D., Fishel R. Proc. Natl. Acad. Sci. U.S.A. 93:13629-13634(1996) [PubMed: 8942985] [Abstract] Cited for: INTERACTION WITH MSH3 AND MSH6.
[12]	"Human exonuclease I interacts with the mismatch repair protein hMSH2." Schmutte C., Marinescu R.C., Sadoff M.M., Guerrette S., Overhauser J., Fishel R. Cancer Res. 58:4537-4542(1998) [PubMed: 9788596] [Abstract] Cited for: INTERACTION WITH EXO1.
[13]	"Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism." Blackwell L.J., Martik D., Bjornson K.P., Bjornson E.S., Modrich P. J. Biol. Chem. 273:32055-32062(1998) [PubMed: 9822680] [Abstract] Cited for: FUNCTION.
[14]	"DNA-dependent activation of the hMutSalpha ATPase." Blackwell L.J., Bjornson K.P., Modrich P. J. Biol. Chem. 273:32049-32054(1998) [PubMed: 9822679] [Abstract] Cited for: FUNCTION.
[15]	"hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha." Iaccarino I., Marra G., Palombo F., Jiricny J. EMBO J. 17:2677-2686(1998) [PubMed: 9564049] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-675.
[16]	"Functional analysis of human MutSalpha and MutSbeta complexes in yeast." Clark A.B., Cook M.E., Tran H.T., Gordenin D.A., Resnick M.A., Kunkel T.A. Nucleic Acids Res. 27:736-742(1999) [PubMed: 9889267] [Abstract] Cited for: MISMATCH-BINDING, CHARACTERIZATION OF VARIANT HNPCC1 PRO-524.
[17]	"hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA." Gradia S., Subramanian D., Wilson T., Acharya S., Makhov A., Griffith J., Fishel R. Mol. Cell 3:255-261(1999) [PubMed: 10078208] [Abstract] Cited for: FUNCTION.
[18]	"BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures." Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J. Genes Dev. 14:927-939(2000) [PubMed: 10783165] [Abstract] Cited for: IDENTIFICATION OF MSH2 AS MEMBER OF BASC.
[19]	"Identification of factors interacting with hMSH2 in the fetal liver utilizing the yeast two-hybrid system. In vivo interaction through the C-terminal domains of hEXO1 and hMSH2 and comparative expression analysis." Rasmussen L.J., Rasmussen M., Lee B.-I., Rasmussen A.K., Wilson D.M. III, Nielsen F.C., Bisgaard H.C. Mutat. Res. 460:41-52(2000) [PubMed: 10856833] [Abstract] Cited for: INTERACTION WITH EXO1, TISSUE SPECIFICITY.
[20]	"The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch." Gradia S., Acharya S., Fishel R. J. Biol. Chem. 275:3922-3930(2000) [PubMed: 10660545] [Abstract] Cited for: FUNCTION.
[21]	"The interaction of DNA mismatch repair proteins with human exonuclease I." Schmutte C., Sadoff M.M., Shim K.-S., Acharya S., Fishel R. J. Biol. Chem. 276:33011-33018(2001) [PubMed: 11427529] [Abstract] Cited for: INTERACTION WITH EXO1.
[22]	"HNPCC mutations in the human DNA mismatch repair gene hMLH1 influence assembly of hMutLalpha and hMLH1-hEXO1 complexes." Jaeger A.C., Rasmussen M., Bisgaard H.C., Singh K.K., Nielsen F.C., Rasmussen L.J. Oncogene 20:3590-3595(2001) [PubMed: 11429708] [Abstract] Cited for: INTERACTION WITH EXO1.
[23]	"Functional alterations of human exonuclease 1 mutants identified in atypical hereditary nonpolyposis colorectal cancer syndrome." Sun X., Zheng L., Shen B. Cancer Res. 62:6026-6030(2002) [PubMed: 12414623] [Abstract] Cited for: INTERACTION WITH EXO1.
[24]	"MSH2 and ATR form a signaling module and regulate two branches of the damage response to DNA methylation." Wang Y., Qin J. Proc. Natl. Acad. Sci. U.S.A. 100:15387-15392(2003) [PubMed: 14657349] [Abstract] Cited for: INTERACTION WITH ATR, IDENTIFICATION BY MASS SPECTROMETRY.
[25]	"Characterization of human exonuclease 1 in complex with mismatch repair proteins, subcellular localization and association with PCNA." Nielsen F.C., Jaeger A.C., Luetzen A., Bundgaard J.R., Rasmussen L.J. Oncogene 23:1457-1468(2004) [PubMed: 14676842] [Abstract] Cited for: INTERACTION WITH EXO1.
[26]	"The mismatch DNA repair heterodimer, hMSH2/6, regulates BLM helicase." Yang Q., Zhang R., Wang X.W., Linke S.P., Sengupta S., Hickson I.D., Pedrazzi G., Perrera C., Stagljar I., Littman S.J., Modrich P., Harris C.C. Oncogene 23:3749-3756(2004) [PubMed: 15064730] [Abstract] Cited for: FUNCTION.
[27]	"hMutS alpha is protected from ubiquitin-proteasome-dependent degradation by atypical protein kinase C zeta phosphorylation." Hernandez-Pigeon H., Quillet-Mary A., Louat T., Schambourg A., Humbert O., Selves J., Salles B., Laurent G., Lautier D. J. Mol. Biol. 348:63-74(2005) [PubMed: 15808853] [Abstract] Cited for: PHOSPHORYLATION BY PRKCZ.
[28]	"The DNA-mismatch repair enzyme hMSH2 modulates UV-B-induced cell cycle arrest and apoptosis in melanoma cells." Seifert M., Scherer S.J., Edelmann W., Bohm M., Meineke V., Lobrich M., Tilgen W., Reichrath J. J. Invest. Dermatol. 128:203-213(2008) [PubMed: 17611581] [Abstract] Cited for: FUNCTION.
[29]	"Colon cancer and DNA repair: have mismatches met their match?" Jiricny J. Trends Genet. 10:164-168(1994) [PubMed: 8036718] [Abstract] Cited for: REVIEW.
[30]	"Molecular basis of HNPCC: mutations of MMR genes." Papadopoulos N., Lindblom A. Hum. Mutat. 10:89-99(1997) [PubMed: 9259192] [Abstract] Cited for: REVIEW ON VARIANTS.
[31]	"The role of the human DNA mismatch repair gene hMSH2 in DNA repair, cell cycle control and apoptosis: implications for pathogenesis, progression and therapy of cancer." Seifert M., Reichrath J. J. Mol. Histol. 37:301-307(2006) [PubMed: 17080293] [Abstract] Cited for: REVIEW.
[32]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860, MASS SPECTROMETRY.
[33]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[34]	"Structure of the human MutSalpha DNA lesion recognition complex." Warren J.J., Pohlhaus T.J., Changela A., Iyer R.R., Modrich P.L., Beese L.S. Mol. Cell 26:579-592(2007) [PubMed: 17531815] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
[35]	"Mutational analysis of the hMSH2 gene reveals a three base pair deletion in a family predisposed to colorectal cancer development." Mary J.-L., Bishop T., Kolodner R.D., Lipford J.R., Kane M.F., Weber W., Torhorst J., Mueller H., Spycher M., Scott R.J. Hum. Mol. Genet. 3:2067-2069(1994) [PubMed: 7874129] [Abstract] Cited for: VARIANT HNPCC1 ASN-596 DEL.
[36]	"Molecular nature of colon tumors in hereditary nonpolyposis colon cancer, familial polyposis, and sporadic colon cancer." Konishi M., Kikuchi-Yanoshita R., Tanaka K., Muraoka M., Onda A., Okumura Y., Kishi N., Iwama T., Mori T., Koike M., Ushio K., Chiba M., Nomizu S., Konishi F., Utsunomiya J., Miyaki M. Gastroenterology 111:307-317(1996) [PubMed: 8690195] [Abstract] Cited for: VARIANTS PHE-390 AND LYS-419.
[37]	"CpG dinucleotides in the hMSH2 and hMLH1 genes are hotspots for HNPCC mutations." Maliaka Y.K., Chudina A.P., Belev N.F., Alday P., Bochkov N.P., Buerstedde J.-M. Hum. Genet. 97:251-255(1996) [PubMed: 8566964] [Abstract] Cited for: VARIANT ASP-322.
[38]	"Microsatellite instability and mutation analysis of hMSH2 and hMLH1 in patients with sporadic, familial and hereditary colorectal cancer." Moslein G., Tester D.J., Lindor N.M., Honchel R., Cunningham J.M., French A.J., Halling K.C., Schwab M., Goretzki P., Thibodeau S.N. Hum. Mol. Genet. 5:1245-1252(1996) [PubMed: 8872463] [Abstract] Cited for: VARIANT HNPCC1 ASN-596 DEL, VARIANT HIS-167.
[39]	"Germline mutations of hMLH1 and hMSH2 genes in Korean hereditary nonpolyposis colorectal cancer." Han H.-J., Yuan Y., Ku J.-L., Oh J.-H., Won Y.-J., Kang K.J., Kim K.Y., Kim S., Kim C.Y., Kim J.-P., Oh N.-G., Lee K.H., Choe K.J., Nakamura Y., Park J.-G. J. Natl. Cancer Inst. 88:1317-1319(1996) [PubMed: 8797773] [Abstract] Cited for: VARIANT CRC TYR-506.
[40]	"Microsatellite instability and the role of hMSH2 in sporadic colorectalcancer." Bubb V.J., Curtis L.J., Cunningham C., Dunlop M.G., Carothers A.D., Morris R.G., White S., Bird C.C., Wyllie A.H. Oncogene 12:2641-2649(1996) [PubMed: 8700523] [Abstract] Cited for: VARIANT HNPCC1 GLN-46.
[41]	"Hereditary nonpolyposis colorectal cancer families not complying with the Amsterdam criteria show extremely low frequency of mismatch-repair-gene mutations." Wijnen J., Khan P.M., Vasen H., van der Klift H., Mulder A., van Leeuwen-Cornelisse I., Bakker B., Losekoot M., Moeller P., Fodde R. Am. J. Hum. Genet. 61:329-335(1997) [PubMed: 9311737] [Abstract] Cited for: VARIANTS HNPCC1 THR-305; ASN-596 DEL AND THR-834.
[42]	"Frequent somatic mutations of hMSH3 with reference to microsatellite instability in hereditary nonpolyposis colorectal cancers." Akiyama Y., Tsubouchi N., Yuasa Y. Biochem. Biophys. Res. Commun. 236:248-252(1997) [PubMed: 9240418] [Abstract] Cited for: VARIANT HNPCC1 CYS-323.
[43]	"Identification of concurrent germ-line mutations in hMSH2 and/or hMLH1 in Japanese hereditary nonpolyposis colorectal cancer kindreds." Nakahara M., Yokozaki H., Yasui W., Dohi K., Tahara E. Cancer Epidemiol. Biomarkers Prev. 6:1057-1064(1997) [PubMed: 9419403] [Abstract] Cited for: VARIANTS HNPCC1 THR-110; ARG-639; LYS-647; HIS-656; THR-679; VAL-729 AND ILE-732.
[44]	"Characterization of MSH2 and MLH1 mutations in Italian families with hereditary nonpolyposis colorectal cancer." Viel A., Genuardi M., Capozzi E., Leonardi F., Bellacosa A., Paravatou-Petsotas M., Pomponi M.G., Fornasarig M., Percesepe A., Roncucci L., Tamassia M.G., Benatti P., Ponz de Leon M., Valenti A., Covino M., Anti M., Foletto M., Boiocchi M., Neri G. Genes Chromosomes Cancer 18:8-18(1997) [PubMed: 8993976] [Abstract] Cited for: VARIANT SER-596.
[45]	"MSH2 and MLH1 mutations in sporadic replication error-positive colorectal carcinoma as assessed by two-dimensional DNA electrophoresis." Wu Y., Nystroem-Lahti M., Osinga J., Looman M.W.G., Peltomaeki P., Aaltonen L.A., de la Chapelle A., Hofstra R.M.W., Buys C.H.C.M. Genes Chromosomes Cancer 18:269-278(1997) [PubMed: 9087566] [Abstract] Cited for: VARIANT ASP-322.
[46]	"Use of SSCP analysis to identify germline mutations in HNPCC families fulfilling the Amsterdam criteria." Beck N.E., Tomlinson I.P.M., Homfray T., Frayling I., Hodgson S.V., Harocopos C.J., Bodmer W.F. Hum. Genet. 99:219-224(1997) [PubMed: 9048925] [Abstract] Cited for: VARIANT HNPCC1 VAL-562.
[47]	"Hereditary nonpolyposis colorectal cancer (HNPCC): eight novel germline mutations in hMSH2 or hMLH1 genes." Wehner M., Buschhausen L., Lamberti C., Kruse R., Caspari R., Propping P., Friedl W. Hum. Mutat. 10:241-244(1997) [PubMed: 9298827] [Abstract] Cited for: VARIANT HNPCC1 PHE-697, VARIANT ASP-322.
[48]	"Systematic analysis of hMSH2 and hMLH1 in young colon cancer patients and controls." Farrington S.M., Lin-Goerke J., Ling J., Wang Y., Burczak J.D., Robbins D.J., Dunlop M.G. Am. J. Hum. Genet. 63:749-759(1998) [PubMed: 9718327] [Abstract] Cited for: VARIANT HNPCC1 265-VAL--GLN-314 DEL, VARIANTS GLY-641 AND VAL-770.
[49]	"Microsatellite instability and mutation of DNA mismatch repair genes in gliomas." Leung S.Y., Chan T.L., Chung L.P., Chan A.S.Y., Fan Y.W., Hung K.N., Kwong W.K., Ho J.W.C., Yuen S.T. Am. J. Pathol. 153:1181-1188(1998) [PubMed: 9777949] [Abstract] Cited for: VARIANT GLIOMA ARG-199.
[50]	"Germline mutations of hMLH1 and hMSH2 genes in patients with suspected hereditary nonpolyposis colorectal cancer and sporadic early-onset colorectal cancer." Yuan Y., Han H.-J., Zheng S., Park J.-G. Dis. Colon Rectum 41:434-440(1998) [PubMed: 9559627] [Abstract] Cited for: VARIANT CRC TYR-506, VARIANT HNPCC1 ILE-688.
[51]	"MSH2 codon 322 Gly to Asp seems not to confer an increased risk for colorectal cancer susceptibility." Liu T., Stathopoulos P., Lindblom P., Rubio C., Wasteson Arver B., Iselius L., Holmberg E., Groenberg H., Lindblom A. Eur. J. Cancer 34:1981-1981(1998) [PubMed: 10023327] [Abstract] Cited for: VARIANT ASP-322.
[52]	"Novel germline mutations of hMSH2 in a patient with hereditary nonpolyposis colorectal cancer 'HNPCC' and in a patient with six primary cancers." Okamura S., Koyama K., Miyoshi Y., Monden M., Takami M. J. Hum. Genet. 43:143-145(1998) [PubMed: 9621522] [Abstract] Cited for: VARIANT PHE-390.
[53]	"Influence of selection criteria on mutation detection in patients with hereditary nonpolyposis colorectal cancer." Heinimann K., Scott R.J., Buerstedde J.-M., Weber W., Siebold K., Attenhofer M., Mueller H., Dobbie Z. Cancer 85:2512-2518(1999) [PubMed: 10375096] [Abstract] Cited for: VARIANTS HNPCC1 SER-336 AND ASN-596 DEL.
[54]	"Mutator phenotypes of common polymorphisms and missense mutations in MSH2." Drotschmann K., Clark A.B., Kunkel T.A. Curr. Biol. 9:907-910(1999) [PubMed: 10469597] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ASP-322; PHE-390; LYS-419; TYR-506; PRO-524; LEU-622 AND PHE-697.
[55]	"Assessment of pathogenicity criteria for constitutional missense mutations of the hereditary nonpolyposis colorectal cancer genes MLH1 and MSH2." Genuardi M., Carrara S., Anti M., Ponz de Leon M., Viel A. Eur. J. Hum. Genet. 7:778-782(1999) [PubMed: 10573010] [Abstract] Cited for: VARIANTS HNPCC1 GLN-246; ASP-322; SER-596 AND THR-834.
[56]	"Novel hMLH1 and hMSH2 germline mutations in African Americans with colorectal cancer." Weber T.K., Chin H.-M., Rodriguez-Bigas M., Keitz B., Gilligan R., O'Malley L., Urf E., Diba N., Pazik J., Petrelli N.J. JAMA 281:2316-2320(1999) [PubMed: 10386556] [Abstract] Cited for: VARIANT HNPCC1 PHE-390.
[57]	"A missense mutation in both hMSH2 and APC in an Ashkenazi Jewish HNPCC kindred: implications for clinical screening." Yuan Z.Q., Wong N., Foulkes W.D., Alpert L., Manganaro F., Andreutti-Zaugg C., Iggo R., Anthony K., Hsieh E., Redston M., Pinsky L., Trifiro M., Gordon P.H., Lasko D. J. Med. Genet. 36:792-793(1999) [PubMed: 10528862] [Abstract] Cited for: VARIANT HNPCC1 PRO-636.
[58]	"Enhanced detection of deleterious and other germline mutations of hMSH2 and hMLH1 in Japanese hereditary nonpolyposis colorectal cancer kindreds." Nomura S., Sugano K., Kashiwabara H., Taniguchi T., Fukayama N., Fujita S., Akasu T., Moriya Y., Ohhigashi S., Kakizoe T., Sekiya T. Biochem. Biophys. Res. Commun. 271:120-129(2000) [PubMed: 10777691] [Abstract] Cited for: VARIANTS HNPCC1 ILE-688 AND GLU-845, VARIANT MET-8.
[59]	"Detection of mutations in mismatch repair genes in Portuguese families with hereditary non-polyposis colorectal cancer (HNPCC) by a multi-method approach." Fidalgo P., Almeida M.R., West S., Gaspar C., Maia L., Wijnen J., Albuquerque C., Curtis A., Cravo M., Fodde R., Leitao C.N., Burn J. Eur. J. Hum. Genet. 8:49-53(2000) [PubMed: 10713887] [Abstract] Cited for: VARIANT ASP-322.
[60]	"Four novel MSH2 / MLH1 gene mutations in Portuguese HNPCC families." Isidro G., Veiga I., Matos P., Almeida S., Bizarro S., Marshall B., Baptista M., Leite J., Regateiro F., Soares J., Castedo S., Boavida M.G. Hum. Mutat. 15:116-116(2000) [PubMed: 10612836] [Abstract] Cited for: VARIANTS HNPCC1 ARG-692 AND ARG-697.
[61]	"Population-based molecular detection of hereditary nonpolyposis colorectal cancer." Salovaara R., Loukola A., Kristo P., Kaeaeriaeinen H., Ahtola H., Eskelinen M., Haerkoenen N., Julkunen R., Kangas E., Ojala S., Tulikoura J., Valkamo E., Jaervinen H., Mecklin J.-P., Aaltonen L.A., de la Chapelle A. J. Clin. Oncol. 18:2193-2200(2000) [PubMed: 10829038] [Abstract] Cited for: VARIANT HNPCC1 ASN-603, VARIANT ASP-322.
[62]	Erratum Salovaara R., Loukola A., Kristo P., Kaeaeriaeinen H., Ahtola H., Eskelinen M., Haerkoenen N., Julkunen R., Kangas E., Ojala S., Tulikoura J., Valkamo E., Jaervinen H., Mecklin J.-P., Aaltonen L.A., de la Chapelle A. J. Clin. Oncol. 18:3456-3456(2000)
[63]	"hMLH1 and hMSH2 mutations in families with familial clustering of gastric cancer and hereditary non-polyposis colorectal cancer." Kim J.C., Kim H.C., Roh S.A., Koo K.H., Lee D.H., Yu C.S., Lee J.H., Kim T.W., Lee H.I., Beck N.E., Bodmer W.F. Cancer Detect. Prev. 25:503-510(2001) [PubMed: 12132870] [Abstract] Cited for: VARIANTS GASTRIC CANCER PHE-17; GLU-824; ALA-868; GLY-870 AND GLY-873, VARIANTS HNPCC1 CYS-98; TYR-323; ILE-335; ARG-629 AND VAL-714.
[64]	"Sixteen rare sequence variants of the hMLH1 and hMSH2 genes found in a cohort of 254 suspected HNPCC (hereditary non-polyposis colorectal cancer) patients: mutations or polymorphisms?" Mueller-Koch Y., Kopp R., Lohse P., Baretton G., Stoetzer A., Aust D., Daum J., Kerker B., Gross M., Dietmeier W., Holinski-Feder E. Eur. J. Med. Res. 6:473-482(2001) [PubMed: 11726306] [Abstract] Cited for: VARIANTS HNPCC1 ASP-161; VAL-216 AND ARG-554.
[65]	"Functional analysis of human MLH1 and MSH2 missense variants and hybrid human-yeast MLH1 proteins in Saccharomyces cerevisiae." Ellison A.R., Lofing J., Bitter G.A. Hum. Mol. Genet. 10:1889-1900(2001) [PubMed: 11555625] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ASP-322; LEU-622 AND TYR-639.
[66]	"Genomic deletions of MSH2 and MLH1 in colorectal cancer families detected by a novel mutation detection approach." Gille J.J.P., Hogervorst F.B.L., Pals G., Wijnen J.T., van Schooten R.J., Dommering C.J., Meijer G.A., Craanen M.E., Nederlof P.M., de Jong D., McElgunn C.J., Schouten J.P., Menko F.H. Br. J. Cancer 87:892-897(2002) [PubMed: 12373605] [Abstract] Cited for: VARIANT HNPCC1 VAL-813.
[67]	"Evaluation of screening strategy for detecting hereditary nonpolyposis colorectal carcinoma." Furukawa T., Konishi F., Shitoh K., Kojima M., Nagai H., Tsukamoto T. Cancer 94:911-920(2002) [PubMed: 11920458] [Abstract] Cited for: VARIANTS HNPCC1 VAL-600 AND PHE-723.
[68]	"HNPCC mutations in hMSH2 result in reduced hMSH2-hMSH6 molecular switch functions." Heinen C.D., Wilson T., Mazurek A., Berardini M., Butz C., Fishel R. Cancer Cell 1:469-478(2002) [PubMed: 12124176] [Abstract] Cited for: VARIANTS HNPCC1 HIS-167; MET-393; PRO-524; ASN-596 DEL; LEU-622; SER-674 AND ARG-905, CHARACTERIZATION OF VARIANTS HNPCC1 HIS-167; MET-393; PRO-524; ASN-596 DEL; LEU-622; SER-674 AND ARG-905.
[69]	"A homozygous germ-line mutation in the human MSH2 gene predisposes to hematological malignancy and multiple cafe-au-lait spots." Whiteside D., McLeod R., Graham G., Steckley J.L., Booth K., Somerville M.J., Andrew S.E. Cancer Res. 62:359-362(2002) [PubMed: 11809679] [Abstract] Cited for: INVOLVEMENT IN MULTIPLE CAFE-AU-LAIT SPOTS WITH LEUKEMIA.
[70]	"Pathogenicity of missense and splice site mutations in hMSH2 and hMLH1 mismatch repair genes: implications for genetic testing." Cravo M., Afonso A.J., Lage P., Albuquerque C., Maia L., Lacerda C., Fidalgo P., Chaves P., Cruz C., Nobre-Leitao C. Gut 50:405-412(2002) [PubMed: 11839723] [Abstract] Cited for: VARIANT ASP-322.
[71]	"Hereditary non-polyposis colorectal cancer (HNPCC): phenotype-genotype correlation between patients with and without identified mutation." Bisgaard M.L., Jaeger A.C., Myrhoej T., Bernstein I., Nielsen F.C. Hum. Mutat. 20:20-27(2002) [PubMed: 12112654] [Abstract] Cited for: VARIANTS HNPCC1 MET-44; VAL-45; ASN-596 DEL; GLY-886 AND GLU-923.
[72]	"Impact of microsatellite testing and mismatch repair protein expression on the clinical interpretation of genetic testing in hereditary non-polyposis colorectal cancer." Ward R., Meldrum C., Williams R., Mokany E., Scott R., Turner J., Hawkins N., Burgess B., Groombridge C., Spigelman A. J. Cancer Res. Clin. Oncol. 128:403-411(2002) [PubMed: 12200596] [Abstract] Cited for: VARIANTS HNPCC1 ILE-102; ASP-163 AND ALA-564, VARIANT ASP-322.
[73]	"Mutations of hMLH1 and hMSH2 in patients with suspected hereditary nonpolyposis colorectal cancer: correlation with microsatellite instability and abnormalities of mismatch repair protein expression." Scartozzi M., Bianchi F., Rosati S., Galizia E., Antolini A., Loretelli C., Piga A., Bearzi I., Cellerino R., Porfiri E. J. Clin. Oncol. 20:1203-1208(2002) [PubMed: 11870161] [Abstract] Cited for: VARIANTS HNPCC1 HIS-167 AND SER-359.
[74]	"Germline MSH2 and MLH1 mutational spectrum in HNPCC families from Poland and the Baltic States." Kurzawski G., Suchy J., Kladny J., Safranow K., Jakubowska A., Elsakov P., Kucinskas V., Gardovski J., Irmejs A., Sibul H., Huzarski T., Byrski T., Debniak T., Cybulski C., Gronwald J., Oszurek O., Clark J., Gozdz S. Lubinski J. J. Med. Genet. 39:E65-E65(2002) [PubMed: 12362047] [Abstract] Cited for: VARIANTS HNPCC1 LEU-92 DEL AND ALA-853, VARIANT ASP-322.
[75]	"Molecular analysis of hereditary nonpolyposis colorectal cancer in the United States: high mutation detection rate among clinically selected families and characterization of an American founder genomic deletion of the MSH2 gene." Wagner A., Barrows A., Wijnen J.T., van der Klift H., Franken P.F., Verkuijlen P., Nakagawa H., Geugien M., Jaghmohan-Changur S., Breukel C., Meijers-Heijboer H., Morreau H., van Puijenbroek M., Burn J., Coronel S., Kinarski Y., Okimoto R., Watson P. Fodde R. Am. J. Hum. Genet. 72:1088-1100(2003) [PubMed: 12658575] [Abstract] Cited for: VARIANTS HNPCC1 PRO-552; SER-583 AND PRO-636.
[76]	"Microsatellite instability and mutation analysis among southern Italian patients with colorectal carcinoma: detection of different alterations accounting for MLH1 and MSH2 inactivation in familial cases." Colombino M., Cossu A., Arba A., Manca A., Curci A., Avallone A., Comella G., Botti G., Scintu F., Amoruso M., D'Abbicco D., d'Agnessa M.R., Spanu A., Tanda F., Palmieri G. Ann. Oncol. 14:1530-1536(2003) [PubMed: 14504054] [Abstract] Cited for: VARIANTS COLORECTAL CANCER ILE-13 AND ILE-342, VARIANT ASP-322.
[77]	"Genetic analysis of familial colorectal cancer in Israeli Arabs." Chen-Shtoyerman R., Theodor L., Harmati E., Friedman E., Dacka S., Kopelman Y., Sternberg A., Zarivach R., Bar-Meir S., Fireman Z. Hum. Mutat. 21:446-447(2003) [PubMed: 12655564] [Abstract] Cited for: VARIANT HNPCC1 SER-127.
[78]	"Novel MLH1 and MSH2 germline mutations in the first HNPCC families identified in Slovakia." Bartosova Z., Fridrichova I., Bujalkova M., Wolf B., Ilencikova D., Krizan P., Hlavcak P., Palaj J., Lukac L., Lukacova M., Boeoer A., Haider R., Jiricny J., Nystroem-Lahti M., Marra G. Hum. Mutat. 21:449-449(2003) [PubMed: 12655568] [Abstract] Cited for: VARIANT HNPCC1 PRO-175.
[79]	"Genomic deletions in MSH2 or MLH1 are a frequent cause of hereditary non-polyposis colorectal cancer: identification of novel and recurrent deletions by MLPA." Taylor C.F., Charlton R.S., Burn J., Sheridan E., Taylor G.R. Hum. Mutat. 22:428-433(2003) [PubMed: 14635101] [Abstract] Cited for: VARIANTS HNPCC1 GLY-163 AND GLY-660.
[80]	"Oncogenic pathway of sporadic colorectal cancer with novel germline missense mutations in the hMSH2 gene." Yamada K., Zhong X., Kanazawa S., Koike J., Tsujita K., Hemmi H. Oncol. Rep. 10:859-866(2003) [PubMed: 12792735] [Abstract] Cited for: VARIANTS CRC MET-8; SER-40; VAL-169; ARG-203; PHE-390; LYS-419; CYS-619 AND ARG-629.
[81]	"Gene symbol: hMSH2. Disease: hereditary nonpolyposis colorectal cancer." Sun M.H., Cai Q., Fu G., Ren S., Mo S., Xu Y., Ding C., Zhang T., Zhu X., Xu X., Min D., Cai S., Luo D., Shi Y., Shi D. Hum. Genet. 114:409-409(2004) [PubMed: 15046096] [Abstract] Cited for: VARIANT HNPCC1 THR-931.
[82]	"RNA analysis reveals splicing mutations and loss of expression defects in MLH1 and BRCA1." Sharp A., Pichert G., Lucassen A., Eccles D. Hum. Mutat. 24:272-272(2004) [PubMed: 15300854] [Abstract] Cited for: VARIANT HNPCC1 TYR-671.
[83]	"Germline mutations in MLH1, MSH2 and MSH6 in Korean hereditary non-polyposis colorectal cancer families." Shin Y.-K., Heo S.-C., Shin J.-H., Hong S.-H., Ku J.-L., Yoo B.-C., Kim I.-J., Park J.-G. Hum. Mutat. 24:351-351(2004) [PubMed: 15365995] [Abstract] Cited for: VARIANTS HNPCC1 LEU-440 DEL; TYR-506; ARG-629 AND ILE-688.
[84]	"Genetic characterization of Chinese hereditary non-polyposis colorectal cancer by DHPLC and multiplex PCR." Yuan Y., Huang Y.-Q., Cai S.-R., Song Y.-M., Zheng S., Zhang S.-Z. Jpn. J. Clin. Oncol. 34:660-666(2004) [PubMed: 15613555] [Abstract] Cited for: VARIANT HNPCC1 ARG-839, VARIANT ARG-629.
[85]	"BRAF screening as a low-cost effective strategy for simplifying HNPCC genetic testing." Domingo E., Laiho P., Ollikainen M., Pinto M., Wang L., French A.J., Westra J., Frebourg T., Espin E., Armengol M., Hamelin R., Yamamoto H., Hofstra R.M.W., Seruca R., Lindblom A., Peltomaeki P., Thibodeau S.N., Aaltonen L.A., Schwartz S. Jr. J. Med. Genet. 41:664-668(2004) [PubMed: 15342696] [Abstract] Cited for: VARIANTS HNPCC1 LEU-349 AND ASN-596 DEL.
[86]	"A novel missense germline mutation in exon 2 of the hMSH2 gene in a HNPCC family from Southern Italy." Baudi F., Fersini G., Lavecchia A., Terracciano R., Leone F., Quaresima B., Faniello M.C., De Paola L., Doldo P., Cuda G., Costanzo F., Venuta S. Cancer Lett. 223:285-291(2005) [PubMed: 15896463] [Abstract] Cited for: VARIANT HNPCC1 PHE-93.
[87]	"Clinical and molecular characteristics of hereditary non-polyposis colorectal cancer families in Southeast Asia." Lee S.-C., Guo J.-Y., Lim R., Soo R., Koay E., Salto-Tellez M., Leong A., Goh B.-C. Clin. Genet. 68:137-145(2005) [PubMed: 15996210] [Abstract] Cited for: VARIANTS HNPCC1 VAL-169; PHE-390; ALA-564 AND ARG-629, VARIANT CRC LYS-419.
[88]	"Hereditary nonpolyposis colorectal cancer: pitfalls in deletion screening in MSH2 and MLH1 genes." Wehner M., Mangold E., Sengteller M., Friedrichs N., Aretz S., Friedl W., Propping P., Pagenstecher C. Eur. J. Hum. Genet. 13:983-986(2005) [PubMed: 15870828] [Abstract] Cited for: VARIANT HNPCC1 TYR-283.
[89]	"Gene symbol: MSH2. Disease: hereditary nonpolyposis colorectal cancer." Kohonen-Corish M.R.J., Otway R., Tetlow N., Hornby J., Doe W.F. Hum. Genet. 116:539-539(2005) [PubMed: 15991316] [Abstract] Cited for: VARIANT HNPCC1 ARG-162.
[90]	"Germline MSH2 and MLH1 mutational spectrum including large rearrangements in HNPCC families from Poland (update study)." Kurzawski G., Suchy J., Lener M., Klujszo-Grabowska E., Kladny J., Safranow K., Jakubowska K., Jakubowska A., Huzarski T., Byrski T., Debniak T., Cybulski C., Gronwald J., Oszurek O., Oszutowska D., Kowalska E., Gozdz S., Niepsuj S. Lubinski J. Clin. Genet. 69:40-47(2006) [PubMed: 16451135] [Abstract] Cited for: VARIANTS HNPCC1 THR-2; LEU-92 DEL; MET-145; PHE-390 AND ALA-853, VARIANT ASP-322.
[91]	"Pathogenicity of MSH2 missense mutations is typically associated with impaired repair capability of the mutated protein." Ollila S., Sarantaus L., Kariola R., Chan P., Hampel H., Holinski-Feder E., Macrae F., Kohonen-Corish M., Gerdes A.-M., Peltomaeki P., Mangold E., de la Chapelle A., Greenblatt M., Nystroem M. Gastroenterology 131:1408-1417(2006) [PubMed: 17101317] [Abstract] Cited for: VARIANTS HNPCC1 PRO-33; ASP-161; ARG-162; ARG-164; PRO-173; PRO-187; TYR-333; ASN-603; PRO-636; PHE-697; 745-ILE-ILE-746 DEL AND LYS-749, VARIANTS VAL-272; THR-834 AND GLU-923, CHARACTERIZATION OF VARIANTS HNPCC1 PRO-33; ASP-161; ARG-162; ARG-164; PRO-173; PRO-187; TYR-333; ASN-603; PRO-636; PHE-697; 745-ILE-ILE-746 DEL AND LYS-749, CHARACTERIZATION OF VARIANTS VAL-272; THR-834 AND GLU-923.
[92]	"Gene symbol: msh2. Disease: hereditary nonpolyposis colorectal cancer." Leonardis D. Hum. Genet. 119:675-675(2006) [PubMed: 17128465] [Abstract] Cited for: VARIANT HNPCC1 ALA-162.
[93]	"Classification of ambiguous mutations in DNA mismatch repair genes identified in a population-based study of colorectal cancer." Barnetson R.A., Cartwright N., van Vliet A., Haq N., Drew K., Farrington S., Williams N., Warner J., Campbell H., Porteous M.E., Dunlop M.G. Hum. Mutat. 29:367-374(2008) [PubMed: 18033691] [Abstract] Cited for: VARIANTS GLN-46; LYS-106; ASP-322; SER-596; LEU-670; ILE-779; SER-807; HIS-835 AND ARG-911.
[94]	"Mechanisms of pathogenicity in human MSH2 missense mutants." Ollila S., Dermadi Bebek D., Jiricny J., Nystroem M. Hum. Mutat. 29:1355-1363(2008) [PubMed: 18951462] [Abstract] Cited for: MUTAGENESIS OF GLY-674, CHARACTERIZATION OF VARIANTS HNPCC1 PRO-33; SER-127; ASP-161; ARG-162; ARG-164; PRO-173; PRO-187; TYR-333; ASN-603; PRO-636; PHE-697; 745-ILE-ILE-746 DEL; LYS-749; THR-834 AND GLU-923, CHARACTERIZATION OF VARIANTS VAL-272 AND ASP-322.
[95]	"A large fraction of unclassified variants of the mismatch repair genes MLH1 and MSH2 is associated with splicing defects." Tournier I., Vezain M., Martins A., Charbonnier F., Baert-Desurmont S., Olschwang S., Wang Q., Buisine M.P., Soret J., Tazi J., Frebourg T., Tosi M. Hum. Mutat. 29:1412-1424(2008) [PubMed: 18561205] [Abstract] Cited for: VARIANTS HNPCC1 LEU-92 DEL AND ARG-199, VARIANTS VAL-272; ASP-331; GLU-470; ASN-596 DEL; ASN-610; GLY-638; GLU-645; TYR-671; LEU-696; ARG-697; PHE-723; TYR-748 AND GLN-839, CHARACTERIZATION OF VARIANTS HNPCC1 LEU-92 DEL AND ARG-199, CHARACTERIZATION OF VARIANTS VAL-272; ASP-331; GLU-470; ASN-596 DEL; ASN-610; GLY-638; GLU-645; TYR-671; LEU-696; ARG-697; PHE-723; TYR-748 AND GLN-839.
[96]	"MSH2 missense mutations and HNPCC syndrome: pathogenicity assessment in a human expression system." Belvederesi L., Bianchi F., Galizia E., Loretelli C., Bracci R., Catalani R., Amati M., Cellerino R. Hum. Mutat. 29:E296-E309(2008) [PubMed: 18781619] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS HNPCC1 ARG-162; HIS-167 AND SER-359.
+	Additional computationally mapped references.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Hereditary non-polyposis colorectal cancer db

NIEHS-SNPs

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Cross-references

Sequence databases

U03911 mRNA. Translation: AAA18643.1.
U04045 mRNA. Translation: AAA61870.1.
U41221

U41220 Genomic DNA. Translation: AAA82080.1. Sequence problems.
L47583 mRNA. Translation: AAB59564.1.
L47582 mRNA. Translation: AAB59565.1.
L47581 mRNA. Translation: AAA76858.1.
AY601851 Genomic DNA. Translation: AAS99351.1.
BC021566 mRNA. Translation: AAH21566.1.
AF066081 Genomic DNA. Translation: AAC27930.1. Frameshift.

IPI

IPI00017303.

PIR

I64819.

RefSeq

NP_000242.1.

UniGene

Hs.597656

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2O8B	X-ray	2.75	A	1-934	[»]
2O8C	X-ray	3.37	A	1-934	[»]
2O8D	X-ray	3.00	A	1-934	[»]
2O8E	X-ray	3.30	A	1-934	[»]
2O8F	X-ray	3.25	A	1-934	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P43246. 15 interactions.

PTM databases

PhosphoSite

P43246.

Proteomic databases

PeptideAtlas

P43246.

PRIDE

P43246.

Genome annotation databases

Ensembl

ENSG00000095002. Homo sapiens. [Contig view]

GeneID

4436.

KEGG

hsa:4436.

Organism-specific databases

GeneCards

GC02P047541.

H-InvDB

HIX0022211.

HGNC

HGNC:7325. MSH2.

HPA

CAB009572.

MIM

120435. phenotype.
158320. phenotype.
608089. phenotype.
609309. gene.

Orphanet

144. Colon cancer, familial nonpolyposis.
587. Muir-Torre syndrome.

PharmGKB

PA31133.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P43246.

HOVERGEN

P43246.

OMA

P43246. WAISEHI.

Gene expression databases

ArrayExpress

P43246.

Bgee

P43246.

CleanEx

HS_MSH2.

GermOnline

ENSG00000095002. Homo sapiens.

Family and domain databases

InterPro

IPR011184. DNA_mismatch_repair_MSH2.
IPR007695. DNA_mismatch_repair_MutS-lik_N.
IPR000432. DNA_mismatch_repair_MutS_C.
IPR007861. DNA_mismatch_repair_MutS_clamp.
IPR007860. DNA_mismatch_repair_MutS_connt.
IPR007696. DNA_mismatch_repair_MutS_core.
[Graphical view]

PANTHER

PTHR11361. MutS_C. 1 hit.

Pfam

PF01624. MutS_I. 1 hit.
PF05188. MutS_II. 1 hit.
PF05192. MutS_III. 1 hit.
PF05190. MutS_IV. 1 hit.
PF00488. MutS_V. 1 hit.
[Graphical view]

PIRSF

PIRSF005813. MSH2. 1 hit.

ProDom

PD001263. MutS_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view]

PROSITE

PS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

17289.

SOURCE

Search...

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Entry information

Entry name

MSH2_HUMAN

Accession

Primary (citable) accession number: P43246
Secondary accession number(s): O75488

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents