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P43246 (MSH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA mismatch repair protein Msh2

Short name=hMSH2
Alternative name(s):
MutS protein homolog 2
Gene names
Name:MSH2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length934 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.29 Ref.32

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. Interacts with SLX4/BTBD12; this interaction is direct and links MutS beta to SLX4, a subunit of different structure-specific endonucleases. Interacts with SMARCAD1. Ref.14 Ref.15 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.36 Ref.37

Subcellular location

Nucleus Potential.

Tissue specificity

Ubiquitously expressed. Ref.22

Post-translational modification

Phosphorylated by PRKCZ, which may prevent MutS alpha degradation by the ubiquitin-proteasome pathway. Ref.30

Involvement in disease

Hereditary non-polyposis colorectal cancer 1 (HNPCC1) [MIM:120435]: An autosomal dominant disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early-onset colorectal carcinoma (CRC) and extra-colonic tumors 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. Clinically, HNPCC is often divided into two subgroups. Type I is characterized by hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II is characterized by 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.19 Ref.42 Ref.45 Ref.47 Ref.48 Ref.49 Ref.50 Ref.53 Ref.54 Ref.55 Ref.57 Ref.60 Ref.62 Ref.63 Ref.64 Ref.65 Ref.67 Ref.68 Ref.70 Ref.71 Ref.73 Ref.74 Ref.75 Ref.78 Ref.79 Ref.80 Ref.81 Ref.82 Ref.84 Ref.85 Ref.86 Ref.88 Ref.89 Ref.90 Ref.91 Ref.92 Ref.93 Ref.94 Ref.95 Ref.96 Ref.97 Ref.98 Ref.99 Ref.100 Ref.102 Ref.103 Ref.104 Ref.105 Ref.106 Ref.108

Muir-Torre syndrome (MRTES) [MIM:158320]: Rare autosomal dominant disorder characterized by sebaceous neoplasms and visceral malignancy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4

Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

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.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hereditary nonpolyposis colorectal cancer
Tumor suppressor
   LigandATP-binding
DNA-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 16403449. Source: GOC

B cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

B cell mediated immunity

Inferred from sequence or structural similarity. Source: BHF-UCL

DNA repair

Inferred from direct assay Ref.14. Source: BHF-UCL

cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

determination of adult lifespan

Inferred from electronic annotation. Source: Ensembl

double-strand break repair

Inferred from Biological aspect of Ancestor. Source: RefGenome

germ cell development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

intra-S DNA damage checkpoint

Inferred from Biological aspect of Ancestor. Source: RefGenome

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from Biological aspect of Ancestor. Source: RefGenome

isotype switching

Inferred from sequence or structural similarity. Source: BHF-UCL

maintenance of DNA repeat elements

Inferred from mutant phenotype PubMed 16388310. Source: HGNC

male gonad development

Inferred from sequence or structural similarity. Source: BHF-UCL

meiotic gene conversion

Inferred from Biological aspect of Ancestor. Source: RefGenome

meiotic mismatch repair

Inferred from Biological aspect of Ancestor. Source: RefGenome

mismatch repair

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of DNA recombination

Inferred from direct assay PubMed 17715146. Source: BHF-UCL

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of reciprocal meiotic recombination

Inferred from Biological aspect of Ancestor. Source: RefGenome

oxidative phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of helicase activity

Inferred from direct assay PubMed 17715146. Source: BHF-UCL

postreplication repair

Inferred from direct assay Ref.12. Source: UniProtKB

response to UV-B

Inferred from sequence or structural similarity. Source: BHF-UCL

response to X-ray

Inferred from sequence or structural similarity. Source: BHF-UCL

somatic hypermutation of immunoglobulin genes

Inferred from Biological aspect of Ancestor. Source: RefGenome

somatic recombination of immunoglobulin gene segments

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentMutSalpha complex

Inferred from direct assay PubMed 23622243. Source: UniProtKB

MutSbeta complex

Inferred from direct assay Ref.14. Source: HGNC

nuclear chromosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from direct assay Ref.12. Source: UniProtKB

DNA-dependent ATPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Y-form DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

centromeric DNA binding

Inferred from electronic annotation. Source: Ensembl

damaged DNA binding

Inferred from electronic annotation. Source: Ensembl

double-strand/single-strand DNA junction binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

enzyme binding

Inferred from physical interaction Ref.22Ref.24Ref.25Ref.26Ref.28PubMed 17715146Ref.15. Source: UniProtKB

guanine/thymine mispair binding

Inferred from mutant phenotype PubMed 16713580. Source: MGI

loop DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein C-terminus binding

Inferred from physical interaction PubMed 14706347. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.14. Source: HGNC

protein kinase binding

Inferred from physical interaction Ref.27. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P43246-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P43246-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.40
Chain2 – 934933DNA mismatch repair protein Msh2
PRO_0000115183

Regions

Nucleotide binding669 – 6768ATP Potential
Region601 – 67171Interaction with EXO1

Amino acid modifications

Modified residue21N-acetylalanine Ref.40
Modified residue5551N6-acetyllysine Ref.38
Modified residue5671N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 6666Missing in isoform 2.
VSP_045536
Natural variant21A → T in HNPCC1. Ref.97
VAR_054511
Natural variant81T → M Could be associated with increased colorectal cancer susceptibility. Ref.9 Ref.65 Ref.87
Corresponds to variant rs17217716 [ dbSNP | Ensembl ].
VAR_013171
Natural variant131S → I in colorectal cancer. Ref.83
VAR_043736
Natural variant171V → F in gastric cancer; unknown pathological significance; cryptic acceptor splice site suppressed on ex vivo splicing assay. Ref.70
VAR_043737
Natural variant331T → P in HNPCC1; shows slightly reduced mismatch binding or release efficiency. Ref.98 Ref.102
VAR_043738
Natural variant401G → S in CRC. Ref.87
VAR_043739
Natural variant431Y → C. Ref.9
Corresponds to variant rs17217723 [ dbSNP | Ensembl ].
VAR_019233
Natural variant441T → M in HNPCC1; repair proficient. Ref.78 Ref.106
VAR_043740
Natural variant451A → V in HNPCC1; repair proficient. Ref.78 Ref.106
VAR_043741
Natural variant461H → Q in HNPCC1. Ref.47 Ref.101
Corresponds to variant rs33946261 [ dbSNP | Ensembl ].
VAR_004470
Natural variant921Missing in HNPCC1; unknown pathological significance. Ref.81 Ref.97 Ref.103
VAR_043742
Natural variant931L → F in HNPCC1. Ref.93
VAR_043743
Natural variant961R → H. Ref.5
VAR_004471
Natural variant981Y → C in HNPCC1; unknown pathological significance. Ref.70
VAR_043744
Natural variant1021V → I in HNPCC1. Ref.79
VAR_043745
Natural variant1061R → K. Ref.101
Corresponds to variant rs41295286 [ dbSNP | Ensembl ].
VAR_038026
Natural variant1101K → T in HNPCC1; somatic mutation. Ref.50
VAR_043746
Natural variant1271N → S in HNPCC1; shows significantly decreased repair efficiency when associated with variant Pro-328; presumed to enhance cancer risk considerably when associated with Pro-328; this concomitant defect with another variant could explain its recurrent occurrence in CRC patients. Ref.9 Ref.84 Ref.102 Ref.107
Corresponds to variant rs17217772 [ dbSNP | Ensembl ].
VAR_019234
Natural variant1391N → S in HNPCC1.
VAR_004472
Natural variant1451I → M in HNPCC1; mismatch repair proficient. Ref.97 Ref.107
Corresponds to variant rs63750124 [ dbSNP | Ensembl ].
VAR_004473
Natural variant1611V → D in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.71 Ref.98 Ref.102
VAR_012936
Natural variant1621G → A in HNPCC1. Ref.99
VAR_054512
Natural variant1621G → 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.96 Ref.98 Ref.102 Ref.104
VAR_043747
Natural variant1631V → D in HNPCC1. Ref.79
VAR_043748
Natural variant1631V → G in HNPCC1. Ref.86
VAR_022670
Natural variant1641G → R in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.98 Ref.102
VAR_043749
Natural variant1651Y → D Associated with HNPCC1; unknown pathological significance; repair deficient. Ref.106
VAR_067284
Natural variant1671D → 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; shows reduced mismatch binding; repair proficient. Ref.45 Ref.75 Ref.80 Ref.104 Ref.105 Ref.106
VAR_004474
Natural variant1691I → V in HNPCC1; unknown pathological significance. Ref.87 Ref.94
Corresponds to variant rs63750716 [ dbSNP | Ensembl ].
VAR_043750
Natural variant1731L → P in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.98 Ref.102
VAR_043751
Natural variant1751L → P in HNPCC1. Ref.85
VAR_043752
Natural variant1771E → H Associated with HNPCC1; requires 2 nucleotide substitutions; unknown pathological significance; repair proficient. Ref.106
VAR_067285
Natural variant1871L → P in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.98 Ref.102
VAR_043753
Natural variant1981E → G in HNPCC1.
VAR_054513
Natural variant1991C → R in glioma; also associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.56 Ref.103
VAR_012937
Natural variant2031G → R in CRC; unknown pathological significance; somatic mutation. Ref.87
VAR_043754
Natural variant2051E → Q Shows no defects; mismatch repair proficient. Ref.107
VAR_068705
Natural variant2161I → V in HNPCC1; unknown pathological significance; shows slightly reduced mismatch binding or release efficiency. Ref.71
VAR_012938
Natural variant2461K → Q in HNPCC1; unknown pathological significance. Ref.62
VAR_043755
Natural variant265 – 31450Missing in HNPCC1.
VAR_004475
Natural variant2721A → V Associated with HNPCC1; unknown pathological significance; shows slightly reduced mismatch binding or release efficiency; results in partial exon 5 skipping on ex vivo splicing assay; repair proficient. Ref.98 Ref.102 Ref.103 Ref.106
Corresponds to variant rs34136999 [ dbSNP | Ensembl ].
VAR_043756
Natural variant2831D → Y in HNPCC1. Ref.95
VAR_043757
Natural variant3051A → T in HNPCC1; repair proficient. Ref.48 Ref.106
VAR_004476
Natural variant3221G → D Common polymorphism; may be associated with increased colorectal cancer susceptibility; the equivalent substitution in yeast reduces the mismatch repair efficiency in vitro; shows significantly decreased repair efficiency when associated with variant Glu-487. Ref.9 Ref.44 Ref.52 Ref.54 Ref.58 Ref.61 Ref.62 Ref.66 Ref.68 Ref.72 Ref.77 Ref.79 Ref.81 Ref.83 Ref.97 Ref.101 Ref.102 Ref.107
Corresponds to variant rs4987188 [ dbSNP | Ensembl ].
VAR_004477
Natural variant3231S → C in HNPCC1; unknown pathological significance. Ref.49
VAR_012939
Natural variant3231S → Y in HNPCC1; unknown pathological significance. Ref.70
VAR_043758
Natural variant3281A → P Shows significantly decreased repair efficiency when associated with variant Ser-127; presumed to enhance cancer risk considerably when associated with variant Ser-127. Ref.107
VAR_068706
Natural variant3311N → D Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.103
VAR_054514
Natural variant3331C → Y in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.98 Ref.102
VAR_043759
Natural variant3351T → I in HNPCC1; unknown pathological significance. Ref.70
VAR_043760
Natural variant3361P → S in HNPCC1. Ref.60
VAR_043761
Natural variant3421V → I in colorectal cancer. Ref.83
VAR_043762
Natural variant3491P → L in HNPCC1. Ref.92
VAR_043763
Natural variant3591R → S in HNPCC1; shows a decreased expression level of the MutS alpha comp lex and is associated with an abnormal subcellular localization pattern. Ref.80 Ref.104
VAR_043764
Natural variant3671V → I Shows no defects; mismatch repair proficient. Ref.107
VAR_068707
Natural variant3851P → L Associated with HNPCC1; unknown pathological significance; repair proficient. Ref.106
VAR_067286
Natural variant3901L → F in HNPCC1; unknown pathological significance; the equivalent substitution in yeast partially affects mismatch repair in vitro; repair proficient. Ref.9 Ref.43 Ref.59 Ref.61 Ref.63 Ref.87 Ref.94 Ref.97 Ref.106
Corresponds to variant rs17224367 [ dbSNP | Ensembl ].
VAR_004478
Natural variant3931K → M in HNPCC1. Ref.75
VAR_043765
Natural variant4191Q → K in CRC; unknown pathological significance; the equivalent substitution in yeast partially affects mismatch repair in vitro. Ref.43 Ref.61 Ref.87 Ref.94
Corresponds to variant rs63750006 [ dbSNP | Ensembl ].
VAR_012940
Natural variant4401Missing in HNPCC1. Ref.90
VAR_043766
Natural variant4701V → E Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.103
VAR_054515
Natural variant4871D → E Mismatch repair deficient; shows significantly decreased repair efficiency when associated with variant Asp-322. Ref.107
VAR_068708
Natural variant4921M → V in HNPCC1.
VAR_043767
Natural variant5061D → Y in CRC; sporadic; early onset; the equivalent substitution in yeast partially affects mismatch repair in vitro. Ref.46 Ref.57 Ref.61 Ref.90
VAR_012941
Natural variant5191F → L Associated with HNPCC1; unknown pathological significance; repair proficient. Ref.106
VAR_067287
Natural variant5241R → P in HNPCC1; defective in mismatch repair activity. Ref.19 Ref.61 Ref.75
VAR_004479
Natural variant5521T → P in HNPCC1. Ref.82
VAR_043768
Natural variant5541S → R in HNPCC1; unknown pathological significance. Ref.71
VAR_012942
Natural variant5621E → V in HNPCC1. Ref.53
VAR_004480
Natural variant5641T → A in HNPCC1; unknown pathological significance. Ref.79 Ref.94
Corresponds to variant rs55778204 [ dbSNP | Ensembl ].
VAR_043769
Natural variant5831N → S in HNPCC1. Ref.82
VAR_043770
Natural variant5961N → S in HNPCC1; unknown pathological significance. Ref.51 Ref.62 Ref.101
Corresponds to variant rs41295288 [ dbSNP | Ensembl ].
VAR_012943
Natural variant5961Missing in HNPCC1; has no effect on ex vivo splicing assay; repair deficient. Ref.42 Ref.45 Ref.48 Ref.60 Ref.75 Ref.78 Ref.92 Ref.103 Ref.106
VAR_004481
Natural variant6001A → V in HNPCC1. Ref.74
VAR_043771
Natural variant6031D → N in HNPCC1; affects protein stability; associated with an absence of the protein in tumors. Ref.68 Ref.98 Ref.102
VAR_043772
Natural variant6101H → N Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.103
VAR_054516
Natural variant6191Y → C in CRC. Ref.87
VAR_043773
Natural variant6221P → L in HNPCC1; the equivalent substitution in yeast causes loss of function in a mismatch repair assay; confers multiple biochemical defects. Ref.3 Ref.61 Ref.72 Ref.75 Ref.105
Corresponds to variant rs28929483 [ dbSNP | Ensembl ].
VAR_004482
Natural variant6291Q → R in HNPCC1; unknown pathological significance. Ref.70 Ref.87 Ref.90 Ref.91 Ref.94
Corresponds to variant rs61756468 [ dbSNP | Ensembl ].
VAR_043774
Natural variant6361A → P in HNPCC1; partial functional loss; mainly causes defects in mismatch binding or release efficiency. Ref.64 Ref.82 Ref.98 Ref.102
VAR_012944
Natural variant6381R → G Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.103
VAR_054517
Natural variant6391H → R in HNPCC1; shows reduced mismatch binding; repair proficient. Ref.50 Ref.105 Ref.106
VAR_043775
Natural variant6391H → Y in HNPCC1; the equivalent substitution in yeast does not affect mismatch repair efficiency in vitro. Ref.3 Ref.72
Corresponds to variant rs28929484 [ dbSNP | Ensembl ].
VAR_004483
Natural variant6411C → G. Ref.55
VAR_004484
Natural variant6451Q → E Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.103
VAR_054518
Natural variant6471E → K in HNPCC1. Ref.50
VAR_043776
Natural variant6561Y → H in HNPCC1; somatic mutation. Ref.50
VAR_043777
Natural variant6601D → G in HNPCC1. Ref.86
VAR_022671
Natural variant6691G → R in HNPCC1. Ref.108
VAR_067761
Natural variant6701P → L. Ref.101
Corresponds to variant rs41294982 [ dbSNP | Ensembl ].
VAR_038027
Natural variant6711N → Y in HNPCC1; unknown pathological significance. Ref.89 Ref.103
VAR_043778
Natural variant6741G → R in HNPCC1; confers resistance to ATP-dependent mismatch release; repair deficient. Ref.100 Ref.105 Ref.106
VAR_067288
Natural variant6741G → S in HNPCC1; somatic mutation. Ref.75
VAR_004485
Natural variant6751K → A Associated with HNPCC1; requires 2 nucleotide substitutions; unknown pathological significance; repair deficient. Ref.106
VAR_067289
Natural variant6791I → T in HNPCC1; somatic mutation. Ref.50
VAR_043779
Natural variant6881M → I in HNPCC1. Ref.57 Ref.65 Ref.90
Corresponds to variant rs63750790 [ dbSNP | Ensembl ].
VAR_012945
Natural variant6921G → R in HNPCC1. Ref.67
VAR_009250
Natural variant6961P → L Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.103
VAR_054519
Natural variant6971C → 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; confers multiple biochemical defects; repair deficient. Ref.54 Ref.61 Ref.98 Ref.102 Ref.105 Ref.106
VAR_004486
Natural variant6971C → R in HNPCC1; has no effect on ex vivo splicing assay. Ref.67 Ref.103
VAR_009251
Natural variant7141A → V in HNPCC1; unknown pathological significance. Ref.70
VAR_043780
Natural variant7231S → F in HNPCC1; has no effect on ex vivo splicing assay; repair deficient. Ref.74 Ref.103 Ref.106
VAR_043781
Natural variant7291M → V in HNPCC1; somatic mutation. Ref.50
VAR_043782
Natural variant7321T → I in HNPCC1; somatic mutation. Ref.50
VAR_043783
Natural variant745 – 7462Missing in HNPCC1; mainly causes defects in mismatch binding or release efficiency.
VAR_043784
Natural variant7481D → Y Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.103
VAR_054520
Natural variant7491E → K in HNPCC1; mainly causes defects in mismatch binding or release efficiency; the mutant protein is well expressed in tumors. Ref.98 Ref.102
VAR_043785
Natural variant7591G → E Associated with HNPCC1; unknown pathological significance; repair deficient. Ref.106
VAR_067290
Natural variant7701I → V. Ref.55
VAR_004487
Natural variant7791M → I. Ref.101
Corresponds to variant rs41295292 [ dbSNP | Ensembl ].
VAR_038028
Natural variant8051L → V Associated with HNPCC1; unknown pathological significance; repair proficient. Ref.106
VAR_067291
Natural variant8071T → S. Ref.101
Corresponds to variant rs41295294 [ dbSNP | Ensembl ].
VAR_038029
Natural variant8131M → V in HNPCC1. Ref.73
VAR_043786
Natural variant8241Q → E in gastric cancer; unknown pathological significance. Ref.70
VAR_043787
Natural variant8341A → T in HNPCC1; shows no functional defects in gel shift assay; is nevertheless repair deficient. Ref.48 Ref.62 Ref.98 Ref.102 Ref.105
VAR_004488
Natural variant8351N → H. Ref.101
Corresponds to variant rs41295296 [ dbSNP | Ensembl ].
VAR_038030
Natural variant8391H → Q Associated with HNPCC1; has no effect on ex vivo splicing assay. Ref.103
VAR_054521
Natural variant8391H → R in HNPCC1. Ref.91
VAR_043788
Natural variant8431C → G Associated with HNPCC1; unknown pathological significance; repair proficient. Ref.106
VAR_067292
Natural variant8451K → E in HNPCC1. Ref.65
Corresponds to variant rs63750571 [ dbSNP | Ensembl ].
VAR_013172
Natural variant8531E → A in HNPCC1; unknown pathological significance. Ref.81 Ref.97
VAR_043789
Natural variant8601S → L Associated with HNPCC1; unknown pathological significance; repair proficient. Ref.106
VAR_067293
Natural variant8681P → A in gastric cancer; unknown pathological significance. Ref.70
VAR_043790
Natural variant8701A → G in gastric cancer; unknown pathological significance. Ref.70
VAR_043791
Natural variant8731C → G in gastric cancer; unknown pathological significance. Ref.70
VAR_043792
Natural variant8861E → G in HNPCC1; repair proficient. Ref.78 Ref.106
VAR_043793
Natural variant9051T → R in HNPCC1; unknown pathological significance. Ref.75
VAR_004489
Natural variant9091K → I Found in a colorectal cancer sample; mismatch repair proficient. Ref.107
VAR_068709
Natural variant9111L → R. Ref.101
Corresponds to variant rs41295182 [ dbSNP | Ensembl ].
VAR_038031
Natural variant9231V → E in HNPCC1; unknown pathological significance. Ref.78 Ref.98 Ref.102
VAR_043794
Natural variant9311K → T in HNPCC1. Ref.88
VAR_043795

Experimental info

Mutagenesis6741G → A: Mainly causes defects in mismatch binding or release efficiency. Ref.102
Mutagenesis6751K → R: No effect on mismatch binding, complete loss of DNA repair function when associated with MSH6 mutant R-1140. Ref.18
Sequence conflict7841F → I in BX649122. Ref.7
Sequence conflict8361F → S in BX649122. Ref.7

Secondary structure

........................................................................................................................................................... 934
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

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

FASTA934104,743
        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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Isoform 2 [UniParc].

Checksum: 1BC5218379005E26
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FASTA86897,323

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [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. expand/collapse author list , Todd S., Lewis T., Leach R.J., Naylor S.L., Weissenbach J., Mecklin J.-P., Jaervinen H., Petersen G.M., Hamilton S.R., Green J., Jass J., Watson P., Lynch H.T., Trent J.M., de la Chapelle A., Kinzler K.W., Vogelstein B.
Cell 75:1215-1225(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN MRTES.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HIS-96.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Uterus.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[8]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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.
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Muscle.
[11]"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.
[12]"Purified human MSH2 protein binds to DNA containing mismatched nucleotides."
Fishel R., Ewel A., Lescoe M.K.
Cancer Res. 54:5539-5542(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[13]"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] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MSH3 AND MSH6.
[15]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EXO1.
[16]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"DNA-dependent activation of the hMutSalpha ATPase."
Blackwell L.J., Bjornson K.P., Modrich P.
J. Biol. Chem. 273:32049-32054(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-675.
[19]"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] [Europe PMC] [Abstract]
Cited for: MISMATCH-BINDING, CHARACTERIZATION OF VARIANT HNPCC1 PRO-524.
[20]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF MSH2 AS MEMBER OF BASC.
[22]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EXO1, TISSUE SPECIFICITY.
[23]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EXO1.
[25]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EXO1.
[26]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EXO1.
[27]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATR, IDENTIFICATION BY MASS SPECTROMETRY.
[28]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EXO1.
[29]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PRKCZ.
[31]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[32]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[33]"Colon cancer and DNA repair: have mismatches met their match?"
Jiricny J.
Trends Genet. 10:164-168(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[34]"Molecular basis of HNPCC: mutations of MMR genes."
Papadopoulos N., Lindblom A.
Hum. Mutat. 10:89-99(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[35]"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] [Europe PMC] [Abstract]
Cited for: REVIEW.
[36]"The novel protein complex with SMARCAD1/KIAA1122 binds to the vicinity of TSS."
Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T., Ohara O., Koga H.
J. Mol. Biol. 382:257-265(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMARCAD1.
[37]"Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair."
Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., Elledge S.J., Harper J.W.
Cell 138:63-77(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLX4.
[38]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[41]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
[42]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 ASN-596 DEL.
[43]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS PHE-390 AND LYS-419.
[44]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-322.
[45]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 ASN-596 DEL, VARIANT HIS-167.
[46]"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] [Europe PMC] [Abstract]
Cited for: VARIANT CRC TYR-506.
[47]"Microsatellite instability and the role of hMSH2 in sporadic colorectal cancer."
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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 GLN-46.
[48]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 THR-305; ASN-596 DEL AND THR-834.
[49]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 CYS-323.
[50]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 THR-110; ARG-639; LYS-647; HIS-656; THR-679; VAL-729 AND ILE-732.
[51]"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] [Europe PMC] [Abstract]
Cited for: VARIANT SER-596.
[52]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-322.
[53]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 VAL-562.
[54]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 PHE-697, VARIANT ASP-322.
[55]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 265-VAL--GLN-314 DEL, VARIANTS GLY-641 AND VAL-770.
[56]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GLIOMA ARG-199.
[57]"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] [Europe PMC] [Abstract]
Cited for: VARIANT CRC TYR-506, VARIANT HNPCC1 ILE-688.
[58]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-322.
[59]"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] [Europe PMC] [Abstract]
Cited for: VARIANT PHE-390.
[60]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 SER-336 AND ASN-596 DEL.
[61]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS ASP-322; PHE-390; LYS-419; TYR-506; PRO-524; LEU-622 AND PHE-697.
[62]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 GLN-246; ASP-322; SER-596 AND THR-834.
[63]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 PHE-390.
[64]"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. 36:790-793(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 PRO-636.
[65]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 ILE-688 AND GLU-845, VARIANT MET-8.
[66]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-322.
[67]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 ARG-692 AND ARG-697.
[68]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 ASN-603, VARIANT ASP-322.
[69]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)
[70]"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] [Europe PMC] [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.
[71]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 ASP-161; VAL-216 AND ARG-554.
[72]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS ASP-322; LEU-622 AND TYR-639.
[73]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 VAL-813.
[74]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 VAL-600 AND PHE-723.
[75]"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] [Europe PMC] [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.
[76]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MULTIPLE CAFE-AU-LAIT SPOTS WITH LEUKEMIA.
[77]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-322.
[78]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 MET-44; VAL-45; ASN-596 DEL; GLY-886 AND GLU-923.
[79]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 ILE-102; ASP-163 AND ALA-564, VARIANT ASP-322.
[80]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 HIS-167 AND SER-359.
[81]"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. expand/collapse author list , Niepsuj S., Slomski R., Plawski A., Lacka-Wojciechowska A., Rozmiarek A., Fiszer-Maliszewska L., Bebenek M., Sorokin D., Stawicka M., Godlewski D., Richter P., Brozek I., Wysocka B., Jawien A., Banaszkiewicz Z., Kowalczyk J., Czudowska D., Goretzki P.E., Moeslein G., Lubinski J.
J. Med. Genet. 39:E65-E65(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 LEU-92 DEL AND ALA-853, VARIANT ASP-322.
[82]"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. expand/collapse author list , Lynch J.F., de la Chapelle A., Lynch H.T., Fodde R.
Am. J. Hum. Genet. 72:1088-1100(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 PRO-552; SER-583 AND PRO-636.
[83]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS COLORECTAL CANCER ILE-13 AND ILE-342, VARIANT ASP-322.
[84]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 SER-127.
[85]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 PRO-175.
[86]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 GLY-163 AND GLY-660.
[87]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS CRC MET-8; SER-40; VAL-169; ARG-203; PHE-390; LYS-419; CYS-619 AND ARG-629.
[88]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 THR-931.
[89]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 TYR-671.
[90]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 LEU-440 DEL; TYR-506; ARG-629 AND ILE-688.
[91]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 ARG-839, VARIANT ARG-629.
[92]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 LEU-349 AND ASN-596 DEL.
[93]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 PHE-93.
[94]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 VAL-169; PHE-390; ALA-564 AND ARG-629, VARIANT CRC LYS-419.
[95]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 TYR-283.
[96]"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] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 ARG-162.
[97]"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. expand/collapse author list , Slomski R., Plawski A., Lacka-Wojciechowska A., Rozmiarek A., Fiszer-Maliszewska L., Bebenek M., Sorokin D., Sasiadek M.M., Stembalska A., Grzebieniak Z., Kilar E., Stawicka M., Godlewski D., Richter P., Brozek I., Wysocka B., Limon J., Jawien A., Banaszkiewicz Z., Janiszewska H., Kowalczyk J., Czudowska D., Scott R.J., Lubinski J.
Clin. Genet. 69:40-47(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC1 THR-2; LEU-92 DEL; MET-145; PHE-390 AND ALA-853, VARIANT ASP-322.
[98]"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] [Europe PMC] [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.
[99]"Gene symbol: msh2. Disease: hereditary nonpolyposis colorectal cancer."
Leonardis D.
Hum. Genet. 119:675-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 ALA-162.
[100]"A high incidence of MSH6 mutations in Amsterdam criteria II-negative families tested in a diagnostic setting."
Ramsoekh D., Wagner A., van Leerdam M.E., Dinjens W.N., Steyerberg E.W., Halley D.J., Kuipers E.J., Dooijes D.
Gut 57:1539-1544(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 ARG-674.
[101]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GLN-46; LYS-106; ASP-322; SER-596; LEU-670; ILE-779; SER-807; HIS-835 AND ARG-911.
[102]"Mechanisms of pathogenicity in human MSH2 missense mutants."
Ollila S., Dermadi Bebek D., Jiricny J., Nystroem M.
Hum. Mutat. 29:1355-1363(2008) [PubMed] [Europe PMC] [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.
[103]"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] [Europe PMC] [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.
[104]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS HNPCC1 ARG-162; HIS-167 AND SER-359.
[105]"Functional analysis of HNPCC-related missense mutations in MSH2."
Lutzen A., de Wind N., Georgijevic D., Nielsen F.C., Rasmussen L.J.
Mutat. Res. 645:44-55(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS HNPCC1 HIS-167; THR-305: LEU-622; ARG-639; ARG-674; PHE-697 AND THR-834.
[106]"A rapid and cell-free assay to test the activity of lynch syndrome-associated MSH2 and MSH6 missense variants."
Drost M., Zonneveld J.B., van Hees S., Rasmussen L.J., Hofstra R.M., de Wind N.
Hum. Mutat. 33:488-494(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS HNPCC1 MET-44; VAL-45; HIS-167; THR-305; PHE-390; ASN-596 DEL; ARG-639; ARG-674; PHE-697; PHE-723 AND GLY-886, CHARACTERIZATION OF VARIANTS ASP-165; HIS-177; VAL-272; LEU-385; LEU-519; ALA-675; GLU-759; VAL-805; GLY-843 AND LEU-860.
[107]"Mismatch repair analysis of inherited MSH2 and/or MSH6 variation pairs found in cancer patients."
Kantelinen J., Kansikas M., Candelin S., Hampel H., Smith B., Holm L., Kariola R., Nystrom M.
Hum. Mutat. 33:1294-1301(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS SER-127; MET-145; GLN-205; ASP-322; PRO-328; ILE-367; GLU-487 AND ILE-909.
[108]"Germline mutation analysis of MLH1 and MSH2 in Malaysian Lynch syndrome patients."
Zahary M.N., Kaur G., Abu Hassan M.R., Singh H., Naik V.R., Ankathil R.
World J. Gastroenterol. 18:814-820(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC1 ARG-669.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03911 mRNA. Translation: AAA18643.1.
U04045 mRNA. Translation: AAA61870.1.
U41221 expand/collapse EMBL AC list , U41206, U41207, U41208, U41210, U41211, U41212, U41213, U41214, U41215, U41216, U41217, U41218, U41219, 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.
AK304496 mRNA. Translation: BAG65304.1.
BX649122 mRNA. No translation available.
AC079775 Genomic DNA. No translation available.
AC138655 Genomic DNA. No translation available.
BC021566 mRNA. Translation: AAH21566.1.
AF066081 Genomic DNA. Translation: AAC27930.1. Frameshift.
PIRI64819.
RefSeqNP_000242.1. NM_000251.2.
NP_001245210.1. NM_001258281.1.
UniGeneHs.597656.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O8BX-ray2.75A1-934[»]
2O8CX-ray3.37A1-934[»]
2O8DX-ray3.00A1-934[»]
2O8EX-ray3.30A1-934[»]
2O8FX-ray3.25A1-934[»]
3THWX-ray3.09A1-934[»]
3THXX-ray2.70A1-934[»]
3THYX-ray2.89A1-934[»]
3THZX-ray4.30A1-934[»]
ProteinModelPortalP43246.
SMRP43246. Positions 1-930.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110573. 90 interactions.
DIPDIP-35054N.
IntActP43246. 21 interactions.
MINTMINT-84789.
STRING9606.ENSP00000233146.

PTM databases

PhosphoSiteP43246.

Polymorphism databases

DMDM1171032.

Proteomic databases

PaxDbP43246.
PeptideAtlasP43246.
PRIDEP43246.

Protocols and materials databases

DNASU4436.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233146; ENSP00000233146; ENSG00000095002. [P43246-1]
ENST00000543555; ENSP00000442697; ENSG00000095002. [P43246-2]
GeneID4436.
KEGGhsa:4436.
UCSCuc002rvy.2. human. [P43246-1]

Organism-specific databases

CTD4436.
GeneCardsGC02P047630.
HGNCHGNC:7325. MSH2.
HPACAB009572.
MIM120435. phenotype.
158320. phenotype.
608089. phenotype.
609309. gene.
neXtProtNX_P43246.
Orphanet252202. Constitutional mismatch repair deficiency syndrome.
144. Hereditary nonpolyposis colon cancer.
587. Muir-Torre syndrome.
99817. Non-polyposis Turcot syndrome.
PharmGKBPA31133.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0249.
HOGENOMHOG000196498.
HOVERGENHBG006399.
InParanoidP43246.
KOK08735.
OMAVGAGDCQ.
OrthoDBEOG76DTRW.
PhylomeDBP43246.
TreeFamTF351780.

Gene expression databases

ArrayExpressP43246.
BgeeP43246.
CleanExHS_MSH2.
GenevestigatorP43246.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR011184. DNA_mismatch_repair_MSH2.
IPR007695. DNA_mismatch_repair_MutS-lik_N.
IPR000432. DNA_mismatch_repair_MutS_C.
IPR007861. DNA_mismatch_repair_MutS_clamp.
IPR007696. DNA_mismatch_repair_MutS_core.
IPR007860. DNA_mmatch_repair_MutS_con_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF01624. 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]
PIRSFPIRSF005813. MSH2. 1 hit.
SMARTSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view]
SUPFAMSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMSH2. human.
EvolutionaryTraceP43246.
GeneWikiMSH2.
GenomeRNAi4436.
NextBio17289.
PROP43246.
SOURCESearch...

Entry information

Entry nameMSH2_HUMAN
AccessionPrimary (citable) accession number: P43246
Secondary accession number(s): B4E2Z2, O75488
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

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