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P52701 (MSH6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA mismatch repair protein Msh6

Short name=hMSH6
Alternative name(s):
G/T mismatch-binding protein
Short name=GTBP
Short name=GTMBP
MutS-alpha 160 kDa subunit
Short name=p160
Gene names
Name:MSH6
Synonyms:GTBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1360 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, 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. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.29

Subunit structure

Heterodimer consisting of MSH2-MSH6 (MutS alpha). Forms 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.

Subcellular location

Nucleus. Chromosome. Note: Associates with H3K36me3 via its PWWP domain. Ref.29

Domain

The PWWP domain specifically recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3) (Ref.29).

Post-translational modification

The N-terminus is blocked.

Phosphorylated by PRKCZ, which may prevent MutS alpha degradation by the ubiquitin-proteasome pathway. Ref.15

Involvement in disease

Hereditary non-polyposis colorectal cancer 5 (HNPCC5) [MIM:614350]: 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.17 Ref.32 Ref.34 Ref.39 Ref.42 Ref.46 Ref.47 Ref.52

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.

Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: Autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts, hyperpigmented and cafe au lait spots.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Sequence similarities

Belongs to the DNA mismatch repair MutS family.

Contains 1 PWWP domain.

Ontologies

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

Inferred from direct assay PubMed 16403449. Source: GOC

DNA repair

Inferred from direct assay Ref.1. Source: BHF-UCL

determination of adult lifespan

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

intrinsic apoptotic signaling pathway

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

intrinsic apoptotic signaling pathway in response to DNA damage

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

isotype switching

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

meiotic mismatch repair

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

mismatch repair

Inferred from direct assay Ref.29. Source: UniProtKB

negative regulation of DNA recombination

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

positive regulation of helicase activity

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

reciprocal meiotic recombination

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to UV

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

somatic hypermutation of immunoglobulin genes

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

somatic recombination of immunoglobulin gene segments

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

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

MutSalpha complex

Inferred from direct assay Ref.29. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nuclear chromosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

chromatin binding

Inferred from electronic annotation. Source: Ensembl

damaged DNA binding

Inferred from electronic annotation. Source: Ensembl

guanine/thymine mispair binding

Inferred from electronic annotation. Source: Ensembl

methylated histone residue binding

Inferred from direct assay Ref.29. Source: UniProtKB

mismatched DNA binding

Inferred from direct assay Ref.29. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MSH2P432464EBI-395529,EBI-355888

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform GTBP-N (identifier: P52701-1)

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 GTBP-alt (identifier: P52701-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1058-1068: DVLLCLANYSR → GKTLNKLVLRL
     1069-1360: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13601360DNA mismatch repair protein Msh6
PRO_0000115207

Regions

Domain92 – 15463PWWP
Nucleotide binding1134 – 11418ATP Potential
Compositional bias34 – 374Poly-Ala
Compositional bias201 – 2099Poly-Glu
Compositional bias1118 – 11236Poly-Glu

Amino acid modifications

Modified residue141Phosphoserine Ref.19 Ref.24 Ref.26 Ref.28
Modified residue411Phosphoserine Ref.19
Modified residue431Phosphoserine Ref.19
Modified residue701N6-acetyllysine Ref.25
Modified residue791Phosphoserine Ref.24
Modified residue911Phosphoserine Ref.24
Modified residue1371Phosphoserine Ref.24 Ref.26 Ref.28
Modified residue2001Phosphoserine Ref.24
Modified residue2191Phosphoserine Ref.18 Ref.28
Modified residue2271Phosphoserine Ref.18 Ref.24 Ref.26 Ref.28
Modified residue2521Phosphoserine Ref.24 Ref.28
Modified residue2541Phosphoserine Ref.24
Modified residue2561Phosphoserine Ref.24
Modified residue2611Phosphoserine Ref.18 Ref.24 Ref.28
Modified residue2691Phosphothreonine Ref.28
Modified residue2741Phosphoserine Ref.28
Modified residue2751Phosphoserine Ref.28
Modified residue2791Phosphoserine Ref.28
Modified residue2801Phosphoserine Ref.28
Modified residue3091Phosphoserine Ref.23 Ref.28
Modified residue5041N6-acetyllysine Ref.25
Modified residue8301Phosphoserine Ref.26

Natural variations

Alternative sequence1058 – 106811DVLLCLANYSR → GKTLNKLVLRL in isoform GTBP-alt.
VSP_003291
Alternative sequence1069 – 1360292Missing in isoform GTBP-alt.
VSP_003292
Natural variant131K → T. Ref.51
Corresponds to variant rs41294988 [ dbSNP | Ensembl ].
VAR_038032
Natural variant201A → V in colorectal/endometrial cancer and HNPCC5; repair proficient. Ref.36 Ref.52
Corresponds to variant rs63750664 [ dbSNP | Ensembl ].
VAR_043943
Natural variant251A → S Associated with HNPCC5; unknown pathologiacl significance; repair proficient. Ref.52
VAR_067294
Natural variant251A → V.
Corresponds to variant rs35462442 [ dbSNP | Ensembl ].
VAR_038033
Natural variant391G → E. Ref.1 Ref.3 Ref.19 Ref.33 Ref.37 Ref.44
Corresponds to variant rs1042821 [ dbSNP | Ensembl ].
VAR_004490
Natural variant541G → A in CRC; unknown pathological significance. Ref.44
Corresponds to variant rs63751098 [ dbSNP | Ensembl ].
VAR_043944
Natural variant651S → L. Ref.51
Corresponds to variant rs41294984 [ dbSNP | Ensembl ].
VAR_038034
Natural variant991K → N in CRC; unknown pathological significance. Ref.49
VAR_043945
Natural variant1281R → L No impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. Ref.45
VAR_043946
Natural variant1441S → I in suspected HNPCC5 and CRC. Ref.32 Ref.40 Ref.51
Corresponds to variant rs3211299 [ dbSNP | Ensembl ].
VAR_012955
Natural variant2201E → D. Ref.33
Corresponds to variant rs1800938 [ dbSNP | Ensembl ].
VAR_012956
Natural variant2211E → D. Ref.50
Corresponds to variant rs41557217 [ dbSNP | Ensembl ].
VAR_042274
Natural variant2851S → I in CRC. Ref.33
VAR_012957
Natural variant2951K → R in multiple colorectal adenoma.
VAR_043947
Natural variant3261A → V Associated with HNPCC5; unknown pathological significance; repair proficient. Ref.52
VAR_067295
Natural variant3401F → S in CRC, breast cancer and leukemia. Ref.37
VAR_043948
Natural variant3961L → V Associated with HNPCC5; unknown pathological significance; repair proficient. Ref.3 Ref.33 Ref.52
Corresponds to variant rs2020908 [ dbSNP | Ensembl ].
VAR_012958
Natural variant4351L → P Mismatch repair deficient. Ref.53
VAR_068710
Natural variant4491L → P in colorectal/endometrial cancer; unknown pathological significance. Ref.48
VAR_043949
Natural variant4681R → H. Ref.51
Corresponds to variant rs41295268 [ dbSNP | Ensembl ].
VAR_038035
Natural variant4921M → V Associated with HNPCC5; unknown pathological significance; repair proficient. Ref.42 Ref.50 Ref.52
VAR_042275
Natural variant5031S → C Associated with HNPCC5; unknown pathological significance; repair proficient. Ref.51 Ref.52
VAR_038036
Natural variant5091V → A. Ref.44
VAR_043950
Natural variant5221Q → R in CRC; also associated with HNPCC5; repair proficient. Ref.40 Ref.52
VAR_043951
Natural variant5381Y → S.
Corresponds to variant rs728619 [ dbSNP | Ensembl ].
VAR_038037
Natural variant5661G → R in CRC; partial functional loss. Ref.33
VAR_012959
Natural variant5801S → L. Ref.51
Corresponds to variant rs41295270 [ dbSNP | Ensembl ].
VAR_038038
Natural variant5851L → P Mismatch repair deficient. Ref.53
VAR_068711
Natural variant6101K → N Associated with HNPCC5; unknown pathological significance; repair proficient. Ref.52
VAR_067296
Natural variant6191E → D in CRC; unknown pathological significance. Ref.49
VAR_043952
Natural variant6231P → A. Ref.3
Corresponds to variant rs3136334 [ dbSNP | Ensembl ].
VAR_029244
Natural variant6231P → L No impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. Ref.45
VAR_043953
Natural variant6771S → T Mismatch repair proficient. Ref.53
VAR_068712
Natural variant6851G → A in CRC. Ref.38
VAR_043954
Natural variant6981Q → E in HNPCC; unknown pathological significance. Ref.34
VAR_012960
Natural variant7251I → M in CRC; unknown pathological significance. Ref.40
VAR_043955
Natural variant7281K → T No impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. Ref.45
Corresponds to variant rs35552856 [ dbSNP | Ensembl ].
VAR_043956
Natural variant7721R → Q in CRC. Ref.38
VAR_043957
Natural variant7721R → W in HNPCC5. Ref.46
VAR_043958
Natural variant7871A → V in CRC; unknown pathological significance. Ref.49
VAR_043959
Natural variant8001V → A in CRC; somatic mutation. Ref.38
VAR_043960
Natural variant8001V → L May be a rare polymorphism. Ref.33
VAR_012961
Natural variant8031D → G in CRC. Ref.33
VAR_012962
Natural variant8501Y → C Associated with HNPCC5 and CRC; unknown pathological significance; repair proficient. Ref.32 Ref.40 Ref.52
VAR_012963
Natural variant8541K → M in CRC; unknown pathological significance. Ref.38 Ref.44
Corresponds to variant rs34374438 [ dbSNP | Ensembl ].
VAR_043961
Natural variant8781V → A in suspected HNPCC5, colorectal/endometrial cancer and CRC; repair proficient. Ref.36 Ref.38 Ref.39 Ref.40 Ref.44 Ref.49 Ref.51 Ref.52 Ref.53
Corresponds to variant rs2020912 [ dbSNP | Ensembl ].
VAR_012964
Natural variant8861I → V. Ref.3
Corresponds to variant rs2020914 [ dbSNP | Ensembl ].
VAR_014902
Natural variant9011R → H in colorectal/endometrial cancer. Ref.36
VAR_043962
Natural variant9761R → H in CRC; sporadic; also associated with HNPCC5; repair proficient. Ref.41 Ref.52
VAR_012965
Natural variant10211A → D in CRC; unknown pathological significance; repair proficient. Ref.40 Ref.52
VAR_043963
Natural variant10261D → Y Associated with HNPCC5; unknown pathological significance; repair proficient. Ref.52
VAR_067297
Natural variant10311D → V in CRC; somatic mutation. Ref.38
VAR_043964
Natural variant10761R → C in CRC; unknown pathological significance. Ref.49
VAR_043965
Natural variant10871P → S Associated with HNPCC5; unknown pathological significance; repair proficient. Ref.52
Corresponds to variant rs63750998 [ dbSNP | Ensembl ].
VAR_067298
Natural variant10871P → T in CRC. Ref.33
Corresponds to variant rs63750998 [ dbSNP | Ensembl ].
VAR_012966
Natural variant10951R → H in CRC; unknown pathological significance; mismatch repair proficient. Ref.43 Ref.53
VAR_043966
Natural variant11001T → M in CRC; unknown pathological significance. Ref.40
VAR_043967
Natural variant11581C → R in CRC; somatic mutation. Ref.38
VAR_043968
Natural variant11631E → V in HNPCC5. Ref.47
Corresponds to variant rs63750252 [ dbSNP | Ensembl ].
VAR_043969
Natural variant11931E → K Found in an endometrial cancer sample; displays marked impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. Ref.45
VAR_043970
Natural variant12131D → V. Ref.31
VAR_004491
Natural variant12191T → I in CRC; unknown pathological significance. Ref.40
VAR_043971
Natural variant12251T → M Associated with HNPCC5; unknown pathological significance; repair proficient. Ref.52
VAR_067299
Natural variant12321V → L. Ref.51
Corresponds to variant rs41295276 [ dbSNP | Ensembl ].
VAR_038039
Natural variant12341E → Q.
Corresponds to variant rs35717727 [ dbSNP | Ensembl ].
VAR_038040
Natural variant12481H → D in CRC; unknown pathological significance. Ref.40
VAR_043972
Natural variant12601V → I. Ref.31
VAR_004492
Natural variant12841T → M in CRC. Ref.35
VAR_043973
Natural variant13211R → G. Ref.51
Corresponds to variant rs41295278 [ dbSNP | Ensembl ].
VAR_038041
Natural variant13541L → Q in CRC; unknown pathological significance; mismatch repair proficient. Ref.43 Ref.53
VAR_043974

Experimental info

Mutagenesis1031Y → A: Abolishes binding to H3K36me3 and DNA mismatch repair activity. Ref.29
Mutagenesis105 – 1062WW → AA: Abolishes binding to H3K36me3 and DNA mismatch repair activity.
Mutagenesis11401K → R: No effect on mismatch binding, complete loss of DNA repair function when associated with MSH2 mutant R-675. Ref.10
Sequence conflict36 – 5722AAPGA…AGPGP → GCPRGLSFPRRGCGLERGWA WA in BAA23674. Ref.2
Sequence conflict36 – 5722AAPGA…AGPGP → GCPRGLSFPRRGCGLERGWA WA in BAA23675. Ref.2
Sequence conflict1358 – 13603KEL → D in AAL87401. Ref.3

Secondary structure

................................................................................................................................................................................................... 1360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform GTBP-N [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 4A4AA9F8ECB8FFE9

FASTA1,360152,786
        10         20         30         40         50         60 
MSRQSTLYSF FPKSPALSDA NKASARASRE GGRAAAAPGA SPSPGGDAAW SEAGPGPRPL 

        70         80         90        100        110        120 
ARSASPPKAK NLNGGLRRSV APAAPTSCDF SPGDLVWAKM EGYPWWPCLV YNHPFDGTFI 

       130        140        150        160        170        180 
REKGKSVRVH VQFFDDSPTR GWVSKRLLKP YTGSKSKEAQ KGGHFYSAKP EILRAMQRAD 

       190        200        210        220        230        240 
EALNKDKIKR LELAVCDEPS EPEEEEEMEV GTTYVTDKSE EDNEIESEEE VQPKTQGSRR 

       250        260        270        280        290        300 
SSRQIKKRRV ISDSESDIGG SDVEFKPDTK EEGSSDEISS GVGDSESEGL NSPVKVARKR 

       310        320        330        340        350        360 
KRMVTGNGSL KRKSSRKETP SATKQATSIS SETKNTLRAF SAPQNSESQA HVSGGGDDSS 

       370        380        390        400        410        420 
RPTVWYHETL EWLKEEKRRD EHRRRPDHPD FDASTLYVPE DFLNSCTPGM RKWWQIKSQN 

       430        440        450        460        470        480 
FDLVICYKVG KFYELYHMDA LIGVSELGLV FMKGNWAHSG FPEIAFGRYS DSLVQKGYKV 

       490        500        510        520        530        540 
ARVEQTETPE MMEARCRKMA HISKYDRVVR REICRIITKG TQTYSVLEGD PSENYSKYLL 

       550        560        570        580        590        600 
SLKEKEEDSS GHTRAYGVCF VDTSLGKFFI GQFSDDRHCS RFRTLVAHYP PVQVLFEKGN 

       610        620        630        640        650        660 
LSKETKTILK SSLSCSLQEG LIPGSQFWDA SKTLRTLLEE EYFREKLSDG IGVMLPQVLK 

       670        680        690        700        710        720 
GMTSESDSIG LTPGEKSELA LSALGGCVFY LKKCLIDQEL LSMANFEEYI PLDSDTVSTT 

       730        740        750        760        770        780 
RSGAIFTKAY QRMVLDAVTL NNLEIFLNGT NGSTEGTLLE RVDTCHTPFG KRLLKQWLCA 

       790        800        810        820        830        840 
PLCNHYAIND RLDAIEDLMV VPDKISEVVE LLKKLPDLER LLSKIHNVGS PLKSQNHPDS 

       850        860        870        880        890        900 
RAIMYEETTY SKKKIIDFLS ALEGFKVMCK IIGIMEEVAD GFKSKILKQV ISLQTKNPEG 

       910        920        930        940        950        960 
RFPDLTVELN RWDTAFDHEK ARKTGLITPK AGFDSDYDQA LADIRENEQS LLEYLEKQRN 

       970        980        990       1000       1010       1020 
RIGCRTIVYW GIGRNRYQLE IPENFTTRNL PEEYELKSTK KGCKRYWTKT IEKKLANLIN 

      1030       1040       1050       1060       1070       1080 
AEERRDVSLK DCMRRLFYNF DKNYKDWQSA VECIAVLDVL LCLANYSRGG DGPMCRPVIL 

      1090       1100       1110       1120       1130       1140 
LPEDTPPFLE LKGSRHPCIT KTFFGDDFIP NDILIGCEEE EQENGKAYCV LVTGPNMGGK 

      1150       1160       1170       1180       1190       1200 
STLMRQAGLL AVMAQMGCYV PAEVCRLTPI DRVFTRLGAS DRIMSGESTF FVELSETASI 

      1210       1220       1230       1240       1250       1260 
LMHATAHSLV LVDELGRGTA TFDGTAIANA VVKELAETIK CRTLFSTHYH SLVEDYSQNV 

      1270       1280       1290       1300       1310       1320 
AVRLGHMACM VENECEDPSQ ETITFLYKFI KGACPKSYGF NAARLANLPE EVIQKGHRKA 

      1330       1340       1350       1360 
REFEKMNQSL RLFREVCLAS ERSTVDAEAV HKLLTLIKEL 

« Hide

Isoform GTBP-alt [UniParc].

Checksum: E1E62571A314B51E
Show »

FASTA1,068120,563

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT GLU-39.
[2]"Alternative splicing of GTBP in normal human tissues."
Shiwaku H.O., Wakatsuki S., Mori Y., Fukushige S., Horii A.
DNA Res. 4:359-362(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[3]NIEHS SNPs program
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-39; VAL-396; ALA-623 AND VAL-886.
[4]"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].
Tissue: Placenta.
[5]"GTBP, a 160-kilodalton protein essential for mismatch-binding activity in human cells."
Palombo F., Gallinari P., Iaccarino I., Lettieri T., Hughes M., D'Arrigo A., Truong O., Hsuan J.J., Jiricny J.
Science 268:1912-1914(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-1360, PARTIAL PROTEIN SEQUENCE.
[6]"Molecular cloning of the N-terminus of GTBP."
Nicolaides N.C., Palombo F., Kinzler K.W., Vogelstein B., Jiricny J.
Genomics 31:395-397(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-116.
[7]"Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells."
Drummond J.T., Li G.-M., Longley M.J., Modrich P.
Science 268:1909-1912(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
[8]"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.
[9]"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.
[10]"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-1140.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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 MSH6 AS MEMBER OF BASC.
[17]"Germline mutation of MSH6 as the cause of hereditary nonpolyposis colorectal cancer."
Miyaki M., Konishi M., Tanaka K., Kikuchi-Yanoshita R., Muraoka M., Yasuno M., Igari T., Koike M., Chiba M., Mori T.
Nat. Genet. 17:271-272(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HNPCC5.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-227 AND SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-41 AND SER-43, VARIANT [LARGE SCALE ANALYSIS] GLU-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Novel biallelic mutations in MSH6 and PMS2 genes: gene conversion as a likely cause of PMS2 gene inactivation."
Auclair J., Leroux D., Desseigne F., Lasset C., Saurin J.C., Joly M.O., Pinson S., Xu X.L., Montmain G., Ruano E., Navarro C., Puisieux A., Wang Q.
Hum. Mutat. 28:1084-1090(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MMRCS.
[21]"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.
[22]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-79; SER-91; SER-137; SER-200; SER-227; SER-252; SER-254; SER-256 AND SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"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-70 AND LYS-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-137; SER-227 AND SER-830, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"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].
[28]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-137; SER-219; SER-227; SER-252; SER-261; THR-269; SER-274; SER-275; SER-279; SER-280 AND SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSalpha."
Li F., Mao G., Tong D., Huang J., Gu L., Yang W., Li G.M.
Cell 153:590-600(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-103 AND 105-TRP-TRP-106.
[30]"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).
[31]"Mutations of GTBP in genetically unstable cells."
Papadopoulos N., Nicolaides N.C., Liu B., Parsons R., Lengauer C., Palombo F., D'Arrigo A., Markowitz S., Willson J.K.V., Kinzler K.W., Jiricny J., Vogelstein B.
Science 268:1915-1917(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-1213 AND ILE-1260.
[32]"Association of hereditary nonpolyposis colorectal cancer-related tumors displaying low microsatellite instability with MSH6 germline mutations."
Wu Y., Berends M.J.W., Mensink R.G.J., Kempinga C., Sijmons R.H., van Der Zee A.G.J., Hollema H., Kleibeuker J.H., Buys C.H.C.M., Hofstra R.M.W.
Am. J. Hum. Genet. 65:1291-1298(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HNPCC5 ILE-144 AND CYS-850.
[33]"Germ-line msh6 mutations in colorectal cancer families."
Kolodner R.D., Tytell J.D., Schmeits J.L., Kane M.F., Das Gupta R., Weger J., Wahlberg S., Fox E.A., Peel D., Ziogas A., Garber J.E., Syngal S., Anton-Culver H., Li F.P.
Cancer Res. 59:5068-5074(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CRC ILE-285; ARG-566; GLY-803 AND THR-1087, VARIANTS GLU-39; ASP-220; VAL-396 AND LEU-800.
[34]"Prevalence of germline mutations of hMLH1, hMSH2, hPMS1, hPMS2, and hMSH6 genes in 75 French kindreds with nonpolyposis colorectal cancer."
Wang Q., Lasset C., Desseigne F., Saurin J.-C., Maugard C., Navarro C., Ruano E., Descos L., Trillet-Lenoir V., Bosset J.-F., Puisieux A.
Hum. Genet. 105:79-85(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC5 GLU-698.
[35]"Frequent microsatellite instability and mismatch repair gene mutations in young Chinese patients with colorectal cancer."
Chan T.L., Yuen S.T., Chung L.P., Ho J.W.C., Kwan K.Y.M., Chan A.S.Y., Ho J.C.Y., Leung S.Y., Wyllie A.H.
J. Natl. Cancer Inst. 91:1221-1226(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CRC MET-1284.
[36]"Do MSH6 mutations contribute to double primary cancers of the colorectum and endometrium?"
Charames G.S., Millar A.L., Pal T., Narod S., Bapat B.
Hum. Genet. 107:623-629(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS COLORECTAL/ENDOMETRIAL CANCER VAL-20; ALA-878 AND HIS-901.
[37]"Sequence analysis of the mismatch repair gene hMSH6 in the germline of patients with familial and sporadic colorectal cancer."
Plaschke J., Kruppa C., Tischler R., Bocker T., Pistorius S., Dralle H., Rueschoff J., Saeger H.D., Fishel R., Schackert H.K.
Int. J. Cancer 85:606-613(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CRC SER-340, VARIANT GLU-39.
[38]"Germline and somatic mutations in hMSH6 and hMSH3 in gastrointestinal cancers of the microsatellite mutator phenotype."
Ohmiya N., Matsumoto S., Yamamoto H., Baranovskaya S., Malkhosyan S.R., Perucho M.
Gene 272:301-313(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CRC ALA-685; GLN-772; ALA-800; MET-854; ALA-878; VAL-1031 AND ARG-1158.
[39]"A role for MLH3 in hereditary nonpolyposis colorectal cancer."
Wu Y., Berends M.J.W., Sijmons R.H., Mensink R.G.J., Verlind E., Kooi K.A., van der Sluis T., Kempinga C., van der Zee A.G.J., Hollema H., Buys C.H.C.M., Kleibeuker J.H., Hofstra R.M.W.
Nat. Genet. 29:137-138(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC5 ALA-878.
[40]"Molecular and clinical characteristics of MSH6 variants: an analysis of 25 index carriers of a germline variant."
Berends M.J.W., Wu Y., Sijmons R.H., Mensink R.G.J., van der Sluis T., Hordijk-Hos J.M., de Vries E.G.E., Hollema H., Karrenbeld A., Buys C.H.C.M., van der Zee A.G.J., Hofstra R.M.W., Kleibeuker J.H.
Am. J. Hum. Genet. 70:26-37(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CRC ILE-144; ARG-522; MET-725; CYS-850; ALA-878; ASP-1021; MET-1100; ILE-1219 AND ASP-1248.
[41]"Involvement of hMSH6 in the development of hereditary and sporadic colorectal cancer revealed by immunostaining is based on germline mutations, but rarely on somatic inactivation."
Plaschke J., Krueger S., Pistorius S., Theissig F., Saeger H.D., Schackert H.K.
Int. J. Cancer 97:643-648(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CRC HIS-976.
[42]"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: VARIANT HNPCC5 VAL-492.
[43]"Two mismatch repair gene mutations found in a colon cancer patient - which one is pathogenic?"
Kariola R., Otway R., Loennqvist K.E., Raevaara T.E., Macrae F., Vos Y.J., Kohonen-Corish M., Hofstra R.M.W., Nystroem-Lahti M.
Hum. Genet. 112:105-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CRC HIS-1095 AND GLN-1354.
[44]"MSH6 germline mutations are rare in colorectal cancer families."
Peterlongo P., Nafa K., Lerman G.S., Glogowski E., Shia J., Ye T.Z., Markowitz A.J., Guillem J.G., Kolachana P., Boyd J.A., Offit K., Ellis N.A.
Int. J. Cancer 107:571-579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CRC ALA-54, VARIANTS GLU-39; ALA-509; MET-854 AND ALA-878.
[45]"MSH6 missense mutations are often associated with no or low cancer susceptibility."
Kariola R., Hampel H., Frankel W.L., Raevaara T.E., de la Chapelle A., Nystroem-Lahti M.
Br. J. Cancer 91:1287-1292(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-128; LEU-623; THR-728 AND LYS-1193, CHARACTERIZATION OF VARIANTS LEU-128; LEU-623; THR-728 AND LYS-1193.
[46]"Eight novel MSH6 germline mutations in patients with familial and nonfamilial colorectal cancer selected by loss of protein expression in tumor tissue."
The German HNPCC consortium
Plaschke J., Krueger S., Dietmaier W., Gebert J., Sutter C., Mangold E., Pagenstecher C., Holinski-Feder E., Schulmann K., Moeslein G., Rueschoff J., Engel C., Evans G., Schackert H.K.
Hum. Mutat. 23:285-285(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HNPCC5 TRP-772.
[47]"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: VARIANT HNPCC5 VAL-1163.
[48]"Mutation analysis of the MLH1, MSH2 and MSH6 genes in patients with double primary cancers of the colorectum and the endometrium: a population-based study in northern Sweden."
Cederquist K., Emanuelsson M., Goeransson I., Holinski-Feder E., Mueller-Koch Y., Golovleva I., Groenberg H.
Int. J. Cancer 109:370-376(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT COLORECTAL/ENDOMETRIAL CANCER PRO-449.
[49]"Lower incidence of colorectal cancer and later age of disease onset in 27 families with pathogenic MSH6 germline mutations compared with families with MLH1 or MSH2 mutations: the German hereditary nonpolyposis colorectal cancer consortium."
Plaschke J., Engel C., Krueger S., Holinski-Feder E., Pagenstecher C., Mangold E., Moeslein G., Schulmann K., Gebert J., von Knebel Doeberitz M., Rueschoff J., Loeffler M., Schackert H.K.
J. Clin. Oncol. 22:4486-4494(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CRC ASN-99; ASP-619; VAL-787; ALA-878 AND CYS-1076.
[50]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-221 AND VAL-492.
[51]"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 THR-13; LEU-65; ILE-144; HIS-468; CYS-503; LEU-580; ALA-878; LEU-1232 AND GLY-1321.
[52]"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 VARIANT HNPCC5 VAL-20, CHARACTERIZATION OF VARIANTS CRC HIS-976 AND ASP-1021, CHARACTERIZATION OF VARIANTS SER-25; VAL-326; VAL-396; VAL-492; CYS-503; ARG-522; ASN-610; CYS-850; ALA-878; TYR-1026; SER-1087 AND MET-1225.
[53]"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 PRO-435; PRO-585; THR-677; ALA-878; HIS-1095 AND GLN-1354.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73737 expand/collapse EMBL AC list , U73732, U73733, U73734, U73736 Genomic DNA. Translation: AAB47425.1.
D89645 Genomic DNA. Translation: BAA23674.1.
D89646 mRNA. Translation: BAA23675.1.
AY082894 Genomic DNA. Translation: AAL87401.1.
BC004246 mRNA. Translation: AAH04246.1.
U54777 mRNA. Translation: AAB39212.2.
U28946 mRNA. Translation: AAC50461.1.
PIRJC5839.
RefSeqNP_000170.1. NM_000179.2.
UniGeneHs.445052.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GFUNMR-A68-201[»]
2O8BX-ray2.75B341-1360[»]
2O8CX-ray3.37B341-1360[»]
2O8DX-ray3.00B341-1360[»]
2O8EX-ray3.30B341-1360[»]
2O8FX-ray3.25B341-1360[»]
ProteinModelPortalP52701.
SMRP52701. Positions 68-201, 362-1335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109211. 56 interactions.
DIPDIP-32972N.
IntActP52701. 18 interactions.
MINTMINT-131993.
STRING9606.ENSP00000234420.

PTM databases

PhosphoSiteP52701.

Polymorphism databases

DMDM68067672.

Proteomic databases

PaxDbP52701.
PeptideAtlasP52701.
PRIDEP52701.

Protocols and materials databases

DNASU2956.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234420; ENSP00000234420; ENSG00000116062. [P52701-1]
GeneID2956.
KEGGhsa:2956.
UCSCuc002rwc.2. human. [P52701-2]
uc002rwd.4. human. [P52701-1]

Organism-specific databases

CTD2956.
GeneCardsGC02P047924.
HGNCHGNC:7329. MSH6.
HPACAB009091.
HPA028376.
HPA028446.
MIM276300. phenotype.
600678. gene.
608089. phenotype.
614350. phenotype.
neXtProtNX_P52701.
Orphanet252202. Constitutional mismatch repair deficiency syndrome.
144. Hereditary nonpolyposis colon cancer.
587. Muir-Torre syndrome.
99817. Non-polyposis Turcot syndrome.
PharmGKBPA184.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0249.
HOGENOMHOG000243127.
HOVERGENHBG000101.
InParanoidP52701.
KOK08737.
OMAHMDAVIG.
OrthoDBEOG7K9K27.
PhylomeDBP52701.
TreeFamTF105842.

Gene expression databases

ArrayExpressP52701.
BgeeP52701.
CleanExHS_MSH6.
GenevestigatorP52701.

Family and domain databases

Gene3D3.40.1170.10. 1 hit.
3.40.50.300. 1 hit.
InterProIPR017261. DNA_mismatch_repair_Msh6.
IPR015536. DNA_mismatch_repair_MSH6_C.
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.
IPR016151. DNA_mismatch_repair_MutS_N.
IPR007860. DNA_mmatch_repair_MutS_con_dom.
IPR027417. P-loop_NTPase.
IPR000313. PWWP_dom.
[Graphical view]
PANTHERPTHR11361:SF31. PTHR11361:SF31. 1 hit.
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.
PF00855. PWWP. 1 hit.
[Graphical view]
PIRSFPIRSF037677. DNA_mis_repair_Msh6. 1 hit.
SMARTSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
SM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF55271. SSF55271. 1 hit.
PROSITEPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
PS50812. PWWP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52701.
GeneWikiMSH6.
GenomeRNAi2956.
NextBio11716.
PMAP-CutDBP52701.
PROP52701.
SOURCESearch...

Entry information

Entry nameMSH6_HUMAN
AccessionPrimary (citable) accession number: P52701
Secondary accession number(s): O43706 expand/collapse secondary AC list , O43917, Q8TCX4, Q9BTB5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 21, 2005
Last modified: April 16, 2014
This is version 170 of the entry and version 2 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