Reviewed, UniProtKB/Swiss-Prot P52701 (MSH6_HUMAN)

Names and origin

Protein names

Recommended name:
    DNA mismatch repair protein Msh6
Alternative name(s):
    MutS-alpha 160 kDa subunit
    G/T mismatch-binding protein
      Short name=GTMBP
      Short name=GTBP
    p160

Gene names

Name:	MSH6
Synonyms:	GTBP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14
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.
Post-translational modification	The N-terminus is blocked. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.15 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Phosphorylated by PRKCZ, which may prevent MutS alpha degradation by the ubiquitin-proteasome pathway. Ref.15 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26
Involvement in disease	Defects in MSH6 are the cause of hereditary non-polyposis colorectal cancer type 5 (HNPCC5) [MIM:600678]. Mutations in more than one gene locus can be involved alone or in combination in the production of the HNPCC phenotype (also called Lynch syndrome). Most families with clinically recognized HNPCC have mutations in either MLH1 or MSH2 genes. HNPCC is an autosomal, dominantly inherited disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early onset colorectal carcinoma (CRC) and extra-colonic cancers of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Cancers in HNPCC originate within benign neoplastic polyps termed adenomas. Clinically, HNPCC is often divided into two subgroups. Type I: hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II: patients have an increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. MSH6 mutations appear to be associated with atypical HNPCC and in particular with development of endometrial carcinoma or atypical endometrial hyperplasia, the presumed precursor of endometrial cancer. Defects in MSH6 are also found in familial colorectal cancers (suspected or incomplete HNPCC) that do not fulfill the Amsterdam criteria for HNPCC. Ref.17 Ref.30 Ref.32 Ref.37 Ref.40 Ref.44 Ref.45 Defects in MSH6 are a cause of susceptibility to endometrial cancer [MIM:608089]. Ref.17
Sequence similarities	Belongs to the DNA mismatch repair mutS family. Contains 1 PWWP domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hereditary nonpolyposis colorectal cancer
Ligand	ATP-binding DNA-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction resulting in induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB determination of adult life span Inferred from sequence or structural similarity. Source: UniProtKB isotype switching Inferred from sequence or structural similarity. Source: UniProtKB meiotic mismatch repair Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of DNA recombination Inferred from direct assay. Source: UniProtKB positive regulation of helicase activity Inferred from direct assay. Source: UniProtKB response to UV Inferred from sequence or structural similarity. Source: UniProtKB somatic hypermutation of immunoglobulin genes Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	MutSalpha complex Ref.1 Inferred from direct assay. Source: HGNC
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.1 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASP4	P49662	1	EBI-395529,EBI-1057327
MSH2	P43246	1	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1360

1360

DNA mismatch repair protein Msh6

PRO_0000115207

Regions

Domain

92 – 154

63

PWWP

Nucleotide binding

1134 – 1141

8

ATP Potential

Compositional bias

34 – 37

4

Poly-Ala

Compositional bias

201 – 209

9

Poly-Glu

Compositional bias

1118 – 1123

6

Poly-Glu

Amino acid modifications

Modified residue

14

1

Phosphoserine Ref.20 Ref.26

Modified residue

41

1

Phosphoserine Ref.20

Modified residue

43

1

Phosphoserine Ref.20

Modified residue

79

1

Phosphoserine Ref.26

Modified residue

91

1

Phosphoserine Ref.26

Modified residue

137

1

Phosphoserine Ref.19 Ref.21 Ref.24 Ref.25 Ref.26

Modified residue

139

1

Phosphothreonine Ref.22

Modified residue

200

1

Phosphoserine Ref.26

Modified residue

219

1

Phosphoserine Ref.19 Ref.26

Modified residue

227

1

Phosphoserine Ref.18 Ref.19 Ref.26

Modified residue

252

1

Phosphoserine Ref.18 Ref.19 Ref.20 Ref.25 Ref.26

Modified residue

254

1

Phosphoserine Ref.18 Ref.19 Ref.25 Ref.26

Modified residue

256

1

Phosphoserine Ref.18 Ref.19 Ref.20 Ref.25 Ref.26

Modified residue

261

1

Phosphoserine Ref.18 Ref.19 Ref.25 Ref.26

Modified residue

309

1

Phosphoserine Ref.25

Modified residue

348

1

Phosphoserine Ref.23

Modified residue

830

1

Phosphoserine Ref.18 Ref.25

Modified residue

924

1

Phosphothreonine Ref.19

Natural variations

Alternative sequence

1058 – 1068

11

DVLLCLANYSR → GKTLNKLVLRL in isoform GTBP-alt.

VSP_003291

Alternative sequence

1069 – 1360

292

Missing in isoform GTBP-alt.

VSP_003292

Natural variant

13

1

K → T: dbSNP rs41294988. Ref.49

VAR_038032

Natural variant

20

1

A → V in colorectal/endometrial cancer. Ref.34

VAR_043943

Natural variant

25

1

A → V: dbSNP rs35462442.

VAR_038033

Natural variant

39

1

G → E: dbSNP rs1042821. Ref.1 Ref.31 Ref.35 Ref.42

VAR_004490

Natural variant

54

1

G → A in CRC; uncertain pathogenicity. Ref.42

VAR_043944

Natural variant

65

1

S → L: dbSNP rs41294984. Ref.49

VAR_038034

Natural variant

99

1

K → N in CRC; uncertain pathogenicity. Ref.47

VAR_043945

Natural variant

128

1

R → L No impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. Ref.43

VAR_043946

Natural variant

144

1

S → I in suspected HNPCC5 and CRC. dbSNP rs3211299. Ref.30 Ref.49 Ref.38

VAR_012955

Natural variant

220

1

E → D: dbSNP rs1800938. Ref.31

VAR_012956

Natural variant

221

1

E → D: dbSNP rs41557217. Ref.48

VAR_042274

Natural variant

285

1

S → I in CRC. Ref.31

VAR_012957

Natural variant

295

1

K → R in multiple colorectal adenoma.

VAR_043947

Natural variant

340

1

F → S in CRC, breast cancer and leukemia.

VAR_043948

Natural variant

396

1

L → V Rare polymorphism. dbSNP rs2020908. Ref.31

VAR_012958

Natural variant

449

1

L → P in colorectal/endometrial cancer; uncertain pathogenicity. Ref.46

VAR_043949

Natural variant

468

1

R → H: dbSNP rs41295268. Ref.49

VAR_038035

Natural variant

492

1

M → V in HNPCC5. Ref.40

VAR_042275

Natural variant

503

1

S → C Ref.49

VAR_038036

Natural variant

509

1

V → A Ref.42

VAR_043950

Natural variant

522

1

Q → R in CRC; uncertain pathogenicity. Ref.38

VAR_043951

Natural variant

538

1

Y → S: dbSNP rs728619.

VAR_038037

Natural variant

566

1

G → R in CRC; partial functional loss. Ref.31

VAR_012959

Natural variant

580

1

S → L: dbSNP rs41295270. Ref.49

VAR_038038

Natural variant

619

1

E → D in CRC; uncertain pathogenicity. Ref.47

VAR_043952

Natural variant

623

1

P → A: dbSNP rs3136334. Ref.43

VAR_029244

Natural variant

623

1

P → L No impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. Ref.43

VAR_043953

Natural variant

685

1

G → A in CRC. Ref.36

VAR_043954

Natural variant

698

1

Q → E in suspected HNPCC; could be a polymorphism. Ref.32

VAR_012960

Natural variant

725

1

I → M in CRC; uncertain pathogenicity. Ref.38

VAR_043955

Natural variant

728

1

K → T No impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. dbSNP rs35552856. Ref.43

VAR_043956

Natural variant

772

1

R → Q in CRC. Ref.36

VAR_043957

Natural variant

772

1

R → W in HNPCC5. Ref.44

VAR_043958

Natural variant

787

1

A → V in CRC; uncertain pathogenicity. Ref.47

VAR_043959

Natural variant

800

1

V → A in CRC; somatic mutation. Ref.36

VAR_043960

Natural variant

800

1

V → L May be a rare polymorphism. Ref.31 Ref.36

VAR_012961

Natural variant

803

1

D → G in CRC. Ref.31

VAR_012962

Natural variant

850

1

Y → C in suspected HNPCC5 and CRC. Ref.30 Ref.38

VAR_012963

Natural variant

854

1

K → M in CRC; could be a polymorphism. dbSNP rs34374438. Ref.36

VAR_043961

Natural variant

878

1

V → A in suspected HNPCC5, colorectal/endometrial cancer and CRC. dbSNP rs2020912. Ref.37 Ref.49 Ref.34 Ref.42 Ref.47 Ref.38 Ref.36

VAR_012964

Natural variant

886

1

I → V: dbSNP rs2020914.

VAR_014902

Natural variant

901

1

R → H in colorectal/endometrial cancer. Ref.34

VAR_043962

Natural variant

976

1

R → H in CRC; sporadic. Ref.39

VAR_012965

Natural variant

1021

1

A → D in CRC; uncertain pathogenicity. Ref.38

VAR_043963

Natural variant

1031

1

D → V in CRC; somatic mutation. Ref.36

VAR_043964

Natural variant

1076

1

R → C in CRC; uncertain pathogenicity. Ref.47

VAR_043965

Natural variant

1087

1

P → T in CRC. Ref.31

VAR_012966

Natural variant

1095

1

R → H in CRC; uncertain pathogenicity. Ref.41

VAR_043966

Natural variant

1100

1

T → M in CRC; uncertain pathogenicity. Ref.38

VAR_043967

Natural variant

1158

1

C → R in CRC; somatic mutation. Ref.36

VAR_043968

Natural variant

1163

1

E → V in HNPCC5. Ref.45

VAR_043969

Natural variant

1193

1

E → K in endometrial cancer; display marked impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. Ref.43

VAR_043970

Natural variant

1213

1

D → V Ref.29

VAR_004491

Natural variant

1219

1

T → I in CRC; uncertain pathogenicity. Ref.38

VAR_043971

Natural variant

1232

1

V → L: dbSNP rs41295276. Ref.49

VAR_038039

Natural variant

1234

1

E → Q: dbSNP rs35717727.

VAR_038040

Natural variant

1248

1

H → D in CRC; uncertain pathogenicity. Ref.38

VAR_043972

Natural variant

1260

1

V → I Ref.29

VAR_004492

Natural variant

1284

1

T → M in CRC. Ref.33

VAR_043973

Natural variant

1321

1

R → G: dbSNP rs41295278. Ref.49

VAR_038041

Natural variant

1354

1

L → Q in CRC; uncertain pathogenicity. Ref.41

VAR_043974

Experimental info

Mutagenesis

1140

1

K → R: No effect on mismatch binding, complete loss of DNA repair function when associated with MSH2 mutant R-675. Ref.10

Sequence conflict

36 – 57

22

AAPGA…AGPGP → GCPRGLSFPRRGCGLERGWA WA in BAA23674. Ref.2

Sequence conflict

36 – 57

22

AAPGA…AGPGP → GCPRGLSFPRRGCGLERGWA WA in BAA23675. Ref.2

Sequence conflict

1358 – 1360

3

KEL → D in AAL87401. Ref.3

Secondary structure

1

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1360

Helix Strand Turn

Details...

Beta strand

74 – 79

6

Beta strand

94 – 98

5

Beta strand

106 – 109

4

Beta strand

120 – 125

6

Beta strand

127 – 133

7

Beta strand

135 – 137

3

Beta strand

139 – 143

5

Helix

145 – 147

3

Beta strand

148 – 151

4

Turn

157 – 159

3

Helix

170 – 183

14

Helix

187 – 191

5

Turn

192 – 195

4

Beta strand

197 – 199

3

Helix

366 – 369

4

Helix

371 – 373

3

Turn

375 – 377

3

Helix

400 – 403

4

Helix

408 – 419

12

Beta strand

423 – 429

7

Beta strand

432 – 436

5

Helix

437 – 447

11

Beta strand

453 – 456

4

Beta strand

458 – 462

5

Helix

463 – 465

3

Helix

466 – 475

10

Beta strand

480 – 485

6

Helix

489 – 497

9

Helix

505 – 507

3

Beta strand

511 – 517

7

Beta strand

538 – 546

9

Beta strand

554 – 561

8

Turn

563 – 565

3

Beta strand

568 – 575

8

Helix

580 – 588

9

Beta strand

591 – 597

7

Turn

598 – 600

3

Helix

603 – 609

7

Turn

610 – 615

6

Beta strand

616 – 621

6

Turn

624 – 626

3

Helix

630 – 639

10

Turn

640 – 643

4

Beta strand

644 – 647

4

Helix

657 – 661

5

Beta strand

671 – 673

3

Helix

675 – 677

3

Helix

678 – 693

16

Helix

697 – 701

5

Beta strand

706 – 708

3

Helix

712 – 715

4

Helix

737 – 742

6

Beta strand

750 – 753

4

Helix

758 – 762

5

Helix

768 – 779

12

Helix

785 – 799

15

Helix

802 – 812

11

Helix

818 – 829

12

Helix

831 – 836

6

Helix

838 – 841

4

Helix

847 – 879

33

Helix

885 – 890

6

Turn

894 – 896

3

Beta strand

897 – 900

4

Helix

906 – 913

8

Helix

918 – 923

6

Helix

936 – 955

20

Helix

959 – 961

3

Beta strand

968 – 970

3

Helix

973 – 975

3

Beta strand

978 – 981

4

Turn

983 – 986

4

Beta strand

995 – 999

5

Beta strand

1002 – 1005

4

Turn

1008 – 1010

3

Helix

1011 – 1041

31

Helix

1044 – 1066

23

Beta strand

1070 – 1072

3

Turn

1082 – 1084

3

Beta strand

1089 – 1094

6

Beta strand

1111 – 1116

6

Beta strand

1129 – 1133

5

Helix

1140 – 1154

15

Turn

1155 – 1157

3

Beta strand

1160 – 1167

8

Beta strand

1171 – 1176

6

Helix

1189 – 1203

15

Beta strand

1209 – 1213

5

Turn

1215 – 1218

4

Helix

1221 – 1237

17

Beta strand

1242 – 1246

5

Helix

1250 – 1255

6

Beta strand

1260 – 1269

10

Beta strand

1285 – 1292

8

Helix

1298 – 1305

8

Helix

1310 – 1322

13

Turn

1330 – 1332

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform GTBP-N [UniParc]. Last modified June 21, 2005. Version 2. Checksum: 4A4AA9F8ECB8FFE9	FASTA	1,360	152,786
	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
	Isoform GTBP-alt. Checksum: E1E62571A314B51E	FASTA	1,068	120,563
	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 AEERRDVSLK DCMRRLFYNF DKNYKDWQSA VECIAVLGKT LNKLVLRL

References

	« Hide 'large scale' referencesShow '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: 8942985] [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: 9455487] [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: 15489334] [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: 7604265] [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: 8838326] [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: 7604264] [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: 9822680] [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: 9822679] [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: 9564049] [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: 9889267] [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: 10078208] [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: 10660545] [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: 15064730] [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: 15808853] [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: 10783165] [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: 9354786] [Abstract] Cited for: DISEASE.
[18]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-252; SER-254; SER-256; SER-261 AND SER-830, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-219; SER-227; SER-252; SER-254; SER-256; SER-261 AND THR-924, MASS SPECTROMETRY. Tissue: Epithelium.
[20]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-41; SER-43; SER-252 AND SER-256, MASS SPECTROMETRY. Tissue: Epithelium.
[21]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, MASS SPECTROMETRY. Tissue: Epithelium.
[22]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, MASS SPECTROMETRY. Tissue: Epithelium.
[23]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, MASS SPECTROMETRY.
[24]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, MASS SPECTROMETRY.
[25]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-252; SER-254; SER-256; SER-261; SER-309 AND SER-830, MASS SPECTROMETRY.
[26]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-79; SER-91; SER-137; SER-200; SER-219; SER-227; SER-252; SER-254; SER-256 AND SER-261, MASS SPECTROMETRY.
[27]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[28]	"Structure of the human MutSalpha DNA lesion recognition complex." Warren J.J., Pohlhaus T.J., Changela A., Iyer R.R., Modrich P.L., Beese L.S. Mol. Cell 26:579-592(2007) [PubMed: 17531815] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
[29]	"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: 7604266] [Abstract] Cited for: VARIANTS VAL-1213 AND ILE-1260.
[30]	"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: 10521294] [Abstract] Cited for: VARIANTS HNPCC5 ILE-144 AND CYS-850.
[31]	"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: 10537275] [Abstract] Cited for: VARIANTS CRC ILE-285; ARG-566; GLY-803 AND THR-1087, VARIANTS GLU-39; ASP-220; VAL-396 AND LEU-800.
[32]	"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: 10480359] [Abstract] Cited for: VARIANT HNPCC5 GLU-698.
[33]	"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: 10413423] [Abstract] Cited for: VARIANT CRC MET-1284.
[34]	"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: 11153917] [Abstract] Cited for: VARIANTS COLORECTAL/ENDOMETRIAL CANCER VAL-20; ALA-878 AND HIS-901.
[35]	"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: 10699937] [Abstract] Cited for: VARIANT CRC SER-340, VARIANT GLU-39.
[36]	"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: 11470537] [Abstract] Cited for: VARIANTS CRC ALA-685; GLN-772; ALA-800; MET-854; ALA-878; VAL-1031 AND ARG-1158.
[37]	"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: 11586295] [Abstract] Cited for: VARIANT HNPCC5 ALA-878.
[38]	"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: 11709755] [Abstract] Cited for: VARIANTS CRC ILE-144; ARG-522; MET-725; CYS-850; ALA-878; ASP-1021; MET-1100; ILE-1219 AND ASP-1248.
[39]	"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: 11807791] [Abstract] Cited for: VARIANT CRC HIS-976.
[40]	"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. , Lynch J.F., de la Chapelle A., Lynch H.T., Fodde R. Am. J. Hum. Genet. 72:1088-1100(2003) [PubMed: 12658575] [Abstract] Cited for: VARIANT HNPCC5 VAL-492.
[41]	"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: 12522549] [Abstract] Cited for: VARIANTS CRC HIS-1095 AND GLN-1354.
[42]	"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: 14520694] [Abstract] Cited for: VARIANT CRC ALA-54, VARIANTS GLU-39; ALA-509; MET-854 AND ALA-878.
[43]	"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: 15354210] [Abstract] Cited for: VARIANT ENDOMETRIAL CANCER LYS-1193, VARIANTS LEU-128; LEU-623 AND THR-728, CHARACTERIZATION OF VARIANT ENDOMETRIAL CANCER LYS-1193, CHARACTERIZATION OF VARIANTS LEU-128; LEU-623 AND THR-728.
[44]	"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: 14974087] [Abstract] Cited for: VARIANT HNPCC5 TRP-772.
[45]	"Germline mutations in MLH1, MSH2 and MSH6 in Korean hereditary non-polyposis colorectal cancer families." Shin Y.-K., Heo S.-C., Shin J.-H., Hong S.-H., Ku J.-L., Yoo B.-C., Kim I.-J., Park J.-G. Hum. Mutat. 24:351-351(2004) [PubMed: 15365995] [Abstract] Cited for: VARIANT HNPCC5 VAL-1163.
[46]	"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: 14961575] [Abstract] Cited for: VARIANT COLORECTAL/ENDOMETRIAL CANCER PRO-449.
[47]	"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: 15483016] [Abstract] Cited for: VARIANTS CRC ASN-99; ASP-619; VAL-787; ALA-878 AND CYS-1076.
[48]	"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. , 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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-221 AND VAL-492.
[49]	"Classification of ambiguous mutations in DNA mismatch repair genes identified in a population-based study of colorectal cancer." Barnetson R.A., Cartwright N., van Vliet A., Haq N., Drew K., Farrington S., Williams N., Warner J., Campbell H., Porteous M.E., Dunlop M.G. Hum. Mutat. 29:367-374(2008) [PubMed: 18033691] [Abstract] Cited for: VARIANTS THR-13; LEU-65; ILE-144; HIS-468; CYS-503; LEU-580; ALA-878; LEU-1232 AND GLY-1321.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Hereditary non-polyposis colorectal cancer db

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

U73737 , 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.

IPI

IPI00106847.
IPI00384456.

PIR

JC5839.

RefSeq

NP_000170.1.

UniGene

Hs.352677
Hs.445052

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GFU	NMR	-	A	68-201	[»]
2O8B	X-ray	2.75	B	341-1360	[»]
2O8C	X-ray	3.37	B	341-1360	[»]
2O8D	X-ray	3.00	B	341-1360	[»]
2O8E	X-ray	3.30	B	341-1360	[»]
2O8F	X-ray	3.25	B	341-1360	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P52701. 8 interactions.

PTM databases

PhosphoSite

P52701.

Proteomic databases

PeptideAtlas

P52701.

PRIDE

P52701.

Genome annotation databases

Ensembl

ENSG00000116062. Homo sapiens. [Contig view]

GeneID

2956.

KEGG

hsa:2956.

Organism-specific databases

GeneCards

GC02P047921.

H-InvDB

HIX0002043.

HGNC

HGNC:7329. MSH6.

HPA

CAB009091.

MIM

600678. gene+phenotype.
608089. phenotype.

Orphanet

144. Colon cancer, familial nonpolyposis.

PharmGKB

PA184.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P52701.

HOVERGEN

P52701.

OMA

P52701. QTYSVLD.

Gene expression databases

ArrayExpress

P52701.

Bgee

P52701.

CleanEx

HS_MSH6.

GermOnline

ENSG00000116062. Homo sapiens.

Family and domain databases

InterPro

IPR017261. 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.
IPR007860. DNA_mismatch_repair_MutS_connt.
IPR007696. DNA_mismatch_repair_MutS_core.
IPR016151. DNA_mismatch_repair_MutS_N.
IPR000313. PWWP.
[Graphical view]

Gene3D

G3DSA:3.40.1170.10. DNA_mismatch_repair_MutS_N. 1 hit.

PANTHER

PTHR11361. MutS_C. 1 hit.
PTHR11361:SF31. MutS_Hmlg_MSH6. 1 hit.

Pfam

PF01624. MutS_I. 1 hit.
PF05188. MutS_II. 1 hit.
PF05192. MutS_III. 1 hit.
PF05190. MutS_IV. 1 hit.
PF00488. MutS_V. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]

PIRSF

PIRSF037677. DNA_mis_repair_Msh6. 1 hit.

ProDom

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

SMART

SM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
SM00293. PWWP. 1 hit.
[Graphical view]

PROSITE

PS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
PS50812. PWWP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

11716.

PMAP-CutDB

P52701.

SOURCE

Search...

Entry information

Entry name

MSH6_HUMAN

Accession

Primary (citable) accession number: P52701
Secondary accession number(s): O43706 , O43917, Q8TCX4, Q9BTB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	June 21, 2005
Last modified:	June 16, 2009
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)