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P52701

- MSH6_HUMAN

UniProt

P52701 - MSH6_HUMAN

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Protein

DNA mismatch repair protein Msh6

Gene
MSH6, GTBP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.7 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1134 – 11418ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. chromatin binding Source: Ensembl
  3. damaged DNA binding Source: Ensembl
  4. DNA-dependent ATPase activity Source: RefGenome
  5. guanine/thymine mispair binding Source: Ensembl
  6. methylated histone binding Source: UniProtKB
  7. mismatched DNA binding Source: InterPro
  8. protein binding Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. determination of adult lifespan Source: BHF-UCL
  3. DNA repair Source: BHF-UCL
  4. intrinsic apoptotic signaling pathway Source: BHF-UCL
  5. intrinsic apoptotic signaling pathway in response to DNA damage Source: BHF-UCL
  6. isotype switching Source: BHF-UCL
  7. meiotic mismatch repair Source: BHF-UCL
  8. mismatch repair Source: InterPro
  9. negative regulation of DNA recombination Source: BHF-UCL
  10. positive regulation of helicase activity Source: BHF-UCL
  11. reciprocal meiotic recombination Source: RefGenome
  12. response to UV Source: BHF-UCL
  13. somatic hypermutation of immunoglobulin genes Source: BHF-UCL
  14. somatic recombination of immunoglobulin gene segments Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MSH6
Synonyms:GTBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:7329. MSH6.

Subcellular locationi

Nucleus. Chromosome
Note: Associates with H3K36me3 via its PWWP domain.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. Golgi apparatus Source: HPA
  3. intracellular membrane-bounded organelle Source: HPA
  4. MutSalpha complex Source: UniProtKB
  5. nuclear chromatin Source: Ensembl
  6. nuclear chromosome Source: RefGenome
  7. nucleus Source: HPA
  8. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.8 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201A → V in colorectal/endometrial cancer and HNPCC5; repair proficient. 2 Publications
Corresponds to variant rs63750664 [ dbSNP | Ensembl ].
VAR_043943
Natural varianti25 – 251A → S Associated with HNPCC5; unknown pathologiacl significance; repair proficient. 1 Publication
VAR_067294
Natural varianti144 – 1441S → I in suspected HNPCC5 and CRC. 3 Publications
Corresponds to variant rs3211299 [ dbSNP | Ensembl ].
VAR_012955
Natural varianti326 – 3261A → V Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
VAR_067295
Natural varianti396 – 3961L → V Associated with HNPCC5; unknown pathological significance; repair proficient. 3 Publications
Corresponds to variant rs2020908 [ dbSNP | Ensembl ].
VAR_012958
Natural varianti492 – 4921M → V Associated with HNPCC5; unknown pathological significance; repair proficient. 3 Publications
VAR_042275
Natural varianti503 – 5031S → C Associated with HNPCC5; unknown pathological significance; repair proficient. 2 Publications
VAR_038036
Natural varianti522 – 5221Q → R in CRC; also associated with HNPCC5; repair proficient. 2 Publications
VAR_043951
Natural varianti610 – 6101K → N Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
VAR_067296
Natural varianti772 – 7721R → W in HNPCC5. 1 Publication
VAR_043958
Natural varianti850 – 8501Y → C Associated with HNPCC5 and CRC; unknown pathological significance; repair proficient. 3 Publications
VAR_012963
Natural varianti878 – 8781V → A in suspected HNPCC5, colorectal/endometrial cancer and CRC; repair proficient. 9 Publications
Corresponds to variant rs2020912 [ dbSNP | Ensembl ].
VAR_012964
Natural varianti976 – 9761R → H in CRC; sporadic; also associated with HNPCC5; repair proficient. 2 Publications
VAR_012965
Natural varianti1026 – 10261D → Y Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
VAR_067297
Natural varianti1087 – 10871P → S Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
Corresponds to variant rs63750998 [ dbSNP | Ensembl ].
VAR_067298
Natural varianti1163 – 11631E → V in HNPCC5. 1 Publication
Corresponds to variant rs63750252 [ dbSNP | Ensembl ].
VAR_043969
Natural varianti1225 – 12251T → M Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
VAR_067299
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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031Y → A: Abolishes binding to H3K36me3 and DNA mismatch repair activity. 1 Publication
Mutagenesisi105 – 1062WW → AA: Abolishes binding to H3K36me3 and DNA mismatch repair activity.
Mutagenesisi1140 – 11401K → R: No effect on mismatch binding, complete loss of DNA repair function when associated with MSH2 mutant R-675. 1 Publication

Keywords - Diseasei

Disease mutation, Hereditary nonpolyposis colorectal cancer

Organism-specific databases

MIMi276300. phenotype.
608089. phenotype.
614350. phenotype.
Orphaneti252202. Constitutional mismatch repair deficiency syndrome.
144. Hereditary nonpolyposis colon cancer.
587. Muir-Torre syndrome.
99817. Non-polyposis Turcot syndrome.
PharmGKBiPA184.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13601360DNA mismatch repair protein Msh6PRO_0000115207Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine4 Publications
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei43 – 431Phosphoserine1 Publication
Modified residuei70 – 701N6-acetyllysine1 Publication
Modified residuei79 – 791Phosphoserine1 Publication
Modified residuei91 – 911Phosphoserine1 Publication
Modified residuei137 – 1371Phosphoserine3 Publications
Modified residuei200 – 2001Phosphoserine1 Publication
Modified residuei219 – 2191Phosphoserine2 Publications
Modified residuei227 – 2271Phosphoserine4 Publications
Modified residuei252 – 2521Phosphoserine2 Publications
Modified residuei254 – 2541Phosphoserine1 Publication
Modified residuei256 – 2561Phosphoserine1 Publication
Modified residuei261 – 2611Phosphoserine3 Publications
Modified residuei269 – 2691Phosphothreonine1 Publication
Modified residuei274 – 2741Phosphoserine1 Publication
Modified residuei275 – 2751Phosphoserine1 Publication
Modified residuei279 – 2791Phosphoserine1 Publication
Modified residuei280 – 2801Phosphoserine1 Publication
Modified residuei309 – 3091Phosphoserine2 Publications
Modified residuei504 – 5041N6-acetyllysine1 Publication
Modified residuei830 – 8301Phosphoserine1 Publication

Post-translational modificationi

The N-terminus is blocked.
Phosphorylated by PRKCZ, which may prevent MutS alpha degradation by the ubiquitin-proteasome pathway.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52701.
PaxDbiP52701.
PeptideAtlasiP52701.
PRIDEiP52701.

PTM databases

PhosphoSiteiP52701.

Miscellaneous databases

PMAP-CutDBP52701.

Expressioni

Gene expression databases

ArrayExpressiP52701.
BgeeiP52701.
CleanExiHS_MSH6.
GenevestigatoriP52701.

Organism-specific databases

HPAiCAB009091.
HPA028376.
HPA028446.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
MSH2P432464EBI-395529,EBI-355888

Protein-protein interaction databases

BioGridi109211. 57 interactions.
DIPiDIP-32972N.
IntActiP52701. 18 interactions.
MINTiMINT-131993.
STRINGi9606.ENSP00000234420.

Structurei

Secondary structure

1
1360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi74 – 796
Beta strandi94 – 985
Beta strandi106 – 1094
Beta strandi120 – 1256
Beta strandi127 – 1337
Beta strandi135 – 1373
Beta strandi139 – 1435
Helixi145 – 1473
Beta strandi148 – 1514
Turni157 – 1593
Helixi170 – 18314
Helixi187 – 1915
Turni192 – 1954
Beta strandi197 – 1993
Helixi366 – 3694
Helixi371 – 3733
Turni375 – 3773
Helixi400 – 4034
Helixi408 – 41912
Beta strandi423 – 4297
Beta strandi432 – 4365
Helixi437 – 44711
Beta strandi453 – 4564
Beta strandi458 – 4625
Helixi463 – 4653
Helixi466 – 47510
Beta strandi480 – 4856
Helixi489 – 4979
Helixi505 – 5073
Beta strandi511 – 5177
Helixi519 – 5213
Beta strandi526 – 5283
Beta strandi538 – 5469
Beta strandi554 – 5618
Turni563 – 5653
Beta strandi568 – 5758
Helixi580 – 5889
Beta strandi591 – 5977
Turni598 – 6003
Helixi603 – 6097
Turni610 – 6156
Beta strandi616 – 6216
Turni624 – 6263
Helixi630 – 63910
Turni640 – 6434
Beta strandi644 – 6474
Helixi657 – 6615
Beta strandi667 – 6693
Beta strandi671 – 6733
Helixi675 – 6773
Helixi678 – 69316
Helixi697 – 7015
Beta strandi706 – 7083
Helixi712 – 7154
Helixi737 – 7426
Beta strandi746 – 7483
Beta strandi750 – 7534
Helixi758 – 7625
Helixi768 – 77912
Helixi785 – 79915
Helixi802 – 81211
Helixi818 – 82912
Helixi831 – 8366
Helixi838 – 8414
Helixi847 – 87933
Helixi885 – 8906
Turni894 – 8963
Beta strandi897 – 9004
Helixi906 – 9138
Helixi918 – 9236
Helixi936 – 95520
Helixi959 – 9613
Beta strandi968 – 9703
Helixi973 – 9753
Beta strandi978 – 9814
Turni983 – 9864
Beta strandi995 – 9995
Beta strandi1002 – 10054
Turni1008 – 10103
Helixi1011 – 104131
Helixi1044 – 106623
Beta strandi1070 – 10723
Turni1082 – 10843
Beta strandi1089 – 10946
Beta strandi1111 – 11166
Beta strandi1120 – 11223
Beta strandi1129 – 11335
Beta strandi1136 – 11383
Helixi1140 – 115415
Turni1155 – 11573
Beta strandi1160 – 11678
Beta strandi1171 – 11766
Helixi1189 – 120315
Beta strandi1209 – 12135
Turni1215 – 12184
Helixi1221 – 123717
Beta strandi1242 – 12465
Helixi1250 – 12556
Turni1256 – 12583
Beta strandi1260 – 126910
Beta strandi1285 – 12928
Helixi1298 – 13058
Helixi1310 – 132213
Turni1323 – 13264
Turni1330 – 13323

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP52701.
SMRiP52701. Positions 68-201, 362-1335.

Miscellaneous databases

EvolutionaryTraceiP52701.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 15463PWWPAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi34 – 374Poly-Ala
Compositional biasi201 – 2099Poly-Glu
Compositional biasi1118 – 11236Poly-Glu

Domaini

The PWWP domain specifically recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3) (1 Publication).

Sequence similaritiesi

Contains 1 PWWP domain.

Phylogenomic databases

eggNOGiCOG0249.
HOGENOMiHOG000243127.
HOVERGENiHBG000101.
InParanoidiP52701.
KOiK08737.
OMAiALKDCMR.
OrthoDBiEOG7K9K27.
PhylomeDBiP52701.
TreeFamiTF105842.

Family and domain databases

Gene3Di3.40.1170.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR017261. 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]
PANTHERiPTHR11361:SF31. PTHR11361:SF31. 1 hit.
PfamiPF01624. 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]
PIRSFiPIRSF037677. DNA_mis_repair_Msh6. 1 hit.
SMARTiSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
SM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMiSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF55271. SSF55271. 1 hit.
PROSITEiPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
PS50812. PWWP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform GTBP-N (identifier: P52701-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSRQSTLYSF FPKSPALSDA NKASARASRE GGRAAAAPGA SPSPGGDAAW     50
SEAGPGPRPL ARSASPPKAK NLNGGLRRSV APAAPTSCDF SPGDLVWAKM 100
EGYPWWPCLV YNHPFDGTFI REKGKSVRVH VQFFDDSPTR GWVSKRLLKP 150
YTGSKSKEAQ KGGHFYSAKP EILRAMQRAD EALNKDKIKR LELAVCDEPS 200
EPEEEEEMEV GTTYVTDKSE EDNEIESEEE VQPKTQGSRR SSRQIKKRRV 250
ISDSESDIGG SDVEFKPDTK EEGSSDEISS GVGDSESEGL NSPVKVARKR 300
KRMVTGNGSL KRKSSRKETP SATKQATSIS SETKNTLRAF SAPQNSESQA 350
HVSGGGDDSS RPTVWYHETL EWLKEEKRRD EHRRRPDHPD FDASTLYVPE 400
DFLNSCTPGM RKWWQIKSQN FDLVICYKVG KFYELYHMDA LIGVSELGLV 450
FMKGNWAHSG FPEIAFGRYS DSLVQKGYKV ARVEQTETPE MMEARCRKMA 500
HISKYDRVVR REICRIITKG TQTYSVLEGD PSENYSKYLL SLKEKEEDSS 550
GHTRAYGVCF VDTSLGKFFI GQFSDDRHCS RFRTLVAHYP PVQVLFEKGN 600
LSKETKTILK SSLSCSLQEG LIPGSQFWDA SKTLRTLLEE EYFREKLSDG 650
IGVMLPQVLK GMTSESDSIG LTPGEKSELA LSALGGCVFY LKKCLIDQEL 700
LSMANFEEYI PLDSDTVSTT RSGAIFTKAY QRMVLDAVTL NNLEIFLNGT 750
NGSTEGTLLE RVDTCHTPFG KRLLKQWLCA PLCNHYAIND RLDAIEDLMV 800
VPDKISEVVE LLKKLPDLER LLSKIHNVGS PLKSQNHPDS RAIMYEETTY 850
SKKKIIDFLS ALEGFKVMCK IIGIMEEVAD GFKSKILKQV ISLQTKNPEG 900
RFPDLTVELN RWDTAFDHEK ARKTGLITPK AGFDSDYDQA LADIRENEQS 950
LLEYLEKQRN RIGCRTIVYW GIGRNRYQLE IPENFTTRNL PEEYELKSTK 1000
KGCKRYWTKT IEKKLANLIN AEERRDVSLK DCMRRLFYNF DKNYKDWQSA 1050
VECIAVLDVL LCLANYSRGG DGPMCRPVIL LPEDTPPFLE LKGSRHPCIT 1100
KTFFGDDFIP NDILIGCEEE EQENGKAYCV LVTGPNMGGK STLMRQAGLL 1150
AVMAQMGCYV PAEVCRLTPI DRVFTRLGAS DRIMSGESTF FVELSETASI 1200
LMHATAHSLV LVDELGRGTA TFDGTAIANA VVKELAETIK CRTLFSTHYH 1250
SLVEDYSQNV AVRLGHMACM VENECEDPSQ ETITFLYKFI KGACPKSYGF 1300
NAARLANLPE EVIQKGHRKA REFEKMNQSL RLFREVCLAS ERSTVDAEAV 1350
HKLLTLIKEL 1360
Length:1,360
Mass (Da):152,786
Last modified:June 21, 2005 - v2
Checksum:i4A4AA9F8ECB8FFE9
GO
Isoform GTBP-alt (identifier: P52701-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,068
Mass (Da):120,563
Checksum:iE1E62571A314B51E
GO
Isoform 3 (identifier: P52701-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     80-209: Missing.

Note: No experimental confirmation available.

Show »
Length:1,230
Mass (Da):137,957
Checksum:iBDA2B64A2EA0D51F
GO
Isoform 4 (identifier: P52701-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-302: Missing.

Note: No experimental confirmation available.

Show »
Length:1,058
Mass (Da):119,796
Checksum:i3D50E59BEED4B837
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131K → T.1 Publication
Corresponds to variant rs41294988 [ dbSNP | Ensembl ].
VAR_038032
Natural varianti20 – 201A → V in colorectal/endometrial cancer and HNPCC5; repair proficient. 2 Publications
Corresponds to variant rs63750664 [ dbSNP | Ensembl ].
VAR_043943
Natural varianti25 – 251A → S Associated with HNPCC5; unknown pathologiacl significance; repair proficient. 1 Publication
VAR_067294
Natural varianti25 – 251A → V.
Corresponds to variant rs35462442 [ dbSNP | Ensembl ].
VAR_038033
Natural varianti39 – 391G → E.6 Publications
Corresponds to variant rs1042821 [ dbSNP | Ensembl ].
VAR_004490
Natural varianti54 – 541G → A in CRC; unknown pathological significance. 1 Publication
Corresponds to variant rs63751098 [ dbSNP | Ensembl ].
VAR_043944
Natural varianti65 – 651S → L.1 Publication
Corresponds to variant rs41294984 [ dbSNP | Ensembl ].
VAR_038034
Natural varianti99 – 991K → N in CRC; unknown pathological significance. 1 Publication
VAR_043945
Natural varianti128 – 1281R → L No impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. 1 Publication
VAR_043946
Natural varianti144 – 1441S → I in suspected HNPCC5 and CRC. 3 Publications
Corresponds to variant rs3211299 [ dbSNP | Ensembl ].
VAR_012955
Natural varianti220 – 2201E → D.1 Publication
Corresponds to variant rs1800938 [ dbSNP | Ensembl ].
VAR_012956
Natural varianti221 – 2211E → D.1 Publication
Corresponds to variant rs41557217 [ dbSNP | Ensembl ].
VAR_042274
Natural varianti285 – 2851S → I in CRC. 1 Publication
VAR_012957
Natural varianti295 – 2951K → R in multiple colorectal adenoma.
VAR_043947
Natural varianti326 – 3261A → V Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
VAR_067295
Natural varianti340 – 3401F → S in CRC, breast cancer and leukemia. 1 Publication
VAR_043948
Natural varianti396 – 3961L → V Associated with HNPCC5; unknown pathological significance; repair proficient. 3 Publications
Corresponds to variant rs2020908 [ dbSNP | Ensembl ].
VAR_012958
Natural varianti435 – 4351L → P Mismatch repair deficient. 1 Publication
VAR_068710
Natural varianti449 – 4491L → P in colorectal/endometrial cancer; unknown pathological significance. 1 Publication
VAR_043949
Natural varianti468 – 4681R → H.1 Publication
Corresponds to variant rs41295268 [ dbSNP | Ensembl ].
VAR_038035
Natural varianti492 – 4921M → V Associated with HNPCC5; unknown pathological significance; repair proficient. 3 Publications
VAR_042275
Natural varianti503 – 5031S → C Associated with HNPCC5; unknown pathological significance; repair proficient. 2 Publications
VAR_038036
Natural varianti509 – 5091V → A.1 Publication
VAR_043950
Natural varianti522 – 5221Q → R in CRC; also associated with HNPCC5; repair proficient. 2 Publications
VAR_043951
Natural varianti538 – 5381Y → S.
Corresponds to variant rs728619 [ dbSNP | Ensembl ].
VAR_038037
Natural varianti566 – 5661G → R in CRC; partial functional loss. 1 Publication
VAR_012959
Natural varianti580 – 5801S → L.1 Publication
Corresponds to variant rs41295270 [ dbSNP | Ensembl ].
VAR_038038
Natural varianti585 – 5851L → P Mismatch repair deficient. 1 Publication
VAR_068711
Natural varianti610 – 6101K → N Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
VAR_067296
Natural varianti619 – 6191E → D in CRC; unknown pathological significance. 1 Publication
VAR_043952
Natural varianti623 – 6231P → A.1 Publication
Corresponds to variant rs3136334 [ dbSNP | Ensembl ].
VAR_029244
Natural varianti623 – 6231P → L No impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. 1 Publication
VAR_043953
Natural varianti677 – 6771S → T Mismatch repair proficient. 1 Publication
VAR_068712
Natural varianti685 – 6851G → A in CRC. 1 Publication
VAR_043954
Natural varianti698 – 6981Q → E in HNPCC; unknown pathological significance. 1 Publication
VAR_012960
Natural varianti725 – 7251I → M in CRC; unknown pathological significance. 1 Publication
VAR_043955
Natural varianti728 – 7281K → T No impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. 1 Publication
Corresponds to variant rs35552856 [ dbSNP | Ensembl ].
VAR_043956
Natural varianti772 – 7721R → Q in CRC. 1 Publication
VAR_043957
Natural varianti772 – 7721R → W in HNPCC5. 1 Publication
VAR_043958
Natural varianti787 – 7871A → V in CRC; unknown pathological significance. 1 Publication
VAR_043959
Natural varianti800 – 8001V → A in CRC; somatic mutation. 1 Publication
VAR_043960
Natural varianti800 – 8001V → L May be a rare polymorphism. 1 Publication
VAR_012961
Natural varianti803 – 8031D → G in CRC. 1 Publication
VAR_012962
Natural varianti850 – 8501Y → C Associated with HNPCC5 and CRC; unknown pathological significance; repair proficient. 3 Publications
VAR_012963
Natural varianti854 – 8541K → M in CRC; unknown pathological significance. 2 Publications
Corresponds to variant rs34374438 [ dbSNP | Ensembl ].
VAR_043961
Natural varianti878 – 8781V → A in suspected HNPCC5, colorectal/endometrial cancer and CRC; repair proficient. 9 Publications
Corresponds to variant rs2020912 [ dbSNP | Ensembl ].
VAR_012964
Natural varianti886 – 8861I → V.1 Publication
Corresponds to variant rs2020914 [ dbSNP | Ensembl ].
VAR_014902
Natural varianti901 – 9011R → H in colorectal/endometrial cancer. 1 Publication
VAR_043962
Natural varianti976 – 9761R → H in CRC; sporadic; also associated with HNPCC5; repair proficient. 2 Publications
VAR_012965
Natural varianti1021 – 10211A → D in CRC; unknown pathological significance; repair proficient. 2 Publications
VAR_043963
Natural varianti1026 – 10261D → Y Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
VAR_067297
Natural varianti1031 – 10311D → V in CRC; somatic mutation. 1 Publication
VAR_043964
Natural varianti1076 – 10761R → C in CRC; unknown pathological significance. 1 Publication
VAR_043965
Natural varianti1087 – 10871P → S Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
Corresponds to variant rs63750998 [ dbSNP | Ensembl ].
VAR_067298
Natural varianti1087 – 10871P → T in CRC. 1 Publication
Corresponds to variant rs63750998 [ dbSNP | Ensembl ].
VAR_012966
Natural varianti1095 – 10951R → H in CRC; unknown pathological significance; mismatch repair proficient. 2 Publications
VAR_043966
Natural varianti1100 – 11001T → M in CRC; unknown pathological significance. 1 Publication
VAR_043967
Natural varianti1158 – 11581C → R in CRC; somatic mutation. 1 Publication
VAR_043968
Natural varianti1163 – 11631E → V in HNPCC5. 1 Publication
Corresponds to variant rs63750252 [ dbSNP | Ensembl ].
VAR_043969
Natural varianti1193 – 11931E → K Found in an endometrial cancer sample; displays marked impairment of heterodimerization with MSH2 and of in vitro mismatch repair capacity. 1 Publication
VAR_043970
Natural varianti1213 – 12131D → V.1 Publication
VAR_004491
Natural varianti1219 – 12191T → I in CRC; unknown pathological significance. 1 Publication
VAR_043971
Natural varianti1225 – 12251T → M Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
VAR_067299
Natural varianti1232 – 12321V → L.1 Publication
Corresponds to variant rs41295276 [ dbSNP | Ensembl ].
VAR_038039
Natural varianti1234 – 12341E → Q.
Corresponds to variant rs35717727 [ dbSNP | Ensembl ].
VAR_038040
Natural varianti1248 – 12481H → D in CRC; unknown pathological significance. 1 Publication
VAR_043972
Natural varianti1260 – 12601V → I.1 Publication
VAR_004492
Natural varianti1284 – 12841T → M in CRC. 1 Publication
VAR_043973
Natural varianti1321 – 13211R → G.1 Publication
Corresponds to variant rs41295278 [ dbSNP | Ensembl ].
VAR_038041
Natural varianti1354 – 13541L → Q in CRC; unknown pathological significance; mismatch repair proficient. 2 Publications
VAR_043974

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 302302Missing in isoform 4. VSP_055020Add
BLAST
Alternative sequencei80 – 209130Missing in isoform 3. VSP_054419Add
BLAST
Alternative sequencei1058 – 106811DVLLCLANYSR → GKTLNKLVLRL in isoform GTBP-alt. VSP_003291Add
BLAST
Alternative sequencei1069 – 1360292Missing in isoform GTBP-alt. VSP_003292Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 5722AAPGA…AGPGP → GCPRGLSFPRRGCGLERGWA WA in BAA23674. 1 PublicationAdd
BLAST
Sequence conflicti36 – 5722AAPGA…AGPGP → GCPRGLSFPRRGCGLERGWA WA in BAA23675. 1 PublicationAdd
BLAST
Sequence conflicti868 – 8681M → V in BAG65496. 1 Publication
Sequence conflicti1358 – 13603KEL → D in AAL87401. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U73737
, U73732, U73733, U73734, U73736 Genomic DNA. Translation: AAB47425.1.
D89645 Genomic DNA. Translation: BAA23674.1.
D89646 mRNA. Translation: BAA23675.1.
AK293921 mRNA. Translation: BAG57302.1.
AK304735 mRNA. Translation: BAG65496.1.
AY082894 Genomic DNA. Translation: AAL87401.1.
AC006509 Genomic DNA. No translation available.
BC004246 mRNA. Translation: AAH04246.1.
U54777 mRNA. Translation: AAB39212.2.
U28946 mRNA. Translation: AAC50461.1.
CCDSiCCDS1836.1. [P52701-1]
CCDS62906.1. [P52701-3]
PIRiJC5839.
RefSeqiNP_000170.1. NM_000179.2. [P52701-1]
NP_001268421.1. NM_001281492.1. [P52701-3]
NP_001268422.1. NM_001281493.1.
NP_001268423.1. NM_001281494.1.
UniGeneiHs.445052.

Genome annotation databases

EnsembliENST00000234420; ENSP00000234420; ENSG00000116062. [P52701-1]
ENST00000538136; ENSP00000438580; ENSG00000116062.
ENST00000540021; ENSP00000446475; ENSG00000116062.
GeneIDi2956.
KEGGihsa:2956.
UCSCiuc002rwc.2. human. [P52701-2]
uc002rwd.4. human. [P52701-1]

Polymorphism databases

DMDMi68067672.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Hereditary non-polyposis colorectal cancer db
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U73737
, U73732 , U73733 , U73734 , U73736 Genomic DNA. Translation: AAB47425.1 .
D89645 Genomic DNA. Translation: BAA23674.1 .
D89646 mRNA. Translation: BAA23675.1 .
AK293921 mRNA. Translation: BAG57302.1 .
AK304735 mRNA. Translation: BAG65496.1 .
AY082894 Genomic DNA. Translation: AAL87401.1 .
AC006509 Genomic DNA. No translation available.
BC004246 mRNA. Translation: AAH04246.1 .
U54777 mRNA. Translation: AAB39212.2 .
U28946 mRNA. Translation: AAC50461.1 .
CCDSi CCDS1836.1. [P52701-1 ]
CCDS62906.1. [P52701-3 ]
PIRi JC5839.
RefSeqi NP_000170.1. NM_000179.2. [P52701-1 ]
NP_001268421.1. NM_001281492.1. [P52701-3 ]
NP_001268422.1. NM_001281493.1.
NP_001268423.1. NM_001281494.1.
UniGenei Hs.445052.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P52701.
SMRi P52701. Positions 68-201, 362-1335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109211. 57 interactions.
DIPi DIP-32972N.
IntActi P52701. 18 interactions.
MINTi MINT-131993.
STRINGi 9606.ENSP00000234420.

PTM databases

PhosphoSitei P52701.

Polymorphism databases

DMDMi 68067672.

Proteomic databases

MaxQBi P52701.
PaxDbi P52701.
PeptideAtlasi P52701.
PRIDEi P52701.

Protocols and materials databases

DNASUi 2956.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000234420 ; ENSP00000234420 ; ENSG00000116062 . [P52701-1 ]
ENST00000538136 ; ENSP00000438580 ; ENSG00000116062 .
ENST00000540021 ; ENSP00000446475 ; ENSG00000116062 .
GeneIDi 2956.
KEGGi hsa:2956.
UCSCi uc002rwc.2. human. [P52701-2 ]
uc002rwd.4. human. [P52701-1 ]

Organism-specific databases

CTDi 2956.
GeneCardsi GC02P047924.
GeneReviewsi MSH6.
HGNCi HGNC:7329. MSH6.
HPAi CAB009091.
HPA028376.
HPA028446.
MIMi 276300. phenotype.
600678. gene.
608089. phenotype.
614350. phenotype.
neXtProti NX_P52701.
Orphaneti 252202. Constitutional mismatch repair deficiency syndrome.
144. Hereditary nonpolyposis colon cancer.
587. Muir-Torre syndrome.
99817. Non-polyposis Turcot syndrome.
PharmGKBi PA184.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0249.
HOGENOMi HOG000243127.
HOVERGENi HBG000101.
InParanoidi P52701.
KOi K08737.
OMAi ALKDCMR.
OrthoDBi EOG7K9K27.
PhylomeDBi P52701.
TreeFami TF105842.

Miscellaneous databases

EvolutionaryTracei P52701.
GeneWikii MSH6.
GenomeRNAii 2956.
NextBioi 11716.
PMAP-CutDB P52701.
PROi P52701.
SOURCEi Search...

Gene expression databases

ArrayExpressi P52701.
Bgeei P52701.
CleanExi HS_MSH6.
Genevestigatori P52701.

Family and domain databases

Gene3Di 3.40.1170.10. 1 hit.
3.40.50.300. 1 hit.
InterProi 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.
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 ]
PANTHERi PTHR11361:SF31. PTHR11361:SF31. 1 hit.
Pfami 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 ]
PIRSFi PIRSF037677. DNA_mis_repair_Msh6. 1 hit.
SMARTi SM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
SM00293. PWWP. 1 hit.
[Graphical view ]
SUPFAMi SSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF55271. SSF55271. 1 hit.
PROSITEi PS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
PS50812. PWWP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. "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.
    , 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] (ISOFORMS 3 AND 4).
    Tissue: Cerebellum and Uterus.
  4. 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.
  5. "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.
    , 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].
  6. "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.
  7. "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.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-116.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. Cited for: FUNCTION.
  17. "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.
  18. "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures."
    Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.
    Genes Dev. 14:927-939(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF MSH6 AS MEMBER OF BASC.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. 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.
  27. "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].
  28. "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.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "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].
  31. "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.
  32. "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).
  33. Cited for: VARIANTS VAL-1213 AND ILE-1260.
  34. "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.
  35. "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.
  36. "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.
  37. "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.
  38. "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.
  39. "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.
  40. "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.
  41. Cited for: VARIANT HNPCC5 ALA-878.
  42. Cited for: VARIANTS CRC ILE-144; ARG-522; MET-725; CYS-850; ALA-878; ASP-1021; MET-1100; ILE-1219 AND ASP-1248.
  43. "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.
  44. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT HNPCC5 VAL-492.
  45. "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.
  46. Cited for: VARIANT CRC ALA-54, VARIANTS GLU-39; ALA-509; MET-854 AND ALA-878.
  47. "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.
  48. "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.
  49. "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.
  50. "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.
  51. "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.
  52. "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] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-221 AND VAL-492.
  53. "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.
  54. "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.
  55. "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.

Entry informationi

Entry nameiMSH6_HUMAN
AccessioniPrimary (citable) accession number: P52701
Secondary accession number(s): B4DF41
, B4E3I4, F5H2F9, O43706, O43917, Q8TCX4, Q9BTB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 21, 2005
Last modified: September 3, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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