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P52701

- MSH6_HUMAN

UniProt

P52701 - MSH6_HUMAN

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Protein

DNA mismatch repair protein Msh6

Gene

MSH6

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 – 11418ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  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: 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: UniProtKB
  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 1 Publication. Chromosome 1 Publication
Note: Associates with H3K36me3 via its PWWP domain.

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.7 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201A → V in colorectal/endometrial cancer and HNPCC5; repair proficient. 1 Publication
Corresponds to variant rs63750664 [ dbSNP | Ensembl ].
VAR_043943
Natural varianti25 – 251A → S Associated with HNPCC5; unknown pathologiacl significance; repair proficient.
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.
VAR_067295
Natural varianti396 – 3961L → V Associated with HNPCC5; unknown pathological significance; repair proficient. 2 Publications
Corresponds to variant rs2020908 [ dbSNP | Ensembl ].
VAR_012958
Natural varianti492 – 4921M → V Associated with HNPCC5; unknown pathological significance; repair proficient. 2 Publications
VAR_042275
Natural varianti503 – 5031S → C Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
VAR_038036
Natural varianti522 – 5221Q → R in CRC; also associated with HNPCC5; repair proficient. 1 Publication
VAR_043951
Natural varianti610 – 6101K → N Associated with HNPCC5; unknown pathological significance; repair proficient.
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. 2 Publications
VAR_012963
Natural varianti878 – 8781V → A in suspected HNPCC5, colorectal/endometrial cancer and CRC; repair proficient. 7 Publications
Corresponds to variant rs2020912 [ dbSNP | Ensembl ].
VAR_012964
Natural varianti976 – 9761R → H in CRC; sporadic; also associated with HNPCC5; repair proficient. 1 Publication
VAR_012965
Natural varianti1026 – 10261D → Y Associated with HNPCC5; unknown pathological significance; repair proficient.
VAR_067297
Natural varianti1087 – 10871P → S Associated with HNPCC5; unknown pathological significance; repair proficient.
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.
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.2 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: An autosomal recessive, rare, childhood cancer predisposition syndrome encompassing a broad tumor spectrum. This includes hematological malignancies, central nervous system tumors, Lynch syndrome-associated malignancies such as colorectal tumors as well as multiple intestinal polyps, embryonic tumors and rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature reminiscent of neurofibromatosis type 1, are often found as first manifestation of the underlying cancer. Areas of skin hypopigmentation have also been reported in MMRCS patients.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

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. 1 Publication
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.7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52701.
PaxDbiP52701.
PeptideAtlasiP52701.
PRIDEiP52701.

PTM databases

PhosphoSiteiP52701.

Miscellaneous databases

PMAP-CutDBP52701.

Expressioni

Gene expression databases

BgeeiP52701.
CleanExiHS_MSH6.
ExpressionAtlasiP52701. baseline and differential.
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
MSH2P432465EBI-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 – 796Combined sources
Beta strandi94 – 985Combined sources
Beta strandi106 – 1094Combined sources
Beta strandi120 – 1256Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi139 – 1435Combined sources
Helixi145 – 1473Combined sources
Beta strandi148 – 1514Combined sources
Turni157 – 1593Combined sources
Helixi170 – 18314Combined sources
Helixi187 – 1915Combined sources
Turni192 – 1954Combined sources
Beta strandi197 – 1993Combined sources
Helixi366 – 3694Combined sources
Helixi371 – 3733Combined sources
Turni375 – 3773Combined sources
Helixi400 – 4034Combined sources
Helixi408 – 41912Combined sources
Beta strandi423 – 4297Combined sources
Beta strandi432 – 4365Combined sources
Helixi437 – 44711Combined sources
Beta strandi453 – 4564Combined sources
Beta strandi458 – 4625Combined sources
Helixi463 – 4653Combined sources
Helixi466 – 47510Combined sources
Beta strandi480 – 4856Combined sources
Helixi489 – 4979Combined sources
Helixi505 – 5073Combined sources
Beta strandi511 – 5177Combined sources
Helixi519 – 5213Combined sources
Beta strandi526 – 5283Combined sources
Beta strandi538 – 5469Combined sources
Beta strandi554 – 5618Combined sources
Turni563 – 5653Combined sources
Beta strandi568 – 5758Combined sources
Helixi580 – 5889Combined sources
Beta strandi591 – 5977Combined sources
Turni598 – 6003Combined sources
Helixi603 – 6097Combined sources
Turni610 – 6156Combined sources
Beta strandi616 – 6216Combined sources
Turni624 – 6263Combined sources
Helixi630 – 63910Combined sources
Turni640 – 6434Combined sources
Beta strandi644 – 6474Combined sources
Helixi657 – 6615Combined sources
Beta strandi667 – 6693Combined sources
Beta strandi671 – 6733Combined sources
Helixi675 – 6773Combined sources
Helixi678 – 69316Combined sources
Helixi697 – 7015Combined sources
Beta strandi706 – 7083Combined sources
Helixi712 – 7154Combined sources
Helixi737 – 7426Combined sources
Beta strandi746 – 7483Combined sources
Beta strandi750 – 7534Combined sources
Helixi758 – 7625Combined sources
Helixi768 – 77912Combined sources
Helixi785 – 79915Combined sources
Helixi802 – 81211Combined sources
Helixi818 – 82912Combined sources
Helixi831 – 8366Combined sources
Helixi838 – 8414Combined sources
Helixi847 – 87933Combined sources
Helixi885 – 8906Combined sources
Turni894 – 8963Combined sources
Beta strandi897 – 9004Combined sources
Helixi906 – 9138Combined sources
Helixi918 – 9236Combined sources
Helixi936 – 95520Combined sources
Helixi959 – 9613Combined sources
Beta strandi968 – 9703Combined sources
Helixi973 – 9753Combined sources
Beta strandi978 – 9814Combined sources
Turni983 – 9864Combined sources
Beta strandi995 – 9995Combined sources
Beta strandi1002 – 10054Combined sources
Turni1008 – 10103Combined sources
Helixi1011 – 104131Combined sources
Helixi1044 – 106623Combined sources
Beta strandi1070 – 10723Combined sources
Turni1082 – 10843Combined sources
Beta strandi1089 – 10946Combined sources
Beta strandi1111 – 11166Combined sources
Beta strandi1120 – 11223Combined sources
Beta strandi1129 – 11335Combined sources
Beta strandi1136 – 11383Combined sources
Helixi1140 – 115415Combined sources
Turni1155 – 11573Combined sources
Beta strandi1160 – 11678Combined sources
Beta strandi1171 – 11766Combined sources
Helixi1189 – 120315Combined sources
Beta strandi1209 – 12135Combined sources
Turni1215 – 12184Combined sources
Helixi1221 – 123717Combined sources
Beta strandi1242 – 12465Combined sources
Helixi1250 – 12556Combined sources
Turni1256 – 12583Combined sources
Beta strandi1260 – 126910Combined sources
Beta strandi1285 – 12928Combined sources
Helixi1298 – 13058Combined sources
Helixi1310 – 132213Combined sources
Turni1323 – 13264Combined sources
Turni1330 – 13323Combined sources

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52701.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 15463PWWPPROSITE-ProRule annotationAdd
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

Belongs to the DNA mismatch repair MutS family.Curated
Contains 1 PWWP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0249.
GeneTreeiENSGT00550000075024.
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

        10         20         30         40         50
MSRQSTLYSF FPKSPALSDA NKASARASRE GGRAAAAPGA SPSPGGDAAW
60 70 80 90 100
SEAGPGPRPL ARSASPPKAK NLNGGLRRSV APAAPTSCDF SPGDLVWAKM
110 120 130 140 150
EGYPWWPCLV YNHPFDGTFI REKGKSVRVH VQFFDDSPTR GWVSKRLLKP
160 170 180 190 200
YTGSKSKEAQ KGGHFYSAKP EILRAMQRAD EALNKDKIKR LELAVCDEPS
210 220 230 240 250
EPEEEEEMEV GTTYVTDKSE EDNEIESEEE VQPKTQGSRR SSRQIKKRRV
260 270 280 290 300
ISDSESDIGG SDVEFKPDTK EEGSSDEISS GVGDSESEGL NSPVKVARKR
310 320 330 340 350
KRMVTGNGSL KRKSSRKETP SATKQATSIS SETKNTLRAF SAPQNSESQA
360 370 380 390 400
HVSGGGDDSS RPTVWYHETL EWLKEEKRRD EHRRRPDHPD FDASTLYVPE
410 420 430 440 450
DFLNSCTPGM RKWWQIKSQN FDLVICYKVG KFYELYHMDA LIGVSELGLV
460 470 480 490 500
FMKGNWAHSG FPEIAFGRYS DSLVQKGYKV ARVEQTETPE MMEARCRKMA
510 520 530 540 550
HISKYDRVVR REICRIITKG TQTYSVLEGD PSENYSKYLL SLKEKEEDSS
560 570 580 590 600
GHTRAYGVCF VDTSLGKFFI GQFSDDRHCS RFRTLVAHYP PVQVLFEKGN
610 620 630 640 650
LSKETKTILK SSLSCSLQEG LIPGSQFWDA SKTLRTLLEE EYFREKLSDG
660 670 680 690 700
IGVMLPQVLK GMTSESDSIG LTPGEKSELA LSALGGCVFY LKKCLIDQEL
710 720 730 740 750
LSMANFEEYI PLDSDTVSTT RSGAIFTKAY QRMVLDAVTL NNLEIFLNGT
760 770 780 790 800
NGSTEGTLLE RVDTCHTPFG KRLLKQWLCA PLCNHYAIND RLDAIEDLMV
810 820 830 840 850
VPDKISEVVE LLKKLPDLER LLSKIHNVGS PLKSQNHPDS RAIMYEETTY
860 870 880 890 900
SKKKIIDFLS ALEGFKVMCK IIGIMEEVAD GFKSKILKQV ISLQTKNPEG
910 920 930 940 950
RFPDLTVELN RWDTAFDHEK ARKTGLITPK AGFDSDYDQA LADIRENEQS
960 970 980 990 1000
LLEYLEKQRN RIGCRTIVYW GIGRNRYQLE IPENFTTRNL PEEYELKSTK
1010 1020 1030 1040 1050
KGCKRYWTKT IEKKLANLIN AEERRDVSLK DCMRRLFYNF DKNYKDWQSA
1060 1070 1080 1090 1100
VECIAVLDVL LCLANYSRGG DGPMCRPVIL LPEDTPPFLE LKGSRHPCIT
1110 1120 1130 1140 1150
KTFFGDDFIP NDILIGCEEE EQENGKAYCV LVTGPNMGGK STLMRQAGLL
1160 1170 1180 1190 1200
AVMAQMGCYV PAEVCRLTPI DRVFTRLGAS DRIMSGESTF FVELSETASI
1210 1220 1230 1240 1250
LMHATAHSLV LVDELGRGTA TFDGTAIANA VVKELAETIK CRTLFSTHYH
1260 1270 1280 1290 1300
SLVEDYSQNV AVRLGHMACM VENECEDPSQ ETITFLYKFI KGACPKSYGF
1310 1320 1330 1340 1350
NAARLANLPE EVIQKGHRKA REFEKMNQSL RLFREVCLAS ERSTVDAEAV
1360
HKLLTLIKEL
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 5722AAPGA…AGPGP → GCPRGLSFPRRGCGLERGWA WA in BAA23674. (PubMed:9455487)CuratedAdd
BLAST
Sequence conflicti36 – 5722AAPGA…AGPGP → GCPRGLSFPRRGCGLERGWA WA in BAA23675. (PubMed:9455487)CuratedAdd
BLAST
Sequence conflicti868 – 8681M → V in BAG65496. (PubMed:14702039)Curated
Sequence conflicti1358 – 13603KEL → D in AAL87401. 1 PublicationCurated

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. 1 Publication
Corresponds to variant rs63750664 [ dbSNP | Ensembl ].
VAR_043943
Natural varianti25 – 251A → S Associated with HNPCC5; unknown pathologiacl significance; repair proficient.
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.
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. 2 Publications
Corresponds to variant rs2020908 [ dbSNP | Ensembl ].
VAR_012958
Natural varianti435 – 4351L → P Mismatch repair deficient.
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. 2 Publications
VAR_042275
Natural varianti503 – 5031S → C Associated with HNPCC5; unknown pathological significance; repair proficient. 1 Publication
VAR_038036
Natural varianti509 – 5091V → A.1 Publication
VAR_043950
Natural varianti522 – 5221Q → R in CRC; also associated with HNPCC5; repair proficient. 1 Publication
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.
VAR_068711
Natural varianti610 – 6101K → N Associated with HNPCC5; unknown pathological significance; repair proficient.
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.
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. 2 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. 7 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. 1 Publication
VAR_012965
Natural varianti1021 – 10211A → D in CRC; unknown pathological significance; repair proficient. 1 Publication
VAR_043963
Natural varianti1026 – 10261D → Y Associated with HNPCC5; unknown pathological significance; repair proficient.
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.
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. 1 Publication
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.
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. 1 Publication
VAR_043974

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 302302Missing in isoform 4. 1 PublicationVSP_055020Add
BLAST
Alternative sequencei80 – 209130Missing in isoform 3. 1 PublicationVSP_054419Add
BLAST
Alternative sequencei1058 – 106811DVLLCLANYSR → GKTLNKLVLRL in isoform GTBP-alt. CuratedVSP_003291Add
BLAST
Alternative sequencei1069 – 1360292Missing in isoform GTBP-alt. CuratedVSP_003292Add
BLAST

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]
CCDS62907.1. [P52701-4]
PIRiJC5839.
RefSeqiNP_000170.1. NM_000179.2. [P52701-1]
NP_001268421.1. NM_001281492.1. [P52701-3]
NP_001268422.1. NM_001281493.1. [P52701-4]
NP_001268423.1. NM_001281494.1. [P52701-4]
UniGeneiHs.445052.

Genome annotation databases

EnsembliENST00000234420; ENSP00000234420; ENSG00000116062. [P52701-1]
ENST00000538136; ENSP00000438580; ENSG00000116062. [P52701-4]
ENST00000540021; ENSP00000446475; ENSG00000116062. [P52701-3]
ENST00000614496; ENSP00000477844; ENSG00000116062. [P52701-4]
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 ]
CCDS62907.1. [P52701-4 ]
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. [P52701-4 ]
NP_001268423.1. NM_001281494.1. [P52701-4 ]
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 . [P52701-4 ]
ENST00000540021 ; ENSP00000446475 ; ENSG00000116062 . [P52701-3 ]
ENST00000614496 ; ENSP00000477844 ; ENSG00000116062 . [P52701-4 ]
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.
GeneTreei ENSGT00550000075024.
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

Bgeei P52701.
CleanExi HS_MSH6.
ExpressionAtlasi P52701. baseline and differential.
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: October 29, 2014
This is version 176 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

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