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P20585

- MSH3_HUMAN

UniProt

P20585 - MSH3_HUMAN

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Protein

DNA mismatch repair protein Msh3

Gene

MSH3

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 beta which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to 13 nucleotides long. 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi896 – 9038ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. centromeric DNA binding Source: Ensembl
  3. damaged DNA binding Source: Ensembl
  4. DNA-dependent ATPase activity Source: RefGenome
  5. double-strand/single-strand DNA junction binding Source: RefGenome
  6. enzyme binding Source: UniProtKB
  7. heteroduplex DNA loop binding Source: RefGenome
  8. Y-form DNA binding Source: RefGenome

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA repair Source: BHF-UCL
  3. maintenance of DNA repeat elements Source: HGNC
  4. meiotic mismatch repair Source: RefGenome
  5. mismatch repair Source: HGNC
  6. negative regulation of DNA recombination Source: BHF-UCL
  7. positive regulation of helicase activity Source: BHF-UCL
  8. reciprocal meiotic recombination Source: RefGenome
  9. somatic recombination of immunoglobulin gene segments Source: RefGenome
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_228019. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).

Names & Taxonomyi

Protein namesi
Recommended name:
DNA mismatch repair protein Msh3
Short name:
hMSH3
Alternative name(s):
Divergent upstream protein
Short name:
DUP
Mismatch repair protein 1
Short name:
MRP1
Gene namesi
Name:MSH3
Synonyms:DUC1, DUG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:7326. MSH3.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. MutSbeta complex Source: HGNC
  3. nuclear chromosome Source: RefGenome
  4. nucleus Source: HPA
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.

Organism-specific databases

MIMi608089. phenotype.
PharmGKBiPA31134.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11371137DNA mismatch repair protein Msh3PRO_0000115192Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1099 – 10991Phosphothreonine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP20585.
PaxDbiP20585.
PRIDEiP20585.

PTM databases

PhosphoSiteiP20585.

Expressioni

Gene expression databases

BgeeiP20585.
CleanExiHS_MSH3.
GenevestigatoriP20585.

Organism-specific databases

HPAiHPA036080.
HPA036081.

Interactioni

Subunit structurei

Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a ternary complex with MutL alpha (MLH1-PMS1). Interacts with EXO1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MSH2P432464EBI-1164205,EBI-355888

Protein-protein interaction databases

BioGridi110574. 24 interactions.
DIPiDIP-35127N.
IntActiP20585. 5 interactions.
MINTiMINT-192778.
STRINGi9606.ENSP00000265081.

Structurei

Secondary structure

1
1137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi231 – 24010Combined sources
Turni241 – 2455Combined sources
Beta strandi246 – 2516Combined sources
Beta strandi253 – 2597Combined sources
Helixi260 – 27011Combined sources
Beta strandi275 – 2773Combined sources
Beta strandi280 – 2867Combined sources
Helixi287 – 2893Combined sources
Helixi290 – 30011Combined sources
Beta strandi304 – 3096Combined sources
Helixi313 – 3164Combined sources
Beta strandi328 – 3347Combined sources
Turni342 – 3443Combined sources
Beta strandi347 – 3493Combined sources
Beta strandi354 – 3563Combined sources
Beta strandi368 – 3747Combined sources
Turni382 – 3843Combined sources
Beta strandi386 – 3938Combined sources
Turni395 – 3973Combined sources
Beta strandi400 – 4078Combined sources
Helixi412 – 42110Combined sources
Beta strandi424 – 4318Combined sources
Helixi434 – 44512Combined sources
Beta strandi449 – 4513Combined sources
Beta strandi454 – 4585Combined sources
Helixi460 – 4623Combined sources
Helixi465 – 47511Combined sources
Helixi497 – 51216Combined sources
Helixi516 – 5194Combined sources
Helixi522 – 5243Combined sources
Beta strandi525 – 5284Combined sources
Turni531 – 5333Combined sources
Helixi539 – 5446Combined sources
Beta strandi547 – 5493Combined sources
Turni551 – 5533Combined sources
Helixi560 – 5645Combined sources
Helixi570 – 58112Combined sources
Helixi587 – 60115Combined sources
Helixi607 – 6137Combined sources
Turni614 – 6174Combined sources
Helixi621 – 6299Combined sources
Helixi635 – 66127Combined sources
Helixi666 – 6727Combined sources
Helixi674 – 6785Combined sources
Helixi680 – 6823Combined sources
Helixi683 – 6864Combined sources
Helixi691 – 6966Combined sources
Helixi706 – 7083Combined sources
Helixi710 – 73728Combined sources
Beta strandi745 – 7473Combined sources
Beta strandi750 – 7578Combined sources
Helixi761 – 7633Combined sources
Beta strandi769 – 7735Combined sources
Beta strandi775 – 7817Combined sources
Helixi783 – 81432Combined sources
Helixi815 – 8173Combined sources
Helixi818 – 84124Combined sources
Beta strandi843 – 8453Combined sources
Beta strandi850 – 8545Combined sources
Beta strandi856 – 8627Combined sources
Helixi865 – 8706Combined sources
Beta strandi875 – 8773Combined sources
Beta strandi880 – 8845Combined sources
Beta strandi886 – 8883Combined sources
Beta strandi891 – 8966Combined sources
Helixi900 – 91718Combined sources
Beta strandi922 – 9309Combined sources
Beta strandi933 – 9386Combined sources
Helixi952 – 96514Combined sources
Beta strandi971 – 9766Combined sources
Turni977 – 9804Combined sources
Helixi983 – 99917Combined sources
Beta strandi1004 – 10085Combined sources
Helixi1012 – 10165Combined sources
Helixi1017 – 10204Combined sources
Turni1021 – 10244Combined sources
Beta strandi1025 – 10339Combined sources
Beta strandi1055 – 10628Combined sources
Turni1066 – 10694Combined sources
Helixi1070 – 10734Combined sources
Turni1074 – 10774Combined sources
Helixi1080 – 111132Combined sources
Helixi1116 – 112813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3THWX-ray3.09B219-1134[»]
3THXX-ray2.70B219-1134[»]
3THYX-ray2.89B219-1134[»]
3THZX-ray4.30B219-1134[»]
ProteinModelPortaliP20585.
SMRiP20585. Positions 225-1123.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni75 – 297223Interaction with EXO1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi51 – 6212Poly-AlaAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0249.
GeneTreeiENSGT00550000074949.
HOGENOMiHOG000029776.
HOVERGENiHBG006400.
InParanoidiP20585.
KOiK08736.
OMAiELSIVCI.
OrthoDBiEOG7X6KZF.
PhylomeDBiP20585.
TreeFamiTF300525.

Family and domain databases

Gene3Di3.30.420.110. 1 hit.
3.40.1170.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR007695. 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.
[Graphical view]
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.
[Graphical view]
SMARTiSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view]
SUPFAMiSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53150. SSF53150. 2 hits.
SSF55271. SSF55271. 1 hit.
PROSITEiPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20585-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRRKPASGG LAASSSAPAR QAVLSRFFQS TGSLKSTSSS TGAADQVDPG
60 70 80 90 100
AAAAAAAAAA AAPPAPPAPA FPPQLPPHIA TEIDRRKKRP LENDGPVKKK
110 120 130 140 150
VKKVQQKEGG SDLGMSGNSE PKKCLRTRNV SKSLEKLKEF CCDSALPQSR
160 170 180 190 200
VQTESLQERF AVLPKCTDFD DISLLHAKNA VSSEDSKRQI NQKDTTLFDL
210 220 230 240 250
SQFGSSNTSH ENLQKTASKS ANKRSKSIYT PLELQYIEMK QQHKDAVLCV
260 270 280 290 300
ECGYKYRFFG EDAEIAAREL NIYCHLDHNF MTASIPTHRL FVHVRRLVAK
310 320 330 340 350
GYKVGVVKQT ETAALKAIGD NRSSLFSRKL TALYTKSTLI GEDVNPLIKL
360 370 380 390 400
DDAVNVDEIM TDTSTSYLLC ISENKENVRD KKKGNIFIGI VGVQPATGEV
410 420 430 440 450
VFDSFQDSAS RSELETRMSS LQPVELLLPS ALSEQTEALI HRATSVSVQD
460 470 480 490 500
DRIRVERMDN IYFEYSHAFQ AVTEFYAKDT VDIKGSQIIS GIVNLEKPVI
510 520 530 540 550
CSLAAIIKYL KEFNLEKMLS KPENFKQLSS KMEFMTINGT TLRNLEILQN
560 570 580 590 600
QTDMKTKGSL LWVLDHTKTS FGRRKLKKWV TQPLLKLREI NARLDAVSEV
610 620 630 640 650
LHSESSVFGQ IENHLRKLPD IERGLCSIYH KKCSTQEFFL IVKTLYHLKS
660 670 680 690 700
EFQAIIPAVN SHIQSDLLRT VILEIPELLS PVEHYLKILN EQAAKVGDKT
710 720 730 740 750
ELFKDLSDFP LIKKRKDEIQ GVIDEIRMHL QEIRKILKNP SAQYVTVSGQ
760 770 780 790 800
EFMIEIKNSA VSCIPTDWVK VGSTKAVSRF HSPFIVENYR HLNQLREQLV
810 820 830 840 850
LDCSAEWLDF LEKFSEHYHS LCKAVHHLAT VDCIFSLAKV AKQGDYCRPT
860 870 880 890 900
VQEERKIVIK NGRHPVIDVL LGEQDQYVPN NTDLSEDSER VMIITGPNMG
910 920 930 940 950
GKSSYIKQVA LITIMAQIGS YVPAEEATIG IVDGIFTRMG AADNIYKGQS
960 970 980 990 1000
TFMEELTDTA EIIRKATSQS LVILDELGRG TSTHDGIAIA YATLEYFIRD
1010 1020 1030 1040 1050
VKSLTLFVTH YPPVCELEKN YSHQVGNYHM GFLVSEDESK LDPGAAEQVP
1060 1070 1080 1090 1100
DFVTFLYQIT RGIAARSYGL NVAKLADVPG EILKKAAHKS KELEGLINTK
1110 1120 1130
RKRLKYFAKL WTMHNAQDLQ KWTEEFNMEE TQTSLLH
Length:1,137
Mass (Da):127,412
Last modified:January 11, 2011 - v4
Checksum:iFBAE6B84D3F86032
GO

Sequence cautioni

The sequence AAH11817.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611A → T in AAI30435. (PubMed:15489334)Curated
Sequence conflicti622 – 6221E → G in AAB47281. (PubMed:2722860)Curated
Sequence conflicti622 – 6221E → G in BAD27111. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 659Missing.2 Publications
VAR_020934
Natural varianti62 – 621A → AAAA.1 Publication
VAR_020935
Natural varianti79 – 791I → V.6 Publications
Corresponds to variant rs1650697 [ dbSNP | Ensembl ].
VAR_020936
Natural varianti709 – 7091F → L.1 Publication
Corresponds to variant rs1805354 [ dbSNP | Ensembl ].
VAR_016160
Natural varianti789 – 7891Y → F.
Corresponds to variant rs10067975 [ dbSNP | Ensembl ].
VAR_055251
Natural varianti949 – 9491Q → R.5 Publications
Corresponds to variant rs184967 [ dbSNP | Ensembl ].
VAR_016161
Natural varianti1045 – 10451A → T.5 Publications
Corresponds to variant rs26279 [ dbSNP | Ensembl ].
VAR_016162
Natural varianti1054 – 10541T → A.
Corresponds to variant rs1805131 [ dbSNP | Ensembl ].
VAR_016163

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04810 mRNA. Translation: AAB47281.1.
U61981 mRNA. Translation: AAB06045.1.
D61419 Genomic DNA. Translation: BAD27111.1.
AY275681 Genomic DNA. Translation: AAP13535.1.
AC008434 Genomic DNA. No translation available.
AC010270 Genomic DNA. No translation available.
AC022493 Genomic DNA. No translation available.
BC011817 mRNA. Translation: AAH11817.1. Sequence problems.
BC130434 mRNA. Translation: AAI30435.1.
BC130436 mRNA. Translation: AAI30437.1.
CCDSiCCDS34195.1.
PIRiA33507.
RefSeqiNP_002430.3. NM_002439.4.
UniGeneiHs.280987.
Hs.648635.

Genome annotation databases

EnsembliENST00000265081; ENSP00000265081; ENSG00000113318.
GeneIDi4437.
KEGGihsa:4437.
UCSCiuc003kgz.4. human.

Polymorphism databases

DMDMi317373576.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04810 mRNA. Translation: AAB47281.1 .
U61981 mRNA. Translation: AAB06045.1 .
D61419 Genomic DNA. Translation: BAD27111.1 .
AY275681 Genomic DNA. Translation: AAP13535.1 .
AC008434 Genomic DNA. No translation available.
AC010270 Genomic DNA. No translation available.
AC022493 Genomic DNA. No translation available.
BC011817 mRNA. Translation: AAH11817.1 . Sequence problems.
BC130434 mRNA. Translation: AAI30435.1 .
BC130436 mRNA. Translation: AAI30437.1 .
CCDSi CCDS34195.1.
PIRi A33507.
RefSeqi NP_002430.3. NM_002439.4.
UniGenei Hs.280987.
Hs.648635.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3THW X-ray 3.09 B 219-1134 [» ]
3THX X-ray 2.70 B 219-1134 [» ]
3THY X-ray 2.89 B 219-1134 [» ]
3THZ X-ray 4.30 B 219-1134 [» ]
ProteinModelPortali P20585.
SMRi P20585. Positions 225-1123.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110574. 24 interactions.
DIPi DIP-35127N.
IntActi P20585. 5 interactions.
MINTi MINT-192778.
STRINGi 9606.ENSP00000265081.

PTM databases

PhosphoSitei P20585.

Polymorphism databases

DMDMi 317373576.

Proteomic databases

MaxQBi P20585.
PaxDbi P20585.
PRIDEi P20585.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265081 ; ENSP00000265081 ; ENSG00000113318 .
GeneIDi 4437.
KEGGi hsa:4437.
UCSCi uc003kgz.4. human.

Organism-specific databases

CTDi 4437.
GeneCardsi GC05P079986.
H-InvDB HIX0032037.
HGNCi HGNC:7326. MSH3.
HPAi HPA036080.
HPA036081.
MIMi 600887. gene.
608089. phenotype.
neXtProti NX_P20585.
PharmGKBi PA31134.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0249.
GeneTreei ENSGT00550000074949.
HOGENOMi HOG000029776.
HOVERGENi HBG006400.
InParanoidi P20585.
KOi K08736.
OMAi ELSIVCI.
OrthoDBi EOG7X6KZF.
PhylomeDBi P20585.
TreeFami TF300525.

Enzyme and pathway databases

Reactomei REACT_228019. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).

Miscellaneous databases

ChiTaRSi MSH3. human.
GeneWikii MSH3.
GenomeRNAii 4437.
NextBioi 17293.
PROi P20585.
SOURCEi Search...

Gene expression databases

Bgeei P20585.
CleanExi HS_MSH3.
Genevestigatori P20585.

Family and domain databases

Gene3Di 3.30.420.110. 1 hit.
3.40.1170.10. 1 hit.
3.40.50.300. 1 hit.
InterProi 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.
[Graphical view ]
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.
[Graphical view ]
SMARTi SM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view ]
SUPFAMi SSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53150. SSF53150. 2 hits.
SSF55271. SSF55271. 1 hit.
PROSITEi PS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of cDNA clones derived from the divergently transcribed gene in the region upstream from the human dihydrofolate reductase gene."
    Fujii H., Shimada T.
    J. Biol. Chem. 264:10057-10064(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-79; ARG-949 AND THR-1045.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MSH2, VARIANTS 57-ALA--ALA-65 DEL; VAL-79 AND ARG-949.
  3. Shimada T., Ikejima M., Watanabe A., Orimo H.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-79; ARG-949 AND THR-1045.
  4. NIEHS SNPs program
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-ALA-ALA-62 INS; VAL-79; LEU-709; ARG-949 AND THR-1045.
  5. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [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], VARIANTS 57-ALA--ALA-65 DEL; VAL-79; ARG-949 AND THR-1045.
    Tissue: Muscle.
  7. "The interaction of DNA mismatch repair proteins with human exonuclease I."
    Schmutte C., Sadoff M.M., Shim K.-S., Acharya S., Fishel R.
    J. Biol. Chem. 276:33011-33018(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EXO1.
  8. "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 THR-1099, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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 THR-1099, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Nine-bp repeat polymorphism in exon 1 of the hMSH3 gene."
    Nakajima E., Orimo H., Ikejima M., Shimada T.
    Jpn. J. Hum. Genet. 40:343-345(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALA-ALA-ALA-62 INS.
  12. "Association between single nucleotide polymorphisms in the hMSH3 gene and sporadic colon cancer with microsatellite instability."
    Orimo H., Nakajima E., Yamamoto M., Ikejima M., Emi M., Shimada T.
    J. Hum. Genet. 45:228-230(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VAL-79 AND THR-1045.

Entry informationi

Entry nameiMSH3_HUMAN
AccessioniPrimary (citable) accession number: P20585
Secondary accession number(s): A1L480
, A1L482, A6NMM6, Q6PJT5, Q86UQ6, Q92867
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 11, 2011
Last modified: November 26, 2014
This is version 138 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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