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P20585

- MSH3_HUMAN

UniProt

P20585 - MSH3_HUMAN

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
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    9. 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

    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 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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MSRRKPASGG LAASSSAPAR QAVLSRFFQS TGSLKSTSSS TGAADQVDPG     50
    AAAAAAAAAA AAPPAPPAPA FPPQLPPHIA TEIDRRKKRP LENDGPVKKK 100
    VKKVQQKEGG SDLGMSGNSE PKKCLRTRNV SKSLEKLKEF CCDSALPQSR 150
    VQTESLQERF AVLPKCTDFD DISLLHAKNA VSSEDSKRQI NQKDTTLFDL 200
    SQFGSSNTSH ENLQKTASKS ANKRSKSIYT PLELQYIEMK QQHKDAVLCV 250
    ECGYKYRFFG EDAEIAAREL NIYCHLDHNF MTASIPTHRL FVHVRRLVAK 300
    GYKVGVVKQT ETAALKAIGD NRSSLFSRKL TALYTKSTLI GEDVNPLIKL 350
    DDAVNVDEIM TDTSTSYLLC ISENKENVRD KKKGNIFIGI VGVQPATGEV 400
    VFDSFQDSAS RSELETRMSS LQPVELLLPS ALSEQTEALI HRATSVSVQD 450
    DRIRVERMDN IYFEYSHAFQ AVTEFYAKDT VDIKGSQIIS GIVNLEKPVI 500
    CSLAAIIKYL KEFNLEKMLS KPENFKQLSS KMEFMTINGT TLRNLEILQN 550
    QTDMKTKGSL LWVLDHTKTS FGRRKLKKWV TQPLLKLREI NARLDAVSEV 600
    LHSESSVFGQ IENHLRKLPD IERGLCSIYH KKCSTQEFFL IVKTLYHLKS 650
    EFQAIIPAVN SHIQSDLLRT VILEIPELLS PVEHYLKILN EQAAKVGDKT 700
    ELFKDLSDFP LIKKRKDEIQ GVIDEIRMHL QEIRKILKNP SAQYVTVSGQ 750
    EFMIEIKNSA VSCIPTDWVK VGSTKAVSRF HSPFIVENYR HLNQLREQLV 800
    LDCSAEWLDF LEKFSEHYHS LCKAVHHLAT VDCIFSLAKV AKQGDYCRPT 850
    VQEERKIVIK NGRHPVIDVL LGEQDQYVPN NTDLSEDSER VMIITGPNMG 900
    GKSSYIKQVA LITIMAQIGS YVPAEEATIG IVDGIFTRMG AADNIYKGQS 950
    TFMEELTDTA EIIRKATSQS LVILDELGRG TSTHDGIAIA YATLEYFIRD 1000
    VKSLTLFVTH YPPVCELEKN YSHQVGNYHM GFLVSEDESK LDPGAAEQVP 1050
    DFVTFLYQIT RGIAARSYGL NVAKLADVPG EILKKAAHKS KELEGLINTK 1100
    RKRLKYFAKL WTMHNAQDLQ KWTEEFNMEE TQTSLLH 1137
    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.

    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.
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMi HOG000029776.
    HOVERGENi HBG006400.
    InParanoidi P20585.
    KOi K08736.
    OMAi ELSIVCI.
    OrthoDBi EOG7X6KZF.
    PhylomeDBi P20585.
    TreeFami TF300525.

    Miscellaneous databases

    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

    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: October 1, 2014
    This is version 136 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