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Protein

DNA mismatch repair protein PMS1

Gene

PMS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLalpha heterodimer that forms a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downsteam MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats and in the repair of heteroduplex sites present in meiotic recombination intermediates.3 Publications

Kineticsi

  1. KM=1.5 mM for ATP1 Publication

    GO - Molecular functioni

    • ATPase activity Source: SGD
    • ATP binding Source: SGD
    • mismatched DNA binding Source: InterPro

    GO - Biological processi

    • meiotic mismatch repair Source: SGD
    • mismatch repair Source: SGD
    Complete GO annotation...

    Keywords - Biological processi

    DNA damage, DNA repair

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33111-MONOMER.
    ReactomeiREACT_321734. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
    REACT_330788. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA mismatch repair protein PMS1
    Alternative name(s):
    Postmeiotic segregation protein 1
    Gene namesi
    Name:PMS1
    Ordered Locus Names:YNL082W
    ORF Names:N2317
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome XIV

    Organism-specific databases

    CYGDiYNL082w.
    EuPathDBiFungiDB:YNL082W.
    SGDiS000005026. PMS1.

    Subcellular locationi

    GO - Cellular componenti

    • MutLalpha complex Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 301E → A: Reduces ATPase activity by 62%. Displays 60-fold increase in spontaneous mutation accumulation. 2 Publications
    Mutagenesisi34 – 341N → A: Reduces ATPase activity by 84%. Displays 11000-fold increase in spontaneous mutation accumulation. 1 Publication
    Mutagenesisi95 – 951F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication
    Mutagenesisi97 – 971G → A: Displays an increase in spontaneous mutation accumulation. 1 Publication
    Mutagenesisi297 – 2971K → E: Displays a 60-fold increase in spontaneous mutation accumulation. 1 Publication
    Mutagenesisi851 – 8511G → E: Confers a strong defect in the repair of primer strand-specific 1-bp loops during DNA replication, but not during meoitic recombination. Does not impair heterodimer formation. 1 Publication
    Mutagenesisi857 – 8571H → R: Confers a strong defect in the repair of primer strand-specific 1-bp loops during DNA replication, but not during meoitic recombination. Does not impair heterodimer formation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 873873DNA mismatch repair protein PMS1PRO_0000245571Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei393 – 3931Phosphoserine1 Publication
    Modified residuei566 – 5661Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP14242.
    PaxDbiP14242.
    PeptideAtlasiP14242.

    Expressioni

    Gene expression databases

    GenevestigatoriP14242.

    Interactioni

    Subunit structurei

    Heterodimer of MLH1 and PMS1, called MutLalpha, which is the major MMR MutL activity correcting base-base mismatches as well as IDLs. The heterodimer binds double strand DNA independently of a mismatch with positive cooperativity and has more than one DNA binding site. Forms a ternary complex with either the MSH2-MSH6 (MutSalpha) or the MSH2-MSH3 heterodimer (MutSbeta), which recognize and bind to mismatch DNA. Ternary complex formation is promoted by ATP binding.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MLH1P389207EBI-13561,EBI-11003

    Protein-protein interaction databases

    BioGridi35741. 51 interactions.
    DIPiDIP-2416N.
    IntActiP14242. 5 interactions.
    MINTiMINT-625253.

    Structurei

    Secondary structure

    1
    873
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 208Combined sources
    Helixi24 – 3714Combined sources
    Beta strandi41 – 488Combined sources
    Turni49 – 524Combined sources
    Beta strandi53 – 597Combined sources
    Helixi66 – 683Combined sources
    Turni69 – 735Combined sources
    Beta strandi92 – 954Combined sources
    Helixi98 – 1058Combined sources
    Beta strandi106 – 11611Combined sources
    Beta strandi120 – 1256Combined sources
    Beta strandi131 – 1377Combined sources
    Beta strandi140 – 14910Combined sources
    Turni150 – 1534Combined sources
    Helixi155 – 1628Combined sources
    Helixi165 – 18218Combined sources
    Beta strandi187 – 1937Combined sources
    Beta strandi199 – 2046Combined sources
    Helixi211 – 2199Combined sources
    Turni221 – 2266Combined sources
    Beta strandi227 – 2359Combined sources
    Helixi237 – 2393Combined sources
    Beta strandi259 – 2679Combined sources
    Beta strandi274 – 28512Combined sources
    Beta strandi288 – 2903Combined sources
    Helixi293 – 30412Combined sources
    Beta strandi314 – 3196Combined sources
    Helixi322 – 3243Combined sources
    Beta strandi330 – 3323Combined sources
    Helixi341 – 36121Combined sources
    Helixi650 – 6523Combined sources
    Helixi653 – 66513Combined sources
    Helixi668 – 6725Combined sources
    Beta strandi675 – 6806Combined sources
    Turni681 – 6833Combined sources
    Beta strandi684 – 6907Combined sources
    Beta strandi695 – 7017Combined sources
    Helixi702 – 71716Combined sources
    Beta strandi722 – 73110Combined sources
    Helixi739 – 7424Combined sources
    Helixi747 – 7504Combined sources
    Beta strandi767 – 7737Combined sources
    Helixi782 – 79413Combined sources
    Helixi806 – 81914Combined sources
    Helixi829 – 83810Combined sources
    Helixi839 – 8413Combined sources
    Beta strandi842 – 8443Combined sources
    Beta strandi853 – 8608Combined sources
    Helixi869 – 8713Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H4LX-ray2.50A/B1-365[»]
    4E4WX-ray2.50B635-873[»]
    4FMNX-ray2.69B635-873[»]
    4FMOX-ray3.04B635-873[»]
    ProteinModelPortaliP14242.
    SMRiP14242. Positions 6-362, 651-873.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14242.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 357357DNA- and ATP-bindingAdd
    BLAST
    Regioni661 – 873213Interaction with MLH1Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0323.
    GeneTreeiENSGT00530000063289.
    InParanoidiP14242.
    KOiK10858.
    OMAiHIPRPSK.
    OrthoDBiEOG72RN8H.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.565.10. 1 hit.
    InterProiIPR013507. DNA_mismatch_repair_C.
    IPR014762. DNA_mismatch_repair_CS.
    IPR002099. DNA_mismatch_repair_fam.
    IPR003594. HATPase_C.
    IPR014790. MutL_C.
    IPR028831. Pms1/Pms2/PMS2L.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view]
    PANTHERiPTHR10073:SF9. PTHR10073:SF9. 1 hit.
    PfamiPF01119. DNA_mis_repair. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF08676. MutL_C. 1 hit.
    [Graphical view]
    SMARTiSM00387. HATPase_c. 1 hit.
    SM00853. MutL_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 2 hits.
    SSF55874. SSF55874. 1 hit.
    TIGRFAMsiTIGR00585. mutl. 1 hit.
    PROSITEiPS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14242-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTQIHQINDI DVHRITSGQV ITDLTTAVKE LVDNSIDANA NQIEIIFKDY
    60 70 80 90 100
    GLESIECSDN GDGIDPSNYE FLALKHYTSK IAKFQDVAKV QTLGFRGEAL
    110 120 130 140 150
    SSLCGIAKLS VITTTSPPKA DKLEYDMVGH ITSKTTTSRN KGTTVLVSQL
    160 170 180 190 200
    FHNLPVRQKE FSKTFKRQFT KCLTVIQGYA IINAAIKFSV WNITPKGKKN
    210 220 230 240 250
    LILSTMRNSS MRKNISSVFG AGGMRGLEEV DLVLDLNPFK NRMLGKYTDD
    260 270 280 290 300
    PDFLDLDYKI RVKGYISQNS FGCGRNSKDR QFIYVNKRPV EYSTLLKCCN
    310 320 330 340 350
    EVYKTFNNVQ FPAVFLNLEL PMSLIDVNVT PDKRVILLHN ERAVIDIFKT
    360 370 380 390 400
    TLSDYYNRQE LALPKRMCSQ SEQQAQKRLK TEVFDDRSTT HESDNENYHT
    410 420 430 440 450
    ARSESNQSNH AHFNSTTGVI DKSNGTELTS VMDGNYTNVT DVIGSECEVS
    460 470 480 490 500
    VDSSVVLDEG NSSTPTKKLP SIKTDSQNLS DLNLNNFSNP EFQNITSPDK
    510 520 530 540 550
    ARSLEKVVEE PVYFDIDGEK FQEKAVLSQA DGLVFVDNEC HEHTNDCCHQ
    560 570 580 590 600
    ERRGSTDTEQ DDEADSIYAE IEPVEINVRT PLKNSRKSIS KDNYRSLSDG
    610 620 630 640 650
    LTHRKFEDEI LEYNLSTKNF KEISKNGKQM SSIISKRKSE AQENIIKNKD
    660 670 680 690 700
    ELEDFEQGEK YLTLTVSKND FKKMEVVGQF NLGFIIVTRK VDNKYDLFIV
    710 720 730 740 750
    DQHASDEKYN FETLQAVTVF KSQKLIIPQP VELSVIDELV VLDNLPVFEK
    760 770 780 790 800
    NGFKLKIDEE EEFGSRVKLL SLPTSKQTLF DLGDFNELIH LIKEDGGLRR
    810 820 830 840 850
    DNIRCSKIRS MFAMRACRSS IMIGKPLNKK TMTRVVHNLS ELDKPWNCPH
    860 870
    GRPTMRHLME LRDWSSFSKD YEI
    Length:873
    Mass (Da):99,355
    Last modified:July 11, 2006 - v3
    Checksum:i2E0FFBC59B718854
    GO

    Sequence cautioni

    The sequence AAA34885.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAM00521.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAM00533.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAM00545.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAM00551.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAM00563.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence AAM00569.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence CAA60176.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence CAA61428.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence CAA95956.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence CAA95957.1 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti695 – 6951Y → S in AAA34885 (PubMed:2676974).Curated
    Sequence conflicti861 – 8611L → I in AAA34885 (PubMed:2676974).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411N → S in strain: SK1 and YJM421. 2 Publications
    Natural varianti112 – 1121I → T in strain: SK1 and YJM421. 2 Publications
    Natural varianti384 – 3841F → V in strain: SK1, YJM320, YJM339 and YJM421. 2 Publications
    Natural varianti392 – 3921E → V in strain: YJM320. 1 Publication
    Natural varianti400 – 4001T → S in strain: SK1, YJM320, YJM339 and YJM421. 2 Publications
    Natural varianti401 – 4011A → S in strain: YJM320 and YJM421. 1 Publication
    Natural varianti416 – 4161T → TCEGT in strain: SK1, YJM320, YJM339 and YJM421.
    Natural varianti458 – 4581D → Y in strain: EAY1068. 1 Publication
    Natural varianti475 – 4751D → N in strain: YJM339. 1 Publication
    Natural varianti513 – 5131Y → F in strain: SK1. 1 Publication
    Natural varianti564 – 5641A → V in strain: YJM320. 1 Publication
    Natural varianti768 – 7681K → R in strain: YJM320. 1 Publication
    Natural varianti818 – 8181R → K in strain: SK1 and YJM320; forms a non-functional heterodimer with MHL1 from strain S288c, resulting in an accumulation of mutations in spore progeny of crosses between these strains. 2 Publications

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M29688 Genomic DNA. Translation: AAA34885.1. Different initiation.
    AF458969 Genomic DNA. Translation: AAM00521.1. Different initiation.
    AF458971 Genomic DNA. Translation: AAM00533.1. Different initiation.
    AF458973 Genomic DNA. Translation: AAM00545.1. Different initiation.
    AF458974 Genomic DNA. Translation: AAM00551.1. Different initiation.
    AF458976 Genomic DNA. Translation: AAM00563.1. Different initiation.
    AF458977 Genomic DNA. Translation: AAM00569.1. Different initiation.
    DQ115393 Genomic DNA. Translation: AAZ22526.1.
    DQ356628 Genomic DNA. Translation: ABC86932.1.
    DQ356629 Genomic DNA. Translation: ABC86933.1.
    DQ356630 Genomic DNA. Translation: ABC86934.1.
    DQ356631 Genomic DNA. Translation: ABC86935.1.
    DQ356632 Genomic DNA. Translation: ABC86936.1.
    X86470 Genomic DNA. Translation: CAA60176.1. Different initiation.
    Z71357 Genomic DNA. Translation: CAA95956.1. Different initiation.
    Z71358 Genomic DNA. Translation: CAA95957.1. Different initiation.
    X89016 Genomic DNA. Translation: CAA61428.1. Different initiation.
    BK006947 Genomic DNA. Translation: DAA10463.1.
    PIRiS53896.
    RefSeqiNP_014317.4. NM_001182920.3.

    Genome annotation databases

    EnsemblFungiiYNL082W; YNL082W; YNL082W.
    GeneIDi855642.
    KEGGisce:YNL082W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M29688 Genomic DNA. Translation: AAA34885.1. Different initiation.
    AF458969 Genomic DNA. Translation: AAM00521.1. Different initiation.
    AF458971 Genomic DNA. Translation: AAM00533.1. Different initiation.
    AF458973 Genomic DNA. Translation: AAM00545.1. Different initiation.
    AF458974 Genomic DNA. Translation: AAM00551.1. Different initiation.
    AF458976 Genomic DNA. Translation: AAM00563.1. Different initiation.
    AF458977 Genomic DNA. Translation: AAM00569.1. Different initiation.
    DQ115393 Genomic DNA. Translation: AAZ22526.1.
    DQ356628 Genomic DNA. Translation: ABC86932.1.
    DQ356629 Genomic DNA. Translation: ABC86933.1.
    DQ356630 Genomic DNA. Translation: ABC86934.1.
    DQ356631 Genomic DNA. Translation: ABC86935.1.
    DQ356632 Genomic DNA. Translation: ABC86936.1.
    X86470 Genomic DNA. Translation: CAA60176.1. Different initiation.
    Z71357 Genomic DNA. Translation: CAA95956.1. Different initiation.
    Z71358 Genomic DNA. Translation: CAA95957.1. Different initiation.
    X89016 Genomic DNA. Translation: CAA61428.1. Different initiation.
    BK006947 Genomic DNA. Translation: DAA10463.1.
    PIRiS53896.
    RefSeqiNP_014317.4. NM_001182920.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H4LX-ray2.50A/B1-365[»]
    4E4WX-ray2.50B635-873[»]
    4FMNX-ray2.69B635-873[»]
    4FMOX-ray3.04B635-873[»]
    ProteinModelPortaliP14242.
    SMRiP14242. Positions 6-362, 651-873.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35741. 51 interactions.
    DIPiDIP-2416N.
    IntActiP14242. 5 interactions.
    MINTiMINT-625253.

    Proteomic databases

    MaxQBiP14242.
    PaxDbiP14242.
    PeptideAtlasiP14242.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYNL082W; YNL082W; YNL082W.
    GeneIDi855642.
    KEGGisce:YNL082W.

    Organism-specific databases

    CYGDiYNL082w.
    EuPathDBiFungiDB:YNL082W.
    SGDiS000005026. PMS1.

    Phylogenomic databases

    eggNOGiCOG0323.
    GeneTreeiENSGT00530000063289.
    InParanoidiP14242.
    KOiK10858.
    OMAiHIPRPSK.
    OrthoDBiEOG72RN8H.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33111-MONOMER.
    ReactomeiREACT_321734. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
    REACT_330788. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).

    Miscellaneous databases

    EvolutionaryTraceiP14242.
    NextBioi979872.
    PROiP14242.

    Gene expression databases

    GenevestigatoriP14242.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.565.10. 1 hit.
    InterProiIPR013507. DNA_mismatch_repair_C.
    IPR014762. DNA_mismatch_repair_CS.
    IPR002099. DNA_mismatch_repair_fam.
    IPR003594. HATPase_C.
    IPR014790. MutL_C.
    IPR028831. Pms1/Pms2/PMS2L.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view]
    PANTHERiPTHR10073:SF9. PTHR10073:SF9. 1 hit.
    PfamiPF01119. DNA_mis_repair. 1 hit.
    PF02518. HATPase_c. 1 hit.
    PF08676. MutL_C. 1 hit.
    [Graphical view]
    SMARTiSM00387. HATPase_c. 1 hit.
    SM00853. MutL_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 2 hits.
    SSF55874. SSF55874. 1 hit.
    TIGRFAMsiTIGR00585. mutl. 1 hit.
    PROSITEiPS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and nucleotide sequence of DNA mismatch repair gene PMS1 from Saccharomyces cerevisiae: homology of PMS1 to procaryotic MutL and HexB."
      Kramer W., Kramer B., Williamson M.S., Fogel S.
      J. Bacteriol. 171:5339-5346(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Dissecting the architecture of a quantitative trait locus in yeast."
      Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J., McCusker J.H., Davis R.W.
      Nature 416:326-330(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-41; THR-112; VAL-384; VAL-392; SER-400; SER-401; 416-THR--THR-420; ASN-475; VAL-564; ARG-768 AND LYS-818.
      Strain: ATCC 200060 / W303, S96, SK1, YJM 339 and YJM 421.
    3. "Quantitative trait loci mapped to single-nucleotide resolution in yeast."
      Deutschbauer A.M., Davis R.W.
      Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-41; THR-112; VAL-384; SER-400; 416-THR--THR-420; PHE-513 AND LYS-818.
      Strain: SK1.
    4. "Negative epistasis between natural variants of the Saccharomyces cerevisiae MLH1 and PMS1 genes results in a defect in mismatch repair."
      Heck J.A., Argueso J.L., Gemici Z., Reeves R.G., Bernard A., Aquadro C.F., Alani E.
      Proc. Natl. Acad. Sci. U.S.A. 103:3256-3261(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-458.
      Strain: EAY1066, EAY1068, M2-8, M5-7 and M7-8.
    5. "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs."
      Poehlmann R., Philippsen P.
      Yeast 12:391-402(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    6. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    8. "The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading frames."
      Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.
      Yeast 12:485-491(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-225.
      Strain: ATCC 96604 / S288c / FY1679.
    9. "Functional domains of the Saccharomyces cerevisiae Mlh1p and Pms1p DNA mismatch repair proteins and their relevance to human hereditary nonpolyposis colorectal cancer-associated mutations."
      Pang Q., Prolla T.A., Liskay R.M.
      Mol. Cell. Biol. 17:4465-4473(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLH1, MUTAGENESIS OF PHE-95.
    10. "ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes."
      Habraken Y., Sung P., Prakash L., Prakash S.
      J. Biol. Chem. 273:9837-9841(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    11. "Functional specificity of MutL homologs in yeast: evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction."
      Wang T.-F., Kleckner N., Hunter N.
      Proc. Natl. Acad. Sci. U.S.A. 96:13914-13919(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MLH1.
    12. "Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha."
      Tran P.T., Liskay R.M.
      Mol. Cell. Biol. 20:6390-6398(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLH1, ATP-BINDING, MUTAGENESIS OF GLU-30 AND GLY-97.
    13. "DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1 heterodimers."
      Drotschmann K., Hall M.C., Shcherbakova P.V., Wang H., Erie D.A., Brownewell F.R., Kool E.T., Kunkel T.A.
      Biol. Chem. 383:969-975(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING.
    14. "Differential ATP binding and intrinsic ATP hydrolysis by amino-terminal domains of the yeast Mlh1 and Pms1 proteins."
      Hall M.C., Shcherbakova P.V., Kunkel T.A.
      J. Biol. Chem. 277:3673-3679(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ATP-BINDING, MUTAGENESIS OF GLU-30 AND ASN-34, BIOPHYSICOCHEMICAL PROPERTIES.
    15. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
      Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
      Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
    16. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    17. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    18. "DNA binding by yeast Mlh1 and Pms1: implications for DNA mismatch repair."
      Hall M.C., Shcherbakova P.V., Fortune J.M., Borchers C.H., Dial J.M., Tomer K.B., Kunkel T.A.
      Nucleic Acids Res. 31:2025-2034(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, MUTAGENESIS OF LYS-297.
    19. "Novel PMS1 alleles preferentially affect the repair of primer strand loops during DNA replication."
      Erdeniz N., Dudley S., Gealy R., Jinks-Robertson S., Liskay R.M.
      Mol. Cell. Biol. 25:9221-9231(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-851 AND HIS-857.
    20. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPMS1_YEAST
    AccessioniPrimary (citable) accession number: P14242
    Secondary accession number(s): D6W197
    , Q2I044, Q2I045, Q45TY4, Q8TG48, Q8TG50, Q8TG54, Q8TG57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: July 11, 2006
    Last modified: April 29, 2015
    This is version 156 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 521 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.