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P14242

- PMS1_YEAST

UniProt

P14242 - PMS1_YEAST

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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: 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

  1. ATPase activity Source: SGD
  2. ATP binding Source: SGD
  3. mismatched DNA binding Source: InterPro

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. meiotic mismatch repair Source: SGD
  3. mismatch repair Source: SGD
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BioCyciYEAST:G3O-33111-MONOMER.
ReactomeiREACT_238711. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_239457. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).

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: Chromosome XIV

Organism-specific databases

CYGDiYNL082w.
SGDiS000005026. PMS1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. 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.
OMAiGQFNHGF.
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 .
PIRi S53896.
RefSeqi NP_014317.4. NM_001182920.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3H4L X-ray 2.50 A/B 1-365 [» ]
4E4W X-ray 2.50 B 635-873 [» ]
4FMN X-ray 2.69 B 635-873 [» ]
4FMO X-ray 3.04 B 635-873 [» ]
ProteinModelPortali P14242.
SMRi P14242. Positions 6-362, 651-873.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35741. 51 interactions.
DIPi DIP-2416N.
IntActi P14242. 5 interactions.
MINTi MINT-625253.

Proteomic databases

MaxQBi P14242.
PaxDbi P14242.
PeptideAtlasi P14242.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YNL082W ; YNL082W ; YNL082W .
GeneIDi 855642.
KEGGi sce:YNL082W.

Organism-specific databases

CYGDi YNL082w.
SGDi S000005026. PMS1.

Phylogenomic databases

eggNOGi COG0323.
GeneTreei ENSGT00530000063289.
InParanoidi P14242.
KOi K10858.
OMAi GQFNHGF.
OrthoDBi EOG72RN8H.

Enzyme and pathway databases

BioCyci YEAST:G3O-33111-MONOMER.
Reactomei REACT_238711. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
REACT_239457. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).

Miscellaneous databases

EvolutionaryTracei P14242.
NextBioi 979872.
PROi P14242.

Gene expression databases

Genevestigatori P14242.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
InterProi IPR013507. 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 ]
PANTHERi PTHR10073:SF9. PTHR10073:SF9. 1 hit.
Pfami PF01119. DNA_mis_repair. 1 hit.
PF02518. HATPase_c. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view ]
SMARTi SM00387. HATPase_c. 1 hit.
SM00853. MutL_C. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 2 hits.
SSF55874. SSF55874. 1 hit.
TIGRFAMsi TIGR00585. mutl. 1 hit.
PROSITEi PS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 152 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