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P38920

- MLH1_YEAST

UniProt

P38920 - MLH1_YEAST

Protein

DNA mismatch repair protein MLH1

Gene

MLH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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 different MutL heterodimers that form 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, the repair of heteroduplex sites present in meiotic recombination intermediates, and the promotion of meiotic crossing-over.3 Publications

    Kineticsi

    1. KM=69 µM for ATP1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. meiotic heteroduplex formation Source: SGD
    3. meiotic mismatch repair Source: SGD
    4. mismatch repair Source: SGD
    5. reciprocal meiotic recombination Source: SGD

    Keywords - Biological processi

    DNA damage, DNA repair

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32857-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA mismatch repair protein MLH1
    Alternative name(s):
    MutL protein homolog 1
    Post meiotic segregation protein 2
    Gene namesi
    Name:MLH1
    Synonyms:PMS2
    Ordered Locus Names:YMR167W
    ORF Names:YM8520.16
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR167w.
    SGDiS000004777. MLH1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. MutLalpha complex Source: SGD
    2. MutLgamma complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi31 – 311E → A: Reduces ATPase activity by 98%. Displays 3300-fold increase in spontaneous mutation accumulation. 3 Publications
    Mutagenesisi35 – 351N → A: Abolishes ATP binding, reducing ATPase activity by 95%. Displays 9800-fold increase in spontaneous mutation accumulation. 2 Publications
    Mutagenesisi41 – 411A → F: Defective in a mismatch repair assay. Abolishes heterodimer formation. Displays an increases spontaneous mutation accumulation. 3 Publications
    Mutagenesisi41 – 411A → G: Reduces heterodimer formation. Displays an weak increase in spontaneous mutation accumulation. 3 Publications
    Mutagenesisi41 – 411A → S: Fully functional in a mismatch repair assay. 3 Publications
    Mutagenesisi64 – 641G → R: Defective in a mismatch repair assay. 2 Publications
    Mutagenesisi65 – 651I → N: Defective in a mismatch repair assay. 2 Publications
    Mutagenesisi96 – 961F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 2 Publications
    Mutagenesisi97 – 971R → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 2 Publications
    Mutagenesisi98 – 981G → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 3 Publications
    Mutagenesisi98 – 981G → V: Abolishes heterodimer formation. Displays an increase in spontaneous mutation accumulation. 3 Publications
    Mutagenesisi99 – 991E → K: Defective in a mismatch repair assay. 2 Publications
    Mutagenesisi104 – 1041I → R: Defective in a mismatch repair assay. 2 Publications
    Mutagenesisi114 – 1141T → R: Defective in a mismatch repair assay. 2 Publications
    Mutagenesisi214 – 2141R → C: Partially defective in a mismatch repair assay. 2 Publications
    Mutagenesisi216 – 2161V → I: Fully functional in a mismatch repair assay. 2 Publications
    Mutagenesisi265 – 2651R → C: Partially defective in a mismatch repair assay. 2 Publications
    Mutagenesisi265 – 2651R → H: Partially defective in a mismatch repair assay. 2 Publications
    Mutagenesisi273 – 2731R → E: Strongly reduces DNA-binding and displays 12000-fold increase in spontaneous mutation accumulation; when associated with E-274. 2 Publications
    Mutagenesisi274 – 2741R → E: Reduces DNA-binding and displays a 1700-fold increase in spontaneous mutation accumulation. Strongly reduces DNA-binding and displays 12000-fold increase in spontaneous mutation accumulation; when associated with E-273. 2 Publications
    Mutagenesisi326 – 3261I → A: Partially defective in a mismatch repair assay. 2 Publications
    Mutagenesisi326 – 3261I → V: Fully functional in a mismatch repair assay. 2 Publications
    Mutagenesisi552 – 5521Q → L: Defective in a mismatch repair assay. 2 Publications
    Mutagenesisi672 – 6721R → P: Defective in a mismatch repair assay. 2 Publications
    Mutagenesisi694 – 6941A → T: Fully functional in a mismatch repair assay. 2 Publications
    Mutagenesisi764 – 7641K → E: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 2 Publications
    Mutagenesisi764 – 7641K → R: No effect. 2 Publications
    Mutagenesisi766 – 7661F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 2 Publications
    Mutagenesisi767 – 7671E → D: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 2 Publications
    Mutagenesisi769 – 7691C → A: No effect. 2 Publications
    Mutagenesisi769 – 7691C → S: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 769769DNA mismatch repair protein MLH1PRO_0000178008Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei441 – 4411Phosphoserine; by ATM or ATR1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38920.

    Expressioni

    Gene expression databases

    GenevestigatoriP38920.

    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. Heterodimer of MLH1 and MLH3, called MutLbeta, which is involved in correction of a specific subset of IDLs when associated with MutSbeta. Heterodimer of MLH1 and MLH2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MLH2Q079805EBI-11003,EBI-33369
    MLH3Q120834EBI-11003,EBI-31634
    PMS1P142427EBI-11003,EBI-13561

    Protein-protein interaction databases

    BioGridi35345. 96 interactions.
    DIPiDIP-2412N.
    IntActiP38920. 7 interactions.
    MINTiMINT-625234.

    Structurei

    Secondary structure

    1
    769
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi512 – 52413
    Helixi527 – 5348
    Beta strandi537 – 5437
    Turni544 – 5474
    Beta strandi548 – 5536
    Beta strandi556 – 5616
    Helixi562 – 57716
    Beta strandi582 – 5854
    Helixi591 – 5933
    Helixi597 – 6015
    Helixi610 – 62213
    Helixi624 – 6318
    Beta strandi634 – 6396
    Helixi644 – 6463
    Beta strandi647 – 6548
    Helixi666 – 67510
    Helixi682 – 69716
    Helixi714 – 73320
    Helixi735 – 7428
    Helixi747 – 7526
    Beta strandi753 – 7586
    Helixi759 – 7657

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4E4WX-ray2.50A485-769[»]
    4FMNX-ray2.69A485-769[»]
    4FMOX-ray3.04A485-769[»]
    ProteinModelPortaliP38920.
    SMRiP38920. Positions 5-324, 509-769.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 335335DNA- and ATP-bindingAdd
    BLAST
    Regioni501 – 756256Interaction with PMS1Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00550000074923.
    KOiK08734.
    OMAiINHRCVE.
    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.
    IPR011186. DNA_mismatch_repair_MLH1/HexB.
    IPR003594. HATPase_ATP-bd.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view]
    PANTHERiPTHR10073:SF12. PTHR10073:SF12. 1 hit.
    PfamiPF01119. DNA_mis_repair. 1 hit.
    [Graphical view]
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    TIGRFAMsiTIGR00585. mutl. 1 hit.
    PROSITEiPS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38920-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLRIKALDA SVVNKIAAGE IIISPVNALK EMMENSIDAN ATMIDILVKE    50
    GGIKVLQITD NGSGINKADL PILCERFTTS KLQKFEDLSQ IQTYGFRGEA 100
    LASISHVARV TVTTKVKEDR CAWRVSYAEG KMLESPKPVA GKDGTTILVE 150
    DLFFNIPSRL RALRSHNDEY SKILDVVGRY AIHSKDIGFS CKKFGDSNYS 200
    LSVKPSYTVQ DRIRTVFNKS VASNLITFHI SKVEDLNLES VDGKVCNLNF 250
    ISKKSISPIF FINNRLVTCD LLRRALNSVY SNYLPKGNRP FIYLGIVIDP 300
    AAVDVNVHPT KREVRFLSQD EIIEKIANQL HAELSAIDTS RTFKASSIST 350
    NKPESLIPFN DTIESDRNRK SLRQAQVVEN SYTTANSQLR KAKRQENKLV 400
    RIDASQAKIT SFLSSSQQFN FEGSSTKRQL SEPKVTNVSH SQEAEKLTLN 450
    ESEQPRDANT INDNDLKDQP KKKQKLGDYK VPSIADDEKN ALPISKDGYI 500
    RVPKERVNVN LTSIKKLREK VDDSIHRELT DIFANLNYVG VVDEERRLAA 550
    IQHDLKLFLI DYGSVCYELF YQIGLTDFAN FGKINLQSTN VSDDIVLYNL 600
    LSEFDELNDD ASKEKIISKI WDMSSMLNEY YSIELVNDGL DNDLKSVKLK 650
    SLPLLLKGYI PSLVKLPFFI YRLGKEVDWE DEQECLDGIL REIALLYIPD 700
    MVPKVDTSDA SLSEDEKAQF INRKEHISSL LEHVLFPCIK RRFLAPRHIL 750
    KDVVEIANLP DLYKVFERC 769
    Length:769
    Mass (Da):87,062
    Last modified:October 1, 1996 - v2
    Checksum:iB2DBB31DE3943171
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti258 – 2581P → L in AAA16835. (PubMed:8264608)Curated
    Sequence conflicti288 – 2881N → F in AAA16835. (PubMed:8264608)Curated
    Sequence conflicti708 – 7081S → L in AAA16835. (PubMed:8264608)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti240 – 2401S → R in strain: SK1. 1 Publication
    Natural varianti242 – 2421D → E in strain: YJM326 and YJM339. 1 Publication
    Natural varianti271 – 2711L → P in strain: EAY1066, EAY1068, M2-8, M7-8, M5-7, SK1, YJM269, YJM280, YJM320, YJM326, YJM339 and YJM627. 1 Publication
    Natural varianti309 – 3091P → L in strain: M2-8. 1 Publication
    Natural varianti321 – 3211E → D in strain: EAY1066. 1 Publication
    Natural varianti333 – 3331E → K in strain: SK1. 1 Publication
    Natural varianti375 – 3751A → T in strain: YJM339. 1 Publication
    Natural varianti452 – 4521S → G in strain: EAY1068, M2-8, M7-8, M5-7, YJM269 and YJM627. 1 Publication
    Natural varianti465 – 4651D → N in strain: EAY1066 and YJM280. 1 Publication
    Natural varianti470 – 4701P → S in strain: YJM339. 1 Publication
    Natural varianti607 – 6071L → F in strain: EAY1068, M2-8, M7-8, M5-7 and YJM627. 1 Publication
    Natural varianti678 – 6781D → N in strain: SK1, YJM320 and YJM339. 1 Publication
    Natural varianti703 – 7031P → L in strain: SK1, YJM320 and YJM339. 1 Publication
    Natural varianti761 – 7611D → G in strain: EAY1066, EAY1068, M2-8, M7-8, M5-7, SK1, YJM145, YJM269, YJM320, YJM339 and YJM627; forms a non-functional heterodimer with PMS1 from strain S288c, resulting in an accumulation of mutations in spore progeny of crosses between these strains. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07187 Unassigned DNA. Translation: AAA16835.1.
    DQ356633 Genomic DNA. Translation: ABC86937.1.
    DQ356634 Genomic DNA. Translation: ABC86938.1.
    DQ356635 Genomic DNA. Translation: ABC86939.1.
    DQ356636 Genomic DNA. Translation: ABC86940.1.
    DQ356637 Genomic DNA. Translation: ABC86941.1.
    DQ356638 Genomic DNA. Translation: ABC86942.1.
    DQ356639 Genomic DNA. Translation: ABC86943.1.
    DQ356640 Genomic DNA. Translation: ABC86944.1.
    DQ356641 Genomic DNA. Translation: ABC86945.1.
    DQ356642 Genomic DNA. Translation: ABC86946.1.
    DQ356643 Genomic DNA. Translation: ABC86947.1.
    DQ356644 Genomic DNA. Translation: ABC86948.1.
    DQ356645 Genomic DNA. Translation: ABC86949.1.
    DQ356646 Genomic DNA. Translation: ABC86950.1.
    Z49705 Genomic DNA. Translation: CAA89803.1.
    BK006946 Genomic DNA. Translation: DAA10063.1.
    PIRiS54525.
    RefSeqiNP_013890.1. NM_001182671.1.

    Genome annotation databases

    EnsemblFungiiYMR167W; YMR167W; YMR167W.
    GeneIDi855203.
    KEGGisce:YMR167W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07187 Unassigned DNA. Translation: AAA16835.1 .
    DQ356633 Genomic DNA. Translation: ABC86937.1 .
    DQ356634 Genomic DNA. Translation: ABC86938.1 .
    DQ356635 Genomic DNA. Translation: ABC86939.1 .
    DQ356636 Genomic DNA. Translation: ABC86940.1 .
    DQ356637 Genomic DNA. Translation: ABC86941.1 .
    DQ356638 Genomic DNA. Translation: ABC86942.1 .
    DQ356639 Genomic DNA. Translation: ABC86943.1 .
    DQ356640 Genomic DNA. Translation: ABC86944.1 .
    DQ356641 Genomic DNA. Translation: ABC86945.1 .
    DQ356642 Genomic DNA. Translation: ABC86946.1 .
    DQ356643 Genomic DNA. Translation: ABC86947.1 .
    DQ356644 Genomic DNA. Translation: ABC86948.1 .
    DQ356645 Genomic DNA. Translation: ABC86949.1 .
    DQ356646 Genomic DNA. Translation: ABC86950.1 .
    Z49705 Genomic DNA. Translation: CAA89803.1 .
    BK006946 Genomic DNA. Translation: DAA10063.1 .
    PIRi S54525.
    RefSeqi NP_013890.1. NM_001182671.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4E4W X-ray 2.50 A 485-769 [» ]
    4FMN X-ray 2.69 A 485-769 [» ]
    4FMO X-ray 3.04 A 485-769 [» ]
    ProteinModelPortali P38920.
    SMRi P38920. Positions 5-324, 509-769.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35345. 96 interactions.
    DIPi DIP-2412N.
    IntActi P38920. 7 interactions.
    MINTi MINT-625234.

    Proteomic databases

    MaxQBi P38920.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR167W ; YMR167W ; YMR167W .
    GeneIDi 855203.
    KEGGi sce:YMR167W.

    Organism-specific databases

    CYGDi YMR167w.
    SGDi S000004777. MLH1.

    Phylogenomic databases

    GeneTreei ENSGT00550000074923.
    KOi K08734.
    OMAi INHRCVE.
    OrthoDBi EOG72RN8H.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32857-MONOMER.

    Miscellaneous databases

    NextBioi 978693.
    PROi P38920.

    Gene expression databases

    Genevestigatori P38920.

    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.
    IPR011186. DNA_mismatch_repair_MLH1/HexB.
    IPR003594. HATPase_ATP-bd.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view ]
    PANTHERi PTHR10073:SF12. PTHR10073:SF12. 1 hit.
    Pfami PF01119. DNA_mis_repair. 1 hit.
    [Graphical view ]
    SMARTi SM00387. HATPase_c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    TIGRFAMsi TIGR00585. mutl. 1 hit.
    PROSITEi PS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dual requirement in yeast DNA mismatch repair for MLH1 and PMS1, two homologs of the bacterial mutL gene."
      Prolla T.A., Christie D.-M., Liskay R.M.
      Mol. Cell. Biol. 14:407-415(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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], VARIANTS ARG-240; GLU-242; PRO-271; LEU-309; ASP-321; LYS-333; THR-375; GLY-452; ASN-465; SER-470; PHE-607; ASN-678; LEU-703 AND GLY-761.
      Strain: ATCC 200060 / W303, EAY1066, EAY1068, M2-8, M5-7, M7-8, SK1, YJM 145, YJM 269, YJM 280, YJM 320, YJM 326, YJM 339 and YJM 627.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Functional analysis of human MLH1 and MSH2 missense variants and hybrid human-yeast MLH1 proteins in Saccharomyces cerevisiae."
      Ellison A.R., Lofing J., Bitter G.A.
      Hum. Mol. Genet. 10:1889-1900(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ALA-41; GLY-64; ILE-65; GLU-99; ILE-104; THR-114; ARG-214; VAL-216; ARG-265; ILE-326; GLN-552; ARG-672 AND ALA-694.
    6. "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 PMS1, MUTAGENESIS OF ALA-41; PHE-96; ARG-97; GLY-98; LYS-764; PHE-766; GLU-767 AND CYS-769.
    7. "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.
    8. "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 MLH2; MLH3 AND PMS1.
    9. "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 PMS1, ATP-BINDING, MUTAGENESIS OF GLU-31 AND GLY-98.
    10. "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.
    11. "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-31 AND ASN-35, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "Systematic mutagenesis of the Saccharomyces cerevisiae MLH1 gene reveals distinct roles for Mlh1p in meiotic crossing over and in vegetative and meiotic mismatch repair."
      Argueso J.L., Kijas A.W., Sarin S., Heck J.A., Waase M., Alani E.
      Mol. Cell. Biol. 23:873-886(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS.
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    15. "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 ARG-273 AND ARG-274.
    16. "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-441, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMLH1_YEAST
    AccessioniPrimary (citable) accession number: P38920
    Secondary accession number(s): D6VZY9
    , Q2I028, Q2I029, Q2I031, Q2I032, Q2I033, Q2I034, Q2I035, Q2I036, Q2I038, Q2I039, Q2I041
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 319 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3