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Protein

DNA mismatch repair protein MLH1

Gene

MLH1

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 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

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

    GO - Biological processi

    • meiotic heteroduplex formation Source: SGD
    • meiotic mismatch repair Source: SGD
    • mismatch repair Source: SGD
    • reciprocal meiotic recombination Source: SGD
    Complete GO annotation...

    Keywords - Biological processi

    DNA damage, DNA repair

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32857-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 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 Componenti: Chromosome XIII

    Organism-specific databases

    CYGDiYMR167w.
    EuPathDBiFungiDB:YMR167W.
    SGDiS000004777. MLH1.

    Subcellular locationi

    GO - Cellular componenti

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

    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. 2 Publications
    Mutagenesisi35 – 351N → A: Abolishes ATP binding, reducing ATPase activity by 95%. Displays 9800-fold increase in spontaneous mutation accumulation. 1 Publication
    Mutagenesisi41 – 411A → F: Defective in a mismatch repair assay. Abolishes heterodimer formation. Displays an increases spontaneous mutation accumulation. 2 Publications
    Mutagenesisi41 – 411A → G: Reduces heterodimer formation. Displays an weak increase in spontaneous mutation accumulation. 2 Publications
    Mutagenesisi41 – 411A → S: Fully functional in a mismatch repair assay. 2 Publications
    Mutagenesisi64 – 641G → R: Defective in a mismatch repair assay. 1 Publication
    Mutagenesisi65 – 651I → N: Defective in a mismatch repair assay. 1 Publication
    Mutagenesisi96 – 961F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication
    Mutagenesisi97 – 971R → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication
    Mutagenesisi98 – 981G → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 2 Publications
    Mutagenesisi98 – 981G → V: Abolishes heterodimer formation. Displays an increase in spontaneous mutation accumulation. 2 Publications
    Mutagenesisi99 – 991E → K: Defective in a mismatch repair assay. 1 Publication
    Mutagenesisi104 – 1041I → R: Defective in a mismatch repair assay. 1 Publication
    Mutagenesisi114 – 1141T → R: Defective in a mismatch repair assay. 1 Publication
    Mutagenesisi214 – 2141R → C: Partially defective in a mismatch repair assay. 1 Publication
    Mutagenesisi216 – 2161V → I: Fully functional in a mismatch repair assay. 1 Publication
    Mutagenesisi265 – 2651R → C: Partially defective in a mismatch repair assay. 1 Publication
    Mutagenesisi265 – 2651R → H: Partially defective in a mismatch repair assay. 1 Publication
    Mutagenesisi273 – 2731R → E: Strongly reduces DNA-binding and displays 12000-fold increase in spontaneous mutation accumulation; when associated with E-274. 1 Publication
    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. 1 Publication
    Mutagenesisi326 – 3261I → A: Partially defective in a mismatch repair assay. 1 Publication
    Mutagenesisi326 – 3261I → V: Fully functional in a mismatch repair assay. 1 Publication
    Mutagenesisi552 – 5521Q → L: Defective in a mismatch repair assay. 1 Publication
    Mutagenesisi672 – 6721R → P: Defective in a mismatch repair assay. 1 Publication
    Mutagenesisi694 – 6941A → T: Fully functional in a mismatch repair assay. 1 Publication
    Mutagenesisi764 – 7641K → E: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication
    Mutagenesisi764 – 7641K → R: No effect. 1 Publication
    Mutagenesisi766 – 7661F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication
    Mutagenesisi767 – 7671E → D: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication
    Mutagenesisi769 – 7691C → A: No effect. 1 Publication
    Mutagenesisi769 – 7691C → S: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication

    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 – 52413Combined sources
    Helixi527 – 5348Combined sources
    Beta strandi537 – 5437Combined sources
    Turni544 – 5474Combined sources
    Beta strandi548 – 5536Combined sources
    Beta strandi556 – 5616Combined sources
    Helixi562 – 57716Combined sources
    Beta strandi582 – 5854Combined sources
    Helixi591 – 5933Combined sources
    Helixi597 – 6015Combined sources
    Helixi610 – 62213Combined sources
    Helixi624 – 6318Combined sources
    Beta strandi634 – 6396Combined sources
    Helixi644 – 6463Combined sources
    Beta strandi647 – 6548Combined sources
    Helixi666 – 67510Combined sources
    Helixi682 – 69716Combined sources
    Helixi714 – 73320Combined sources
    Helixi735 – 7428Combined sources
    Helixi747 – 7526Combined sources
    Beta strandi753 – 7586Combined sources
    Helixi759 – 7657Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4E4WX-ray2.50A485-769[»]
    4FMNX-ray2.69A485-769[»]
    4FMOX-ray3.04A485-769[»]
    ProteinModelPortaliP38920.
    SMRiP38920. Positions 5-303, 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

    GeneTreeiENSGT00790000123052.
    InParanoidiP38920.
    KOiK08734.
    OMAiMVRTDCR.
    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_C.
    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

            10         20         30         40         50
    MSLRIKALDA SVVNKIAAGE IIISPVNALK EMMENSIDAN ATMIDILVKE
    60 70 80 90 100
    GGIKVLQITD NGSGINKADL PILCERFTTS KLQKFEDLSQ IQTYGFRGEA
    110 120 130 140 150
    LASISHVARV TVTTKVKEDR CAWRVSYAEG KMLESPKPVA GKDGTTILVE
    160 170 180 190 200
    DLFFNIPSRL RALRSHNDEY SKILDVVGRY AIHSKDIGFS CKKFGDSNYS
    210 220 230 240 250
    LSVKPSYTVQ DRIRTVFNKS VASNLITFHI SKVEDLNLES VDGKVCNLNF
    260 270 280 290 300
    ISKKSISPIF FINNRLVTCD LLRRALNSVY SNYLPKGNRP FIYLGIVIDP
    310 320 330 340 350
    AAVDVNVHPT KREVRFLSQD EIIEKIANQL HAELSAIDTS RTFKASSIST
    360 370 380 390 400
    NKPESLIPFN DTIESDRNRK SLRQAQVVEN SYTTANSQLR KAKRQENKLV
    410 420 430 440 450
    RIDASQAKIT SFLSSSQQFN FEGSSTKRQL SEPKVTNVSH SQEAEKLTLN
    460 470 480 490 500
    ESEQPRDANT INDNDLKDQP KKKQKLGDYK VPSIADDEKN ALPISKDGYI
    510 520 530 540 550
    RVPKERVNVN LTSIKKLREK VDDSIHRELT DIFANLNYVG VVDEERRLAA
    560 570 580 590 600
    IQHDLKLFLI DYGSVCYELF YQIGLTDFAN FGKINLQSTN VSDDIVLYNL
    610 620 630 640 650
    LSEFDELNDD ASKEKIISKI WDMSSMLNEY YSIELVNDGL DNDLKSVKLK
    660 670 680 690 700
    SLPLLLKGYI PSLVKLPFFI YRLGKEVDWE DEQECLDGIL REIALLYIPD
    710 720 730 740 750
    MVPKVDTSDA SLSEDEKAQF INRKEHISSL LEHVLFPCIK RRFLAPRHIL
    760
    KDVVEIANLP DLYKVFERC
    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:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4E4WX-ray2.50A485-769[»]
    4FMNX-ray2.69A485-769[»]
    4FMOX-ray3.04A485-769[»]
    ProteinModelPortaliP38920.
    SMRiP38920. Positions 5-303, 509-769.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Proteomic databases

    MaxQBiP38920.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CYGDiYMR167w.
    EuPathDBiFungiDB:YMR167W.
    SGDiS000004777. MLH1.

    Phylogenomic databases

    GeneTreeiENSGT00790000123052.
    InParanoidiP38920.
    KOiK08734.
    OMAiMVRTDCR.
    OrthoDBiEOG72RN8H.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32857-MONOMER.
    ReactomeiREACT_321734. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
    REACT_330788. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).

    Miscellaneous databases

    NextBioi978693.
    PROiP38920.

    Gene expression databases

    GenevestigatoriP38920.

    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_C.
    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: May 27, 2015
    This is version 146 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

    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.