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P38920

- MLH1_YEAST

UniProt

P38920 - MLH1_YEAST

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Protein
DNA mismatch repair protein MLH1
Gene
MLH1, PMS2, YMR167W, YM8520.16
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 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. ATP binding Source: SGD
  2. ATPase activity 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
Complete GO annotation...

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
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 MLH1
PRO_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

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 335335DNA- and ATP-binding
Add
BLAST
Regioni501 – 756256Interaction with PMS1
Add
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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti258 – 2581P → L in AAA16835. 1 Publication
Sequence conflicti288 – 2881N → F in AAA16835. 1 Publication
Sequence conflicti708 – 7081S → L in AAA16835. 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

« 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: July 9, 2014
This is version 138 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.

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

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