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Entry version 199 (29 Sep 2021)
Sequence version 2 (01 Oct 1996)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

Present with 319 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=69 µM for ATP1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processDNA damage, DNA repair

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.1.3, 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA mismatch repair protein MLH1
Alternative name(s):
MutL protein homolog 1
Post meiotic segregation protein 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MLH1
Synonyms:PMS2
Ordered Locus Names:YMR167W
ORF Names:YM8520.16
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XIII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000004777, MLH1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YMR167W

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi31E → A: Reduces ATPase activity by 98%. Displays 3300-fold increase in spontaneous mutation accumulation. 2 Publications1
Mutagenesisi35N → A: Abolishes ATP binding, reducing ATPase activity by 95%. Displays 9800-fold increase in spontaneous mutation accumulation. 1 Publication1
Mutagenesisi41A → F: Defective in a mismatch repair assay. Abolishes heterodimer formation. Displays an increases spontaneous mutation accumulation. 2 Publications1
Mutagenesisi41A → G: Reduces heterodimer formation. Displays an weak increase in spontaneous mutation accumulation. 2 Publications1
Mutagenesisi41A → S: Fully functional in a mismatch repair assay. 2 Publications1
Mutagenesisi64G → R: Defective in a mismatch repair assay. 1 Publication1
Mutagenesisi65I → N: Defective in a mismatch repair assay. 1 Publication1
Mutagenesisi96F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication1
Mutagenesisi97R → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication1
Mutagenesisi98G → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 2 Publications1
Mutagenesisi98G → V: Abolishes heterodimer formation. Displays an increase in spontaneous mutation accumulation. 2 Publications1
Mutagenesisi99E → K: Defective in a mismatch repair assay. 1 Publication1
Mutagenesisi104I → R: Defective in a mismatch repair assay. 1 Publication1
Mutagenesisi114T → R: Defective in a mismatch repair assay. 1 Publication1
Mutagenesisi214R → C: Partially defective in a mismatch repair assay. 1 Publication1
Mutagenesisi216V → I: Fully functional in a mismatch repair assay. 1 Publication1
Mutagenesisi265R → C: Partially defective in a mismatch repair assay. 1 Publication1
Mutagenesisi265R → H: Partially defective in a mismatch repair assay. 1 Publication1
Mutagenesisi273R → E: Strongly reduces DNA-binding and displays 12000-fold increase in spontaneous mutation accumulation; when associated with E-274. 1 Publication1
Mutagenesisi274R → 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 Publication1
Mutagenesisi326I → A: Partially defective in a mismatch repair assay. 1 Publication1
Mutagenesisi326I → V: Fully functional in a mismatch repair assay. 1 Publication1
Mutagenesisi552Q → L: Defective in a mismatch repair assay. 1 Publication1
Mutagenesisi672R → P: Defective in a mismatch repair assay. 1 Publication1
Mutagenesisi694A → T: Fully functional in a mismatch repair assay. 1 Publication1
Mutagenesisi764K → E: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication1
Mutagenesisi764K → R: No effect. 1 Publication1
Mutagenesisi766F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication1
Mutagenesisi767E → D: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication1
Mutagenesisi769C → A: No effect. 1 Publication1
Mutagenesisi769C → S: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001780081 – 769DNA mismatch repair protein MLH1Add BLAST769

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei441Phosphoserine; by ATM or ATRCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P38920

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P38920

PRoteomics IDEntifications database

More...
PRIDEi
P38920

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P38920

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
35345, 229 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1666, MutLalpha endonuclease complex
CPX-1667, MutLbeta endonuclease complex
CPX-1668, MLH1-MLH3 endonuclease complex

Database of interacting proteins

More...
DIPi
DIP-2412N

Protein interaction database and analysis system

More...
IntActi
P38920, 17 interactors

Molecular INTeraction database

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MINTi
P38920

STRING: functional protein association networks

More...
STRINGi
4932.YMR167W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P38920, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1769
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P38920

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 335DNA- and ATP-bindingAdd BLAST335
Regioni422 – 480DisorderedSequence analysisAdd BLAST59
Regioni501 – 756Interaction with PMS1Add BLAST256

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi422 – 445Polar residuesSequence analysisAdd BLAST24
Compositional biasi446 – 480Basic and acidic residuesSequence analysisAdd BLAST35

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1979, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00800000124177

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_004131_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P38920

Identification of Orthologs from Complete Genome Data

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OMAi
GHPFIYL

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.230.10, 1 hit
3.30.565.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR014762, DNA_mismatch_repair_CS
IPR002099, DNA_mismatch_repair_N
IPR013507, DNA_mismatch_S5_2-like
IPR036890, HATPase_C_sf
IPR032189, Mlh1_C
IPR038973, MutL/Mlh/Pms
IPR020568, Ribosomal_S5_D2-typ_fold
IPR014721, Ribosomal_S5_D2-typ_fold_subgr

The PANTHER Classification System

More...
PANTHERi
PTHR10073, PTHR10073, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01119, DNA_mis_repair, 1 hit
PF16413, Mlh1_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01340, DNA_mis_repair, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54211, SSF54211, 1 hit
SSF55874, SSF55874, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00585, mutl, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00058, DNA_MISMATCH_REPAIR_1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB2DBB31DE3943171
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti258P → L in AAA16835 (PubMed:8264608).Curated1
Sequence conflicti288N → F in AAA16835 (PubMed:8264608).Curated1
Sequence conflicti708S → L in AAA16835 (PubMed:8264608).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti240S → R in strain: SK1. 1 Publication1
Natural varianti242D → E in strain: YJM326 and YJM339. 1 Publication1
Natural varianti271L → P in strain: EAY1066, EAY1068, M2-8, M7-8, M5-7, SK1, YJM269, YJM280, YJM320, YJM326, YJM339 and YJM627. 1 Publication1
Natural varianti309P → L in strain: M2-8. 1 Publication1
Natural varianti321E → D in strain: EAY1066. 1 Publication1
Natural varianti333E → K in strain: SK1. 1 Publication1
Natural varianti375A → T in strain: YJM339. 1 Publication1
Natural varianti452S → G in strain: EAY1068, M2-8, M7-8, M5-7, YJM269 and YJM627. 1 Publication1
Natural varianti465D → N in strain: EAY1066 and YJM280. 1 Publication1
Natural varianti470P → S in strain: YJM339. 1 Publication1
Natural varianti607L → F in strain: EAY1068, M2-8, M7-8, M5-7 and YJM627. 1 Publication1
Natural varianti678D → N in strain: SK1, YJM320 and YJM339. 1 Publication1
Natural varianti703P → L in strain: SK1, YJM320 and YJM339. 1 Publication1
Natural varianti761D → 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 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

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PIRi
S54525

NCBI Reference Sequences

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RefSeqi
NP_013890.1, NM_001182671.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YMR167W_mRNA; YMR167W; YMR167W

Database of genes from NCBI RefSeq genomes

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GeneIDi
855203

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YMR167W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4E4WX-ray2.50A485-769[»]
4FMNX-ray2.69A485-769[»]
4FMOX-ray3.04A485-769[»]
6RMNX-ray2.20A505-769[»]
6SHXX-ray2.40A505-769[»]
6SNSX-ray2.60A505-769[»]
6SNVX-ray2.50A/D505-769[»]
SMRiP38920
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi35345, 229 interactors
ComplexPortaliCPX-1666, MutLalpha endonuclease complex
CPX-1667, MutLbeta endonuclease complex
CPX-1668, MLH1-MLH3 endonuclease complex
DIPiDIP-2412N
IntActiP38920, 17 interactors
MINTiP38920
STRINGi4932.YMR167W

PTM databases

iPTMnetiP38920

Proteomic databases

MaxQBiP38920
PaxDbiP38920
PRIDEiP38920

Genome annotation databases

EnsemblFungiiYMR167W_mRNA; YMR167W; YMR167W
GeneIDi855203
KEGGisce:YMR167W

Organism-specific databases

SGDiS000004777, MLH1
VEuPathDBiFungiDB:YMR167W

Phylogenomic databases

eggNOGiKOG1979, Eukaryota
GeneTreeiENSGT00800000124177
HOGENOMiCLU_004131_2_0_1
InParanoidiP38920
OMAiGHPFIYL

Enzyme and pathway databases

BRENDAi3.6.1.3, 984
ReactomeiR-SCE-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)

Miscellaneous databases

Protein Ontology

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PROi
PR:P38920
RNActiP38920, protein

Family and domain databases

Gene3Di3.30.230.10, 1 hit
3.30.565.10, 1 hit
InterProiView protein in InterPro
IPR014762, DNA_mismatch_repair_CS
IPR002099, DNA_mismatch_repair_N
IPR013507, DNA_mismatch_S5_2-like
IPR036890, HATPase_C_sf
IPR032189, Mlh1_C
IPR038973, MutL/Mlh/Pms
IPR020568, Ribosomal_S5_D2-typ_fold
IPR014721, Ribosomal_S5_D2-typ_fold_subgr
PANTHERiPTHR10073, PTHR10073, 1 hit
PfamiView protein in Pfam
PF01119, DNA_mis_repair, 1 hit
PF16413, Mlh1_C, 1 hit
SMARTiView protein in SMART
SM01340, DNA_mis_repair, 1 hit
SUPFAMiSSF54211, SSF54211, 1 hit
SSF55874, SSF55874, 1 hit
TIGRFAMsiTIGR00585, mutl, 1 hit
PROSITEiView protein in PROSITE
PS00058, DNA_MISMATCH_REPAIR_1, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMLH1_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P38920
Secondary accession number(s): D6VZY9
, Q2I028, Q2I029, Q2I031, Q2I032, Q2I033, Q2I034, Q2I035, Q2I036, Q2I038, Q2I039, Q2I041
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: September 29, 2021
This is version 199 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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