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Entry version 188 (16 Oct 2019)
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 activity 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

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:G3O-32857-MONOMER

    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

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YMR167W

    Saccharomyces Genome Database

    More...
    SGDi
    S000004777 MLH1

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    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.<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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    35345, 223 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

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

    Database of interacting proteins

    More...
    DIPi
    DIP-2412N

    Protein interaction database and analysis system

    More...
    IntActi
    P38920, 17 interactors

    Molecular INTeraction database

    More...
    MINTi
    P38920

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YMR167W

    <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

    More...
    SMRi
    P38920

    Database of comparative protein structure models

    More...
    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
    Regioni501 – 756Interaction with PMS1Add BLAST256

    <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

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P38920

    KEGG Orthology (KO)

    More...
    KOi
    K08734

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    AGSSCAW

    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

    More...
    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

    More...
    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

    More...
    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

    More...
    PIRi
    S54525

    NCBI Reference Sequences

    More...
    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

    More...
    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

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4E4WX-ray2.50A485-769[»]
    4FMNX-ray2.69A485-769[»]
    4FMOX-ray3.04A485-769[»]
    SMRiP38920
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi35345, 223 interactors
    ComplexPortaliCPX-1666 MutLalpha complex
    CPX-1667 MutLbeta complex
    CPX-1668 MLH1-MLH3 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

    EuPathDBiFungiDB:YMR167W
    SGDiS000004777 MLH1

    Phylogenomic databases

    InParanoidiP38920
    KOiK08734
    OMAiAGSSCAW

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32857-MONOMER
    ReactomeiR-SCE-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P38920

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    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: October 16, 2019
    This is version 188 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, Complete proteome, Reference proteome

    Documents

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