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Entry version 174 (13 Feb 2019)
Sequence version 2 (01 Nov 1997)
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Protein

DNA mismatch repair protein MSH2

Gene

MSH2

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

Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer), which bind to DNA mismatches thereby initiating DNA repair. MSH2 seems to act as a scaffold for the other MutS homologs that provide substrate-binding and substrate specificity. When bound, heterodimers bend the DNA helix and shield approximately 20 base pairs. MutS alpha acts mainly to repair base-base and single insertion-deletion mismatches that occur during replication, but can also repair longer insertion-deletion loops (IDLs), although with decreasing efficiency as the size of the extrahelical loop increases. MutS beta acts mainly to repair IDLs from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches. After mismatch binding, MutS alpha or beta form a ternary complex with a MutL heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. Both subunits bind ATP, but with differing affinities, and their ATPase kinetics are also very different. MSH6 binds and hydrolyzes ATP rapidly, whereas MSH2 catalyzes ATP at a substantially slower rate. Binding to a mismatched base pair suppresses MSH6-catalyzed ATP hydrolysis, but not the activity of MSH2. ATP binding to both subunits is necessary to trigger a change in MutS alpha interaction with mismatched DNA, converting MutS alpha into a sliding clamp capable of hydrolysis-independent movement along DNA, and also facilitates formation of ternary complexes containing MutS and MutL proteins and the mismatch. MutS beta also has a role in regulation of heteroduplex formation during mitotic and meiotic recombination. MutS beta binds to DNA flap structures predicted to form during recombination, and is required for 3' non-homologous tail removal (NHTR). MutS beta-binding alters the DNA conformation of its substrate at the ds/ssDNA junction and may facilitate its recognition and/or cleavage by the downstream nucleotide excision repair (NER) RAD1-RAD10 endonuclease.19 Publications

Miscellaneous

Present with 1230 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by Cd2+.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi688 – 695ATPSequence analysis8

<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

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

Molecular functionDNA-binding
Biological processDNA damage, DNA repair
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33490-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-SCE-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)

<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 MSH2
Alternative name(s):
MutS protein homolog 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:MSH2
Ordered Locus Names:YOL090W
ORF Names:O0935
<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 XV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YOL090W

Saccharomyces Genome Database

More...
SGDi
S000005450 MSH2

<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; 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>Mutagenesisi42Y → A: Moderately reduced activity in a mismatch repair assay. 1 Publication1
Mutagenesisi65K → A: Defective in a mismatch repair assay. 1 Publication1
Mutagenesisi317G → D: Partially defective in a mismatch repair assay. 2 Publications1
Mutagenesisi402L → F: Partially defective in a mismatch repair assay. 1 Publication1
Mutagenesisi430Q → K: Partially defective in a mismatch repair assay. 1 Publication1
Mutagenesisi518A → P: Defective in MMR, but not in NHTR. 1 Publication1
Mutagenesisi524D → Y: Partially defective in a mismatch repair assay. 1 Publication1
Mutagenesisi542R → P: Defective in a mismatch repair assay. 1 Publication1
Mutagenesisi561S → P: Causes strong defects in MutS alpha mismatch binding. Defective in MMR, but not in NHTR. 1 Publication1
Mutagenesisi564K → E: Causes strong defects in MutS alpha mismatch binding. Defective in MMR, but not in NHTR. 1 Publication1
Mutagenesisi566G → D: Defective in MMR, but not in NHTR. 1 Publication1
Mutagenesisi574L → S: Defective in MMR and in NHTR. 1 Publication1
Mutagenesisi584L → P: Defective in MMR and in NHTR. 1 Publication1
Mutagenesisi640P → L: Defective in a mismatch repair assay. 2 Publications1
Mutagenesisi656S → P: Causes defects in ATP-dependent dissociation of MutS alpha from mismatch DNA and in interactions between MutS alpha and MutL alpha. Defective in MMR, but not in NHTR. 1 Publication1
Mutagenesisi658H → Y: Fully functional in a mismatch repair assay. 1 Publication1
Mutagenesisi688G → A: Moderately reduced activity in a mismatch repair assay. 1 Publication1
Mutagenesisi693G → A or S: Has a dominant negative mutator effect. 2 Publications1
Mutagenesisi693G → D: Has no defect in mismatch DNA binding, but lacks ATP-induced conformational change. Defective in MMR and in NHTR. 2 Publications1
Mutagenesisi694K → A: Impairs ATP binding; reduces catalytic activity 1.6-fold for ATP hydrolysis. Has a dominant negative mutator effect. 3 Publications1
Mutagenesisi694K → R: Defective in MMR and in NHTR. 3 Publications1
Mutagenesisi695S → A: Has a dominant negative mutator effect. 1 Publication1
Mutagenesisi716C → F: Defective in a mismatch repair assay. 1 Publication1
Mutagenesisi730R → W: Disruptes MutS alpha ATPase activity, but does not affect ATP binding or interactions with MutL alpha. Defective in MMR, but not in NHTR. 1 Publication1
Mutagenesisi742S → F: Defective in MMR, but not in NHTR. 1 Publication1
Mutagenesisi742S → P: Defective in MMR and in NHTR. 1 Publication1
Mutagenesisi768E → A: Reduces catalytic activity 50-fold for ATP hydrolysis. 3 Publications1
Mutagenesisi773T → I: Defective in MMR and in NHTR. 1 Publication1
Mutagenesisi855G → D: Defective in MMR, but not in NHTR. 1 Publication1
Mutagenesisi859A → E: Defective in MMR, but not in NHTR. 1 Publication1
Mutagenesisi862V → D: Defective in MMR, but not in NHTR. 1 Publication1
Mutagenesisi863 – 868Missing : Defective in MMR and in NHTR. 1 Publication6

<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_00001151911 – 964DNA mismatch repair protein MSH2Add BLAST964

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P25847

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

More...
PaxDbi
P25847

PRoteomics IDEntifications database

More...
PRIDEi
P25847

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P25847

<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 consisting of MSH2-MSH6 (MutS alpha) or MSH2-MSH3 (MutS beta). Both heterodimers form a ternary complex with MutL alpha (MLH1-PMS1). MutS beta also forms a ternary complex with MutL beta (MLH1-MLH3), and possibly with a MLH1-MLH2 heterodimer. Both heterodimers interact with proliferating cell nuclear antigen (PCNA/POL30). This interaction is disrupted upon binding of the MutS heterodimers to mismatch DNA. Interacts with SAW1.7 Publications

<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
34312, 322 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1036 DNA mismatch repair MutSbeta complex
CPX-1037 DNA mismatch repair MutSalpha complex

Database of interacting proteins

More...
DIPi
DIP-2415N

Protein interaction database and analysis system

More...
IntActi
P25847, 38 interactors

Molecular INTeraction database

More...
MINTi
P25847

STRING: functional protein association networks

More...
STRINGi
4932.YOL090W

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P25847

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

More...
SMRi
P25847

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Regioni851 – 964Interaction with MSH6Add BLAST114

<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

Belongs to the DNA mismatch repair MutS family.Curated

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000074867

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000196498

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P25847

KEGG Orthology (KO)

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KOi
K08735

Identification of Orthologs from Complete Genome Data

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OMAi
IPDILML

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.420.110, 1 hit
3.40.1170.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011184 DNA_mismatch_repair_Msh2
IPR007695 DNA_mismatch_repair_MutS-lik_N
IPR000432 DNA_mismatch_repair_MutS_C
IPR007861 DNA_mismatch_repair_MutS_clamp
IPR007696 DNA_mismatch_repair_MutS_core
IPR016151 DNA_mismatch_repair_MutS_N
IPR036187 DNA_mismatch_repair_MutS_sf
IPR007860 DNA_mmatch_repair_MutS_con_dom
IPR032642 Msh2
IPR036678 MutS_con_dom_sf
IPR027417 P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR11361:SF35 PTHR11361:SF35, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01624 MutS_I, 1 hit
PF05188 MutS_II, 1 hit
PF05192 MutS_III, 1 hit
PF05190 MutS_IV, 1 hit
PF00488 MutS_V, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005813 MSH2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00534 MUTSac, 1 hit
SM00533 MUTSd, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48334 SSF48334, 1 hit
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00486 DNA_MISMATCH_REPAIR_2, 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>.<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.

P25847-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSTRPELKF SDVSEERNFY KKYTGLPKKP LKTIRLVDKG DYYTVIGSDA
60 70 80 90 100
IFVADSVYHT QSVLKNCQLD PVTAKNFHEP TKYVTVSLQV LATLLKLCLL
110 120 130 140 150
DLGYKVEIYD KGWKLIKSAS PGNIEQVNEL MNMNIDSSII IASLKVQWNS
160 170 180 190 200
QDGNCIIGVA FIDTTAYKVG MLDIVDNEVY SNLESFLIQL GVKECLVQDL
210 220 230 240 250
TSNSNSNAEM QKVINVIDRC GCVVTLLKNS EFSEKDVELD LTKLLGDDLA
260 270 280 290 300
LSLPQKYSKL SMGACNALIG YLQLLSEQDQ VGKYELVEHK LKEFMKLDAS
310 320 330 340 350
AIKALNLFPQ GPQNPFGSNN LAVSGFTSAG NSGKVTSLFQ LLNHCKTNAG
360 370 380 390 400
VRLLNEWLKQ PLTNIDEINK RHDLVDYLID QIELRQMLTS EYLPMIPDIR
410 420 430 440 450
RLTKKLNKRG NLEDVLKIYQ FSKRIPEIVQ VFTSFLEDDS PTEPVNELVR
460 470 480 490 500
SVWLAPLSHH VEPLSKFEEM VETTVDLDAY EENNEFMIKV EFNEELGKIR
510 520 530 540 550
SKLDTLRDEI HSIHLDSAED LGFDPDKKLK LENHHLHGWC MRLTRNDAKE
560 570 580 590 600
LRKHKKYIEL STVKAGIFFS TKQLKSIANE TNILQKEYDK QQSALVREII
610 620 630 640 650
NITLTYTPVF EKLSLVLAHL DVIASFAHTS SYAPIPYIRP KLHPMDSERR
660 670 680 690 700
THLISSRHPV LEMQDDISFI SNDVTLESGK GDFLIITGPN MGGKSTYIRQ
710 720 730 740 750
VGVISLMAQI GCFVPCEEAE IAIVDAILCR VGAGDSQLKG VSTFMVEILE
760 770 780 790 800
TASILKNASK NSLIIVDELG RGTSTYDGFG LAWAIAEHIA SKIGCFALFA
810 820 830 840 850
THFHELTELS EKLPNVKNMH VVAHIEKNLK EQKHDDEDIT LLYKVEPGIS
860 870 880 890 900
DQSFGIHVAE VVQFPEKIVK MAKRKANELD DLKTNNEDLK KAKLSLQEVN
910 920 930 940 950
EGNIRLKALL KEWIRKVKEE GLHDPSKITE EASQHKIQEL LRAIANEPEK
960
ENDNYLKYIK ALLL
Length:964
Mass (Da):108,884
Last modified:November 1, 1997 - 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:i43FFD8A640138AE4
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 conflicti957 – 964KYIKALLL → EIYKSPCCYN in AAA34802 (PubMed:1459447).Curated8

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
M84170 Genomic DNA Translation: AAA34802.1
X83121 Genomic DNA Translation: CAA58189.1
Z74832 Genomic DNA Translation: CAA99102.1
BK006948 Genomic DNA Translation: DAA10694.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S57379

NCBI Reference Sequences

More...
RefSeqi
NP_014551.1, NM_001183344.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YOL090W_mRNA; YOL090W_mRNA; YOL090W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854063

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YOL090W

<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
M84170 Genomic DNA Translation: AAA34802.1
X83121 Genomic DNA Translation: CAA58189.1
Z74832 Genomic DNA Translation: CAA99102.1
BK006948 Genomic DNA Translation: DAA10694.1
PIRiS57379
RefSeqiNP_014551.1, NM_001183344.1

3D structure databases

ProteinModelPortaliP25847
SMRiP25847
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34312, 322 interactors
ComplexPortaliCPX-1036 DNA mismatch repair MutSbeta complex
CPX-1037 DNA mismatch repair MutSalpha complex
DIPiDIP-2415N
IntActiP25847, 38 interactors
MINTiP25847
STRINGi4932.YOL090W

PTM databases

iPTMnetiP25847

Proteomic databases

MaxQBiP25847
PaxDbiP25847
PRIDEiP25847

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL090W_mRNA; YOL090W_mRNA; YOL090W
GeneIDi854063
KEGGisce:YOL090W

Organism-specific databases

EuPathDBiFungiDB:YOL090W
SGDiS000005450 MSH2

Phylogenomic databases

GeneTreeiENSGT00550000074867
HOGENOMiHOG000196498
InParanoidiP25847
KOiK08735
OMAiIPDILML

Enzyme and pathway databases

BioCyciYEAST:G3O-33490-MONOMER
ReactomeiR-SCE-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-SCE-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P25847

Family and domain databases

Gene3Di3.30.420.110, 1 hit
3.40.1170.10, 1 hit
InterProiView protein in InterPro
IPR011184 DNA_mismatch_repair_Msh2
IPR007695 DNA_mismatch_repair_MutS-lik_N
IPR000432 DNA_mismatch_repair_MutS_C
IPR007861 DNA_mismatch_repair_MutS_clamp
IPR007696 DNA_mismatch_repair_MutS_core
IPR016151 DNA_mismatch_repair_MutS_N
IPR036187 DNA_mismatch_repair_MutS_sf
IPR007860 DNA_mmatch_repair_MutS_con_dom
IPR032642 Msh2
IPR036678 MutS_con_dom_sf
IPR027417 P-loop_NTPase
PANTHERiPTHR11361:SF35 PTHR11361:SF35, 1 hit
PfamiView protein in Pfam
PF01624 MutS_I, 1 hit
PF05188 MutS_II, 1 hit
PF05192 MutS_III, 1 hit
PF05190 MutS_IV, 1 hit
PF00488 MutS_V, 1 hit
PIRSFiPIRSF005813 MSH2, 1 hit
SMARTiView protein in SMART
SM00534 MUTSac, 1 hit
SM00533 MUTSd, 1 hit
SUPFAMiSSF48334 SSF48334, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00486 DNA_MISMATCH_REPAIR_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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<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 nameiMSH2_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: P25847
Secondary accession number(s): D6W1X8, Q12423
<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: May 1, 1992
Last sequence update: November 1, 1997
Last modified: February 13, 2019
This is version 174 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

Complete proteome, Reference proteome

Documents

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