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Entry version 181 (22 Apr 2020)
Sequence version 1 (01 Nov 1996)
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Protein

DNA mismatch repair protein MSH6

Gene

MSH6

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). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. MSH6 provides substrate-binding and substrate specificity to the complex. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs. 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. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis by the MutS alpha complex is crucial for MMR. 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. May also be involved in resolution of recombination intermediates.19 Publications

Miscellaneous

Present with 5330 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi228 – 299Add BLAST72
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi982 – 989ATPSequence 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-29700-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%5Fand%5Ftaxonomy%5Fsection">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 MSH6
Alternative name(s):
MutS protein homolog 6
Postmeiotic segregation protein 3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:MSH6
Synonyms:PMS3
Ordered Locus Names:YDR097C
ORF Names:YD8557.04C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 IV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YDR097C

Saccharomyces Genome Database

More...
SGDi
S000002504 MSH6

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi26 – 27KQ → AA: Partially functional in a mismatch repair assay; when associated with 33-AA-34. 1 Publication2
Mutagenesisi33 – 34FF → AA: Abolishes interaction with PCNA (POL30), but only causes a moderate mismatch repair defect. Partially functional in a mismatch repair assay; when associated with 26-AA-27. 2 Publications2
Mutagenesisi301L → V: Fully functional in a mismatch repair assay. 1 Publication1
Mutagenesisi313P → A: Fully functional in a mismatch repair assay. 1 Publication1
Mutagenesisi337F → A: Shows defects in both homoduplex and mispair DNA binding and is only partially functional in a mismatch repair assay. 3 Publications1
Mutagenesisi337F → H, I or Y: Partially functional in a mismatch repair assay. 3 Publications1
Mutagenesisi337F → K: Completely abolishes mismatch repair. 3 Publications1
Mutagenesisi337F → S in MSH6-6; partially functional in a mismatch repair assay. 3 Publications1
Mutagenesisi339E → A: Defective in repairing 8-oxo-G-A mismatches. 2 Publications1
Mutagenesisi340 – 343LYEK → CFAE in MSH6-340; shows defects in mispair DNA binding, but not in homoduplex DNA binding. 1 Publication4
Mutagenesisi368G → A: Moderately reduced activity in a mismatch repair assay. 1 Publication1
Mutagenesisi370P → A: Partially functional in a mismatch repair assay. 1 Publication1
Mutagenesisi393Q → A: Moderately reduced activity in a mismatch repair assay. 1 Publication1
Mutagenesisi393Q → R in MSH6-5; partially functional in a mismatch repair assay. 1 Publication1
Mutagenesisi412R → A: Completely abolishes mismatch repair. 1 Publication1
Mutagenesisi412R → G in MSH6-7; partially functional in a mismatch repair assay. 1 Publication1
Mutagenesisi421G → D in PMS3-1; completely abolishes mismatch repair. 1 Publication1
Mutagenesisi477G → R: Partially functional in a mismatch repair assay. 1 Publication1
Mutagenesisi848K → A: Fully functional in a mismatch repair assay. 1 Publication1
Mutagenesisi852R → A: Moderately reduced activity in a mismatch repair assay. 1 Publication1
Mutagenesisi987G → D: Has no defect in mismatch DNA binding, but lacks ATP-induced conformational change. 1 Publication1
Mutagenesisi988K → A: Impairs ATP binding; reduces catalytic activity 13-fold for ATP hydrolysis. 2 Publications1
Mutagenesisi1036S → P in MSH6-4; defective for ATP-induced sliding clamp formation and assembly of ternary complexes with MutL alpha. 2 Publications1
Mutagenesisi1062E → A: Reduces catalytic activity 13-fold for ATP hydrolysis. 3 Publications1
Mutagenesisi1067G → D in MSH6-3; defective for ATP-induced sliding clamp formation and assembly of ternary complexes with MutL alpha. 2 Publications1
Mutagenesisi1096H → A in MSH6-9; shows normal mispair binding and dissociation, but fails to show complete mispair activation of the ATPase. 1 Publication1
Mutagenesisi1142G → D in MSH6-2; defective for ATP-induced sliding clamp formation, but assembles ternary complexes with MutL alpha. 2 Publications1

<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_00001152131 – 1242DNA mismatch repair protein MSH6Add BLAST1242

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 residuei102PhosphoserineCombined sources1
Modified residuei145PhosphoserineCombined sources1
Modified residuei150PhosphoserineCombined sources1
Modified residuei201PhosphoserineCombined sources1
Modified residuei451PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q03834

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

More...
PaxDbi
Q03834

PRoteomics IDEntifications database

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PRIDEi
Q03834

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q03834

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer consisting of MSH2-MSH6 (MutS alpha).

Forms a ternary complex with MutL alpha (MLH1-PMS1). MutS alpha interacts with proliferating cell nuclear antigen (PCNA/POL30). This interaction is disrupted upon binding of MutS alpha to mismatch DNA.

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="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

Show more details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
32152, 115 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1037 DNA mismatch repair MutSalpha complex

Database of interacting proteins

More...
DIPi
DIP-2423N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q03834

Protein interaction database and analysis system

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IntActi
Q03834, 35 interactors

Molecular INTeraction database

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MINTi
Q03834

STRING: functional protein association networks

More...
STRINGi
4932.YDR097C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q03834 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

3D structure databases

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

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SMRi
Q03834

Database of comparative protein structure models

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ModBasei
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>Regioni305 – 421Mispair-binding domainAdd BLAST117

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi27 – 34PIP box8

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PIP box serves as a PCNA(POL30)-recognition and -binding motif.

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_002472_1_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q03834

KEGG Orthology (KO)

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KOi
K08737

Identification of Orthologs from Complete Genome Data

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OMAi
TPMMAQY

Family and domain databases

Database of protein disorder

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DisProti
DP01623

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.420.110, 1 hit
3.40.1170.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR007695 DNA_mismatch_repair_MutS-lik_N
IPR017261 DNA_mismatch_repair_MutS/MSH
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
IPR036678 MutS_con_dom_sf
IPR027417 P-loop_NTPase

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

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PIRSFi
PIRSF037677 DNA_mis_repair_Msh6, 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

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SUPFAMi
SSF48334 SSF48334, 1 hit
SSF52540 SSF52540, 1 hit
SSF53150 SSF53150, 1 hit
SSF55271 SSF55271, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q03834-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPATPKTSK TAHFENGSTS SQKKMKQSSL LSFFSKQVPS GTPSKKVQKP
60 70 80 90 100
TPATLENTAT DKITKNPQGG KTGKLFVDVD EDNDLTIAEE TVSTVRSDIM
110 120 130 140 150
HSQEPQSDTM LNSNTTEPKS TTTDEDLSSS QSRRNHKRRV NYAESDDDDS
160 170 180 190 200
DTTFTAKRKK GKVVDSESDE DEYLPDKNDG DEDDDIADDK EDIKGELAED
210 220 230 240 250
SGDDDDLISL AETTSKKKFS YNTSHSSSPF TRNISRDNSK KKSRPNQAPS
260 270 280 290 300
RSYNPSHSQP SATSKSSKFN KQNEERYQWL VDERDAQRRP KSDPEYDPRT
310 320 330 340 350
LYIPSSAWNK FTPFEKQYWE IKSKMWDCIV FFKKGKFFEL YEKDALLANA
360 370 380 390 400
LFDLKIAGGG RANMQLAGIP EMSFEYWAAQ FIQMGYKVAK VDQRESMLAK
410 420 430 440 450
EMREGSKGIV KRELQCILTS GTLTDGDMLH SDLATFCLAI REEPGNFYNE
460 470 480 490 500
TQLDSSTIVQ KLNTKIFGAA FIDTATGELQ MLEFEDDSEC TKLDTLMSQV
510 520 530 540 550
RPMEVVMERN NLSTLANKIV KFNSAPNAIF NEVKAGEEFY DCDKTYAEII
560 570 580 590 600
SSEYFSTEED WPEVLKSYYD TGKKVGFSAF GGLLYYLKWL KLDKNLISMK
610 620 630 640 650
NIKEYDFVKS QHSMVLDGIT LQNLEIFSNS FDGSDKGTLF KLFNRAITPM
660 670 680 690 700
GKRMMKKWLM HPLLRKNDIE SRLDSVDSLL QDITLREQLE ITFSKLPDLE
710 720 730 740 750
RMLARIHSRT IKVKDFEKVI TAFETIIELQ DSLKNNDLKG DVSKYISSFP
760 770 780 790 800
EGLVEAVKSW TNAFERQKAI NENIIVPQRG FDIEFDKSMD RIQELEDELM
810 820 830 840 850
EILMTYRKQF KCSNIQYKDS GKEIYTIEIP ISATKNVPSN WVQMAANKTY
860 870 880 890 900
KRYYSDEVRA LARSMAEAKE IHKTLEEDLK NRLCQKFDAH YNTIWMPTIQ
910 920 930 940 950
AISNIDCLLA ITRTSEYLGA PSCRPTIVDE VDSKTNTQLN GFLKFKSLRH
960 970 980 990 1000
PCFNLGATTA KDFIPNDIEL GKEQPRLGLL TGANAAGKST ILRMACIAVI
1010 1020 1030 1040 1050
MAQMGCYVPC ESAVLTPIDR IMTRLGANDN IMQGKSTFFV ELAETKKILD
1060 1070 1080 1090 1100
MATNRSLLVV DELGRGGSSS DGFAIAESVL HHVATHIQSL GFFATHYGTL
1110 1120 1130 1140 1150
ASSFKHHPQV RPLKMSILVD EATRNVTFLY KMLEGQSEGS FGMHVASMCG
1160 1170 1180 1190 1200
ISKEIIDNAQ IAADNLEHTS RLVKERDLAA NNLNGEVVSV PGGLQSDFVR
1210 1220 1230 1240
IAYGDGLKNT KLGSGEGVLN YDWNIKRNVL KSLFSIIDDL QS
Length:1,242
Mass (Da):140,080
Last modified:November 1, 1996 - v1
<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:i11A6883AADCFA222
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z47746 Genomic DNA Translation: CAA87671.1
BK006938 Genomic DNA Translation: DAA11942.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S51246

NCBI Reference Sequences

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RefSeqi
NP_010382.3, NM_001180405.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDR097C_mRNA; YDR097C; YDR097C

Database of genes from NCBI RefSeq genomes

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GeneIDi
851671

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR097C

<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
Z47746 Genomic DNA Translation: CAA87671.1
BK006938 Genomic DNA Translation: DAA11942.1
PIRiS51246
RefSeqiNP_010382.3, NM_001180405.3

3D structure databases

SMRiQ03834
ModBaseiSearch...

Protein-protein interaction databases

BioGridi32152, 115 interactors
ComplexPortaliCPX-1037 DNA mismatch repair MutSalpha complex
DIPiDIP-2423N
ELMiQ03834
IntActiQ03834, 35 interactors
MINTiQ03834
STRINGi4932.YDR097C

PTM databases

iPTMnetiQ03834

Proteomic databases

MaxQBiQ03834
PaxDbiQ03834
PRIDEiQ03834

Genome annotation databases

EnsemblFungiiYDR097C_mRNA; YDR097C; YDR097C
GeneIDi851671
KEGGisce:YDR097C

Organism-specific databases

EuPathDBiFungiDB:YDR097C
SGDiS000002504 MSH6

Phylogenomic databases

HOGENOMiCLU_002472_1_0_1
InParanoidiQ03834
KOiK08737
OMAiTPMMAQY

Enzyme and pathway databases

BioCyciYEAST:G3O-29700-MONOMER
ReactomeiR-SCE-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)

Miscellaneous databases

Protein Ontology

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PROi
PR:Q03834
RNActiQ03834 protein

Family and domain databases

DisProtiDP01623
Gene3Di3.30.420.110, 1 hit
3.40.1170.10, 1 hit
InterProiView protein in InterPro
IPR007695 DNA_mismatch_repair_MutS-lik_N
IPR017261 DNA_mismatch_repair_MutS/MSH
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
IPR036678 MutS_con_dom_sf
IPR027417 P-loop_NTPase
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
PIRSFiPIRSF037677 DNA_mis_repair_Msh6, 1 hit
SMARTiView protein in SMART
SM00534 MUTSac, 1 hit
SM00533 MUTSd, 1 hit
SUPFAMiSSF48334 SSF48334, 1 hit
SSF52540 SSF52540, 1 hit
SSF53150 SSF53150, 1 hit
SSF55271 SSF55271, 1 hit
PROSITEiView protein in PROSITE
PS00486 DNA_MISMATCH_REPAIR_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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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 nameiMSH6_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: Q03834
Secondary accession number(s): D6VS82
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 22, 2020
This is version 181 of the entry and version 1 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

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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
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