Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P25847 (MSH2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA mismatch repair protein MSH2
Alternative name(s):
MutS protein homolog 2
Gene names
Name:MSH2
Ordered Locus Names:YOL090W
ORF Names:O0935
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length964 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.20 Ref.26 Ref.27 Ref.28 Ref.30 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42

Enzyme regulation

Inhibited by Cd2+. Ref.33 Ref.36

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.23 Ref.29 Ref.43

Subcellular location

Nucleus Ref.31.

Miscellaneous

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

Sequence similarities

Belongs to the DNA mismatch repair MutS family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.15. Source: GOC

DNA recombination

Inferred from mutant phenotype PubMed 15920474. Source: SGD

chromatin silencing at silent mating-type cassette

Inferred from genetic interaction PubMed 16157874. Source: SGD

interstrand cross-link repair

Inferred from genetic interaction PubMed 22912599. Source: SGD

meiotic gene conversion

Inferred from mutant phenotype Ref.5. Source: SGD

meiotic mismatch repair

Inferred from mutant phenotype Ref.5Ref.38PubMed 8056309. Source: SGD

mismatch repair

Inferred from mutant phenotype Ref.21PubMed 9520271. Source: SGD

mitotic recombination

Inferred from mutant phenotype PubMed 8849883. Source: SGD

removal of nonhomologous ends

Inferred from mutant phenotype Ref.21Ref.13. Source: SGD

   Cellular_componentMutSalpha complex

Inferred from physical interaction Ref.10. Source: SGD

MutSbeta complex

Inferred from physical interaction Ref.8. Source: SGD

nuclear chromosome

Inferred from direct assay PubMed 10882115. Source: SGD

   Molecular_functionATP binding

Inferred from direct assay Ref.14. Source: SGD

ATPase activity

Inferred from direct assay Ref.15. Source: SGD

double-strand/single-strand DNA junction binding

Inferred from direct assay Ref.40. Source: SGD

four-way junction DNA binding

Inferred from direct assay Ref.18PubMed 9018043. Source: SGD

mismatched DNA binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 11805826PubMed 16429126PubMed 23267104Ref.8Ref.10PubMed 9207118PubMed 9374523. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 964964DNA mismatch repair protein MSH2
PRO_0000115191

Regions

Nucleotide binding688 – 6958ATP Potential
Region851 – 964114Interaction with MSH6

Experimental info

Mutagenesis421Y → A: Moderately reduced activity in a mismatch repair assay. Ref.25
Mutagenesis651K → A: Defective in a mismatch repair assay. Ref.25
Mutagenesis3171G → D: Partially defective in a mismatch repair assay. Ref.17 Ref.24
Mutagenesis4021L → F: Partially defective in a mismatch repair assay. Ref.17
Mutagenesis4301Q → K: Partially defective in a mismatch repair assay. Ref.17
Mutagenesis5181A → P: Defective in MMR, but not in NHTR.
Mutagenesis5241D → Y: Partially defective in a mismatch repair assay. Ref.17
Mutagenesis5421R → P: Defective in a mismatch repair assay. Ref.17
Mutagenesis5611S → P: Causes strong defects in MutS alpha mismatch binding. Defective in MMR, but not in NHTR. Ref.30
Mutagenesis5641K → E: Causes strong defects in MutS alpha mismatch binding. Defective in MMR, but not in NHTR. Ref.30
Mutagenesis5661G → D: Defective in MMR, but not in NHTR. Ref.30
Mutagenesis5741L → S: Defective in MMR and in NHTR.
Mutagenesis5841L → P: Defective in MMR and in NHTR.
Mutagenesis6401P → L: Defective in a mismatch repair assay. Ref.17 Ref.24
Mutagenesis6561S → 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. Ref.30
Mutagenesis6581H → Y: Fully functional in a mismatch repair assay. Ref.24
Mutagenesis6881G → A: Moderately reduced activity in a mismatch repair assay. Ref.22
Mutagenesis6931G → A or S: Has a dominant negative mutator effect. Ref.15 Ref.22
Mutagenesis6931G → D: Has no defect in mismatch DNA binding, but lacks ATP-induced conformational change. Defective in MMR and in NHTR. Ref.15 Ref.22
Mutagenesis6941K → A: Impairs ATP binding; reduces catalytic activity 1.6-fold for ATP hydrolysis. Has a dominant negative mutator effect. Ref.22 Ref.37 Ref.39
Mutagenesis6941K → R: Defective in MMR and in NHTR. Ref.22 Ref.37 Ref.39
Mutagenesis6951S → A: Has a dominant negative mutator effect. Ref.22
Mutagenesis7161C → F: Defective in a mismatch repair assay. Ref.17
Mutagenesis7301R → W: Disruptes MutS alpha ATPase activity, but does not affect ATP binding or interactions with MutL alpha. Defective in MMR, but not in NHTR. Ref.30
Mutagenesis7421S → F: Defective in MMR, but not in NHTR.
Mutagenesis7421S → P: Defective in MMR and in NHTR.
Mutagenesis7681E → A: Reduces catalytic activity 50-fold for ATP hydrolysis. Ref.27 Ref.33 Ref.37
Mutagenesis7731T → I: Defective in MMR and in NHTR.
Mutagenesis8551G → D: Defective in MMR, but not in NHTR.
Mutagenesis8591A → E: Defective in MMR, but not in NHTR.
Mutagenesis8621V → D: Defective in MMR, but not in NHTR.
Mutagenesis863 – 8686Missing: Defective in MMR and in NHTR.
Sequence conflict957 – 9648KYIKALLL → EIYKSPCCYN in AAA34802. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P25847 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 43FFD8A640138AE4

FASTA964108,884
        10         20         30         40         50         60 
MSSTRPELKF SDVSEERNFY KKYTGLPKKP LKTIRLVDKG DYYTVIGSDA IFVADSVYHT 

        70         80         90        100        110        120 
QSVLKNCQLD PVTAKNFHEP TKYVTVSLQV LATLLKLCLL DLGYKVEIYD KGWKLIKSAS 

       130        140        150        160        170        180 
PGNIEQVNEL MNMNIDSSII IASLKVQWNS QDGNCIIGVA FIDTTAYKVG MLDIVDNEVY 

       190        200        210        220        230        240 
SNLESFLIQL GVKECLVQDL TSNSNSNAEM QKVINVIDRC GCVVTLLKNS EFSEKDVELD 

       250        260        270        280        290        300 
LTKLLGDDLA LSLPQKYSKL SMGACNALIG YLQLLSEQDQ VGKYELVEHK LKEFMKLDAS 

       310        320        330        340        350        360 
AIKALNLFPQ GPQNPFGSNN LAVSGFTSAG NSGKVTSLFQ LLNHCKTNAG VRLLNEWLKQ 

       370        380        390        400        410        420 
PLTNIDEINK RHDLVDYLID QIELRQMLTS EYLPMIPDIR RLTKKLNKRG NLEDVLKIYQ 

       430        440        450        460        470        480 
FSKRIPEIVQ VFTSFLEDDS PTEPVNELVR SVWLAPLSHH VEPLSKFEEM VETTVDLDAY 

       490        500        510        520        530        540 
EENNEFMIKV EFNEELGKIR SKLDTLRDEI HSIHLDSAED LGFDPDKKLK LENHHLHGWC 

       550        560        570        580        590        600 
MRLTRNDAKE LRKHKKYIEL STVKAGIFFS TKQLKSIANE TNILQKEYDK QQSALVREII 

       610        620        630        640        650        660 
NITLTYTPVF EKLSLVLAHL DVIASFAHTS SYAPIPYIRP KLHPMDSERR THLISSRHPV 

       670        680        690        700        710        720 
LEMQDDISFI SNDVTLESGK GDFLIITGPN MGGKSTYIRQ VGVISLMAQI GCFVPCEEAE 

       730        740        750        760        770        780 
IAIVDAILCR VGAGDSQLKG VSTFMVEILE TASILKNASK NSLIIVDELG RGTSTYDGFG 

       790        800        810        820        830        840 
LAWAIAEHIA SKIGCFALFA THFHELTELS EKLPNVKNMH VVAHIEKNLK EQKHDDEDIT 

       850        860        870        880        890        900 
LLYKVEPGIS DQSFGIHVAE VVQFPEKIVK MAKRKANELD DLKTNNEDLK KAKLSLQEVN 

       910        920        930        940        950        960 
EGNIRLKALL KEWIRKVKEE GLHDPSKITE EASQHKIQEL LRAIANEPEK ENDNYLKYIK 


ALLL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of two Saccharomyces cerevisiae genes encoding homologs of the bacterial HexA and MutS mismatch repair proteins."
Reenan R.A.G., Kolodner R.D.
Genetics 132:963-973(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A 29.425 kb segment on the left arm of yeast chromosome XV contains more than twice as many unknown as known open reading frames."
Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.
Yeast 11:975-986(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Characterization of insertion mutations in the Saccharomyces cerevisiae MSH1 and MSH2 genes: evidence for separate mitochondrial and nuclear functions."
Reenan R.A.G., Kolodner R.D.
Genetics 132:975-985(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeast."
Prolla T.A., Pang Q., Alani E., Kolodner R.D., Liskay R.M.
Science 265:1091-1093(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPLEX FORMATION WITH MLH1-PMS1.
[7]"Requirement for PCNA in DNA mismatch repair at a step preceding DNA resynthesis."
Umar A., Buermeyer A.B., Simon J.A., Thomas D.C., Clark A.B., Liskay R.M., Kunkel T.A.
Cell 87:65-73(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POL30.
[8]"Binding of insertion/deletion DNA mismatches by the heterodimer of yeast mismatch repair proteins MSH2 and MSH3."
Habraken Y., Sung P., Prakash L., Prakash S.
Curr. Biol. 6:1185-1187(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING SPECIFICITY, INTERACTION WITH MSH3.
[9]"Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair."
Marsischky G.T., Filosi N., Kane M.F., Kolodner R.D.
Genes Dev. 10:407-420(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MSH3 AND MSH6.
[10]"The Saccharomyces cerevisiae Msh2 and Msh6 proteins form a complex that specifically binds to duplex oligonucleotides containing mismatched DNA base pairs."
Alani E.
Mol. Cell. Biol. 16:5604-5615(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, INTERACTION WITH MSH6.
[11]"Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-PMS1 complex."
Habraken Y., Sung P., Prakash L., Prakash S.
Curr. Biol. 7:790-793(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING SPECIFICITY, COMPLEX FORMATION WITH MLH1-PMS1.
[12]"Microsatellite instability in yeast: dependence on repeat unit size and DNA mismatch repair genes."
Sia E.A., Kokoska R.J., Dominska M., Greenwell P., Petes T.D.
Mol. Cell. Biol. 17:2851-2858(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MMR.
[13]"Role of Saccharomyces cerevisiae Msh2 and Msh3 repair proteins in double-strand break-induced recombination."
Sugawara N., Paques F., Colaiacovo M., Haber J.E.
Proc. Natl. Acad. Sci. U.S.A. 94:9214-9219(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NHTR.
[14]"ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes."
Habraken Y., Sung P., Prakash L., Prakash S.
J. Biol. Chem. 273:9837-9841(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, COMPLEX FORMATION WITH MLH1-PMS1.
[15]"Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair."
Studamire B., Quach T., Alani E.
Mol. Cell. Biol. 18:7590-7601(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-693.
[16]"The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent suppression of frameshift mutations."
Flores-Rozas H., Kolodner R.D.
Proc. Natl. Acad. Sci. U.S.A. 95:12404-12409(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Mutator phenotypes of common polymorphisms and missense mutations in MSH2."
Drotschmann K., Clark A.B., Kunkel T.A.
Curr. Biol. 9:907-910(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-317; LEU-402; GLN-430; ASP-524; ARG-542; PRO-640 AND CYS-716.
[18]"Saccharomyces cerevisiae MSH2/6 complex interacts with Holliday junctions and facilitates their cleavage by phage resolution enzymes."
Marsischky G.T., Lee S., Griffith J., Kolodner R.D.
J. Biol. Chem. 274:7200-7206(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING SPECIFICITY.
[19]"Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA."
Marsischky G.T., Kolodner R.D.
J. Biol. Chem. 274:26668-26682(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING SPECIFICITY.
[20]"MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae."
Ni T.T., Marsischky G.T., Kolodner R.D.
Mol. Cell 4:439-444(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Separation-of-function mutations in Saccharomyces cerevisiae MSH2 that confer mismatch repair defects but do not affect nonhomologous-tail removal during recombination."
Studamire B., Price G., Sugawara N., Haber J.E., Alani E.
Mol. Cell. Biol. 19:7558-7567(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[22]"Mutator phenotypes of yeast strains heterozygous for mutations in the MSH2 gene."
Drotschmann K., Clark A.B., Tran H.T., Resnick M.A., Gordenin D.A., Kunkel T.A.
Proc. Natl. Acad. Sci. U.S.A. 96:2970-2975(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-688; GLY-693; LYS-694 AND SER-695.
[23]"Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes."
Clark A.B., Valle F., Drotschmann K., Gary R.K., Kunkel T.A.
J. Biol. Chem. 275:36498-36501(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POL30.
[24]"Functional analysis of human MLH1 and MSH2 missense variants and hybrid human-yeast MLH1 proteins in Saccharomyces cerevisiae."
Ellison A.R., Lofing J., Bitter G.A.
Hum. Mol. Genet. 10:1889-1900(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-317; PRO-640 AND HIS-658.
[25]"Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6."
Drotschmann K., Yang W., Brownewell F.E., Kool E.T., Kunkel T.A.
J. Biol. Chem. 276:46225-46229(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, MUTAGENESIS OF TYR-42 AND LYS-65.
[26]"MSH-MLH complexes formed at a DNA mismatch are disrupted by the PCNA sliding clamp."
Bowers J., Tran P.T., Joshi A., Liskay R.M., Alani E.
J. Mol. Biol. 306:957-968(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPLEX FORMATION WITH MLH1-PMS1.
[27]"Evidence for sequential action of two ATPase active sites in yeast Msh2-Msh6."
Drotschmann K., Yang W., Kunkel T.A.
DNA Repair 1:743-753(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLU-768.
[28]"Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair."
Antony E., Hingorani M.M.
Biochemistry 42:7682-7693(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[29]"Transfer of the MSH2.MSH6 complex from proliferating cell nuclear antigen to mispaired bases in DNA."
Lau P.J., Kolodner R.D.
J. Biol. Chem. 278:14-17(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POL30.
[30]"Msh2 separation of function mutations confer defects in the initiation steps of mismatch repair."
Kijas A.W., Studamire B., Alani E.
J. Mol. Biol. 331:123-138(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-561; LYS-564; GLY-566; SER-656 AND ARG-730.
[31]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[32]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[33]"Cadmium inhibits the functions of eukaryotic MutS complexes."
Clark A.B., Kunkel T.A.
J. Biol. Chem. 279:53903-53906(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, MUTAGENESIS OF GLU-768.
[34]"Analysis of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-blocking system."
Mendillo M.L., Mazur D.J., Kolodner R.D.
J. Biol. Chem. 280:22245-22257(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPLEX FORMATION WITH MLH1-PMS1.
[35]"Detection of high-affinity and sliding clamp modes for MSH2-MSH6 by single-molecule unzipping force analysis."
Jiang J., Bai L., Surtees J.A., Gemici Z., Wang M.D., Alani E.
Mol. Cell 20:771-781(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[36]"Cadmium inhibits mismatch repair by blocking the ATPase activity of the MSH2-MSH6 complex."
Banerjee S., Flores-Rozas H.
Nucleic Acids Res. 33:1410-1419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[37]"Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6 mismatch repair protein."
Antony E., Khubchandani S., Chen S., Hingorani M.M.
DNA Repair 5:153-162(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-694 AND GLU-768.
[38]"Analysis of the proteins involved in the in vivo repair of base-base mismatches and four-base loops formed during meiotic recombination in the yeast Saccharomyces cerevisiae."
Stone J.E., Petes T.D.
Genetics 173:1223-1239(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[39]"Inhibition of Msh6 ATPase activity by mispaired DNA induces a Msh2(ATP)-Msh6(ATP) state capable of hydrolysis-independent movement along DNA."
Mazur D.J., Mendillo M.L., Kolodner R.D.
Mol. Cell 22:39-49(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-694.
[40]"Mismatch repair factor MSH2-MSH3 binds and alters the conformation of branched DNA structures predicted to form during genetic recombination."
Surtees J.A., Alani E.
J. Mol. Biol. 360:523-536(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NHTR, DNA-BINDING.
[41]"Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display distinct requirements for DNA binding domain I in mismatch recognition."
Lee S.D., Surtees J.A., Alani E.
J. Mol. Biol. 366:53-66(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING.
[42]"Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs."
Harrington J.M., Kolodner R.D.
Mol. Cell. Biol. 27:6546-6554(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[43]"Microarray-based genetic screen defines SAW1, a gene required for Rad1/Rad10-dependent processing of recombination intermediates."
Li F., Dong J., Pan X., Oum J.-H., Boeke J.D., Lee S.E.
Mol. Cell 30:325-335(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SAW1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84170 Genomic DNA. Translation: AAA34802.1.
X83121 Genomic DNA. Translation: CAA58189.1.
Z74832 Genomic DNA. Translation: CAA99102.1.
BK006948 Genomic DNA. Translation: DAA10694.1.
PIRS57379.
RefSeqNP_014551.1. NM_001183344.1.

3D structure databases

ProteinModelPortalP25847.
SMRP25847. Positions 14-913.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34312. 137 interactions.
DIPDIP-2415N.
IntActP25847. 35 interactions.
MINTMINT-631153.
STRING4932.YOL090W.

Proteomic databases

MaxQBP25847.
PaxDbP25847.
PeptideAtlasP25847.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL090W; YOL090W; YOL090W.
GeneID854063.
KEGGsce:YOL090W.

Organism-specific databases

CYGDYOL090w.
SGDS000005450. MSH2.

Phylogenomic databases

eggNOGCOG0249.
GeneTreeENSGT00550000074867.
HOGENOMHOG000196498.
KOK08735.
OMALNKCRTP.
OrthoDBEOG773XQH.

Enzyme and pathway databases

BioCycYEAST:G3O-33490-MONOMER.

Gene expression databases

GenevestigatorP25847.

Family and domain databases

Gene3D3.30.420.110. 1 hit.
3.40.50.300. 1 hit.
InterProIPR011184. 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.
IPR007860. DNA_mmatch_repair_MutS_con_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF01624. MutS_I. 1 hit.
PF05188. MutS_II. 1 hit.
PF05192. MutS_III. 1 hit.
PF05190. MutS_IV. 1 hit.
PF00488. MutS_V. 1 hit.
[Graphical view]
PIRSFPIRSF005813. MSH2. 1 hit.
SMARTSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view]
SUPFAMSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio975668.
PROP25847.

Entry information

Entry nameMSH2_YEAST
AccessionPrimary (citable) accession number: P25847
Secondary accession number(s): D6W1X8, Q12423
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families