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DNA mismatch repair protein MSH2 (MutS protein homolog 2)

 MSH2_YEAST              Reviewed;         964 AA.
P25847; D6W1X8; Q12423;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
31-JAN-2018, entry version 164.
RecName: Full=DNA mismatch repair protein MSH2;
AltName: Full=MutS protein homolog 2;
Name=MSH2; OrderedLocusNames=YOL090W; ORFNames=O0935;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1459447;
Reenan R.A.G., Kolodner R.D.;
"Isolation and characterization of two Saccharomyces cerevisiae genes
encoding homologs of the bacterial HexA and MutS mismatch repair
proteins.";
Genetics 132:963-973(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8533473; DOI=10.1002/yea.320111009;
Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
"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.";
Yeast 11:975-986(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
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.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
CHARACTERIZATION.
PubMed=1334021;
Reenan R.A.G., Kolodner R.D.;
"Characterization of insertion mutations in the Saccharomyces
cerevisiae MSH1 and MSH2 genes: evidence for separate mitochondrial
and nuclear functions.";
Genetics 132:975-985(1992).
[6]
COMPLEX FORMATION WITH MLH1-PMS1.
PubMed=8066446; DOI=10.1126/science.8066446;
Prolla T.A., Pang Q., Alani E., Kolodner R.D., Liskay R.M.;
"MLH1, PMS1, and MSH2 interactions during the initiation of DNA
mismatch repair in yeast.";
Science 265:1091-1093(1994).
[7]
INTERACTION WITH POL30.
PubMed=8858149; DOI=10.1016/S0092-8674(00)81323-9;
Umar A., Buermeyer A.B., Simon J.A., Thomas D.C., Clark A.B.,
Liskay R.M., Kunkel T.A.;
"Requirement for PCNA in DNA mismatch repair at a step preceding DNA
resynthesis.";
Cell 87:65-73(1996).
[8]
DNA-BINDING SPECIFICITY, AND INTERACTION WITH MSH3.
PubMed=8805366; DOI=10.1016/S0960-9822(02)70686-6;
Habraken Y., Sung P., Prakash L., Prakash S.;
"Binding of insertion/deletion DNA mismatches by the heterodimer of
yeast mismatch repair proteins MSH2 and MSH3.";
Curr. Biol. 6:1185-1187(1996).
[9]
FUNCTION, AND INTERACTION WITH MSH3 AND MSH6.
PubMed=8600025; DOI=10.1101/gad.10.4.407;
Marsischky G.T., Filosi N., Kane M.F., Kolodner R.D.;
"Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-
dependent mismatch repair.";
Genes Dev. 10:407-420(1996).
[10]
CHARACTERIZATION, AND INTERACTION WITH MSH6.
PubMed=8816473; DOI=10.1128/MCB.16.10.5604;
Alani E.;
"The Saccharomyces cerevisiae Msh2 and Msh6 proteins form a complex
that specifically binds to duplex oligonucleotides containing
mismatched DNA base pairs.";
Mol. Cell. Biol. 16:5604-5615(1996).
[11]
FUNCTION, DNA-BINDING SPECIFICITY, AND COMPLEX FORMATION WITH
MLH1-PMS1.
PubMed=9368761; DOI=10.1016/S0960-9822(06)00337-X;
Habraken Y., Sung P., Prakash L., Prakash S.;
"Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast
MLH1-PMS1 complex.";
Curr. Biol. 7:790-793(1997).
[12]
FUNCTION IN MMR.
PubMed=9111357; DOI=10.1128/MCB.17.5.2851;
Sia E.A., Kokoska R.J., Dominska M., Greenwell P., Petes T.D.;
"Microsatellite instability in yeast: dependence on repeat unit size
and DNA mismatch repair genes.";
Mol. Cell. Biol. 17:2851-2858(1997).
[13]
FUNCTION IN NHTR.
PubMed=9256462; DOI=10.1073/pnas.94.17.9214;
Sugawara N., Paques F., Colaiacovo M., Haber J.E.;
"Role of Saccharomyces cerevisiae Msh2 and Msh3 repair proteins in
double-strand break-induced recombination.";
Proc. Natl. Acad. Sci. U.S.A. 94:9214-9219(1997).
[14]
FUNCTION, DNA-BINDING, AND COMPLEX FORMATION WITH MLH1-PMS1.
PubMed=9545323; DOI=10.1074/jbc.273.16.9837;
Habraken Y., Sung P., Prakash L., Prakash S.;
"ATP-dependent assembly of a ternary complex consisting of a DNA
mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes.";
J. Biol. Chem. 273:9837-9841(1998).
[15]
MUTAGENESIS OF GLY-693.
PubMed=9819445; DOI=10.1128/MCB.18.12.7590;
Studamire B., Quach T., Alani E.;
"Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both
required during mismatch repair.";
Mol. Cell. Biol. 18:7590-7601(1998).
[16]
FUNCTION.
PubMed=9770499; DOI=10.1073/pnas.95.21.12404;
Flores-Rozas H., Kolodner R.D.;
"The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent
suppression of frameshift mutations.";
Proc. Natl. Acad. Sci. U.S.A. 95:12404-12409(1998).
[17]
MUTAGENESIS OF GLY-317; LEU-402; GLN-430; ASP-524; ARG-542; PRO-640
AND CYS-716.
PubMed=10469597; DOI=10.1016/S0960-9822(99)80396-0;
Drotschmann K., Clark A.B., Kunkel T.A.;
"Mutator phenotypes of common polymorphisms and missense mutations in
MSH2.";
Curr. Biol. 9:907-910(1999).
[18]
DNA-BINDING SPECIFICITY.
PubMed=10066781; DOI=10.1074/jbc.274.11.7200;
Marsischky G.T., Lee S., Griffith J., Kolodner R.D.;
"Saccharomyces cerevisiae MSH2/6 complex interacts with Holliday
junctions and facilitates their cleavage by phage resolution
enzymes.";
J. Biol. Chem. 274:7200-7206(1999).
[19]
DNA-BINDING SPECIFICITY.
PubMed=10480869; DOI=10.1074/jbc.274.38.26668;
Marsischky G.T., Kolodner R.D.;
"Biochemical characterization of the interaction between the
Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in
DNA.";
J. Biol. Chem. 274:26668-26682(1999).
[20]
FUNCTION.
PubMed=10518225; DOI=10.1016/S1097-2765(00)80346-9;
Ni T.T., Marsischky G.T., Kolodner R.D.;
"MSH2 and MSH6 are required for removal of adenine misincorporated
opposite 8-oxo-guanine in S. cerevisiae.";
Mol. Cell 4:439-444(1999).
[21]
MUTAGENESIS.
PubMed=10523644; DOI=10.1128/MCB.19.11.7558;
Studamire B., Price G., Sugawara N., Haber J.E., Alani E.;
"Separation-of-function mutations in Saccharomyces cerevisiae MSH2
that confer mismatch repair defects but do not affect nonhomologous-
tail removal during recombination.";
Mol. Cell. Biol. 19:7558-7567(1999).
[22]
MUTAGENESIS OF GLY-688; GLY-693; LYS-694 AND SER-695.
PubMed=10077621; DOI=10.1073/pnas.96.6.2970;
Drotschmann K., Clark A.B., Tran H.T., Resnick M.A., Gordenin D.A.,
Kunkel T.A.;
"Mutator phenotypes of yeast strains heterozygous for mutations in the
MSH2 gene.";
Proc. Natl. Acad. Sci. U.S.A. 96:2970-2975(1999).
[23]
INTERACTION WITH POL30.
PubMed=11005803; DOI=10.1074/jbc.C000513200;
Clark A.B., Valle F., Drotschmann K., Gary R.K., Kunkel T.A.;
"Functional interaction of proliferating cell nuclear antigen with
MSH2-MSH6 and MSH2-MSH3 complexes.";
J. Biol. Chem. 275:36498-36501(2000).
[24]
MUTAGENESIS OF GLY-317; PRO-640 AND HIS-658.
PubMed=11555625; DOI=10.1093/hmg/10.18.1889;
Ellison A.R., Lofing J., Bitter G.A.;
"Functional analysis of human MLH1 and MSH2 missense variants and
hybrid human-yeast MLH1 proteins in Saccharomyces cerevisiae.";
Hum. Mol. Genet. 10:1889-1900(2001).
[25]
DNA-BINDING, AND MUTAGENESIS OF TYR-42 AND LYS-65.
PubMed=11641390; DOI=10.1074/jbc.C100450200;
Drotschmann K., Yang W., Brownewell F.E., Kool E.T., Kunkel T.A.;
"Asymmetric recognition of DNA local distortion. Structure-based
functional studies of eukaryotic Msh2-Msh6.";
J. Biol. Chem. 276:46225-46229(2001).
[26]
FUNCTION, AND COMPLEX FORMATION WITH MLH1-PMS1.
PubMed=11237611; DOI=10.1006/jmbi.2001.4467;
Bowers J., Tran P.T., Joshi A., Liskay R.M., Alani E.;
"MSH-MLH complexes formed at a DNA mismatch are disrupted by the PCNA
sliding clamp.";
J. Mol. Biol. 306:957-968(2001).
[27]
FUNCTION, AND MUTAGENESIS OF GLU-768.
PubMed=12509278; DOI=10.1016/S1568-7864(02)00081-2;
Drotschmann K., Yang W., Kunkel T.A.;
"Evidence for sequential action of two ATPase active sites in yeast
Msh2-Msh6.";
DNA Repair 1:743-753(2002).
[28]
FUNCTION.
PubMed=12820877; DOI=10.1021/bi034602h;
Antony E., Hingorani M.M.;
"Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-
bound state at the initiation of DNA repair.";
Biochemistry 42:7682-7693(2003).
[29]
INTERACTION WITH POL30.
PubMed=12435741; DOI=10.1074/jbc.C200627200;
Lau P.J., Kolodner R.D.;
"Transfer of the MSH2.MSH6 complex from proliferating cell nuclear
antigen to mispaired bases in DNA.";
J. Biol. Chem. 278:14-17(2003).
[30]
FUNCTION, AND MUTAGENESIS OF SER-561; LYS-564; GLY-566; SER-656 AND
ARG-730.
PubMed=12875840; DOI=10.1016/S0022-2836(03)00694-6;
Kijas A.W., Studamire B., Alani E.;
"Msh2 separation of function mutations confer defects in the
initiation steps of mismatch repair.";
J. Mol. Biol. 331:123-138(2003).
[31]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[32]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[33]
ENZYME REGULATION, AND MUTAGENESIS OF GLU-768.
PubMed=15513922; DOI=10.1074/jbc.C400495200;
Clark A.B., Kunkel T.A.;
"Cadmium inhibits the functions of eukaryotic MutS complexes.";
J. Biol. Chem. 279:53903-53906(2004).
[34]
FUNCTION, AND COMPLEX FORMATION WITH MLH1-PMS1.
PubMed=15811858; DOI=10.1074/jbc.M407545200;
Mendillo M.L., Mazur D.J., Kolodner R.D.;
"Analysis of the interaction between the Saccharomyces cerevisiae
MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-
blocking system.";
J. Biol. Chem. 280:22245-22257(2005).
[35]
FUNCTION.
PubMed=16337600; DOI=10.1016/j.molcel.2005.10.014;
Jiang J., Bai L., Surtees J.A., Gemici Z., Wang M.D., Alani E.;
"Detection of high-affinity and sliding clamp modes for MSH2-MSH6 by
single-molecule unzipping force analysis.";
Mol. Cell 20:771-781(2005).
[36]
ENZYME REGULATION.
PubMed=15746000; DOI=10.1093/nar/gki291;
Banerjee S., Flores-Rozas H.;
"Cadmium inhibits mismatch repair by blocking the ATPase activity of
the MSH2-MSH6 complex.";
Nucleic Acids Res. 33:1410-1419(2005).
[37]
FUNCTION, AND MUTAGENESIS OF LYS-694 AND GLU-768.
PubMed=16214425; DOI=10.1016/j.dnarep.2005.08.016;
Antony E., Khubchandani S., Chen S., Hingorani M.M.;
"Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and
DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6
mismatch repair protein.";
DNA Repair 5:153-162(2006).
[38]
FUNCTION.
PubMed=16702432; DOI=10.1534/genetics.106.055616;
Stone J.E., Petes T.D.;
"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.";
Genetics 173:1223-1239(2006).
[39]
FUNCTION, AND MUTAGENESIS OF LYS-694.
PubMed=16600868; DOI=10.1016/j.molcel.2006.02.010;
Mazur D.J., Mendillo M.L., Kolodner R.D.;
"Inhibition of Msh6 ATPase activity by mispaired DNA induces a
Msh2(ATP)-Msh6(ATP) state capable of hydrolysis-independent movement
along DNA.";
Mol. Cell 22:39-49(2006).
[40]
FUNCTION IN NHTR, AND DNA-BINDING.
PubMed=16781730; DOI=10.1016/j.jmb.2006.05.032;
Surtees J.A., Alani E.;
"Mismatch repair factor MSH2-MSH3 binds and alters the conformation of
branched DNA structures predicted to form during genetic
recombination.";
J. Mol. Biol. 360:523-536(2006).
[41]
FUNCTION, AND DNA-BINDING.
PubMed=17157869; DOI=10.1016/j.jmb.2006.10.099;
Lee S.D., Surtees J.A., Alani E.;
"Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display
distinct requirements for DNA binding domain I in mismatch
recognition.";
J. Mol. Biol. 366:53-66(2007).
[42]
FUNCTION.
PubMed=17636021; DOI=10.1128/MCB.00855-07;
Harrington J.M., Kolodner R.D.;
"Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base
mispairs.";
Mol. Cell. Biol. 27:6546-6554(2007).
[43]
INTERACTION WITH SAW1.
PubMed=18471978; DOI=10.1016/j.molcel.2008.02.028;
Li F., Dong J., Pan X., Oum J.-H., Boeke J.D., Lee S.E.;
"Microarray-based genetic screen defines SAW1, a gene required for
Rad1/Rad10-dependent processing of recombination intermediates.";
Mol. Cell 30:325-335(2008).
-!- 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. {ECO:0000269|PubMed:10518225,
ECO:0000269|PubMed:11237611, ECO:0000269|PubMed:12509278,
ECO:0000269|PubMed:12820877, ECO:0000269|PubMed:12875840,
ECO:0000269|PubMed:15811858, ECO:0000269|PubMed:16214425,
ECO:0000269|PubMed:16337600, ECO:0000269|PubMed:16600868,
ECO:0000269|PubMed:16702432, ECO:0000269|PubMed:16781730,
ECO:0000269|PubMed:17157869, ECO:0000269|PubMed:17636021,
ECO:0000269|PubMed:8600025, ECO:0000269|PubMed:9111357,
ECO:0000269|PubMed:9256462, ECO:0000269|PubMed:9368761,
ECO:0000269|PubMed:9545323, ECO:0000269|PubMed:9770499}.
-!- ENZYME REGULATION: Inhibited by Cd(2+).
{ECO:0000269|PubMed:15513922, ECO:0000269|PubMed:15746000}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:11005803, ECO:0000269|PubMed:12435741,
ECO:0000269|PubMed:18471978, ECO:0000269|PubMed:8600025,
ECO:0000269|PubMed:8805366, ECO:0000269|PubMed:8816473,
ECO:0000269|PubMed:8858149}.
-!- INTERACTION:
P39875:EXO1; NbExp=3; IntAct=EBI-11352, EBI-6738;
P25336:MSH3; NbExp=3; IntAct=EBI-11352, EBI-11362;
Q03834:MSH6; NbExp=6; IntAct=EBI-11352, EBI-11383;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 1230 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
{ECO:0000305}.
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EMBL; M84170; AAA34802.1; -; Genomic_DNA.
EMBL; X83121; CAA58189.1; -; Genomic_DNA.
EMBL; Z74832; CAA99102.1; -; Genomic_DNA.
EMBL; BK006948; DAA10694.1; -; Genomic_DNA.
PIR; S57379; S57379.
RefSeq; NP_014551.1; NM_001183344.1.
ProteinModelPortal; P25847; -.
SMR; P25847; -.
BioGrid; 34312; 273.
DIP; DIP-2415N; -.
IntAct; P25847; 38.
MINT; MINT-631153; -.
STRING; 4932.YOL090W; -.
iPTMnet; P25847; -.
MaxQB; P25847; -.
PaxDb; P25847; -.
PRIDE; P25847; -.
EnsemblFungi; YOL090W; YOL090W; YOL090W.
GeneID; 854063; -.
KEGG; sce:YOL090W; -.
EuPathDB; FungiDB:YOL090W; -.
SGD; S000005450; MSH2.
GeneTree; ENSGT00550000074867; -.
HOGENOM; HOG000196498; -.
InParanoid; P25847; -.
KO; K08735; -.
OMA; GDFYTAH; -.
OrthoDB; EOG092C0EWT; -.
BioCyc; YEAST:G3O-33490-MONOMER; -.
Reactome; R-SCE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
Reactome; R-SCE-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
PRO; PR:P25847; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0032301; C:MutSalpha complex; IPI:SGD.
GO; GO:0032302; C:MutSbeta complex; IPI:SGD.
GO; GO:0000228; C:nuclear chromosome; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants.
GO; GO:0005524; F:ATP binding; IDA:SGD.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
GO; GO:0000406; F:double-strand/single-strand DNA junction binding; IDA:SGD.
GO; GO:0000400; F:four-way junction DNA binding; IDA:SGD.
GO; GO:0030983; F:mismatched DNA binding; IEA:EnsemblPlants.
GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IGI:SGD.
GO; GO:0006310; P:DNA recombination; IMP:SGD.
GO; GO:0036297; P:interstrand cross-link repair; IGI:SGD.
GO; GO:0043570; P:maintenance of DNA repeat elements; IBA:GO_Central.
GO; GO:0006311; P:meiotic gene conversion; IMP:SGD.
GO; GO:0000710; P:meiotic mismatch repair; IMP:SGD.
GO; GO:0006298; P:mismatch repair; IMP:SGD.
GO; GO:0006312; P:mitotic recombination; IMP:SGD.
GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IBA:GO_Central.
GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
GO; GO:0006290; P:pyrimidine dimer repair; IEA:EnsemblPlants.
GO; GO:0000735; P:removal of nonhomologous ends; IMP:SGD.
GO; GO:0043111; P:replication fork arrest; IMP:SGD.
Gene3D; 3.30.420.110; -; 1.
Gene3D; 3.40.1170.10; -; 1.
InterPro; IPR011184; DNA_mismatch_repair_Msh2.
InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
InterPro; IPR032642; Msh2.
InterPro; IPR036678; MutS_con_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11361:SF35; PTHR11361:SF35; 1.
Pfam; PF01624; MutS_I; 1.
Pfam; PF05188; MutS_II; 1.
Pfam; PF05192; MutS_III; 1.
Pfam; PF05190; MutS_IV; 1.
Pfam; PF00488; MutS_V; 1.
PIRSF; PIRSF005813; MSH2; 1.
SMART; SM00534; MUTSac; 1.
SMART; SM00533; MUTSd; 1.
SUPFAM; SSF48334; SSF48334; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding;
Nucleotide-binding; Nucleus; Reference proteome.
CHAIN 1 964 DNA mismatch repair protein MSH2.
/FTId=PRO_0000115191.
NP_BIND 688 695 ATP. {ECO:0000255}.
REGION 851 964 Interaction with MSH6.
MUTAGEN 42 42 Y->A: Moderately reduced activity in a
mismatch repair assay.
{ECO:0000269|PubMed:11641390}.
MUTAGEN 65 65 K->A: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:11641390}.
MUTAGEN 317 317 G->D: Partially defective in a mismatch
repair assay.
{ECO:0000269|PubMed:10469597,
ECO:0000269|PubMed:11555625}.
MUTAGEN 402 402 L->F: Partially defective in a mismatch
repair assay.
{ECO:0000269|PubMed:10469597}.
MUTAGEN 430 430 Q->K: Partially defective in a mismatch
repair assay.
{ECO:0000269|PubMed:10469597}.
MUTAGEN 518 518 A->P: Defective in MMR, but not in NHTR.
{ECO:0000269|PubMed:10523644}.
MUTAGEN 524 524 D->Y: Partially defective in a mismatch
repair assay.
{ECO:0000269|PubMed:10469597}.
MUTAGEN 542 542 R->P: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:10469597}.
MUTAGEN 561 561 S->P: Causes strong defects in MutS alpha
mismatch binding. Defective in MMR, but
not in NHTR.
{ECO:0000269|PubMed:12875840}.
MUTAGEN 564 564 K->E: Causes strong defects in MutS alpha
mismatch binding. Defective in MMR, but
not in NHTR.
{ECO:0000269|PubMed:12875840}.
MUTAGEN 566 566 G->D: Defective in MMR, but not in NHTR.
{ECO:0000269|PubMed:12875840}.
MUTAGEN 574 574 L->S: Defective in MMR and in NHTR.
{ECO:0000269|PubMed:10523644}.
MUTAGEN 584 584 L->P: Defective in MMR and in NHTR.
{ECO:0000269|PubMed:10523644}.
MUTAGEN 640 640 P->L: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:10469597,
ECO:0000269|PubMed:11555625}.
MUTAGEN 656 656 S->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.
{ECO:0000269|PubMed:12875840}.
MUTAGEN 658 658 H->Y: Fully functional in a mismatch
repair assay.
{ECO:0000269|PubMed:11555625}.
MUTAGEN 688 688 G->A: Moderately reduced activity in a
mismatch repair assay.
{ECO:0000269|PubMed:10077621}.
MUTAGEN 693 693 G->A,S: Has a dominant negative mutator
effect. {ECO:0000269|PubMed:10077621,
ECO:0000269|PubMed:9819445}.
MUTAGEN 693 693 G->D: Has no defect in mismatch DNA
binding, but lacks ATP-induced
conformational change. Defective in MMR
and in NHTR.
{ECO:0000269|PubMed:10077621,
ECO:0000269|PubMed:9819445}.
MUTAGEN 694 694 K->A: Impairs ATP binding; reduces
catalytic activity 1.6-fold for ATP
hydrolysis. Has a dominant negative
mutator effect.
{ECO:0000269|PubMed:10077621,
ECO:0000269|PubMed:16214425,
ECO:0000269|PubMed:16600868}.
MUTAGEN 694 694 K->R: Defective in MMR and in NHTR.
{ECO:0000269|PubMed:10077621,
ECO:0000269|PubMed:16214425,
ECO:0000269|PubMed:16600868}.
MUTAGEN 695 695 S->A: Has a dominant negative mutator
effect. {ECO:0000269|PubMed:10077621}.
MUTAGEN 716 716 C->F: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:10469597}.
MUTAGEN 730 730 R->W: Disruptes MutS alpha ATPase
activity, but does not affect ATP binding
or interactions with MutL alpha.
Defective in MMR, but not in NHTR.
{ECO:0000269|PubMed:12875840}.
MUTAGEN 742 742 S->F: Defective in MMR, but not in NHTR.
{ECO:0000269|PubMed:10523644}.
MUTAGEN 742 742 S->P: Defective in MMR and in NHTR.
{ECO:0000269|PubMed:10523644}.
MUTAGEN 768 768 E->A: Reduces catalytic activity 50-fold
for ATP hydrolysis.
{ECO:0000269|PubMed:12509278,
ECO:0000269|PubMed:15513922,
ECO:0000269|PubMed:16214425}.
MUTAGEN 773 773 T->I: Defective in MMR and in NHTR.
{ECO:0000269|PubMed:10523644}.
MUTAGEN 855 855 G->D: Defective in MMR, but not in NHTR.
{ECO:0000269|PubMed:10523644}.
MUTAGEN 859 859 A->E: Defective in MMR, but not in NHTR.
{ECO:0000269|PubMed:10523644}.
MUTAGEN 862 862 V->D: Defective in MMR, but not in NHTR.
{ECO:0000269|PubMed:10523644}.
MUTAGEN 863 868 Missing: Defective in MMR and in NHTR.
{ECO:0000269|PubMed:10523644}.
CONFLICT 957 964 KYIKALLL -> EIYKSPCCYN (in Ref. 1;
AAA34802). {ECO:0000305}.
SEQUENCE 964 AA; 108884 MW; 43FFD8A640138AE4 CRC64;
MSSTRPELKF SDVSEERNFY KKYTGLPKKP LKTIRLVDKG DYYTVIGSDA IFVADSVYHT
QSVLKNCQLD PVTAKNFHEP TKYVTVSLQV LATLLKLCLL DLGYKVEIYD KGWKLIKSAS
PGNIEQVNEL MNMNIDSSII IASLKVQWNS QDGNCIIGVA FIDTTAYKVG MLDIVDNEVY
SNLESFLIQL GVKECLVQDL TSNSNSNAEM QKVINVIDRC GCVVTLLKNS EFSEKDVELD
LTKLLGDDLA LSLPQKYSKL SMGACNALIG YLQLLSEQDQ VGKYELVEHK LKEFMKLDAS
AIKALNLFPQ GPQNPFGSNN LAVSGFTSAG NSGKVTSLFQ LLNHCKTNAG VRLLNEWLKQ
PLTNIDEINK RHDLVDYLID QIELRQMLTS EYLPMIPDIR RLTKKLNKRG NLEDVLKIYQ
FSKRIPEIVQ VFTSFLEDDS PTEPVNELVR SVWLAPLSHH VEPLSKFEEM VETTVDLDAY
EENNEFMIKV EFNEELGKIR SKLDTLRDEI HSIHLDSAED LGFDPDKKLK LENHHLHGWC
MRLTRNDAKE LRKHKKYIEL STVKAGIFFS TKQLKSIANE TNILQKEYDK QQSALVREII
NITLTYTPVF EKLSLVLAHL DVIASFAHTS SYAPIPYIRP KLHPMDSERR THLISSRHPV
LEMQDDISFI SNDVTLESGK GDFLIITGPN MGGKSTYIRQ VGVISLMAQI GCFVPCEEAE
IAIVDAILCR VGAGDSQLKG VSTFMVEILE TASILKNASK NSLIIVDELG RGTSTYDGFG
LAWAIAEHIA SKIGCFALFA THFHELTELS EKLPNVKNMH VVAHIEKNLK EQKHDDEDIT
LLYKVEPGIS DQSFGIHVAE VVQFPEKIVK MAKRKANELD DLKTNNEDLK KAKLSLQEVN
EGNIRLKALL KEWIRKVKEE GLHDPSKITE EASQHKIQEL LRAIANEPEK ENDNYLKYIK
ALLL


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