P25847 (MSH2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA mismatch repair protein MSH2

Alternative name(s):
MutS protein homolog 2

Gene names

Name:	MSH2
Ordered Locus Names:	YOL090W
ORF Names:	O0935

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	964 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 maintenance of DNA repeat elements Inferred from Biological aspect of Ancestor. Source: RefGenome meiotic gene conversion Inferred from mutant phenotype Ref.5. Source: SGD meiotic mismatch repair Inferred from mutant phenotype Ref.5Ref.38PubMed 8056309. Source: SGD negative regulation of reciprocal meiotic recombination Inferred from Biological aspect of Ancestor. Source: RefGenome postreplication repair Inferred from Biological aspect of Ancestor. Source: RefGenome removal of nonhomologous ends Inferred from mutant phenotype Ref.21Ref.13. Source: SGD
Cellular_component	MutSalpha 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_function	ATP binding Inferred from direct assay Ref.14. Source: SGD DNA-dependent ATPase activity Inferred from Biological aspect of Ancestor. Source: RefGenome damaged DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EXO1	P39875	3	EBI-11352,EBI-6738
MSH3	P25336	3	EBI-11352,EBI-11362
MSH6	Q03834	7	EBI-11352,EBI-11383

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 964	964	DNA mismatch repair protein MSH2		PRO_0000115191
Regions
	Nucleotide binding	688 – 695	8	ATP Potential
	Region	851 – 964	114	Interaction with MSH6
Experimental info
	Mutagenesis	42	1	Y → A: Moderately reduced activity in a mismatch repair assay. Ref.25
	Mutagenesis	65	1	K → A: Defective in a mismatch repair assay. Ref.25
	Mutagenesis	317	1	G → D: Partially defective in a mismatch repair assay. Ref.17 Ref.24
	Mutagenesis	402	1	L → F: Partially defective in a mismatch repair assay. Ref.17
	Mutagenesis	430	1	Q → K: Partially defective in a mismatch repair assay. Ref.17
	Mutagenesis	518	1	A → P: Defective in MMR, but not in NHTR.
	Mutagenesis	524	1	D → Y: Partially defective in a mismatch repair assay. Ref.17
	Mutagenesis	542	1	R → P: Defective in a mismatch repair assay. Ref.17
	Mutagenesis	561	1	S → P: Causes strong defects in MutS alpha mismatch binding. Defective in MMR, but not in NHTR. Ref.30
	Mutagenesis	564	1	K → E: Causes strong defects in MutS alpha mismatch binding. Defective in MMR, but not in NHTR. Ref.30
	Mutagenesis	566	1	G → D: Defective in MMR, but not in NHTR. Ref.30
	Mutagenesis	574	1	L → S: Defective in MMR and in NHTR.
	Mutagenesis	584	1	L → P: Defective in MMR and in NHTR.
	Mutagenesis	640	1	P → L: Defective in a mismatch repair assay. Ref.17 Ref.24
	Mutagenesis	656	1	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. Ref.30
	Mutagenesis	658	1	H → Y: Fully functional in a mismatch repair assay. Ref.24
	Mutagenesis	688	1	G → A: Moderately reduced activity in a mismatch repair assay. Ref.22
	Mutagenesis	693	1	G → A or S: Has a dominant negative mutator effect. Ref.15 Ref.22
	Mutagenesis	693	1	G → D: Has no defect in mismatch DNA binding, but lacks ATP-induced conformational change. Defective in MMR and in NHTR. Ref.15 Ref.22
	Mutagenesis	694	1	K → 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
	Mutagenesis	694	1	K → R: Defective in MMR and in NHTR. Ref.22 Ref.37 Ref.39
	Mutagenesis	695	1	S → A: Has a dominant negative mutator effect. Ref.22
	Mutagenesis	716	1	C → F: Defective in a mismatch repair assay. Ref.17
	Mutagenesis	730	1	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. Ref.30
	Mutagenesis	742	1	S → F: Defective in MMR, but not in NHTR.
	Mutagenesis	742	1	S → P: Defective in MMR and in NHTR.
	Mutagenesis	768	1	E → A: Reduces catalytic activity 50-fold for ATP hydrolysis. Ref.27 Ref.33 Ref.37
	Mutagenesis	773	1	T → I: Defective in MMR and in NHTR.
	Mutagenesis	855	1	G → D: Defective in MMR, but not in NHTR.
	Mutagenesis	859	1	A → E: Defective in MMR, but not in NHTR.
	Mutagenesis	862	1	V → D: Defective in MMR, but not in NHTR.
	Mutagenesis	863 – 868	6	Missing: Defective in MMR and in NHTR.
	Sequence conflict	957 – 964	8	KYIKALLL → EIYKSPCCYN in AAA34802. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P25847 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 43FFD8A640138AE4	FASTA	964	108,884
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.
PIR	S57379.
RefSeq	NP_014551.1. NM_001183344.1.
3D structure databases
ProteinModelPortal	P25847.
SMR	P25847. Positions 14-913.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2415N.
IntAct	P25847. 36 interactions.
MINT	MINT-631153.
STRING	4932.YOL090W.
Proteomic databases
PaxDb	P25847.
PeptideAtlas	P25847.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOL090W; YOL090W; YOL090W.
GeneID	854063.
KEGG	sce:YOL090W.
Organism-specific databases
CYGD	YOL090w.
SGD	S000005450. MSH2.
Phylogenomic databases
eggNOG	COG0249.
GeneTree	ENSGT00550000074867.
HOGENOM	HOG000196498.
KO	K08735.
OMA	WAISEHI.
OrthoDB	EOG4S7NZ5.
Gene expression databases
Genevestigator	P25847.
GermOnline	YOL090W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.420.110. 1 hit.
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. IPR007860. DNA_mmatch_repair_MutS_con_dom. [Graphical view]
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. [Graphical view]
PIRSF	PIRSF005813. MSH2. 1 hit.
SMART	SM00534. MUTSac. 1 hit. SM00533. MUTSd. 1 hit. [Graphical view]
SUPFAM	SSF48334. DNA_repair_MutS_domIII. 1 hit.
PROSITE	PS00486. DNA_MISMATCH_REPAIR_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	975668.

Entry information

Entry name

MSH2_YEAST

Accession

Primary (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:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program