Q03834 (MSH6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA mismatch repair protein MSH6

Alternative name(s):
MutS protein homolog 6
Postmeiotic segregation protein 3

Gene names

Name:	MSH6
Synonyms:	PMS3
Ordered Locus Names:	YDR097C
ORF Names:	YD8557.04C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1242 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4 Ref.6 Ref.7 Ref.9 Ref.14 Ref.16 Ref.20 Ref.21 Ref.23 Ref.28 Ref.29 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.41
Enzyme regulation	Inhibited by Cd2+. Ref.27 Ref.30
Subunit structure	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. Ref.4 Ref.5 Ref.15 Ref.18 Ref.24
Subcellular location	Nucleus Ref.25.
Domain	The PIP box serves as a PCNA(POL30)-recognition and -binding motif. Ref.38
Miscellaneous	Present with 5330 molecules/cell in log phase SD medium. Ref.26
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
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	maintenance of DNA repeat elements Inferred from Biological aspect of Ancestor. Source: RefGenome meiotic mismatch repair Inferred from mutant phenotype Ref.32. Source: SGD negative regulation of DNA recombination Inferred from Biological aspect of Ancestor. Source: RefGenome reciprocal meiotic recombination Inferred from Biological aspect of Ancestor. Source: RefGenome response to UV Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	MutSalpha complex Inferred from physical interaction Ref.5. Source: SGD nuclear chromosome Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	ATP binding Inferred from direct assay Ref.7. 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 four-way junction DNA binding Inferred from direct assay Ref.11. Source: SGD mismatched DNA binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MSH2	P25847	6	EBI-11383,EBI-11352

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1242	1242	DNA mismatch repair protein MSH6		PRO_0000115213
Regions
	DNA binding	228 – 299	72	Ref.7 Ref.11 Ref.13 Ref.19 Ref.38
	Nucleotide binding	982 – 989	8	ATP Potential
	Region	305 – 421	117	Mispair-binding domain
	Motif	27 – 34	8	PIP box
Amino acid modifications
	Modified residue	20	1	Phosphoserine Ref.39 Ref.40 Ref.42
	Modified residue	21	1	Phosphoserine Ref.39 Ref.40 Ref.42
	Modified residue	97	1	Phosphoserine Ref.42
	Modified residue	102	1	Phosphoserine; by ATM or ATR Ref.40 Ref.42
	Modified residue	107	1	Phosphoserine Ref.42
	Modified residue	129	1	Phosphoserine Ref.39 Ref.42
	Modified residue	130	1	Phosphoserine; by ATM or ATR Ref.39 Ref.40 Ref.42
	Modified residue	145	1	Phosphoserine Ref.37 Ref.39 Ref.40 Ref.42
	Modified residue	150	1	Phosphoserine Ref.37 Ref.39 Ref.40 Ref.42
	Modified residue	152	1	Phosphothreonine Ref.40
	Modified residue	201	1	Phosphoserine Ref.42
	Modified residue	258	1	Phosphoserine Ref.40
	Modified residue	451	1	Phosphothreonine Ref.42
Experimental info
	Mutagenesis	26 – 27	2	KQ → AA: Partially functional in a mismatch repair assay; when associated with 33-AA-34. Ref.15 Ref.18
	Mutagenesis	33 – 34	2	FF → 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. Ref.15 Ref.18
	Mutagenesis	301	1	L → V: Fully functional in a mismatch repair assay. Ref.10 Ref.15 Ref.18
	Mutagenesis	313	1	P → A: Fully functional in a mismatch repair assay. Ref.15 Ref.18 Ref.19
	Mutagenesis	337	1	F → A: Shows defects in both homoduplex and mispair DNA binding and is only partially functional in a mismatch repair assay. Ref.12 Ref.15 Ref.16 Ref.18 Ref.19
	Mutagenesis	337	1	F → H, I or Y: Partially functional in a mismatch repair assay. Ref.12 Ref.15 Ref.16 Ref.18 Ref.19
	Mutagenesis	337	1	F → K: Completely abolishes mismatch repair. Ref.12 Ref.15 Ref.16 Ref.18 Ref.19
	Mutagenesis	337	1	F → S in MSH6-6; partially functional in a mismatch repair assay. Ref.12 Ref.15 Ref.16 Ref.18 Ref.19
	Mutagenesis	339	1	E → A: Defective in repairing 8-oxo-G-A mismatches. Ref.15 Ref.18 Ref.19 Ref.35
	Mutagenesis	340 – 343	4	LYEK → CFAE in MSH6-340; shows defects in mispair DNA binding, but not in homoduplex DNA binding. Ref.15 Ref.18
	Mutagenesis	368	1	G → A: Moderately reduced activity in a mismatch repair assay. Ref.15 Ref.18 Ref.19
	Mutagenesis	370	1	P → A: Partially functional in a mismatch repair assay. Ref.15 Ref.18 Ref.19
	Mutagenesis	393	1	Q → A: Moderately reduced activity in a mismatch repair assay. Ref.15 Ref.18 Ref.19
	Mutagenesis	393	1	Q → R in MSH6-5; partially functional in a mismatch repair assay. Ref.15 Ref.18 Ref.19
	Mutagenesis	412	1	R → A: Completely abolishes mismatch repair. Ref.15 Ref.18 Ref.19
	Mutagenesis	412	1	R → G in MSH6-7; partially functional in a mismatch repair assay. Ref.15 Ref.18 Ref.19
	Mutagenesis	421	1	G → D in PMS3-1; completely abolishes mismatch repair. Ref.4 Ref.15 Ref.18
	Mutagenesis	477	1	G → R: Partially functional in a mismatch repair assay. Ref.10 Ref.15 Ref.18
	Mutagenesis	848	1	K → A: Fully functional in a mismatch repair assay. Ref.15 Ref.18 Ref.19
	Mutagenesis	852	1	R → A: Moderately reduced activity in a mismatch repair assay. Ref.15 Ref.18 Ref.19
	Mutagenesis	987	1	G → D: Has no defect in mismatch DNA binding, but lacks ATP-induced conformational change. Ref.8 Ref.15 Ref.18
	Mutagenesis	988	1	K → A: Impairs ATP binding; reduces catalytic activity 13-fold for ATP hydrolysis. Ref.15 Ref.18 Ref.31 Ref.33
	Mutagenesis	1036	1	S → P in MSH6-4; defective for ATP-induced sliding clamp formation and assembly of ternary complexes with MutL alpha. Ref.15 Ref.18 Ref.22 Ref.34
	Mutagenesis	1062	1	E → A: Reduces catalytic activity 13-fold for ATP hydrolysis. Ref.15 Ref.18 Ref.21 Ref.27 Ref.31
	Mutagenesis	1067	1	G → D in MSH6-3; defective for ATP-induced sliding clamp formation and assembly of ternary complexes with MutL alpha. Ref.15 Ref.18 Ref.22 Ref.34
	Mutagenesis	1096	1	H → A in MSH6-9; shows normal mispair binding and dissociation, but fails to show complete mispair activation of the ATPase. Ref.15 Ref.18 Ref.22
	Mutagenesis	1142	1	G → D in MSH6-2; defective for ATP-induced sliding clamp formation, but assembles ternary complexes with MutL alpha. Ref.15 Ref.18 Ref.22 Ref.34

Sequences

	Sequence		Length	Mass (Da)
	Q03834 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 11A6883AADCFA222	FASTA	1,242	140,080
	10 20 30 40 50 60 MAPATPKTSK TAHFENGSTS SQKKMKQSSL LSFFSKQVPS GTPSKKVQKP TPATLENTAT 70 80 90 100 110 120 DKITKNPQGG KTGKLFVDVD EDNDLTIAEE TVSTVRSDIM HSQEPQSDTM LNSNTTEPKS 130 140 150 160 170 180 TTTDEDLSSS QSRRNHKRRV NYAESDDDDS DTTFTAKRKK GKVVDSESDE DEYLPDKNDG 190 200 210 220 230 240 DEDDDIADDK EDIKGELAED SGDDDDLISL AETTSKKKFS YNTSHSSSPF TRNISRDNSK 250 260 270 280 290 300 KKSRPNQAPS RSYNPSHSQP SATSKSSKFN KQNEERYQWL VDERDAQRRP KSDPEYDPRT 310 320 330 340 350 360 LYIPSSAWNK FTPFEKQYWE IKSKMWDCIV FFKKGKFFEL YEKDALLANA LFDLKIAGGG 370 380 390 400 410 420 RANMQLAGIP EMSFEYWAAQ FIQMGYKVAK VDQRESMLAK EMREGSKGIV KRELQCILTS 430 440 450 460 470 480 GTLTDGDMLH SDLATFCLAI REEPGNFYNE TQLDSSTIVQ KLNTKIFGAA FIDTATGELQ 490 500 510 520 530 540 MLEFEDDSEC TKLDTLMSQV RPMEVVMERN NLSTLANKIV KFNSAPNAIF NEVKAGEEFY 550 560 570 580 590 600 DCDKTYAEII SSEYFSTEED WPEVLKSYYD TGKKVGFSAF GGLLYYLKWL KLDKNLISMK 610 620 630 640 650 660 NIKEYDFVKS QHSMVLDGIT LQNLEIFSNS FDGSDKGTLF KLFNRAITPM GKRMMKKWLM 670 680 690 700 710 720 HPLLRKNDIE SRLDSVDSLL QDITLREQLE ITFSKLPDLE RMLARIHSRT IKVKDFEKVI 730 740 750 760 770 780 TAFETIIELQ DSLKNNDLKG DVSKYISSFP EGLVEAVKSW TNAFERQKAI NENIIVPQRG 790 800 810 820 830 840 FDIEFDKSMD RIQELEDELM EILMTYRKQF KCSNIQYKDS GKEIYTIEIP ISATKNVPSN 850 860 870 880 890 900 WVQMAANKTY KRYYSDEVRA LARSMAEAKE IHKTLEEDLK NRLCQKFDAH YNTIWMPTIQ 910 920 930 940 950 960 AISNIDCLLA ITRTSEYLGA PSCRPTIVDE VDSKTNTQLN GFLKFKSLRH PCFNLGATTA 970 980 990 1000 1010 1020 KDFIPNDIEL GKEQPRLGLL TGANAAGKST ILRMACIAVI MAQMGCYVPC ESAVLTPIDR 1030 1040 1050 1060 1070 1080 IMTRLGANDN IMQGKSTFFV ELAETKKILD MATNRSLLVV DELGRGGSSS DGFAIAESVL 1090 1100 1110 1120 1130 1140 HHVATHIQSL GFFATHYGTL ASSFKHHPQV RPLKMSILVD EATRNVTFLY KMLEGQSEGS 1150 1160 1170 1180 1190 1200 FGMHVASMCG ISKEIIDNAQ IAADNLEHTS RLVKERDLAA NNLNGEVVSV PGGLQSDFVR 1210 1220 1230 1240 IAYGDGLKNT KLGSGEGVLN YDWNIKRNVL KSLFSIIDDL QS

References

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[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"MSH6, a Saccharomyces cerevisiae protein that binds to mismatches as a heterodimer with MSH2." Iaccarino I., Palombo F., Drummond J.T., Totty N.F., Hsuan J.J., Modrich P., Jiricny J. Curr. Biol. 6:484-486(1996) [PubMed: 8723353] [Abstract] Cited for: CHARACTERIZATION.
[4]	"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: 8600025] [Abstract] Cited for: FUNCTION, INTERACTION WITH MSH2, MUTAGENESIS OF GLY-421.
[5]	"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: 8816473] [Abstract] Cited for: CHARACTERIZATION, INTERACTION WITH MSH2.
[6]	"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: 9111357] [Abstract] Cited for: FUNCTION IN MMR.
[7]	"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: 9545323] [Abstract] Cited for: FUNCTION, DNA-BINDING, COMPLEX FORMATION WITH MLH1-PMS1.
[8]	"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: 9819445] [Abstract] Cited for: MUTAGENESIS OF GLY-987.
[9]	"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: 9770499] [Abstract] Cited for: FUNCTION.
[10]	"Germ-line msh6 mutations in colorectal cancer families." Kolodner R.D., Tytell J.D., Schmeits J.L., Kane M.F., Das Gupta R., Weger J., Wahlberg S., Fox E.A., Peel D., Ziogas A., Garber J.E., Syngal S., Anton-Culver H., Li F.P. Cancer Res. 59:5068-5074(1999) [PubMed: 10537275] [Abstract] Cited for: MUTAGENESIS OF LEU-301 AND GLY-477.
[11]	"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: 10066781] [Abstract] Cited for: DNA-BINDING SPECIFICITY.
[12]	"A mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition." Bowers J., Sokolsky T., Quach T., Alani E. J. Biol. Chem. 274:16115-16125(1999) [PubMed: 10347163] [Abstract] Cited for: MUTAGENESIS OF PHE-337.
[13]	"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: 10480869] [Abstract] Cited for: DNA-BINDING SPECIFICITY.
[14]	"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: 10518225] [Abstract] Cited for: FUNCTION.
[15]	"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: 11005803] [Abstract] Cited for: INTERACTION WITH POL30, MUTAGENESIS OF 26-LYS-GLN-27 AND 33-PHE-PHE-34.
[16]	"Analysis of yeast MSH2-MSH6 suggests that the initiation of mismatch repair can be separated into discrete steps." Bowers J., Tran P.T., Liskay R.M., Alani E. J. Mol. Biol. 302:327-338(2000) [PubMed: 10970737] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PHE-337.
[17]	"Novel dominant mutations in Saccharomyces cerevisiae MSH6." Das Gupta R., Kolodner R.D. Nat. Genet. 24:53-56(2000) [PubMed: 10615127] [Abstract] Cited for: MUTAGENESIS.
[18]	"Proliferating cell nuclear antigen and Msh2p-Msh6p interact to form an active mispair recognition complex." Flores-Rozas H., Clark D., Kolodner R.D. Nat. Genet. 26:375-378(2000) [PubMed: 11062484] [Abstract] Cited for: INTERACTION WITH POL30, MUTAGENESIS OF 33-PHE-PHE-34.
[19]	"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: 11641390] [Abstract] Cited for: DNA-BINDING, MUTAGENESIS OF PRO-313; PHE-337; GLU-339; GLY-368; PRO-370; GLN-393; ARG-412; LYS-848 AND ARG-852.
[20]	"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: 11237611] [Abstract] Cited for: FUNCTION, COMPLEX FORMATION WITH MLH1-PMS1.
[21]	"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: 12509278] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-1062.
[22]	"Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP." Hess M.T., Das Gupta R., Kolodner R.D. J. Biol. Chem. 277:25545-25553(2002) [PubMed: 11986324] [Abstract] Cited for: MUTAGENESIS OF SER-1036; GLY-1067; HIS-1096 AND GLY-1142.
[23]	"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: 12820877] [Abstract] Cited for: FUNCTION.
[24]	"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: 12435741] [Abstract] Cited for: INTERACTION WITH POL30.
[25]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[26]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[27]	"Cadmium inhibits the functions of eukaryotic MutS complexes." Clark A.B., Kunkel T.A. J. Biol. Chem. 279:53903-53906(2004) [PubMed: 15513922] [Abstract] Cited for: ENZYME REGULATION, MUTAGENESIS OF GLU-1062.
[28]	"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: 15811858] [Abstract] Cited for: FUNCTION, COMPLEX FORMATION WITH MLH1-PMS1.
[29]	"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: 16337600] [Abstract] Cited for: FUNCTION.
[30]	"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: 15746000] [Abstract] Cited for: ENZYME REGULATION.
[31]	"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: 16214425] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-988 AND GLU-1062.
[32]	"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: 16702432] [Abstract] Cited for: FUNCTION.
[33]	"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: 16600868] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-988.
[34]	"Biochemical basis for dominant mutations in the Saccharomyces cerevisiae MSH6 gene." Hess M.T., Mendillo M.L., Mazur D.J., Kolodner R.D. Proc. Natl. Acad. Sci. U.S.A. 103:558-563(2006) [PubMed: 16407100] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-1036; GLY-1067 AND GLY-1142.
[35]	"Specialized mismatch repair function of Glu339 in the Phe-X-Glu motif of yeast Msh6." Holmes S.F., Scarpinato K.D., McCulloch S.D., Schaaper R.M., Kunkel T.A. DNA Repair 6:293-303(2007) [PubMed: 17141577] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-339.
[36]	"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: 17157869] [Abstract] Cited for: FUNCTION.
[37]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-150, MASS SPECTROMETRY. Strain: ADR376.
[38]	"Multiple functions for the N-terminal region of Msh6." Clark A.B., Deterding L., Tomer K.B., Kunkel T.A. Nucleic Acids Res. 35:4114-4123(2007) [PubMed: 17567610] [Abstract] Cited for: FUNCTION, DNA-BINDING DOMAIN.
[39]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-21; SER-129; SER-130; SER-145 AND SER-150, MASS SPECTROMETRY.
[40]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-21; SER-102; SER-130; SER-145; SER-150; THR-152 AND SER-258, MASS SPECTROMETRY.
[41]	"Chimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-binding domain combines properties of both proteins." Shell S.S., Putnam C.D., Kolodner R.D. Proc. Natl. Acad. Sci. U.S.A. 104:10956-10961(2007) [PubMed: 17573527] [Abstract] Cited for: FUNCTION.
[42]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-21; SER-97; SER-102; SER-107; SER-129; SER-130; SER-145; SER-150; SER-201 AND THR-451, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z47746 Genomic DNA. Translation: CAA87671.1. BK006938 Genomic DNA. Translation: DAA11942.1.
PIR	S51246.
RefSeq	NP_010382.1. NM_001180405.1.
3D structure databases
ProteinModelPortal	Q03834.
SMR	Q03834. Positions 272-1174.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2423N.
IntAct	Q03834. 33 interactions.
MINT	MINT-618151.
STRING	Q03834.
Proteomic databases
PeptideAtlas	Q03834.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR097C; YDR097C; YDR097C.
GeneID	851671.
KEGG	sce:YDR097C.
NMPDR	fig|4932.3.peg.1128.
Organism-specific databases
CYGD	YDR097c.
SGD	S000002504. MSH6.
Phylogenomic databases
eggNOG	fuNOG04168.
GeneTree	EFGT00050000003033.
HOGENOM	HBG633062.
OMA	MAHISKY.
OrthoDB	EOG4F4WK5.
Gene expression databases
ArrayExpress	Q03834.
Genevestigator	Q03834.
GermOnline	YDR097C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR017261. DNA_mismatch_repair_Msh6. IPR007695. DNA_mismatch_repair_MutS-lik_N. IPR000432. DNA_mismatch_repair_MutS_C. IPR007861. DNA_mismatch_repair_MutS_clamp. IPR007860. DNA_mismatch_repair_MutS_connt. IPR007696. DNA_mismatch_repair_MutS_core. IPR016151. DNA_mismatch_repair_MutS_N. [Graphical view]
Gene3D	G3DSA:3.30.420.110. DNA_mismatch_repair_MutS_connt. 1 hit. G3DSA:3.40.1170.10. DNA_mismatch_repair_MutS_N. 1 hit.
KO	K08737.
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	PIRSF037677. DNA_mis_repair_Msh6. 1 hit.
SMART	SM00534. MUTSac. 1 hit. SM00533. MUTSd. 1 hit. [Graphical view]
SUPFAM	SSF53150. DNA_mismatch_repair_MutS_connt. 1 hit. SSF55271. DNA_mismatch_repair_MutS_N. 1 hit. SSF48334. DNA_repair_MutS_domIII. 1 hit.
PROSITE	PS00486. DNA_MISMATCH_REPAIR_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	969292.

Entry information

Entry name

MSH6_YEAST

Accession

Primary (citable) accession number: Q03834
Secondary accession number(s): D6VS82

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program