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Q03834 (MSH6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. 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 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1242 AA.
Sequence statusComplete.
Protein existenceEvidence 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.39

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.

Sequence similarities

Belongs to the DNA mismatch repair MutS family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MSH2P258476EBI-11383,EBI-11352

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12421242DNA mismatch repair protein MSH6
PRO_0000115213

Regions

DNA binding228 – 29972 Ref.7 Ref.11 Ref.13 Ref.19 Ref.38
Nucleotide binding982 – 9898ATP Potential
Region305 – 421117Mispair-binding domain
Motif27 – 348PIP box

Amino acid modifications

Modified residue1021Phosphoserine Ref.41
Modified residue1451Phosphoserine Ref.37 Ref.41 Ref.42
Modified residue1501Phosphoserine Ref.37 Ref.41 Ref.42
Modified residue2011Phosphoserine Ref.42
Modified residue4511Phosphothreonine Ref.41

Experimental info

Mutagenesis26 – 272KQ → AA: Partially functional in a mismatch repair assay; when associated with 33-AA-34. Ref.15 Ref.18
Mutagenesis33 – 342FF → 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
Mutagenesis3011L → V: Fully functional in a mismatch repair assay. Ref.10 Ref.15 Ref.18
Mutagenesis3131P → A: Fully functional in a mismatch repair assay. Ref.15 Ref.18 Ref.19
Mutagenesis3371F → 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
Mutagenesis3371F → H, I or Y: Partially functional in a mismatch repair assay. Ref.12 Ref.15 Ref.16 Ref.18 Ref.19
Mutagenesis3371F → K: Completely abolishes mismatch repair. Ref.12 Ref.15 Ref.16 Ref.18 Ref.19
Mutagenesis3371F → S in MSH6-6; partially functional in a mismatch repair assay. Ref.12 Ref.15 Ref.16 Ref.18 Ref.19
Mutagenesis3391E → A: Defective in repairing 8-oxo-G-A mismatches. Ref.15 Ref.18 Ref.19 Ref.35
Mutagenesis340 – 3434LYEK → CFAE in MSH6-340; shows defects in mispair DNA binding, but not in homoduplex DNA binding. Ref.15 Ref.18
Mutagenesis3681G → A: Moderately reduced activity in a mismatch repair assay. Ref.15 Ref.18 Ref.19
Mutagenesis3701P → A: Partially functional in a mismatch repair assay. Ref.15 Ref.18 Ref.19
Mutagenesis3931Q → A: Moderately reduced activity in a mismatch repair assay. Ref.15 Ref.18 Ref.19
Mutagenesis3931Q → R in MSH6-5; partially functional in a mismatch repair assay. Ref.15 Ref.18 Ref.19
Mutagenesis4121R → A: Completely abolishes mismatch repair. Ref.15 Ref.18 Ref.19
Mutagenesis4121R → G in MSH6-7; partially functional in a mismatch repair assay. Ref.15 Ref.18 Ref.19
Mutagenesis4211G → D in PMS3-1; completely abolishes mismatch repair. Ref.4 Ref.15 Ref.18
Mutagenesis4771G → R: Partially functional in a mismatch repair assay. Ref.10 Ref.15 Ref.18
Mutagenesis8481K → A: Fully functional in a mismatch repair assay. Ref.15 Ref.18 Ref.19
Mutagenesis8521R → A: Moderately reduced activity in a mismatch repair assay. Ref.15 Ref.18 Ref.19
Mutagenesis9871G → D: Has no defect in mismatch DNA binding, but lacks ATP-induced conformational change. Ref.8 Ref.15 Ref.18
Mutagenesis9881K → A: Impairs ATP binding; reduces catalytic activity 13-fold for ATP hydrolysis. Ref.15 Ref.18 Ref.31 Ref.33
Mutagenesis10361S → 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
Mutagenesis10621E → A: Reduces catalytic activity 13-fold for ATP hydrolysis. Ref.15 Ref.18 Ref.21 Ref.27 Ref.31
Mutagenesis10671G → 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
Mutagenesis10961H → 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
Mutagenesis11421G → 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 LengthMass (Da)Tools
Q03834 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 11A6883AADCFA222

FASTA1,242140,080
        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 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING DOMAIN.
[39]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[40]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-145; SER-150 AND THR-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-150 AND SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z47746 Genomic DNA. Translation: CAA87671.1.
BK006938 Genomic DNA. Translation: DAA11942.1.
PIRS51246.
RefSeqNP_010382.3. NM_001180405.3.

3D structure databases

ProteinModelPortalQ03834.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32152. 59 interactions.
DIPDIP-2423N.
IntActQ03834. 32 interactions.
MINTMINT-618151.
STRING4932.YDR097C.

Proteomic databases

PaxDbQ03834.
PeptideAtlasQ03834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR097C; YDR097C; YDR097C.
GeneID851671.
KEGGsce:YDR097C.

Organism-specific databases

CYGDYDR097c.
SGDS000002504. MSH6.

Phylogenomic databases

eggNOGCOG0249.
GeneTreeENSGT00550000075024.
HOGENOMHOG000189303.
KOK08737.
OMAHMDAVIG.
OrthoDBEOG773XQH.

Enzyme and pathway databases

BioCycYEAST:G3O-29700-MONOMER.

Gene expression databases

GenevestigatorQ03834.

Family and domain databases

Gene3D3.30.420.110. 1 hit.
3.40.1170.10. 1 hit.
3.40.50.300. 1 hit.
InterProIPR017261. DNA_mismatch_repair_Msh6.
IPR015536. DNA_mismatch_repair_MSH6_C.
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.
IPR016151. DNA_mismatch_repair_MutS_N.
IPR007860. DNA_mmatch_repair_MutS_con_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11361:SF31. PTHR11361:SF31. 1 hit.
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]
PIRSFPIRSF037677. DNA_mis_repair_Msh6. 1 hit.
SMARTSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view]
SUPFAMSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53150. SSF53150. 1 hit.
SSF55271. SSF55271. 1 hit.
PROSITEPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969292.
PROQ03834.

Entry information

Entry nameMSH6_YEAST
AccessionPrimary (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: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families