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Q03834

- MSH6_YEAST

UniProt

Q03834 - MSH6_YEAST

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Protein

DNA mismatch repair protein MSH6

Gene

MSH6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.19 Publications

Enzyme regulationi

Inhibited by Cd2+.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi228 – 29972Add
BLAST
Nucleotide bindingi982 – 9898ATPSequence Analysis

GO - Molecular functioni

  1. ATPase activity Source: SGD
  2. ATP binding Source: SGD
  3. four-way junction DNA binding Source: SGD
  4. mismatched DNA binding Source: InterPro

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. interstrand cross-link repair Source: SGD
  3. meiotic mismatch repair Source: SGD
  4. mismatch repair Source: SGD
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29700-MONOMER.
ReactomeiREACT_238711. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).

Names & Taxonomyi

Protein namesi
Recommended name:
DNA mismatch repair protein MSH6
Alternative name(s):
MutS protein homolog 6
Postmeiotic segregation protein 3
Gene namesi
Name:MSH6
Synonyms:PMS3
Ordered Locus Names:YDR097C
ORF Names:YD8557.04C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR097c.
SGDiS000002504. MSH6.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. MutSalpha complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 272KQ → AA: Partially functional in a mismatch repair assay; when associated with 33-AA-34. 1 Publication
Mutagenesisi33 – 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. 2 Publications
Mutagenesisi301 – 3011L → V: Fully functional in a mismatch repair assay. 1 Publication
Mutagenesisi313 – 3131P → A: Fully functional in a mismatch repair assay. 1 Publication
Mutagenesisi337 – 3371F → A: Shows defects in both homoduplex and mispair DNA binding and is only partially functional in a mismatch repair assay. 3 Publications
Mutagenesisi337 – 3371F → H, I or Y: Partially functional in a mismatch repair assay. 3 Publications
Mutagenesisi337 – 3371F → K: Completely abolishes mismatch repair. 3 Publications
Mutagenesisi337 – 3371F → S in MSH6-6; partially functional in a mismatch repair assay. 3 Publications
Mutagenesisi339 – 3391E → A: Defective in repairing 8-oxo-G-A mismatches. 2 Publications
Mutagenesisi340 – 3434LYEK → CFAE in MSH6-340; shows defects in mispair DNA binding, but not in homoduplex DNA binding. 1 Publication
Mutagenesisi368 – 3681G → A: Moderately reduced activity in a mismatch repair assay. 1 Publication
Mutagenesisi370 – 3701P → A: Partially functional in a mismatch repair assay. 1 Publication
Mutagenesisi393 – 3931Q → A: Moderately reduced activity in a mismatch repair assay. 1 Publication
Mutagenesisi393 – 3931Q → R in MSH6-5; partially functional in a mismatch repair assay. 1 Publication
Mutagenesisi412 – 4121R → A: Completely abolishes mismatch repair. 1 Publication
Mutagenesisi412 – 4121R → G in MSH6-7; partially functional in a mismatch repair assay. 1 Publication
Mutagenesisi421 – 4211G → D in PMS3-1; completely abolishes mismatch repair. 1 Publication
Mutagenesisi477 – 4771G → R: Partially functional in a mismatch repair assay. 1 Publication
Mutagenesisi848 – 8481K → A: Fully functional in a mismatch repair assay. 1 Publication
Mutagenesisi852 – 8521R → A: Moderately reduced activity in a mismatch repair assay. 1 Publication
Mutagenesisi987 – 9871G → D: Has no defect in mismatch DNA binding, but lacks ATP-induced conformational change. 1 Publication
Mutagenesisi988 – 9881K → A: Impairs ATP binding; reduces catalytic activity 13-fold for ATP hydrolysis. 2 Publications
Mutagenesisi1036 – 10361S → P in MSH6-4; defective for ATP-induced sliding clamp formation and assembly of ternary complexes with MutL alpha. 2 Publications
Mutagenesisi1062 – 10621E → A: Reduces catalytic activity 13-fold for ATP hydrolysis. 3 Publications
Mutagenesisi1067 – 10671G → D in MSH6-3; defective for ATP-induced sliding clamp formation and assembly of ternary complexes with MutL alpha. 2 Publications
Mutagenesisi1096 – 10961H → A in MSH6-9; shows normal mispair binding and dissociation, but fails to show complete mispair activation of the ATPase. 1 Publication
Mutagenesisi1142 – 11421G → D in MSH6-2; defective for ATP-induced sliding clamp formation, but assembles ternary complexes with MutL alpha. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12421242DNA mismatch repair protein MSH6PRO_0000115213Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021Phosphoserine1 Publication
Modified residuei145 – 1451Phosphoserine3 Publications
Modified residuei150 – 1501Phosphoserine3 Publications
Modified residuei201 – 2011Phosphoserine1 Publication
Modified residuei451 – 4511Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03834.
PaxDbiQ03834.
PeptideAtlasiQ03834.

Expressioni

Gene expression databases

GenevestigatoriQ03834.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MSH2P258476EBI-11383,EBI-11352

Protein-protein interaction databases

BioGridi32152. 62 interactions.
DIPiDIP-2423N.
IntActiQ03834. 32 interactions.
MINTiMINT-618151.
STRINGi4932.YDR097C.

Structurei

3D structure databases

ProteinModelPortaliQ03834.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni305 – 421117Mispair-binding domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi27 – 348PIP box

Domaini

The PIP box serves as a PCNA(POL30)-recognition and -binding motif.

Sequence similaritiesi

Belongs to the DNA mismatch repair MutS family.Curated

Phylogenomic databases

eggNOGiCOG0249.
GeneTreeiENSGT00550000075024.
HOGENOMiHOG000189303.
InParanoidiQ03834.
KOiK08737.
OMAiALKDCMR.
OrthoDBiEOG773XQH.

Family and domain databases

Gene3Di3.30.420.110. 1 hit.
3.40.1170.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR017261. 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]
PANTHERiPTHR11361:SF31. PTHR11361:SF31. 1 hit.
PfamiPF01624. 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]
PIRSFiPIRSF037677. DNA_mis_repair_Msh6. 1 hit.
SMARTiSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view]
SUPFAMiSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53150. SSF53150. 1 hit.
SSF55271. SSF55271. 1 hit.
PROSITEiPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03834-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPATPKTSK TAHFENGSTS SQKKMKQSSL LSFFSKQVPS GTPSKKVQKP
60 70 80 90 100
TPATLENTAT DKITKNPQGG KTGKLFVDVD EDNDLTIAEE TVSTVRSDIM
110 120 130 140 150
HSQEPQSDTM LNSNTTEPKS TTTDEDLSSS QSRRNHKRRV NYAESDDDDS
160 170 180 190 200
DTTFTAKRKK GKVVDSESDE DEYLPDKNDG DEDDDIADDK EDIKGELAED
210 220 230 240 250
SGDDDDLISL AETTSKKKFS YNTSHSSSPF TRNISRDNSK KKSRPNQAPS
260 270 280 290 300
RSYNPSHSQP SATSKSSKFN KQNEERYQWL VDERDAQRRP KSDPEYDPRT
310 320 330 340 350
LYIPSSAWNK FTPFEKQYWE IKSKMWDCIV FFKKGKFFEL YEKDALLANA
360 370 380 390 400
LFDLKIAGGG RANMQLAGIP EMSFEYWAAQ FIQMGYKVAK VDQRESMLAK
410 420 430 440 450
EMREGSKGIV KRELQCILTS GTLTDGDMLH SDLATFCLAI REEPGNFYNE
460 470 480 490 500
TQLDSSTIVQ KLNTKIFGAA FIDTATGELQ MLEFEDDSEC TKLDTLMSQV
510 520 530 540 550
RPMEVVMERN NLSTLANKIV KFNSAPNAIF NEVKAGEEFY DCDKTYAEII
560 570 580 590 600
SSEYFSTEED WPEVLKSYYD TGKKVGFSAF GGLLYYLKWL KLDKNLISMK
610 620 630 640 650
NIKEYDFVKS QHSMVLDGIT LQNLEIFSNS FDGSDKGTLF KLFNRAITPM
660 670 680 690 700
GKRMMKKWLM HPLLRKNDIE SRLDSVDSLL QDITLREQLE ITFSKLPDLE
710 720 730 740 750
RMLARIHSRT IKVKDFEKVI TAFETIIELQ DSLKNNDLKG DVSKYISSFP
760 770 780 790 800
EGLVEAVKSW TNAFERQKAI NENIIVPQRG FDIEFDKSMD RIQELEDELM
810 820 830 840 850
EILMTYRKQF KCSNIQYKDS GKEIYTIEIP ISATKNVPSN WVQMAANKTY
860 870 880 890 900
KRYYSDEVRA LARSMAEAKE IHKTLEEDLK NRLCQKFDAH YNTIWMPTIQ
910 920 930 940 950
AISNIDCLLA ITRTSEYLGA PSCRPTIVDE VDSKTNTQLN GFLKFKSLRH
960 970 980 990 1000
PCFNLGATTA KDFIPNDIEL GKEQPRLGLL TGANAAGKST ILRMACIAVI
1010 1020 1030 1040 1050
MAQMGCYVPC ESAVLTPIDR IMTRLGANDN IMQGKSTFFV ELAETKKILD
1060 1070 1080 1090 1100
MATNRSLLVV DELGRGGSSS DGFAIAESVL HHVATHIQSL GFFATHYGTL
1110 1120 1130 1140 1150
ASSFKHHPQV RPLKMSILVD EATRNVTFLY KMLEGQSEGS FGMHVASMCG
1160 1170 1180 1190 1200
ISKEIIDNAQ IAADNLEHTS RLVKERDLAA NNLNGEVVSV PGGLQSDFVR
1210 1220 1230 1240
IAYGDGLKNT KLGSGEGVLN YDWNIKRNVL KSLFSIIDDL QS
Length:1,242
Mass (Da):140,080
Last modified:November 1, 1996 - v1
Checksum:i11A6883AADCFA222
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47746 Genomic DNA. Translation: CAA87671.1.
BK006938 Genomic DNA. Translation: DAA11942.1.
PIRiS51246.
RefSeqiNP_010382.3. NM_001180405.3.

Genome annotation databases

EnsemblFungiiYDR097C; YDR097C; YDR097C.
GeneIDi851671.
KEGGisce:YDR097C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47746 Genomic DNA. Translation: CAA87671.1 .
BK006938 Genomic DNA. Translation: DAA11942.1 .
PIRi S51246.
RefSeqi NP_010382.3. NM_001180405.3.

3D structure databases

ProteinModelPortali Q03834.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32152. 62 interactions.
DIPi DIP-2423N.
IntActi Q03834. 32 interactions.
MINTi MINT-618151.
STRINGi 4932.YDR097C.

Proteomic databases

MaxQBi Q03834.
PaxDbi Q03834.
PeptideAtlasi Q03834.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR097C ; YDR097C ; YDR097C .
GeneIDi 851671.
KEGGi sce:YDR097C.

Organism-specific databases

CYGDi YDR097c.
SGDi S000002504. MSH6.

Phylogenomic databases

eggNOGi COG0249.
GeneTreei ENSGT00550000075024.
HOGENOMi HOG000189303.
InParanoidi Q03834.
KOi K08737.
OMAi ALKDCMR.
OrthoDBi EOG773XQH.

Enzyme and pathway databases

BioCyci YEAST:G3O-29700-MONOMER.
Reactomei REACT_238711. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).

Miscellaneous databases

NextBioi 969292.
PROi Q03834.

Gene expression databases

Genevestigatori Q03834.

Family and domain databases

Gene3Di 3.30.420.110. 1 hit.
3.40.1170.10. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR017261. 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 ]
PANTHERi PTHR11361:SF31. PTHR11361:SF31. 1 hit.
Pfami 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 ]
PIRSFi PIRSF037677. DNA_mis_repair_Msh6. 1 hit.
SMARTi SM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view ]
SUPFAMi SSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53150. SSF53150. 1 hit.
SSF55271. SSF55271. 1 hit.
PROSITEi PS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  26. 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].

Entry informationi

Entry nameiMSH6_YEAST
AccessioniPrimary (citable) accession number: Q03834
Secondary accession number(s): D6VS82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5330 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3