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Protein

MutS protein homolog 5

Gene

MSH5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in meiotic recombination. Facilitate crossovers between homologs during meiosis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi643 – 6508ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • chiasma assembly Source: GO_Central
  • mismatch repair Source: GO_Central
  • reciprocal meiotic recombination 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-29549-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
MutS protein homolog 5
Gene namesi
Name:MSH5
Ordered Locus Names:YDL154W
ORF Names:D1542
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL154W.
SGDiS000002313. MSH5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi643 – 6442GA → DV: Abolishes function; no effect on interaction with MSH4. 1 Publication
Mutagenesisi648 – 6481G → R: Abolishes function; no effect on interaction with MSH4. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 901901MutS protein homolog 5PRO_0000115206Add
BLAST

Proteomic databases

PRIDEiQ12175.

Interactioni

Subunit structurei

Heterooligomer of MSH4 and MSH5.

Binary interactionsi

WithEntry#Exp.IntActNotes
MSH4P409653EBI-11377,EBI-11371

Protein-protein interaction databases

BioGridi31909. 28 interactions.
DIPiDIP-1457N.
IntActiQ12175. 8 interactions.
MINTiMINT-388063.

Structurei

3D structure databases

ProteinModelPortaliQ12175.
SMRiQ12175. Positions 239-899.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DNA mismatch repair MutS family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074977.
HOGENOMiHOG000113662.
InParanoidiQ12175.
KOiK08741.
OMAiARVCVRP.
OrthoDBiEOG7P5T8J.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR011184. DNA_mismatch_repair_MutS.
IPR000432. DNA_mismatch_repair_MutS_C.
IPR007696. DNA_mismatch_repair_MutS_core.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF05192. MutS_III. 1 hit.
PF00488. MutS_V. 1 hit.
[Graphical view]
PIRSFiPIRSF005813. MSH2. 1 hit.
SMARTiSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view]
SUPFAMiSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12175-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHEWLISAS ETMRSIGNGE GLRDKGAVVA NNDGEFNEGD TNREEDSSTI
60 70 80 90 100
FSFDFDEEIV MCIDFSGGKL GCSILDYHTK TLKAFDQDYV VNKTTISSHD
110 120 130 140 150
LIDDADMSSN DISLLLGLLI MEANPTVCLV PARLEDWIFD YIKTKCDEIN
160 170 180 190 200
CRLELQPIKR FKKWDLLQSL QLRGHDNQTI LNDILSNSKF TTTVTLGTVG
210 220 230 240 250
CILANHEQLG EYNDSTASSN MVTGRLVQNA FEDVIHGIRY IDIRDRMVLD
260 270 280 290 300
ENTISALHIF PTAHKLGHDK MMRNGFFSVF ELFNQVSSDY ARRILKSWLI
310 320 330 340 350
NPLTNKKRIE TRYSIIRTLL DKQNAIIFSD LSQSIKRCPD AFGFINQLRS
360 370 380 390 400
GKSTLGTWSK VASFLEKGIA IFQLVSSLKL GSDEANILHD IKNKVDISAL
410 420 430 440 450
KECLRKVETV IDFDTSRDTK TLTINTGVDN RLDECRNIYN HLEGILLDVA
460 470 480 490 500
RETQIFLLNT MPQEDCKTTK SLEKLVNAVY IPQLGYLVTI SVLMEPLLDG
510 520 530 540 550
IPNLQWEEIF RSSENIYFKN GRVLELDETY GDIYGAISDF EIEILFSLQE
560 570 580 590 600
QILRRKTQLT AYNILLSELE ILLSFAQVSA ERNYAEPQLV EDECILEIIN
610 620 630 640 650
GRHALYETFL DNYIPNSTMI DGGLFSELSW CEQNKGRIIV VTGANASGKS
660 670 680 690 700
VYLTQNGLIV YLAQIGCFVP AERARIGIAD KILTRIRTQE TVYKTQSSFL
710 720 730 740 750
LDSQQMAKSL SLATEKSLIL IDEYGKGTDI LDGPSLFGSI MLNMSKSEKC
760 770 780 790 800
PRIIACTHFH ELFNENVLTE NIKGIKHYCT DILISQKYNL LETAHVGEDH
810 820 830 840 850
ESEGITFLFK VKEGISKQSF GIYCAKVCGL SRDIVERAEE LSRMINRGDD
860 870 880 890 900
VVQQCGNLTE KEMREFQKNQ EIVKKFLSWD LDLETTTTSE NLRLKLKNFL

R
Length:901
Mass (Da):102,209
Last modified:November 1, 1997 - v1
Checksum:i505E0344391E30E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42517 Genomic DNA. Translation: AAA67649.1.
X97751 Genomic DNA. Translation: CAA66337.1.
Z74202 Genomic DNA. Translation: CAA98728.1.
BK006938 Genomic DNA. Translation: DAA11706.1.
PIRiS67702.
RefSeqiNP_010127.1. NM_001180214.1.

Genome annotation databases

EnsemblFungiiYDL154W; YDL154W; YDL154W.
GeneIDi851401.
KEGGisce:YDL154W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42517 Genomic DNA. Translation: AAA67649.1.
X97751 Genomic DNA. Translation: CAA66337.1.
Z74202 Genomic DNA. Translation: CAA98728.1.
BK006938 Genomic DNA. Translation: DAA11706.1.
PIRiS67702.
RefSeqiNP_010127.1. NM_001180214.1.

3D structure databases

ProteinModelPortaliQ12175.
SMRiQ12175. Positions 239-899.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31909. 28 interactions.
DIPiDIP-1457N.
IntActiQ12175. 8 interactions.
MINTiMINT-388063.

Proteomic databases

PRIDEiQ12175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL154W; YDL154W; YDL154W.
GeneIDi851401.
KEGGisce:YDL154W.

Organism-specific databases

EuPathDBiFungiDB:YDL154W.
SGDiS000002313. MSH5.

Phylogenomic databases

GeneTreeiENSGT00550000074977.
HOGENOMiHOG000113662.
InParanoidiQ12175.
KOiK08741.
OMAiARVCVRP.
OrthoDBiEOG7P5T8J.

Enzyme and pathway databases

BioCyciYEAST:G3O-29549-MONOMER.

Miscellaneous databases

PROiQ12175.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR011184. DNA_mismatch_repair_MutS.
IPR000432. DNA_mismatch_repair_MutS_C.
IPR007696. DNA_mismatch_repair_MutS_core.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF05192. MutS_III. 1 hit.
PF00488. MutS_V. 1 hit.
[Graphical view]
PIRSFiPIRSF005813. MSH2. 1 hit.
SMARTiSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view]
SUPFAMiSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MSH5, a novel MutS homolog, facilitates meiotic reciprocal recombination between homologs in Saccharomyces cerevisiae but not mismatch repair."
    Hollingsworth N.M., Ponte L., Halsey C.
    Genes Dev. 9:1728-1739(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Analysis of a 23 kb region on the left arm of yeast chromosome IV."
    Delaveau T.T.D., Blugeon C., Jacq C., Perea J.
    Yeast 12:1587-1592(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Conserved properties between functionally distinct MutS homologs in yeast."
    Pochart P., Woltering D., Hollingsworth N.M.
    J. Biol. Chem. 272:30345-30349(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MSH4, MUTAGENESIS OF 643-GLY-ALA-644 AND GLY-648.

Entry informationi

Entry nameiMSH5_YEAST
AccessioniPrimary (citable) accession number: Q12175
Secondary accession number(s): D6VRJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Two distinct classes of crossovers have been demonstrated in budding yeast. Class I is MSH4/MSH5 dependent and exhibits crossover interference. Class II is MUS81/MMS4 dependent and exhibits no interference.

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.