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Protein

DNA mismatch repair protein MSH3

Gene

MSH3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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 beta, which binds to DNA mismatches thereby initiating DNA repair. MSH3 provides substrate-binding and substrate specificity to the complex. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches that occur during replication. After mismatch binding, forms a ternary complex with either the MutL alpha or MutL beta heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. MutS beta also has a role in regulation of heteroduplex formation during mitotic and meiotic recombination. MutS beta binds to DNA flap structures predicted to form during recombination, and is required for 3' non-homologous tail removal (NHTR). MutS beta-binding alters the DNA conformation of its substrate at the ds/ssDNA junction and may facilitate its recognition and/or cleavage by the downstream nucleotide excision repair (NER) RAD1-RAD10 endonuclease. ATP binding and hydrolysis play a pivotal role in MMR and NHTR.10 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi791 – 7988ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA insertion or deletion binding Source: SGD
  • double-strand/single-strand DNA junction binding Source: SGD

GO - Biological processi

  • DNA recombination Source: SGD
  • meiotic mismatch repair Source: SGD
  • mismatch repair Source: SGD
  • mitotic recombination Source: SGD
  • removal of nonhomologous ends 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-29386-MONOMER.
ReactomeiR-SCE-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).

Names & Taxonomyi

Protein namesi
Recommended name:
DNA mismatch repair protein MSH3
Alternative name(s):
Mismatch-binding protein
Short name:
MBP
MutS protein homolog 3
Gene namesi
Name:MSH3
Ordered Locus Names:YCR092C
ORF Names:YCR1152, YCR92C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCR092C.
SGDiS000000688. MSH3.

Subcellular locationi

GO - Cellular componenti

  • MutSbeta complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 41Q → A: Partially functional in a mismatch repair assay; when associated with 10-AA-11. 1 Publication
Mutagenesisi10 – 112FF → AA: Partially functional in a mismatch repair assay; when associated with A-4. 1 Publication
Mutagenesisi158 – 1581K → A: Alters DNA-binding activity and impairs MSH2-MSH3-mediated DNA mismatch repair; when associated with ALA-160. 1 Publication
Mutagenesisi160 – 1601K → A: Alters DNA-binding activity and impairs MSH2-MSH3-mediated DNA mismatch repair; when associated with ALA-158. 1 Publication
Mutagenesisi203 – 2031P → A: No effect. 1 Publication
Mutagenesisi226 – 2261Q → A: No effect. 1 Publication
Mutagenesisi247 – 2471R → A: Impairs MSH2-MSH3-mediated DNA mismatch repair. 1 Publication
Mutagenesisi796 – 7961G → D: Defective in MMR and in NHTR. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10181018DNA mismatch repair protein MSH3PRO_0000115195Add
BLAST

Proteomic databases

MaxQBiP25336.
PeptideAtlasiP25336.
PRIDEiP25336.

Interactioni

Subunit structurei

Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a ternary complex with either MutL alpha (MLH1-PMS1) or MutL beta (MLH1-MLH3). MutS beta interacts with proliferating cell nuclear antigen (PCNA/POL30). Interacts with SAW1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MSH2P258473EBI-11362,EBI-11352

Protein-protein interaction databases

BioGridi31064. 37 interactions.
DIPiDIP-2422N.
IntActiP25336. 24 interactions.
MINTiMINT-633647.

Structurei

3D structure databases

ProteinModelPortaliP25336.
SMRiP25336. Positions 132-991.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni126 – 256131Mispair-binding domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4 – 118PIP box

Domaini

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

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074949.
HOGENOMiHOG000057130.
InParanoidiP25336.
KOiK08736.
OMAiGYLLCIT.
OrthoDBiEOG773XQH.

Family and domain databases

Gene3Di3.40.1170.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR007695. 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]
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]
SMARTiSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view]
SUPFAMiSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF55271. SSF55271. 1 hit.
PROSITEiPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25336-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGQPTISRF FKKAVKSELT HKQEQEVAVG NGAGSESICL DTDEEDNLSS
60 70 80 90 100
VASTTVTNDS FPLKGSVSSK NSKNSEKTSG TSTTFNDIDF AKKLDRIMKR
110 120 130 140 150
RSDENVEAED DEEEGEEDFV KKKARKSPTA KLTPLDKQVK DLKMHHRDKV
160 170 180 190 200
LVIRVGYKYK CFAEDAVTVS RILHIKLVPG KLTIDESNPQ DCNHRQFAYC
210 220 230 240 250
SFPDVRLNVH LERLVHHNLK VAVVEQAETS AIKKHDPGAS KSSVFERKIS
260 270 280 290 300
NVFTKATFGV NSTFVLRGKR ILGDTNSIWA LSRDVHQGKV AKYSLISVNL
310 320 330 340 350
NNGEVVYDEF EEPNLADEKL QIRIKYLQPI EVLVNTDDLP LHVAKFFKDI
360 370 380 390 400
SCPLIHKQEY DLEDHVVQAI KVMNEKIQLS PSLIRLVSKL YSHMVEYNNE
410 420 430 440 450
QVMLIPSIYS PFASKIHMLL DPNSLQSLDI FTHDGGKGSL FWLLDHTRTS
460 470 480 490 500
FGLRMLREWI LKPLVDVHQI EERLDAIECI TSEINNSIFF ESLNQMLNHT
510 520 530 540 550
PDLLRTLNRI MYGTTSRKEV YFYLKQITSF VDHFKMHQSY LSEHFKSSDG
560 570 580 590 600
RIGKQSPLLF RLFSELNELL STTQLPHFLT MINVSAVMEK NSDKQVMDFF
610 620 630 640 650
NLNNYDCSEG IIKIQRESES VRSQLKEELA EIRKYLKRPY LNFRDEVDYL
660 670 680 690 700
IEVKNSQIKD LPDDWIKVNN TKMVSRFTTP RTQKLTQKLE YYKDLLIRES
710 720 730 740 750
ELQYKEFLNK ITAEYTELRK ITLNLAQYDC ILSLAATSCN VNYVRPTFVN
760 770 780 790 800
GQQAIIAKNA RNPIIESLDV HYVPNDIMMS PENGKINIIT GPNMGGKSSY
810 820 830 840 850
IRQVALLTIM AQIGSFVPAE EIRLSIFENV LTRIGAHDDI INGDSTFKVE
860 870 880 890 900
MLDILHILKN CNKRSLLLLD EVGRGTGTHD GIAISYALIK YFSELSDCPL
910 920 930 940 950
ILFTTHFPML GEIKSPLIRN YHMDYVEEQK TGEDWMSVIF LYKLKKGLTY
960 970 980 990 1000
NSYGMNVAKL ARLDKDIINR AFSISEELRK ESINEDALKL FSSLKRILKS
1010
DNITATDKLA KLLSLDIH
Length:1,018
Mass (Da):116,534
Last modified:June 10, 2008 - v2
Checksum:i1AD91C2E2F2856EF
GO

Sequence cautioni

The sequence AAA34803.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA42247.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA46116.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64954 Genomic DNA. Translation: CAA46116.1. Different initiation.
M96250 Genomic DNA. Translation: AAA34803.1. Different initiation.
X59720 Genomic DNA. Translation: CAA42247.1. Different initiation.
BK006937 Genomic DNA. Translation: DAA07561.1.
PIRiS19508.
RefSeqiNP_010016.2. NM_001178798.1.

Genome annotation databases

EnsemblFungiiCAA42247; CAA42247; CAA42247.
YCR092C; YCR092C; YCR092C.
GeneIDi850454.
KEGGisce:YCR092C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64954 Genomic DNA. Translation: CAA46116.1. Different initiation.
M96250 Genomic DNA. Translation: AAA34803.1. Different initiation.
X59720 Genomic DNA. Translation: CAA42247.1. Different initiation.
BK006937 Genomic DNA. Translation: DAA07561.1.
PIRiS19508.
RefSeqiNP_010016.2. NM_001178798.1.

3D structure databases

ProteinModelPortaliP25336.
SMRiP25336. Positions 132-991.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31064. 37 interactions.
DIPiDIP-2422N.
IntActiP25336. 24 interactions.
MINTiMINT-633647.

Proteomic databases

MaxQBiP25336.
PeptideAtlasiP25336.
PRIDEiP25336.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42247; CAA42247; CAA42247.
YCR092C; YCR092C; YCR092C.
GeneIDi850454.
KEGGisce:YCR092C.

Organism-specific databases

EuPathDBiFungiDB:YCR092C.
SGDiS000000688. MSH3.

Phylogenomic databases

GeneTreeiENSGT00550000074949.
HOGENOMiHOG000057130.
InParanoidiP25336.
KOiK08736.
OMAiGYLLCIT.
OrthoDBiEOG773XQH.

Enzyme and pathway databases

BioCyciYEAST:G3O-29386-MONOMER.
ReactomeiR-SCE-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).

Miscellaneous databases

NextBioi966078.
PROiP25336.

Family and domain databases

Gene3Di3.40.1170.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR007695. 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]
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]
SMARTiSM00534. MUTSac. 1 hit.
SM00533. MUTSd. 1 hit.
[Graphical view]
SUPFAMiSSF48334. SSF48334. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF55271. SSF55271. 1 hit.
PROSITEiPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast gene MSH3 defines a new class of eukaryotic MutS homologues."
    New L., Liu K., Crouse G.F.
    Mol. Gen. Genet. 239:97-108(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of a 6.3 kb segment of yeast chromosome III reveals an open reading frame coding for a putative mismatch binding protein."
    Valle G., Bergantino E., Lanfranchi G., Carignani G.
    Yeast 7:981-988(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [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. "Binding of insertion/deletion DNA mismatches by the heterodimer of yeast mismatch repair proteins MSH2 and MSH3."
    Habraken Y., Sung P., Prakash L., Prakash S.
    Curr. Biol. 6:1185-1187(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING SPECIFICITY, INTERACTION WITH MSH2.
  6. "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.
  7. "Evidence for involvement of yeast proliferating cell nuclear antigen in DNA mismatch repair."
    Johnson R.E., Kovvali G.K., Guzder S.N., Amin N.S., Holm C., Habraken Y., Sung P., Prakash L., Prakash S.
    J. Biol. Chem. 271:27987-27990(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POL30.
  8. "Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-PMS1 complex."
    Habraken Y., Sung P., Prakash L., Prakash S.
    Curr. Biol. 7:790-793(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING SPECIFICITY, COMPLEX FORMATION WITH MLH1-PMS1.
  9. "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.
  10. "Role of Saccharomyces cerevisiae Msh2 and Msh3 repair proteins in double-strand break-induced recombination."
    Sugawara N., Paques F., Colaiacovo M., Haber J.E.
    Proc. Natl. Acad. Sci. U.S.A. 94:9214-9219(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NHTR.
  11. "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.
  12. "Separation-of-function mutations in Saccharomyces cerevisiae MSH2 that confer mismatch repair defects but do not affect nonhomologous-tail removal during recombination."
    Studamire B., Price G., Sugawara N., Haber J.E., Alani E.
    Mol. Cell. Biol. 19:7558-7567(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-796.
  13. "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: MUTAGENESIS OF GLN-4 AND 10-PHE-PHE-11.
  14. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  16. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  17. "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.
  18. "Mismatch repair factor MSH2-MSH3 binds and alters the conformation of branched DNA structures predicted to form during genetic recombination."
    Surtees J.A., Alani E.
    J. Mol. Biol. 360:523-536(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NHTR, DNA-BINDING.
  19. "Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display distinct requirements for DNA binding domain I in mismatch recognition."
    Lee S.D., Surtees J.A., Alani E.
    J. Mol. Biol. 366:53-66(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, MUTAGENESIS OF LYS-158; LYS-160; PRO-203; GLN-226 AND ARG-247.
  20. "Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs."
    Harrington J.M., Kolodner R.D.
    Mol. Cell. Biol. 27:6546-6554(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION OF INITIATION SITE.
  21. "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.
  22. "Microarray-based genetic screen defines SAW1, a gene required for Rad1/Rad10-dependent processing of recombination intermediates."
    Li F., Dong J., Pan X., Oum J.-H., Boeke J.D., Lee S.E.
    Mol. Cell 30:325-335(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAW1.

Entry informationi

Entry nameiMSH3_YEAST
AccessioniPrimary (citable) accession number: P25336
Secondary accession number(s): D6VR92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 10, 2008
Last modified: May 11, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 736 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: 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.