Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q02959 (HOS3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 116. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase HOS3

EC=3.5.1.98
Gene names
Name:HOS3
Ordered Locus Names:YPL116W
ORF Names:LPH11W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length697 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes By similarity.

Catalytic activity

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Subunit structure

Homodimer. Ref.4

Subcellular location

Nucleus By similarity.

Miscellaneous

Present with 4420 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the histone deacetylase family. HD type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 697697Histone deacetylase HOS3
PRO_0000114727

Regions

Region40 – 440401Histone deacetylase

Sites

Active site1961 By similarity

Amino acid modifications

Modified residue5821Phosphoserine Ref.8
Modified residue5831Phosphoserine Ref.8
Modified residue6131Phosphoserine Ref.8
Modified residue6291Phosphoserine Ref.6 Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q02959 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F2B5D09E87B097E5

FASTA69779,200
        10         20         30         40         50         60 
MSSKHSDPLE RFYKQFQAFV QNNPNVISAA RAAAQIPESA KAVVVLSPYS LQHVFPREWV 

        70         80         90        100        110        120 
TKSYRKTIVE RPERLLASSM GISAAITMYP SLFTLKSSHQ RKGSLMAPHV LKVHGSSWPA 

       130        140        150        160        170        180 
ELIELCQMAD AKLLKGEIEV PDTWNSGDIY LSSKTIKALQ GTIGAIETGV DSIFKGPSAE 

       190        200        210        220        230        240 
HISNRAFVAI RPPGHHCHYG TPSGFCLLNN AHVAIEYAYD TYNVTHVVVL DFDLHHGDGT 

       250        260        270        280        290        300 
QDICWKRAGF KPEEEPEDSS YDDFGKKFAE FPKVGYFSMH DINSFPTESG FATKENIKNA 

       310        320        330        340        350        360 
STCIMNSHDL NIWNIHLSKW TTEEEFNVLY RTKYRTLFAK ADEFFRSAKL EMNQQGRPFK 

       370        380        390        400        410        420 
GLVVISAGFD ASEFEQTSMQ RHSVNVPTSF YTTFTKDALK LAQMHCHGKV LSLMEGGYSD 

       430        440        450        460        470        480 
KAICSGVFAH LIGLQNQDWV KEWGSEQVVK EIVRGCKPAW KPYKTKRAKD VIRIWAEEVI 

       490        500        510        520        530        540 
RLGRAMIPEF DDIIFKDAVN SAPSNSLLKA TVEPASTSTI AQRIIRSHRS NASPEKELHE 

       550        560        570        580        590        600 
NKPRSTEKQE QREIRSDTKV KQLSSNNRAA ETQIPFLQQE FSSEDEDEEY VYDEELNKTF 

       610        620        630        640        650        660 
NRTVEDITID DISRHLETLE IEKKGDEDSD HELKEKNWKN SHQRRLQGNG MYKIPSNTKP 

       670        680        690 
HRIRQPQNAN TPTYDDSDIS MISHVSRKHT TRSGGRW 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(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]"HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription."
Rundlett S.E., Carmen A.A., Kobayashi R., Bavykin S., Turner B.M., Grunstein M.
Proc. Natl. Acad. Sci. U.S.A. 93:14503-14508(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE NAME.
[4]"Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with intrinsic histone deacetylase activity."
Carmen A.A., Griffin P.R., Calaycay J.R., Rundlett S.E., Suka Y., Grunstein M.
Proc. Natl. Acad. Sci. U.S.A. 96:12356-12361(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, HOMODIMERIZATION.
[5]"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].
[6]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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-629, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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-582; SER-583 AND SER-613, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43503 Genomic DNA. Translation: AAB68246.1.
BK006949 Genomic DNA. Translation: DAA11318.1.
PIRS62006.
RefSeqNP_015209.1. NM_001183930.1.

3D structure databases

ProteinModelPortalQ02959.
SMRQ02959. Positions 145-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36065. 57 interactions.
DIPDIP-8047N.
IntActQ02959. 45 interactions.
MINTMINT-2781063.
STRING4932.YPL116W.

Proteomic databases

PaxDbQ02959.
PeptideAtlasQ02959.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL116W; YPL116W; YPL116W.
GeneID855987.
KEGGsce:YPL116W.

Organism-specific databases

CYGDYPL116w.
SGDS000006037. HOS3.

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000246666.
KOK11484.
OMAFAEFPKV.
OrthoDBEOG75J0WK.

Enzyme and pathway databases

BioCycYEAST:G3O-34016-MONOMER.

Gene expression databases

GenevestigatorQ02959.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other

NextBio980834.

Entry information

Entry nameHOS3_YEAST
AccessionPrimary (citable) accession number: Q02959
Secondary accession number(s): D6W3Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 116 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 XVI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families