Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q12214 (HOS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. 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
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 HOS1
EC=3.5.1.98
Gene names
Name:HOS1
Ordered Locus Names:YPR068C
ORF Names:YP9499.23C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length470 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 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.

Subcellular location

Nucleus By similarity.

Miscellaneous

Present with 538 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 – 470470Histone deacetylase HOS1
PRO_0000114726

Regions

Region47 – 392346Histone deacetylase

Sites

Active site2111 By similarity

Amino acid modifications

Modified residue1101Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q12214 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5DCFF35D8F6AC87D

FASTA47054,764
        10         20         30         40         50         60 
MSKLVISTSI FQSQVADLLP CNNHQKSQLT YSLINAYDLL QHFDEVLTFP YARKDDLLEF 

        70         80         90        100        110        120 
HSKSYIDYLI NGRFNKMMAQ DVNNPMVESK WSELSELADN WNEKIDYNPS QDLQRFTTRE 

       130        140        150        160        170        180 
NLYNYYLNHS QALENNMDCI NNSEVPTNDK PTDTYILNSE TKQYNLEGDC PIFSYLPMYC 

       190        200        210        220        230        240 
QVITGATLNL LDHLSPTERL IGINWDGGRH HAFKQRASGF CYINDVVLLI QRLRKAKLNK 

       250        260        270        280        290        300 
ITYVDFDLHH GDGVEKAFQY SKQIQTISVH LYEPGFFPGT GSLSDSRKDK NVVNIPLKHG 

       310        320        330        340        350        360 
CDDNYLELIA SKIVNPLIER HEPEALIIEC GGDGLLGDRF NEWQLTIRGL SRIIINIMKS 

       370        380        390        400        410        420 
YPRAHIFLLG GGGYNDLLMS RFYTYLTWCV TKQFSNLRCG DNNSFQIDPF DVCDGDDSEQ 

       430        440        450        460        470 
FIREHDLVEM YNEENYQYWI YEMEGSSRMK MLRNDNKDRD MVELMKFYEL

« 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 204511 / S288c / AB972.
[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]"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].
[5]"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-110, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z71255 Genomic DNA. Translation: CAA94976.1.
Z49219 Genomic DNA. Translation: CAA89185.1.
BK006949 Genomic DNA. Translation: DAA11488.1.
PIRS54089.
RefSeqNP_015393.1. NM_001184165.1.

3D structure databases

ProteinModelPortalQ12214.
SMRQ12214. Positions 152-387.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-7974N.
IntActQ12214. 3 interactions.
STRING4932.YPR068C.

Proteomic databases

PaxDbQ12214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR068C; YPR068C; YPR068C.
GeneID856181.
KEGGsce:YPR068C.

Organism-specific databases

CYGDYPR068c.
SGDS000006272. HOS1.

Phylogenomic databases

eggNOGCOG0123.
GeneTreeENSGT00390000003411.
HOGENOMHOG000225180.
KOK11482.
OrthoDBEOG422DTQ.

Gene expression databases

GenevestigatorQ12214.
GermOnlineYPR068C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.40.800.20. 2 hits.
InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other

NextBio981352.

Entry information

Entry nameHOS1_YEAST
AccessionPrimary (citable) accession number: Q12214
Secondary accession number(s): D6W472
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XVI

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents