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Protein

Histone deacetylase HOS3

Gene

HOS3

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

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei196By similarity1

GO - Molecular functioni

GO - Biological processi

  • histone deacetylation Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • regulation of transcription involved in G1/S transition of mitotic cell cycle Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-34016-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase HOS3 (EC:3.5.1.98)
Gene namesi
Name:HOS3
Ordered Locus Names:YPL116W
ORF Names:LPH11W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL116W.
SGDiS000006037. HOS3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001147271 – 697Histone deacetylase HOS3Add BLAST697

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei582PhosphoserineCombined sources1
Modified residuei583PhosphoserineCombined sources1
Modified residuei613PhosphoserineCombined sources1
Modified residuei629PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02959.
PRIDEiQ02959.

PTM databases

iPTMnetiQ02959.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi36065. 64 interactors.
DIPiDIP-8047N.
IntActiQ02959. 46 interactors.
MINTiMINT-2781063.

Structurei

3D structure databases

ProteinModelPortaliQ02959.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni40 – 440Histone deacetylaseAdd BLAST401

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000246666.
InParanoidiQ02959.
KOiK11484.
OMAiDVIRIWA.
OrthoDBiEOG092C345D.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 4 hits.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PRINTSiPR01270. HDASUPER.

Sequencei

Sequence statusi: Complete.

Q02959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKHSDPLE RFYKQFQAFV QNNPNVISAA RAAAQIPESA KAVVVLSPYS
60 70 80 90 100
LQHVFPREWV TKSYRKTIVE RPERLLASSM GISAAITMYP SLFTLKSSHQ
110 120 130 140 150
RKGSLMAPHV LKVHGSSWPA ELIELCQMAD AKLLKGEIEV PDTWNSGDIY
160 170 180 190 200
LSSKTIKALQ GTIGAIETGV DSIFKGPSAE HISNRAFVAI RPPGHHCHYG
210 220 230 240 250
TPSGFCLLNN AHVAIEYAYD TYNVTHVVVL DFDLHHGDGT QDICWKRAGF
260 270 280 290 300
KPEEEPEDSS YDDFGKKFAE FPKVGYFSMH DINSFPTESG FATKENIKNA
310 320 330 340 350
STCIMNSHDL NIWNIHLSKW TTEEEFNVLY RTKYRTLFAK ADEFFRSAKL
360 370 380 390 400
EMNQQGRPFK GLVVISAGFD ASEFEQTSMQ RHSVNVPTSF YTTFTKDALK
410 420 430 440 450
LAQMHCHGKV LSLMEGGYSD KAICSGVFAH LIGLQNQDWV KEWGSEQVVK
460 470 480 490 500
EIVRGCKPAW KPYKTKRAKD VIRIWAEEVI RLGRAMIPEF DDIIFKDAVN
510 520 530 540 550
SAPSNSLLKA TVEPASTSTI AQRIIRSHRS NASPEKELHE NKPRSTEKQE
560 570 580 590 600
QREIRSDTKV KQLSSNNRAA ETQIPFLQQE FSSEDEDEEY VYDEELNKTF
610 620 630 640 650
NRTVEDITID DISRHLETLE IEKKGDEDSD HELKEKNWKN SHQRRLQGNG
660 670 680 690
MYKIPSNTKP HRIRQPQNAN TPTYDDSDIS MISHVSRKHT TRSGGRW
Length:697
Mass (Da):79,200
Last modified:November 1, 1996 - v1
Checksum:iF2B5D09E87B097E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43503 Genomic DNA. Translation: AAB68246.1.
BK006949 Genomic DNA. Translation: DAA11318.1.
PIRiS62006.
RefSeqiNP_015209.1. NM_001183930.1.

Genome annotation databases

EnsemblFungiiYPL116W; YPL116W; YPL116W.
GeneIDi855987.
KEGGisce:YPL116W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43503 Genomic DNA. Translation: AAB68246.1.
BK006949 Genomic DNA. Translation: DAA11318.1.
PIRiS62006.
RefSeqiNP_015209.1. NM_001183930.1.

3D structure databases

ProteinModelPortaliQ02959.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36065. 64 interactors.
DIPiDIP-8047N.
IntActiQ02959. 46 interactors.
MINTiMINT-2781063.

PTM databases

iPTMnetiQ02959.

Proteomic databases

MaxQBiQ02959.
PRIDEiQ02959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL116W; YPL116W; YPL116W.
GeneIDi855987.
KEGGisce:YPL116W.

Organism-specific databases

EuPathDBiFungiDB:YPL116W.
SGDiS000006037. HOS3.

Phylogenomic databases

HOGENOMiHOG000246666.
InParanoidiQ02959.
KOiK11484.
OMAiDVIRIWA.
OrthoDBiEOG092C345D.

Enzyme and pathway databases

BioCyciYEAST:G3O-34016-MONOMER.

Miscellaneous databases

PROiQ02959.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 4 hits.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PRINTSiPR01270. HDASUPER.
ProtoNetiSearch...

Entry informationi

Entry nameiHOS3_YEAST
AccessioniPrimary (citable) accession number: Q02959
Secondary accession number(s): D6W3Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 138 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 4420 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.