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Protein

Histone acetyltransferase gcn5

Gene

gcn5

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acetylates histone H2B to form H2BK11ac and H2BK16ac, histone H3 to form H3K14ac, and with a lower preference histone H4 to form H4K8ac and H4K16ac. Acetylation of histones gives a specific tag for epigenetic transcription activation (By similarity).By similarity1 Publication

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei191Proton donor/acceptorBy similarity1
Sitei191Important for catalytic activityBy similarity1

GO - Molecular functioni

  • H3 histone acetyltransferase activity Source: PomBase

GO - Biological processi

  • chromatin remodeling Source: PomBase
  • histone H3 acetylation Source: PomBase
  • negative regulation of leucine import Source: PomBase
  • negative regulation of transcription from RNA polymerase II promoter Source: PomBase
  • reciprocal meiotic recombination Source: PomBase
  • regulation of transcription from RNA polymerase II promoter Source: PomBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-SPO-5689880. Ub-specific processing proteases.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase gcn5 (EC:2.3.1.48)
Gene namesi
Name:gcn5
ORF Names:SPAC1952.05
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1952.05.
PomBaseiSPAC1952.05. gcn5.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: PomBase
  • SAGA complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002111991 – 454Histone acetyltransferase gcn5Add BLAST454

Proteomic databases

MaxQBiQ9UUK2.
PRIDEiQ9UUK2.

Interactioni

Subunit structurei

Interacts with taf72.1 Publication

Protein-protein interaction databases

BioGridi278971. 271 interactors.
IntActiQ9UUK2. 3 interactors.
MINTiMINT-8210502.

Structurei

3D structure databases

ProteinModelPortaliQ9UUK2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini118 – 273N-acetyltransferasePROSITE-ProRule annotationAdd BLAST156
Domaini360 – 430BromoPROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni195 – 197Acetyl-CoA bindingBy similarity3
Regioni202 – 208Acetyl-CoA bindingBy similarity7
Regioni234 – 237Acetyl-CoA bindingBy similarity4

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain

Phylogenomic databases

HOGENOMiHOG000192257.
InParanoidiQ9UUK2.
KOiK06062.
OMAiDVMHFLT.
OrthoDBiEOG092C0SVC.
PhylomeDBiQ9UUK2.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UUK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSLNDQTR PPDSSVVDST SSNFPNASND SVHDKPVKQD EQSNPNVREA
60 70 80 90 100
IANSDGQESL AVKENKDTES SSSHFVPNGV SNSKKRKLVA TDLDVDFDIS
110 120 130 140 150
SVRVTEKPSV LEEKSGVIQF RVVSNDDTAD SMIMLTGLKN IFMKQLPKMP
160 170 180 190 200
KEYITRLIYD RNHLSMTIVK DNLHVVGGIT YRPFEQRGFA EIVFCAIASN
210 220 230 240 250
EQVRGYGSHL MNHLKDYVRG TTTIQHFLTY ADNYAIGYFK KQGFTKEITL
260 270 280 290 300
DKSIWVGYIK DYEGGTLMQC TMIPKIKYLE ANLILAIQKA AVVSKINRIT
310 320 330 340 350
RSNVVYPGLD VFKDGPAHIE PSQVPGLMEV GWCKEMEELS KKPRPKPFFA
360 370 380 390 400
VLEMLFTEMQ NHPSSWPFMQ PVSKEDVPDY YEVIEHPMDL STMEFRLRNN
410 420 430 440 450
QYESVEEFIR DAKYIFDNCR SYNDSNTTYY KNADRLEKFF QKKLRETEYS

HLAD
Length:454
Mass (Da):51,976
Last modified:May 1, 2000 - v1
Checksum:iFF99039B00E8ECB3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB162439 Genomic DNA. Translation: BAD11106.1.
CU329670 Genomic DNA. Translation: CAB52569.1.
PIRiT37933.
RefSeqiNP_594807.1. NM_001020236.2.

Genome annotation databases

EnsemblFungiiSPAC1952.05.1; SPAC1952.05.1:pep; SPAC1952.05.
GeneIDi2542513.
KEGGispo:SPAC1952.05.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB162439 Genomic DNA. Translation: BAD11106.1.
CU329670 Genomic DNA. Translation: CAB52569.1.
PIRiT37933.
RefSeqiNP_594807.1. NM_001020236.2.

3D structure databases

ProteinModelPortaliQ9UUK2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278971. 271 interactors.
IntActiQ9UUK2. 3 interactors.
MINTiMINT-8210502.

Proteomic databases

MaxQBiQ9UUK2.
PRIDEiQ9UUK2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1952.05.1; SPAC1952.05.1:pep; SPAC1952.05.
GeneIDi2542513.
KEGGispo:SPAC1952.05.

Organism-specific databases

EuPathDBiFungiDB:SPAC1952.05.
PomBaseiSPAC1952.05. gcn5.

Phylogenomic databases

HOGENOMiHOG000192257.
InParanoidiQ9UUK2.
KOiK06062.
OMAiDVMHFLT.
OrthoDBiEOG092C0SVC.
PhylomeDBiQ9UUK2.

Enzyme and pathway databases

ReactomeiR-SPO-5689880. Ub-specific processing proteases.

Miscellaneous databases

PROiQ9UUK2.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGCN5_SCHPO
AccessioniPrimary (citable) accession number: Q9UUK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: May 1, 2000
Last modified: October 5, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.