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Q756G9 (GCN5_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 acetyltransferase GCN5

EC=2.3.1.48
Gene names
Name:GCN5
Ordered Locus Names:AER297C
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Acetylates histone H2B to form H2BK11ac and H2BK16ac, histone H3 to form H3K14ac, with a lower preference histone H4 to form H4K8ac and H4K16ac, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation By similarity.

Catalytic activity

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

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the acetyltransferase family. GCN5 subfamily.

Contains 1 bromo domain.

Contains 1 N-acetyltransferase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Histone acetyltransferase GCN5
PRO_0000211195

Regions

Domain113 – 268156N-acetyltransferase
Domain357 – 42771Bromo

Sites

Site1861Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q756G9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 9BA78D49039CAC66

FASTA45252,414
        10         20         30         40         50         60 
MSMPLKRRNK QSQGNEPKKI KVEEQEAEEK ISEDIPVTDL KEPEALADIQ STSGGDEVSE 

        70         80         90        100        110        120 
GAQGDADPAE KSVGGLKEEV EDEEKGIVKF MFDGVEYKFR ERPSVIEEKE GKIEFRVVNN 

       130        140        150        160        170        180 
DNTRENMMVL TGLKNIFQKQ LPKMPKEYIA RLVYDRSHLS MAVIRKPLTV VGGITYRPFE 

       190        200        210        220        230        240 
KGEFAEIVFC AISSTEQVRG YGAHLMNHLK DYVRATTNIK YFLTYADNYA IGYFKKQGFT 

       250        260        270        280        290        300 
KEITLDKSVW MGYIKDYEGG TLMQCFMLPR IRYLDAAKIL LLQEAAIQRK IRTISRSHIV 

       310        320        330        340        350        360 
RPGLRQFEDL DNIEPIDPMS VPGLREAGWT PEMDELAQRP KRGPHYATMQ NVLTELQNHA 

       370        380        390        400        410        420 
AAWPFLQPVN RDEVPDYYEF IKEPMDLSTM EIKLENNRYE KMEDFIYDAR LIFNNCRAYN 

       430        440        450 
GENTSYFKYA NRLEKFFNTK MKEIPEYSHL LD 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016818 Genomic DNA. Translation: AAS52978.1.
RefSeqNP_985154.1. NM_210508.1.

3D structure databases

ProteinModelPortalQ756G9.
SMRQ756G9. Positions 112-275, 342-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_AER297C.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAS52978; AAS52978; AGOS_AER297C.
GeneID4621367.
KEGGago:AGOS_AER297C.

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000192257.
KOK06062.
OMADNCRKYN.
OrthoDBEOG7XM37B.
PhylomeDBQ756G9.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGCN5_ASHGO
AccessionPrimary (citable) accession number: Q756G9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families