Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q756G9 (GCN5_ASHGO)

Last modified February 9, 2010. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Histone acetyltransferase GCN5
    EC=2.3.1.48
Gene names
Name: GCN5
Ordered Locus Names: AER297C
OrganismAshbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier33169 [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 GCN5 family.

Contains 1 bromo domain.

Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainBromodomain
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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
Q756G9-1 [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

[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: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.

3D structure databases

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

Protein-protein interaction databases

STRINGQ756G9.

Genome annotation databases

GeneID4621367.
GenomeReviewsGene locus AER297C in contig AE016818_GR.
KEGGago:AGOS_AER297C.
NMPDRfig|33169.1.peg.2799.

Organism-specific databases

AGDAER297C.

Phylogenomic databases

eggNOGfuNOG05844.
HOGENOMHBG749648.
OMAGLKNIFQ.
OrthoDBEOG9BP2TZ.

Enzyme and pathway databases

BRENDA2.3.1.48. 279361.

Family and domain databases

InterProIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GCN5-rel_AcTrfase.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
G3DSA:1.20.920.10. Bromodomain. 1 hit.
PfamPF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
[Graphical view]
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: February 9, 2010
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents