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Q6FTW5 (GCN5_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:CAGL0F08283g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces

Protein attributes

Sequence length546 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.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainBromodomain
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546Histone acetyltransferase GCN5
PRO_0000211196

Regions

Domain207 – 362156N-acetyltransferase
Domain451 – 52171Bromo
Compositional bias37 – 208172Glu-rich
Compositional bias45 – 11571Asp-rich

Sites

Site2801Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FTW5 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 977FDACF889D0189

FASTA54663,512
        10         20         30         40         50         60 
MVTRRRLHHP EVEQVSKRQK VDKAESKNKK HADVAAERGE QSTEDHEDES QDKKDKKVVG 

        70         80         90        100        110        120 
DNRDEDEEVS PNGQEAAEDN DDRKDKDAKE KDTETNDEGT EKSHTDVNDD DDDVDESKEE 

       130        140        150        160        170        180 
DAAAAVDITK EKKDEQESDN KTEEKKVQEN EEEEEEDENK NDEDVEELGS TEPVDDEKKG 

       190        200        210        220        230        240 
LVKFEFDGVE YKFKERASVI EENEGKIEFR VVSNDNTREN MMVLTGLKNI FQKQLPKMPK 

       250        260        270        280        290        300 
EYIARLVYDR SHLSMAVIRK PLTVVGGITY KPFNKRQFAE IVFCAISSTE QVRGYGAHLM 

       310        320        330        340        350        360 
NHLKDYVRNT SDIRYFLTYA DNYAIGYFKK QGFTKDITLD KKVWMGYIKD YEGGTLMQCS 

       370        380        390        400        410        420 
MLPRIRYLDA AKILLLQEAA LRRKIRTISK SHVVHPGLEC FNDIENIKPI DPMSIPGLKE 

       430        440        450        460        470        480 
AGWTPEMDEL AQRPKRGPHY AAIQNILVEL QNHAAAWPFL RPVNKEEVPD YYEFIKEPMD 

       490        500        510        520        530        540 
LSTMELKLEN NKYEKMEEFI YDARLVCNNC RLYNGENTSY YKYANRLEKF FNNKVKEIPE 


YSHLID 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR380952 Genomic DNA. Translation: CAG59253.1.
RefSeqXP_446329.1. XM_446329.1.

3D structure databases

ProteinModelPortalQ6FTW5.
SMRQ6FTW5. Positions 206-369, 436-545.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2887572.
KEGGcgr:CAGL0F08283g.

Phylogenomic databases

HOGENOMHOG000192257.
KOK06062.
OMAAKSENND.
OrthoDBEOG7XM37B.

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_CANGA
AccessionPrimary (citable) accession number: Q6FTW5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 19, 2004
Last modified: May 14, 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