Skip Header

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

Q6CXW4 (GCN5_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 54. 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
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:KLLA0A05115g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length516 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 processregulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-dependent

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 – 516516Histone acetyltransferase GCN5
PRO_0000211198

Regions

Domain177 – 332156N-acetyltransferase
Domain421 – 49171Bromo

Sites

Site2501Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6CXW4 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: F11C13FA976421F0

FASTA51659,291
        10         20         30         40         50         60 
MPPKRRHHGA GRVQNKRGKV DTVKEEIKPK DEPVETEIDG GSAVDEDVTD DLEHKTSKED 

        70         80         90        100        110        120 
QKEDQKEEDG PIDAQNGTSE TKVAGESVKT VEDKIESVTT NEEVVESPVN DYNASSTTTK 

       130        140        150        160        170        180 
AEEKQLEEEA NEKTDTSPIV ENEVVDEEAG TTKFDFDGQE YSYKDRPSVI EEKEGKIEFR 

       190        200        210        220        230        240 
VVNNDNSKEN MMVLTGLKNI FQKQLPKMPK EYIARLVYDR SHLSMAVVRK PLTVVGGITY 

       250        260        270        280        290        300 
RPFDKREFAE IVFCAISSTE QVRGYGAHLM NHLKDYVRAT SPIKYFLTYA DNYAIGYFKK 

       310        320        330        340        350        360 
QGFTKEITLD KNVWMGYIKD YEGGTLMQCS MLPRIRYLDA AKILLLQEAA IRRKIRSISQ 

       370        380        390        400        410        420 
SHIVRPGLKQ FLDLDNIKPI DPMTIPGLKE AGWTPEMDEL AQRPKRGPHY AAMQNLLTEL 

       430        440        450        460        470        480 
QNHAAAWPFL QPVNKEEVPD YYEFIKEPMD LSSMEMKLNG NRYEKMENFI YDARLIFNNC 

       490        500        510 
RAYNGENTSY FKYANRLEKF FNSKVKEIPE YSHLVD

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR382121 Genomic DNA. Translation: CAH02813.1.
RefSeqXP_451225.1. XM_451225.1.

3D structure databases

ProteinModelPortalQ6CXW4.
SMRQ6CXW4. Positions 176-339, 406-515.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6CXW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2896739.
GenomeReviewsGene locus KLLA0A05115g in contig CR382121_GR.
KEGGkla:KLLA0A05115g.

Phylogenomic databases

eggNOGfuNOG05844.
HOGENOMHBG749648.
OMALVYDRSH.
OrthoDBEOG412QF2.

Family and domain databases

InterProIPR000182. AcTrfase_GCN5-related_dom.
IPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
G3DSA:1.20.920.10. Bromodomain. 1 hit.
KOK06062.
PfamPF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF47370. Bromodomain. 1 hit.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGCN5_KLULA
AccessionPrimary (citable) accession number: Q6CXW4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: August 16, 2004
Last modified: December 14, 2011
This is version 54 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents