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Protein

Histone acetyltransferase GCN5

Gene

GCN5

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei280 – 2801Proton donor/acceptorBy similarity
Sitei280 – 2801Important for catalytic activityBy similarity

GO - Molecular functioni

  1. histone acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase GCN5 (EC:2.3.1.48)
Gene namesi
Name:GCN5
Ordered Locus Names:CAGL0F08283g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
ProteomesiUP000002428 Componenti: Chromosome F

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 546546Histone acetyltransferase GCN5PRO_0000211196Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ6FTW5.
SMRiQ6FTW5. Positions 206-369, 436-545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini207 – 362156N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST
Domaini451 – 52171BromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni284 – 2863Acetyl-CoA bindingBy similarity
Regioni291 – 2977Acetyl-CoA bindingBy similarity
Regioni323 – 3264Acetyl-CoA bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi37 – 208172Glu-richAdd
BLAST
Compositional biasi45 – 11571Asp-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Bromodomain

Phylogenomic databases

HOGENOMiHOG000192257.
InParanoidiQ6FTW5.
KOiK06062.
OMAiLLKQKEC.
OrthoDBiEOG7XM37B.

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]
PfamiPF13508. Acetyltransf_7. 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.

Q6FTW5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTRRRLHHP EVEQVSKRQK VDKAESKNKK HADVAAERGE QSTEDHEDES
60 70 80 90 100
QDKKDKKVVG DNRDEDEEVS PNGQEAAEDN DDRKDKDAKE KDTETNDEGT
110 120 130 140 150
EKSHTDVNDD DDDVDESKEE DAAAAVDITK EKKDEQESDN KTEEKKVQEN
160 170 180 190 200
EEEEEEDENK NDEDVEELGS TEPVDDEKKG LVKFEFDGVE YKFKERASVI
210 220 230 240 250
EENEGKIEFR VVSNDNTREN MMVLTGLKNI FQKQLPKMPK EYIARLVYDR
260 270 280 290 300
SHLSMAVIRK PLTVVGGITY KPFNKRQFAE IVFCAISSTE QVRGYGAHLM
310 320 330 340 350
NHLKDYVRNT SDIRYFLTYA DNYAIGYFKK QGFTKDITLD KKVWMGYIKD
360 370 380 390 400
YEGGTLMQCS MLPRIRYLDA AKILLLQEAA LRRKIRTISK SHVVHPGLEC
410 420 430 440 450
FNDIENIKPI DPMSIPGLKE AGWTPEMDEL AQRPKRGPHY AAIQNILVEL
460 470 480 490 500
QNHAAAWPFL RPVNKEEVPD YYEFIKEPMD LSTMELKLEN NKYEKMEEFI
510 520 530 540
YDARLVCNNC RLYNGENTSY YKYANRLEKF FNNKVKEIPE YSHLID
Length:546
Mass (Da):63,512
Last modified:July 19, 2004 - v1
Checksum:i977FDACF889D0189
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380952 Genomic DNA. Translation: CAG59253.1.
RefSeqiXP_446329.1. XM_446329.1.

Genome annotation databases

GeneIDi2887572.
KEGGicgr:CAGL0F08283g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380952 Genomic DNA. Translation: CAG59253.1.
RefSeqiXP_446329.1. XM_446329.1.

3D structure databases

ProteinModelPortaliQ6FTW5.
SMRiQ6FTW5. Positions 206-369, 436-545.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2887572.
KEGGicgr:CAGL0F08283g.

Phylogenomic databases

HOGENOMiHOG000192257.
InParanoidiQ6FTW5.
KOiK06062.
OMAiLLKQKEC.
OrthoDBiEOG7XM37B.

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]
PfamiPF13508. Acetyltransf_7. 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_CANGA
AccessioniPrimary (citable) accession number: Q6FTW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 19, 2004
Last modified: January 7, 2015
This is version 74 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.