Histone acetyltransferase GCN5 - Arabidopsis thaliana (Mouse-ear cress)

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Q9AR19 (GCN5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 83. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Histone acetyltransferase GCN5
Short name=AtGCN5
EC=2.3.1.48

Alternative name(s):
BIG TOP protein

Gene names

Name:	HAG1
Synonyms:	BGT, GCN5, HAT1
Ordered Locus Names:	At3g54610
ORF Names:	T14E10.180

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acetylates histone H3 and ADA2 proteins in vitro. Acetylates 'Lys-14' of histone H3. Acetylation of histones gives a specific tag for epigenetic transcription activation. Operates in concert with certain DNA-binding transcriptional activators. Acts via the formation of large multiprotein complexes that modify the chromatin By similarity. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Enzyme regulation	Histone acetyltransferase activity stimulated by the presence of ADA2 proteins.
Subunit structure	Interacts in vitro with ADA2a, ADA2b and the transcriptional activator DREB1B/CBF1. Interacts with PP2C1. Ref.2 Ref.8 Ref.11
Subcellular location	Nucleus Probable.
Tissue specificity	Expressed in roots and leaves. Ref.2
Domain	The N-terminal part (1-150) is not required for interactions with the ADA2 proteins.
Disruption phenotype	Pleiotropic effects on plant growth and development, including dwarf size, aberrant root development, and short petals and stamens in flowers. No embryonic phenotype. Ref.7 Ref.10
Miscellaneous	Mutations in HAG1 suppress the tpl-1 phenotype showing a transformation during embryogenesis of the shoot pole into a second root pole.
Sequence similarities	Belongs to the GCN5 family. Contains 1 bromo domain. Contains 1 N-acetyltransferase domain.
Sequence caution	The sequence AAB92257.1 differs from that shown. Reason: Frameshift at positions 42, 163 and 548. The sequence CAB77581.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Bromodomain
Molecular function	Activator Acyltransferase Chromatin regulator Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	flower development Inferred from mutant phenotype PubMed 12740375. Source: TAIR positive regulation of transcription, DNA-dependent Traceable author statement Ref.2. Source: TAIR response to light stimulus Inferred from mutant phenotype PubMed 17085686. Source: TAIR root morphogenesis Inferred from mutant phenotype PubMed 17085686. Source: TAIR transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	histone acetyltransferase complex Inferred from physical interaction Ref.2. Source: TAIR
Molecular_function	DNA binding Inferred from direct assay PubMed 17085686. Source: TAIR H3 histone acetyltransferase activity Inferred from direct assay PubMed 17877703. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADA2B	Q9ATB4	5	EBI-979271,EBI-979237

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 568

568

Histone acetyltransferase GCN5

PRO_0000269748

Regions

Domain

222 – 371

150

N-acetyltransferase

Domain

472 – 543

Bromo

Compositional bias

3 – 66

Ser-rich

Compositional bias

89 – 116

Asp-rich

Experimental info

Mutagenesis

478 – 568

Missing in bgt-1/hag1-3; no embryonic phenotypes, but suppresses the tpl-1 phenotype. Ref.10

Sequence conflict

D → S in AAB92257. Ref.1

Sequence conflict

230

H → R in AAB92257. Ref.1

Sequence conflict

243

R → G in AAB92257. Ref.1

Sequence conflict

247

N → K in AAB92257. Ref.1

Sequence conflict

247

N → K in AAB87070. Ref.1

Sequence conflict

363

G → A in AAB92257. Ref.1

Sequence conflict

363

G → A in AAB87070. Ref.1

Sequence conflict

365

L → P in AAB92257. Ref.1

Sequence conflict

474

H → R in AAB92257. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9AR19 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 505C4A1816C376CC
Show »

FASTA

568

63,124

        10         20         30         40         50         60 
MDSHSSHLNA ANRSRSSQTP SPSHSASASV TSSLHKRKLA ATTAANAAAS EDHAPPSSSF 

        70         80         90        100        110        120 
PPSSFSADTR DGALTSNDEL ESISARGADT DSDPDESEDI VVDDDEDEFA PEQDQDSSIR 

       130        140        150        160        170        180 
TFTAARLDSS SGVNGSSRNT KLKTESSTVK LESSDGGKDG GSSVVGTGVS GTVGGSSISG 

       190        200        210        220        230        240 
LVPKDESVKV LAENFQTSGA YIAREEALKR EEQAGRLKFV CYSNDSIDEH MMCLIGLKNI 

       250        260        270        280        290        300 
FARQLPNMPK EYIVRLLMDR KHKSVMVLRG NLVVGGITYR PYHSQKFGEI AFCAITADEQ 

       310        320        330        340        350        360 
VKGYGTRLMN HLKQHARDVD GLTHFLTYAD NNAVGYFVKQ GFTKEIYLEK DVWHGFIKDY 

       370        380        390        400        410        420 
DGGLLMECKI DPKLPYTDLS SMIRQQRKAI DERIRELSNC QNVYPKIEFL KNEAGIPRKI 

       430        440        450        460        470        480 
IKVEEIRGLR EAGWTPDQWG HTRFKLFNGS ADMVTNQKQL NALMRALLKT MQDHADAWPF 

       490        500        510        520        530        540 
KEPVDSRDVP DYYDIIKDPI DLKVIAKRVE SEQYYVTLDM FVADARRMFN NCRTYNSPDT 

       550        560 
IYYKCATRLE THFHSKVQAG LQSGAKSQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of Arabidopsis histone acetyltransferase." Tomihama T., Shoji K., Okano T. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Transcriptional adaptor and histone acetyltransferase proteins in Arabidopsis and their interactions with CBF1, a transcriptional activator involved in cold-regulated gene expression." Stockinger E.J., Mao Y., Regier M.K., Triezenberg S.J., Thomashow M.F. Nucleic Acids Res. 29:1524-1533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ADA2A; ADA2B AND DREB1B.
[3]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes." Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S., Richards E.J., Bender J., Mount D.W., Jorgensen R.A. Nucleic Acids Res. 30:5036-5055(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
[7]	"Disruption mutations of ADA2b and GCN5 transcriptional adaptor genes dramatically affect Arabidopsis growth, development, and gene expression." Vlachonasios K.E., Thomashow M.F., Triezenberg S.J. Plant Cell 15:626-638(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]	"Physical and functional interactions of Arabidopsis ADA2 transcriptional coactivator proteins with the acetyltransferase GCN5 and with the cold-induced transcription factor CBF1." Mao Y., Pavangadkar K.A., Thomashow M.F., Triezenberg S.J. Biochim. Biophys. Acta 1759:69-79(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ADA2A AND ADA2B, FUNCTION.
[9]	"Erasure of histone acetylation by Arabidopsis HDA6 mediates large-scale gene silencing in nucleolar dominance." Earley K., Lawrence R.J., Pontes O., Reuther R., Enciso A.J., Silva M., Neves N., Gross M., Viegas W., Pikaard C.S. Genes Dev. 20:1283-1293(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"TOPLESS regulates apical embryonic fate in Arabidopsis." Long J.A., Ohno C., Smith Z.R., Meyerowitz E.M. Science 312:1520-1523(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 478-TRP--GLN-568, DISRUPTION PHENOTYPE.
[11]	"Characterization of a phosphatase 2C protein as an interacting partner of the histone acetyltransferase GCN5 in Arabidopsis." Servet C., Benhamed M., Latrasse D., Kim W., Delarue M., Zhou D.-X. Biochim. Biophys. Acta 1779:376-382(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PP2C1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF037442 mRNA. Translation: AAB92257.1. Frameshift. AF031958 mRNA. Translation: AAB87070.1. AF338768 mRNA. Translation: AAK31318.1. AF338771 Genomic DNA. Translation: AAK31321.1. AL138656 Genomic DNA. Translation: CAB77581.1. Sequence problems. CP002686 Genomic DNA. Translation: AEE79255.1. BT008909 mRNA. Translation: AAP68348.1. BT002057 mRNA. Translation: AAN72068.1.
IPI	IPI00531535.
PIR	T47620.
RefSeq	NP_567002.1. NM_115318.2.
UniGene	At.10490.
3D structure databases
ProteinModelPortal	Q9AR19.
SMR	Q9AR19. Positions 216-378, 457-559.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9AR19. 3 interactions.
STRING	3702.AT3G54610.1-P.
Proteomic databases
PaxDb	Q9AR19.
PRIDE	Q9AR19.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G54610.1; AT3G54610.1; AT3G54610.
GeneID	824626.
KEGG	ath:AT3G54610.
Organism-specific databases
TAIR	At3g54610.
Phylogenomic databases
eggNOG	COG5076.
HOGENOM	HOG000192257.
InParanoid	Q9AR19.
KO	K06062.
OMA	GYFVKQG.
PhylomeDB	Q9AR19.
ProtClustDB	CLSN2689164.
Gene expression databases
Genevestigator	Q9AR19.
Family and domain databases
Gene3D	1.20.920.10. 1 hit. 3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR000182. GNAT_dom. [Graphical view]
Pfam	PF00583. Acetyltransf_1. 1 hit. PF00439. Bromodomain. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF47370. Bromodomain. 1 hit.
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GCN5_ARATH

Accession

Primary (citable) accession number: Q9AR19
Secondary accession number(s): O22654, Q7G1G9, Q9M1G7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents