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Q9AR19 (GCN5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Protein existenceEvidence 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 acetyltransferase family. GCN5 subfamily.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADA2BQ9ATB45EBI-979271,EBI-979237

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568Histone acetyltransferase GCN5
PRO_0000269748

Regions

Domain222 – 371150N-acetyltransferase
Domain472 – 54372Bromo
Compositional bias3 – 6664Ser-rich
Compositional bias89 – 11628Asp-rich

Experimental info

Mutagenesis478 – 56891Missing in bgt-1/hag1-3; no embryonic phenotypes, but suppresses the tpl-1 phenotype. Ref.10
Sequence conflict681D → S in AAB92257. Ref.1
Sequence conflict2301H → R in AAB92257. Ref.1
Sequence conflict2431R → G in AAB92257. Ref.1
Sequence conflict2471N → K in AAB92257. Ref.1
Sequence conflict2471N → K in AAB87070. Ref.1
Sequence conflict3631G → A in AAB92257. Ref.1
Sequence conflict3631G → A in AAB87070. Ref.1
Sequence conflict3651L → P in AAB92257. Ref.1
Sequence conflict4741H → R in AAB92257. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9AR19 [UniParc].

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

FASTA56863,124
        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' 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. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., 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. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.
PIRT47620.
RefSeqNP_567002.1. NM_115318.2.
UniGeneAt.10490.

3D structure databases

ProteinModelPortalQ9AR19.
SMRQ9AR19. Positions 216-561.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid9942. 27 interactions.
IntActQ9AR19. 3 interactions.
STRING3702.AT3G54610.1-P.

Proteomic databases

PaxDbQ9AR19.
PRIDEQ9AR19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G54610.1; AT3G54610.1; AT3G54610.
GeneID824626.
KEGGath:AT3G54610.

Organism-specific databases

TAIRAT3G54610.

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000192257.
InParanoidQ9AR19.
KOK06062.
OMAYIVRLLM.
PhylomeDBQ9AR19.
ProtClustDBCLSN2689164.

Enzyme and pathway databases

BioCycARA:AT3G54610-MONOMER.

Gene expression databases

GenevestigatorQ9AR19.

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]
PfamPF00583. Acetyltransf_1. 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_ARATH
AccessionPrimary (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: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names