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Q9AR19

- GCN5_ARATH

UniProt

Q9AR19 - GCN5_ARATH

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Protein

Histone acetyltransferase GCN5

Gene

HAG1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Enzyme regulationi

Histone acetyltransferase activity stimulated by the presence of ADA2 proteins.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei289 – 2891Proton donor/acceptorBy similarity

GO - Molecular functioni

  1. DNA binding Source: TAIR
  2. H3 histone acetyltransferase activity Source: TAIR
  3. histone acetyltransferase activity Source: TAIR

GO - Biological processi

  1. flower development Source: TAIR
  2. histone acetylation Source: TAIR
  3. histone H3 acetylation Source: GOC
  4. positive regulation of transcription, DNA-templated Source: TAIR
  5. response to light stimulus Source: TAIR
  6. root morphogenesis Source: TAIR
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciARA:AT3G54610-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase GCN5 (EC:2.3.1.48)
Short name:
AtGCN5
Alternative name(s):
BIG TOP protein
Gene namesi
Name:HAG1
Synonyms:BGT, GCN5, HAT1
Ordered Locus Names:At3g54610
ORF Names:T14E10.180
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G54610.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. histone acetyltransferase complex Source: TAIR
  2. nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Pleiotropic effects on plant growth and development, including dwarf size, aberrant root development, and short petals and stamens in flowers. No embryonic phenotype.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi478 – 56891Missing in bgt-1/hag1-3; no embryonic phenotypes, but suppresses the tpl-1 phenotype. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 568568Histone acetyltransferase GCN5PRO_0000269748Add
BLAST

Proteomic databases

PaxDbiQ9AR19.
PRIDEiQ9AR19.

Expressioni

Tissue specificityi

Expressed in roots and leaves.1 Publication

Gene expression databases

GenevestigatoriQ9AR19.

Interactioni

Subunit structurei

Interacts in vitro with ADA2a, ADA2b and the transcriptional activator DREB1B/CBF1. Interacts with PP2C1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADA2BQ9ATB45EBI-979271,EBI-979237

Protein-protein interaction databases

BioGridi9942. 27 interactions.
IntActiQ9AR19. 3 interactions.
STRINGi3702.AT3G54610.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9AR19.
SMRiQ9AR19. Positions 216-378, 457-559.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini222 – 371150N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST
Domaini472 – 54372BromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni293 – 2953Acetyl-CoA bindingBy similarity
Regioni300 – 3067Acetyl-CoA bindingBy similarity
Regioni332 – 3354Acetyl-CoA bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 6664Ser-richAdd
BLAST
Compositional biasi89 – 11628Asp-richAdd
BLAST

Domaini

The N-terminal part (1-150) is not required for interactions with the ADA2 proteins.

Sequence similaritiesi

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

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiCOG5076.
HOGENOMiHOG000192257.
InParanoidiQ9AR19.
KOiK06062.
OMAiMVIRNNI.
PhylomeDBiQ9AR19.

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]
PfamiPF00583. Acetyltransf_1. 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.

Q9AR19-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSHSSHLNA ANRSRSSQTP SPSHSASASV TSSLHKRKLA ATTAANAAAS
60 70 80 90 100
EDHAPPSSSF PPSSFSADTR DGALTSNDEL ESISARGADT DSDPDESEDI
110 120 130 140 150
VVDDDEDEFA PEQDQDSSIR TFTAARLDSS SGVNGSSRNT KLKTESSTVK
160 170 180 190 200
LESSDGGKDG GSSVVGTGVS GTVGGSSISG LVPKDESVKV LAENFQTSGA
210 220 230 240 250
YIAREEALKR EEQAGRLKFV CYSNDSIDEH MMCLIGLKNI FARQLPNMPK
260 270 280 290 300
EYIVRLLMDR KHKSVMVLRG NLVVGGITYR PYHSQKFGEI AFCAITADEQ
310 320 330 340 350
VKGYGTRLMN HLKQHARDVD GLTHFLTYAD NNAVGYFVKQ GFTKEIYLEK
360 370 380 390 400
DVWHGFIKDY DGGLLMECKI DPKLPYTDLS SMIRQQRKAI DERIRELSNC
410 420 430 440 450
QNVYPKIEFL KNEAGIPRKI IKVEEIRGLR EAGWTPDQWG HTRFKLFNGS
460 470 480 490 500
ADMVTNQKQL NALMRALLKT MQDHADAWPF KEPVDSRDVP DYYDIIKDPI
510 520 530 540 550
DLKVIAKRVE SEQYYVTLDM FVADARRMFN NCRTYNSPDT IYYKCATRLE
560
THFHSKVQAG LQSGAKSQ
Length:568
Mass (Da):63,124
Last modified:June 1, 2001 - v1
Checksum:i505C4A1816C376CC
GO

Sequence cautioni

The sequence AAB92257.1 differs from that shown. Reason: Frameshift at positions 42, 163 and 548. Curated
The sequence CAB77581.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681D → S in AAB92257. 1 PublicationCurated
Sequence conflicti230 – 2301H → R in AAB92257. 1 PublicationCurated
Sequence conflicti243 – 2431R → G in AAB92257. 1 PublicationCurated
Sequence conflicti247 – 2471N → K in AAB92257. 1 PublicationCurated
Sequence conflicti247 – 2471N → K in AAB87070. 1 PublicationCurated
Sequence conflicti363 – 3631G → A in AAB92257. 1 PublicationCurated
Sequence conflicti363 – 3631G → A in AAB87070. 1 PublicationCurated
Sequence conflicti365 – 3651L → P in AAB92257. 1 PublicationCurated
Sequence conflicti474 – 4741H → R in AAB92257. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT47620.
RefSeqiNP_567002.1. NM_115318.2.
UniGeneiAt.10490.

Genome annotation databases

EnsemblPlantsiAT3G54610.1; AT3G54610.1; AT3G54610.
GeneIDi824626.
KEGGiath:AT3G54610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi T47620.
RefSeqi NP_567002.1. NM_115318.2.
UniGenei At.10490.

3D structure databases

ProteinModelPortali Q9AR19.
SMRi Q9AR19. Positions 216-378, 457-559.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 9942. 27 interactions.
IntActi Q9AR19. 3 interactions.
STRINGi 3702.AT3G54610.1-P.

Proteomic databases

PaxDbi Q9AR19.
PRIDEi Q9AR19.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G54610.1 ; AT3G54610.1 ; AT3G54610 .
GeneIDi 824626.
KEGGi ath:AT3G54610.

Organism-specific databases

TAIRi AT3G54610.

Phylogenomic databases

eggNOGi COG5076.
HOGENOMi HOG000192257.
InParanoidi Q9AR19.
KOi K06062.
OMAi MVIRNNI.
PhylomeDBi Q9AR19.

Enzyme and pathway databases

BioCyci ARA:AT3G54610-MONOMER.

Gene expression databases

Genevestigatori Q9AR19.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
[Graphical view ]
Pfami PF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiGCN5_ARATH
AccessioniPrimary (citable) accession number: Q9AR19
Secondary accession number(s): O22654, Q7G1G9, Q9M1G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Mutations in HAG1 suppress the tpl-1 phenotype showing a transformation during embryogenesis of the shoot pole into a second root pole.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3