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Q9AR19

- GCN5_ARATH

UniProt

Q9AR19 - GCN5_ARATH

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
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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.

    GO - Molecular functioni

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

    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

    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

    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, 461-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    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

    MDSHSSHLNA ANRSRSSQTP SPSHSASASV TSSLHKRKLA ATTAANAAAS    50
    EDHAPPSSSF PPSSFSADTR DGALTSNDEL ESISARGADT DSDPDESEDI 100
    VVDDDEDEFA PEQDQDSSIR TFTAARLDSS SGVNGSSRNT KLKTESSTVK 150
    LESSDGGKDG GSSVVGTGVS GTVGGSSISG LVPKDESVKV LAENFQTSGA 200
    YIAREEALKR EEQAGRLKFV CYSNDSIDEH MMCLIGLKNI FARQLPNMPK 250
    EYIVRLLMDR KHKSVMVLRG NLVVGGITYR PYHSQKFGEI AFCAITADEQ 300
    VKGYGTRLMN HLKQHARDVD GLTHFLTYAD NNAVGYFVKQ GFTKEIYLEK 350
    DVWHGFIKDY DGGLLMECKI DPKLPYTDLS SMIRQQRKAI DERIRELSNC 400
    QNVYPKIEFL KNEAGIPRKI IKVEEIRGLR EAGWTPDQWG HTRFKLFNGS 450
    ADMVTNQKQL NALMRALLKT MQDHADAWPF KEPVDSRDVP DYYDIIKDPI 500
    DLKVIAKRVE SEQYYVTLDM FVADARRMFN NCRTYNSPDT IYYKCATRLE 550
    THFHSKVQAG LQSGAKSQ 568
    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.
    The sequence CAB77581.1 differs from that shown. Reason: Erroneous gene model prediction.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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, 461-558.
    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

    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: October 1, 2014
    This is version 95 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