GCN5_ARATH
ID GCN5_ARATH Reviewed; 568 AA.
AC Q9AR19; O22654; Q7G1G9; Q9M1G7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Histone acetyltransferase GCN5 {ECO:0000303|PubMed:11266554, ECO:0000303|PubMed:12615937};
DE Short=AtGCN5 {ECO:0000303|PubMed:11266554, ECO:0000303|PubMed:12615937};
DE EC=2.3.1.48 {ECO:0000255|PROSITE-ProRule:PRU00532};
DE AltName: Full=BIG TOP protein {ECO:0000303|PubMed:16763149};
GN Name=HAG1 {ECO:0000303|PubMed:12466527};
GN Synonyms=BGT {ECO:0000303|PubMed:16763149},
GN GCN5 {ECO:0000303|PubMed:11266554, ECO:0000303|PubMed:12615937},
GN HAT1 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At3g54610 {ECO:0000312|Araport:AT3G54610};
GN ORFNames=T14E10.180 {ECO:0000312|EMBL:CAB77581.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Tomihama T., Shoji K., Okano T.;
RT "Cloning of Arabidopsis histone acetyltransferase.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH ADA2A; ADA2B AND DREB1B.
RX PubMed=11266554; DOI=10.1093/nar/29.7.1524;
RA Stockinger E.J., Mao Y., Regier M.K., Triezenberg S.J., Thomashow M.F.;
RT "Transcriptional adaptor and histone acetyltransferase proteins in
RT Arabidopsis and their interactions with CBF1, a transcriptional activator
RT involved in cold-regulated gene expression.";
RL Nucleic Acids Res. 29:1524-1533(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NOMENCLATURE.
RX PubMed=12466527; DOI=10.1093/nar/gkf660;
RA Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT "Analysis of histone acetyltransferase and histone deacetylase families of
RT Arabidopsis thaliana suggests functional diversification of chromatin
RT modification among multicellular eukaryotes.";
RL Nucleic Acids Res. 30:5036-5055(2002).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12615937; DOI=10.1105/tpc.007922;
RA Vlachonasios K.E., Thomashow M.F., Triezenberg S.J.;
RT "Disruption mutations of ADA2b and GCN5 transcriptional adaptor genes
RT dramatically affect Arabidopsis growth, development, and gene expression.";
RL Plant Cell 15:626-638(2003).
RN [8]
RP INTERACTION WITH ADA2A AND ADA2B, AND FUNCTION.
RX PubMed=16603259; DOI=10.1016/j.bbaexp.2006.02.006;
RA Mao Y., Pavangadkar K.A., Thomashow M.F., Triezenberg S.J.;
RT "Physical and functional interactions of Arabidopsis ADA2 transcriptional
RT coactivator proteins with the acetyltransferase GCN5 and with the cold-
RT induced transcription factor CBF1.";
RL Biochim. Biophys. Acta 1759:69-79(2006).
RN [9]
RP FUNCTION.
RX PubMed=16648464; DOI=10.1101/gad.1417706;
RA Earley K., Lawrence R.J., Pontes O., Reuther R., Enciso A.J., Silva M.,
RA Neves N., Gross M., Viegas W., Pikaard C.S.;
RT "Erasure of histone acetylation by Arabidopsis HDA6 mediates large-scale
RT gene silencing in nucleolar dominance.";
RL Genes Dev. 20:1283-1293(2006).
RN [10]
RP FUNCTION, MUTAGENESIS OF 478-TRP--GLN-568, AND DISRUPTION PHENOTYPE.
RX PubMed=16763149; DOI=10.1126/science.1123841;
RA Long J.A., Ohno C., Smith Z.R., Meyerowitz E.M.;
RT "TOPLESS regulates apical embryonic fate in Arabidopsis.";
RL Science 312:1520-1523(2006).
RN [11]
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH EML.
RC STRAIN=cv. Columbia;
RX PubMed=17151888; DOI=10.1007/s00425-006-0446-2;
RA Gao M.J., Hegedus D.D., Sharpe A.G., Robinson S.J., Lydiate D.J.,
RA Hannoufa A.;
RT "Isolation and characterization of a GCN5-interacting protein from
RT Arabidopsis thaliana.";
RL Planta 225:1367-1379(2007).
RN [12]
RP INTERACTION WITH PP2C1.
RX PubMed=18498779; DOI=10.1016/j.bbagrm.2008.04.007;
RA Servet C., Benhamed M., Latrasse D., Kim W., Delarue M., Zhou D.-X.;
RT "Characterization of a phosphatase 2C protein as an interacting partner of
RT the histone acetyltransferase GCN5 in Arabidopsis.";
RL Biochim. Biophys. Acta 1779:376-382(2008).
CC -!- FUNCTION: Acetylates histone H3 and ADA2 proteins in vitro. Acetylates
CC 'Lys-14' of histone H3. Acetylation of histones gives a specific tag
CC for epigenetic transcription activation. Operates in concert with
CC certain DNA-binding transcriptional activators. Acts via the formation
CC of large multiprotein complexes that modify the chromatin (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:11266554,
CC ECO:0000269|PubMed:12615937, ECO:0000269|PubMed:16603259,
CC ECO:0000269|PubMed:16648464, ECO:0000269|PubMed:16763149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00532};
CC -!- ACTIVITY REGULATION: Histone acetyltransferase activity stimulated by
CC the presence of ADA2 proteins.
CC -!- SUBUNIT: Interacts in vitro with ADA2a, ADA2b and the transcriptional
CC activator DREB1B/CBF1. Interacts with PP2C1. Binds to EML
CC (PubMed:17151888). {ECO:0000269|PubMed:11266554,
CC ECO:0000269|PubMed:16603259, ECO:0000269|PubMed:17151888,
CC ECO:0000269|PubMed:18498779}.
CC -!- INTERACTION:
CC Q9AR19; Q9SFD5: ADA2A; NbExp=5; IntAct=EBI-979271, EBI-979206;
CC Q9AR19; Q9ATB4: ADA2B; NbExp=5; IntAct=EBI-979271, EBI-979237;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC {ECO:0000269|PubMed:11266554}.
CC -!- DOMAIN: The N-terminal part (1-150) is not required for interactions
CC with the ADA2 proteins.
CC -!- DISRUPTION PHENOTYPE: Pleiotropic effects on plant growth and
CC development, including dwarf size, aberrant root development, and short
CC petals and stamens in flowers. No embryonic phenotype. Increased
CC expression of EML (PubMed:17151888). {ECO:0000269|PubMed:12615937,
CC ECO:0000269|PubMed:16763149, ECO:0000269|PubMed:17151888}.
CC -!- MISCELLANEOUS: Mutations in HAG1 suppress the tpl-1 phenotype showing a
CC transformation during embryogenesis of the shoot pole into a second
CC root pole.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB92257.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB77581.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF037442; AAB92257.1; ALT_FRAME; mRNA.
DR EMBL; AF031958; AAB87070.1; -; mRNA.
DR EMBL; AF338768; AAK31318.1; -; mRNA.
DR EMBL; AF338771; AAK31321.1; -; Genomic_DNA.
DR EMBL; AL138656; CAB77581.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79255.1; -; Genomic_DNA.
DR EMBL; BT008909; AAP68348.1; -; mRNA.
DR EMBL; BT002057; AAN72068.1; -; mRNA.
DR PIR; T47620; T47620.
DR RefSeq; NP_567002.1; NM_115318.3.
DR AlphaFoldDB; Q9AR19; -.
DR SMR; Q9AR19; -.
DR BioGRID; 9942; 32.
DR IntAct; Q9AR19; 3.
DR STRING; 3702.AT3G54610.1; -.
DR iPTMnet; Q9AR19; -.
DR PaxDb; Q9AR19; -.
DR PRIDE; Q9AR19; -.
DR ProteomicsDB; 222022; -.
DR EnsemblPlants; AT3G54610.1; AT3G54610.1; AT3G54610.
DR GeneID; 824626; -.
DR Gramene; AT3G54610.1; AT3G54610.1; AT3G54610.
DR KEGG; ath:AT3G54610; -.
DR Araport; AT3G54610; -.
DR TAIR; locus:3354973; AT3G54610.
DR eggNOG; KOG1472; Eukaryota.
DR HOGENOM; CLU_015741_5_0_1; -.
DR InParanoid; Q9AR19; -.
DR OMA; RWMGYIK; -.
DR OrthoDB; 349249at2759; -.
DR PhylomeDB; Q9AR19; -.
DR BRENDA; 2.3.1.48; 399.
DR PRO; PR:Q9AR19; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9AR19; baseline and differential.
DR Genevisible; Q9AR19; AT.
DR GO; GO:0000123; C:histone acetyltransferase complex; IPI:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:TAIR.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:TAIR.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0016573; P:histone acetylation; IDA:TAIR.
DR GO; GO:0043966; P:histone H3 acetylation; IBA:GO_Central.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:TAIR.
DR GO; GO:0043970; P:histone H3-K9 acetylation; IDA:TAIR.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:1904278; P:positive regulation of wax biosynthetic process; IDA:TAIR.
DR GO; GO:0010321; P:regulation of vegetative phase change; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
DR GO; GO:0010015; P:root morphogenesis; IMP:TAIR.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR037800; GCN5.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR45750; PTHR45750; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Activator; Acyltransferase; Bromodomain; Chromatin regulator; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..568
FT /note="Histone acetyltransferase GCN5"
FT /id="PRO_0000269748"
FT DOMAIN 222..371
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 472..543
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..112
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 289
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 293..295
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 300..306
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 332..335
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT MUTAGEN 478..568
FT /note="Missing: In bgt-1/hag1-3; no embryonic phenotypes,
FT but suppresses the tpl-1 phenotype."
FT /evidence="ECO:0000269|PubMed:16763149"
FT CONFLICT 68
FT /note="D -> S (in Ref. 1; AAB92257)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="H -> R (in Ref. 1; AAB92257)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="R -> G (in Ref. 1; AAB92257)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="N -> K (in Ref. 1; AAB92257/AAB87070)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="G -> A (in Ref. 1; AAB92257/AAB87070)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="L -> P (in Ref. 1; AAB92257)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="H -> R (in Ref. 1; AAB92257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 63124 MW; 505C4A1816C376CC CRC64;
MDSHSSHLNA ANRSRSSQTP SPSHSASASV TSSLHKRKLA ATTAANAAAS EDHAPPSSSF
PPSSFSADTR DGALTSNDEL ESISARGADT DSDPDESEDI VVDDDEDEFA PEQDQDSSIR
TFTAARLDSS SGVNGSSRNT KLKTESSTVK LESSDGGKDG GSSVVGTGVS GTVGGSSISG
LVPKDESVKV LAENFQTSGA YIAREEALKR EEQAGRLKFV CYSNDSIDEH MMCLIGLKNI
FARQLPNMPK EYIVRLLMDR KHKSVMVLRG NLVVGGITYR PYHSQKFGEI AFCAITADEQ
VKGYGTRLMN HLKQHARDVD GLTHFLTYAD NNAVGYFVKQ GFTKEIYLEK DVWHGFIKDY
DGGLLMECKI DPKLPYTDLS SMIRQQRKAI DERIRELSNC QNVYPKIEFL KNEAGIPRKI
IKVEEIRGLR EAGWTPDQWG HTRFKLFNGS ADMVTNQKQL NALMRALLKT MQDHADAWPF
KEPVDSRDVP DYYDIIKDPI DLKVIAKRVE SEQYYVTLDM FVADARRMFN NCRTYNSPDT
IYYKCATRLE THFHSKVQAG LQSGAKSQ
