GTE9_ARATH
ID GTE9_ARATH Reviewed; 688 AA.
AC Q93YS6; B9DFD6; Q9LYA2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Transcription factor GTE9;
DE AltName: Full=BROMODOMAIN AND EXTRATERMINAL DOMAIN PROTEIN 9;
DE Short=AtBET9;
DE AltName: Full=Bromodomain-containing protein GTE9;
DE AltName: Full=Protein GLOBAL TRANSCRIPTION FACTOR GROUP E9;
GN Name=GTE9; Synonyms=BET9; OrderedLocusNames=At5g14270; ORFNames=F18O22.60;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-554.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP GENE FAMILY, AND 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 [6]
RP INTERACTION WITH BT1.
RX PubMed=15316289; DOI=10.1023/b:plan.0000038269.98972.bb;
RA Du L., Poovaiah B.W.;
RT "A novel family of Ca2+/calmodulin-binding proteins involved in
RT transcriptional regulation: interaction with fsh/Ring3 class transcription
RT activators.";
RL Plant Mol. Biol. 54:549-569(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- SUBUNIT: Interacts with BT1. {ECO:0000269|PubMed:15316289}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q93YS6-1; Sequence=Displayed;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87766.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163817; CAB87766.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92010.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71197.1; -; Genomic_DNA.
DR EMBL; AY059785; AAL24133.1; -; mRNA.
DR EMBL; AK316726; BAH19453.1; -; mRNA.
DR PIR; T48600; T48600.
DR RefSeq; NP_001332743.1; NM_001343329.1. [Q93YS6-1]
DR RefSeq; NP_568297.1; NM_121431.3. [Q93YS6-1]
DR AlphaFoldDB; Q93YS6; -.
DR SMR; Q93YS6; -.
DR IntAct; Q93YS6; 1.
DR STRING; 3702.AT5G14270.2; -.
DR iPTMnet; Q93YS6; -.
DR PaxDb; Q93YS6; -.
DR PRIDE; Q93YS6; -.
DR EnsemblPlants; AT5G14270.1; AT5G14270.1; AT5G14270. [Q93YS6-1]
DR EnsemblPlants; AT5G14270.3; AT5G14270.3; AT5G14270. [Q93YS6-1]
DR GeneID; 831277; -.
DR Gramene; AT5G14270.1; AT5G14270.1; AT5G14270. [Q93YS6-1]
DR Gramene; AT5G14270.3; AT5G14270.3; AT5G14270. [Q93YS6-1]
DR KEGG; ath:AT5G14270; -.
DR Araport; AT5G14270; -.
DR eggNOG; KOG1474; Eukaryota.
DR HOGENOM; CLU_007920_1_0_1; -.
DR InParanoid; Q93YS6; -.
DR OMA; GFWLKAM; -.
DR PhylomeDB; Q93YS6; -.
DR PRO; PR:Q93YS6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93YS6; baseline and differential.
DR Genevisible; Q93YS6; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR CDD; cd05506; Bromo_plant1; 1.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR037377; GTE_bromo.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51525; NET; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Bromodomain; Coiled coil; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..688
FT /note="Transcription factor GTE9"
FT /id="PRO_0000406340"
FT DOMAIN 149..221
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 280..361
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..688
FT /note="Transcription activation domain"
FT /evidence="ECO:0000250"
FT REGION 660..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 534..613
FT /evidence="ECO:0000255"
FT COMPBIAS 459..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 554
FT /note="E -> K (in Ref. 4; BAH19453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 688 AA; 75895 MW; B6D08D263A243033 CRC64;
MTERNGGFPG DYCFEAPGGD YDEGSDSPRV SEGSNCSKRK VGETFGVSKM VLPLSGLSSS
DRKELIRRLR QELEQIRVFQ KNFELSRTVA LTSSSASGLT RVKSFGMSRC STGPGKTVNP
ISAASKPTPV TTAVMLLMKQ CEALLKRLMS HQYGWVFNTP VDVVKLNILD YFNVIEHPMD
LGTVKNKLTS GTYSCPSEFA ADVRLTFSNA MTYNPPGNDV YVMADTLRKF FEVRWKTLEK
KLSGTKVHTE PSNLDAHKEK HIVIPVPMAK KRKTTAVDCE NVVDPAKRVM TDEDRLKLGK
DLESLTEFPA QLINFLRDHN SNEGGIGDDE IEIDINDLSD HALFQLRDLL DEHLREIQNK
KSSVEPCEIE LLHGSVPGNS SMQHCDGSEL DDEVVDIGEN EHPTSSISPV TIEKDLVLGN
SNGNSLGSVS GDPKMSSLPR ASKGLGTIDL EPMLDGATSA SPTRGSSVGG LDQLESASPE
KISSVEADCQ QDGNSAQNEK QLPPEKSYRA AILKNRFADI ILKAREKPLN QNDTRDPEKL
QREREELELQ KKKEKARLQA EAKAAEEARR KAEAQAAAEA AAEAKRKLEL EREAARQALM
EMEQSVELNE NAKFLEDLEL LKTVDTDHLT NTIEEEDGPD VGLRSFSFGG SNPLEQLGLF
MKQDEDEEEA DPLTSPAPEI DIEEGEID
