GAGA_DROME
ID GAGA_DROME Reviewed; 581 AA.
AC Q08605; O18349; O18350; O18526; Q08083; Q7JN57; Q8MYL3; Q8T387; Q9V3X7;
AC Q9VUH2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Transcription factor GAGA;
DE AltName: Full=Adh transcription factor 2;
DE AltName: Full=GAGA factor;
DE Short=GAF;
DE AltName: Full=Neural conserved at 70F;
DE AltName: Full=Trithorax-like protein;
GN Name=Trl; Synonyms=Adf-2, GAGA, Nc70F, TFGAGA; ORFNames=CG33261;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), PROTEIN SEQUENCE OF 393-405 AND
RP 498-518 (ISOFORM B), FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=7504178; DOI=10.1128/mcb.13.12.7961-7970.1993;
RA Soeller W.C., Oh C.E., Kornberg T.B.;
RT "Isolation of cDNAs encoding the Drosophila GAGA transcription factor.";
RL Mol. Cell. Biol. 13:7961-7970(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION,
RP HETERODIMERIZATION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9241251; DOI=10.1093/nar/25.16.3345;
RA Benyajati C., Mueller L., Xu N., Pappano M., Gao J., Mosammaparast M.,
RA Conklin D., Granok H., Craig C., Elgin S.C.R.;
RT "Multiple isoforms of GAGA factor, a critical component of chromatin
RT structure.";
RL Nucleic Acids Res. 25:3345-3353(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=11421119;
RA Katokhin A.V., Pindiurin A.V., Fedorova E.V., Baricheva E.M.;
RT "Molecular genetic analysis of Thrithorax-like gene encoded transcriptional
RT factor GAGA in Drosophila melanogaster.";
RL Genetika 37:467-474(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-197 (ISOFORM G), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 363-581 (ISOFORM I).
RA Karagodin D.A., Baricheva E.M.;
RT "New forms mRNA of the Trl gene.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 136-581 (ISOFORM B), AND TISSUE SPECIFICITY.
RC TISSUE=Prepupa;
RX PubMed=8307350;
RA Perelygina L.M., Baricheva E.M., Sebeleva T.E., Kokoza V.A.;
RT "The evolutionarily conserved gene Nc70F, expressed in nerve tissue of
RT Drosophila melanogaster, encodes a protein homologous to the mouse delta
RT transcription factor.";
RL Genetika 29:1597-1607(1993).
RN [10]
RP PROTEIN SEQUENCE OF 197-209; 274-288 AND 475-494 (ISOFORM B), AND
RP INTERACTION WITH E(BX).
RX PubMed=11583616; DOI=10.1016/s1097-2765(01)00345-8;
RA Xiao H., Sandaltzopoulos R., Wang H.-M., Hamiche A., Ranallo R., Lee K.-M.,
RA Fu D., Wu C.;
RT "Dual functions of largest NURF subunit NURF301 in nucleosome sliding and
RT transcription factor interactions.";
RL Mol. Cell 8:531-543(2001).
RN [11]
RP FUNCTION.
RX PubMed=8620838; DOI=10.1242/dev.122.4.1113;
RA Bhat K.M., Farkas G., Karch F., Gyurkovics H., Gausz J., Schedl P.;
RT "The GAGA factor is required in the early Drosophila embryo not only for
RT transcriptional regulation but also for nuclear division.";
RL Development 122:1113-1124(1996).
RN [12]
RP DNA-BINDING, PROTEIN OLIGOMERIZATION, AND CHARACTERIZATION OF PTB DOMAIN.
RX PubMed=10347208; DOI=10.1074/jbc.274.23.16461;
RA Espinas M.L., Jimenez-Garcia E., Vaquero A., Canudas S., Bernues J.,
RA Azorin F.;
RT "The N-terminal POZ domain of GAGA mediates the formation of oligomers that
RT bind DNA with high affinity and specificity.";
RL J. Biol. Chem. 274:16461-16469(1999).
RN [13]
RP INTERACTION WITH BIN1.
RX PubMed=11256608; DOI=10.1093/embo-reports/kvd046;
RA Espinas M.L., Canudas S., Fanti L., Pimpinelli S., Casanova J., Azorin F.;
RT "The GAGA factor of Drosophila interacts with SAP18, a Sin3-associated
RT polypeptide.";
RL EMBO Rep. 1:253-259(2000).
RN [14]
RP CHARACTERIZATION OF GLN-RICH DOMAIN.
RX PubMed=10764754; DOI=10.1074/jbc.m000967200;
RA Vaquero A., Espinas M.L., Azorin F., Bernues J.;
RT "Functional mapping of the GAGA factor assigns its transcriptional activity
RT to the C-terminal glutamine-rich domain.";
RL J. Biol. Chem. 275:19461-19468(2000).
RN [15]
RP FUNCTION.
RX PubMed=12200449; DOI=10.1074/jbc.m207505200;
RA Kosoy A., Pagans S., Espinas M.L., Azorin F., Bernues J.;
RT "GAGA factor down-regulates its own promoter.";
RL J. Biol. Chem. 277:42280-42288(2002).
RN [16]
RP INTERACTION WITH TTK.
RX PubMed=12384587; DOI=10.1093/nar/gkf570;
RA Pagans S., Ortiz-Lombardia M., Espinas M.L., Bernues J., Azorin F.;
RT "The Drosophila transcription factor tramtrack (TTK) interacts with
RT Trithorax-like (GAGA) and represses GAGA-mediated activation.";
RL Nucleic Acids Res. 30:4406-4413(2002).
RN [17]
RP FUNCTION, AND INTERACTION WITH SSRP AND DRE4.
RX PubMed=12815073; DOI=10.1101/gad.1086803;
RA Shimojima T., Okada M., Nakayama T., Ueda H., Okawa K., Iwamatsu A.,
RA Handa H., Hirose S.;
RT "Drosophila FACT contributes to Hox gene expression through physical and
RT functional interactions with GAGA factor.";
RL Genes Dev. 17:1605-1616(2003).
RN [18]
RP FUNCTION, AND INTERACTION WITH LOLAL AND PHP.
RX PubMed=12834867; DOI=10.1016/s0925-4773(03)00046-7;
RA Mishra K., Chopra V.S., Srinivasan A., Mishra R.K.;
RT "Trl-GAGA directly interacts with lola like and both are part of the
RT repressive complex of Polycomb group of genes.";
RL Mech. Dev. 120:681-689(2003).
RN [19]
RP INTERACTION WITH CORTO.
RX PubMed=12771214; DOI=10.1093/nar/gkg381;
RA Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F.;
RT "The Drosophila Corto protein interacts with Polycomb-group proteins and
RT the GAGA factor.";
RL Nucleic Acids Res. 31:2873-2882(2003).
RN [20]
RP DNA-BINDING SPECIFICITY.
RX PubMed=12601174; DOI=10.1073/pnas.0438000100;
RA van Steensel B., Delrow J., Bussemaker H.J.;
RT "Genomewide analysis of Drosophila GAGA factor target genes reveals
RT context-dependent DNA binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2580-2585(2003).
RN [21]
RP FUNCTION.
RX PubMed=15063171; DOI=10.1016/j.ydbio.2004.01.006;
RA Bejarano F., Busturia A.;
RT "Function of the Trithorax-like gene during Drosophila development.";
RL Dev. Biol. 268:327-341(2004).
RN [22]
RP FUNCTION.
RX PubMed=15020425; DOI=10.1534/genetics.166.1.279;
RA Greenberg A.J., Yanowitz J.L., Schedl P.;
RT "The Drosophila GAGA factor is required for dosage compensation in males
RT and for the formation of the male-specific-lethal complex chromatin entry
RT site at 12DE.";
RL Genetics 166:279-289(2004).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [24]
RP STRUCTURE BY NMR OF 310-372.
RX PubMed=9033593; DOI=10.1038/nsb0297-122;
RA Omichinski J.G., Pedone P.V., Felsenfeld G., Gronenborn A.M., Clore G.M.;
RT "The solution structure of a specific GAGA factor-DNA complex reveals a
RT modular binding mode.";
RL Nat. Struct. Biol. 4:122-132(1997).
RN [25]
RP INTERACTION WITH NUP98.
RX PubMed=28366641; DOI=10.1016/j.molcel.2017.02.020;
RA Pascual-Garcia P., Debo B., Aleman J.R., Talamas J.A., Lan Y., Nguyen N.H.,
RA Won K.J., Capelson M.;
RT "Metazoan nuclear pores provide a scaffold for poised genes and mediate
RT induced enhancer-promoter contacts.";
RL Mol. Cell 66:63-76(2017).
CC -!- FUNCTION: Transcriptional activator that functions by regulating
CC chromatin structure. Overcomes the repressive effects of chromatin by
CC promoting the open chromatin conformation in promoter gene regions,
CC thereby allowing access to other transcription factors. Binds to DNA
CC Polycomb response elements (PREs) at the bithorax complex and to the
CC proximal region of the engrailed promoter, and positively regulates
CC transcription of many genes including homeotic ones. Binds to the DNA
CC sequence (GA)n, with optimal binding to the pentamer 5'-GAGAG-3'. Binds
CC DNA as an oligomer. May also act as a transcriptional repressor,
CC maintaining the repressed state of genes including lolal, and down-
CC regulating its own transcription. Required for dosage compensation in
CC males and may be involved in oogenesis. Also has a role in nuclear
CC division. {ECO:0000269|PubMed:12200449, ECO:0000269|PubMed:12815073,
CC ECO:0000269|PubMed:12834867, ECO:0000269|PubMed:15020425,
CC ECO:0000269|PubMed:15063171, ECO:0000269|PubMed:7504178,
CC ECO:0000269|PubMed:8620838, ECO:0000269|PubMed:9241251}.
CC -!- SUBUNIT: Interacts with Bin1, lolal, corto, ttk and ph-p
CC (PubMed:11256608, PubMed:12384587, PubMed:12834867, PubMed:12771214).
CC Interacts with FACT subunits Ssrp and dre4/SPT16 (PubMed:12815073).
CC Interacts with E(bx) (PubMed:11583616). Upon ecdysone stimulation,
CC interacts with Nup98 (PubMed:28366641). {ECO:0000269|PubMed:11256608,
CC ECO:0000269|PubMed:11583616, ECO:0000269|PubMed:12384587,
CC ECO:0000269|PubMed:12771214, ECO:0000269|PubMed:12815073,
CC ECO:0000269|PubMed:12834867, ECO:0000269|PubMed:28366641}.
CC -!- INTERACTION:
CC Q08605; P41046: corto; NbExp=2; IntAct=EBI-300317, EBI-300379;
CC Q08605; Q7KRI2: lolal; NbExp=6; IntAct=EBI-300317, EBI-84493;
CC Q08605-2; Q9VEX9: Bin1; NbExp=4; IntAct=EBI-665803, EBI-129424;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7504178,
CC ECO:0000269|PubMed:9241251}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A; Synonyms=F, GAGA-581;
CC IsoId=Q08605-1; Sequence=Displayed;
CC Name=B; Synonyms=C, D, E, H, GAGA-519a, GAGA-519b;
CC IsoId=Q08605-2; Sequence=VSP_015537;
CC Name=G; Synonyms=GAGA-566;
CC IsoId=Q08605-3; Sequence=VSP_015536;
CC Name=I;
CC IsoId=Q08605-4; Sequence=VSP_015538;
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system throughout
CC development. {ECO:0000269|PubMed:8307350}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously during embryogenesis with
CC higher levels found from 9-12 hours after egg laying. Low levels are
CC found in larvae and adults. {ECO:0000269|PubMed:9241251}.
CC -!- DOMAIN: The N-terminal BTB domain mediates protein oligomerization. The
CC C-terminal glutamine-rich region is required for transcriptional
CC activation activity.
CC -!- PTM: The N-terminus is blocked.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L22205; AAA16072.1; -; mRNA.
DR EMBL; U16728; AAB81112.1; -; mRNA.
DR EMBL; U18386; AAB81113.1; -; mRNA.
DR EMBL; U68563; AAB81117.1; -; mRNA.
DR EMBL; AJ225042; CAA12383.1; -; Genomic_DNA.
DR EMBL; AJ225042; CAB86986.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49709.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49710.1; -; Genomic_DNA.
DR EMBL; AY069651; AAL39796.1; -; mRNA.
DR EMBL; BT003649; AAO39653.1; -; mRNA.
DR EMBL; AJ441087; CAD29581.1; -; mRNA.
DR EMBL; AJ459425; CAD30828.1; -; mRNA.
DR EMBL; X59784; CAA42446.1; -; mRNA.
DR PIR; A54590; A54590.
DR RefSeq; NP_001034014.1; NM_001038925.3. [Q08605-2]
DR RefSeq; NP_996077.1; NM_206355.4. [Q08605-2]
DR RefSeq; NP_996078.1; NM_206356.3. [Q08605-2]
DR RefSeq; NP_996079.1; NM_206357.3. [Q08605-2]
DR RefSeq; NP_996080.1; NM_206358.4.
DR RefSeq; NP_996081.1; NM_206359.4. [Q08605-2]
DR RefSeq; NP_996082.1; NM_206360.1.
DR PDB; 1YUI; NMR; -; A=319-372.
DR PDB; 1YUJ; NMR; -; A=319-372.
DR PDBsum; 1YUI; -.
DR PDBsum; 1YUJ; -.
DR AlphaFoldDB; Q08605; -.
DR SMR; Q08605; -.
DR BioGRID; 77830; 68.
DR IntAct; Q08605; 21.
DR STRING; 7227.FBpp0305260; -.
DR iPTMnet; Q08605; -.
DR PeptideAtlas; Q08605; -.
DR DNASU; 2768981; -.
DR EnsemblMetazoa; FBtr0075704; FBpp0089416; FBgn0013263. [Q08605-2]
DR EnsemblMetazoa; FBtr0075706; FBpp0089418; FBgn0013263. [Q08605-2]
DR EnsemblMetazoa; FBtr0075707; FBpp0089419; FBgn0013263. [Q08605-2]
DR EnsemblMetazoa; FBtr0075708; FBpp0089411; FBgn0013263. [Q08605-2]
DR EnsemblMetazoa; FBtr0100444; FBpp0099866; FBgn0013263. [Q08605-2]
DR GeneID; 2768981; -.
DR KEGG; dme:Dmel_CG33261; -.
DR CTD; 2768981; -.
DR FlyBase; FBgn0013263; Trl.
DR VEuPathDB; VectorBase:FBgn0013263; -.
DR eggNOG; ENOG502S0X1; Eukaryota.
DR InParanoid; Q08605; -.
DR SignaLink; Q08605; -.
DR BioGRID-ORCS; 2768981; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Trl; fly.
DR GenomeRNAi; 2768981; -.
DR PRO; PR:Q08605; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0013263; Expressed in thoracico-abdominal ganglion (Drosophila) and 52 other tissues.
DR ExpressionAtlas; Q08605; baseline and differential.
DR Genevisible; Q08605; DM.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0031208; F:POZ domain binding; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IMP:CAFA.
DR GO; GO:1990000; P:amyloid fibril formation; IMP:CAFA.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031497; P:chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; NAS:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:CAFA.
DR GO; GO:0007549; P:dosage compensation; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:FlyBase.
DR GO; GO:0000280; P:nuclear division; IMP:FlyBase.
DR GO; GO:0034728; P:nucleosome organization; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:1901409; P:positive regulation of phosphorylation of RNA polymerase II C-terminal domain; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035075; P:response to ecdysone; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
DR DisProt; DP00328; -.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR015318; Znf_GAGA-bd_fac.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF09237; GAGA; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cell cycle; Cell division;
KW Chromatin regulator; Developmental protein; Differentiation;
KW Direct protein sequencing; DNA-binding; Metal-binding; Mitosis; Nucleus;
KW Oogenesis; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..581
FT /note="Transcription factor GAGA"
FT /id="PRO_0000047071"
FT DOMAIN 34..99
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 343..366
FT /note="C2H2-type; degenerate"
FT REGION 201..397
FT /note="Interaction with E(bx)"
FT REGION 298..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 65..107
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_015536"
FT VAR_SEQ 378..581
FT /note="TTSGKKSSSGSSGSGSGALSSSGSVPQVQTVQSLHTLQGVQVKKDPDAQQQQ
FT QQQQQQQQQQQQAMTVSGATGGQVQQQVQQVQQQVQQQQQQQQQQQQQLQHHQIIDSSG
FT NITTATTSAQAAAAAQQQAAGQQQQLVAQSDGSESGAPLSIAQVQTLQGHQIIGNLNQV
FT NMTDFQQQQPQQQQQQQQQQQQQQQQQQQTQQTL -> SKSGNDTTLDSSMEMNTTAEG
FT DNTVGSDGAGGAGSAGGQSSGTTPTRVISNAPQAAGAPAILAQGVLPQQQQQQQLQQQH
FT QQHLTATLAGGGQAYIKHEGGGGGGTGQQQQQQAAQQQGMQNVIHIVGDQVFIPQQQQP
FT QPQ (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:7504178, ECO:0000303|PubMed:8307350,
FT ECO:0000303|PubMed:9241251"
FT /id="VSP_015537"
FT VAR_SEQ 547..581
FT /note="VNMTDFQQQQPQQQQQQQQQQQQQQQQQQQTQQTL -> GNNKNILVKKVFI
FT LKGGNNT (in isoform I)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_015538"
FT CONFLICT 23..24
FT /note="AI -> DL (in Ref. 2; AAB81113)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="V -> L (in Ref. 1; AAA16072)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="Q -> QQ (in Ref. 4; AAF49709)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="M -> I (in Ref. 4; AAF49709)"
FT /evidence="ECO:0000305"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:1YUI"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:1YUI"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:1YUI"
FT HELIX 355..365
FT /evidence="ECO:0007829|PDB:1YUI"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:1YUI"
FT CONFLICT Q08605-2:437
FT /note="A -> G (in Ref. 2; AAB81113/AAB81117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 62489 MW; 04826A1B630E3320 CRC64;
MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLL
DLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQ
TVTKDDYTTH SIQLQHMIPQ HHDQDQLIAT IATAPQQTVH AQVVEDIHHQ GQILQATTQT
NAAGQQQTIV TTDAAKHDQA VIQAFLPARK RKPRVKKMSP TAPKISKVEG MDTIMGTPTS
SHGSGSVQQV LGENGAEGQL LSSTPIIKSE GQKVETIVTM DPNNMIPVTS ANAATGEITP
AQGATGSSGG NTSGVLSTPK AKRAKHPPGT EKPRSRSQSE QPATCPICYA VIRQSRNLRR
HLELRHFAKP GVKKEKKTTS GKKSSSGSSG SGSGALSSSG SVPQVQTVQS LHTLQGVQVK
KDPDAQQQQQ QQQQQQQQQQ QAMTVSGATG GQVQQQVQQV QQQVQQQQQQ QQQQQQQLQH
HQIIDSSGNI TTATTSAQAA AAAQQQAAGQ QQQLVAQSDG SESGAPLSIA QVQTLQGHQI
IGNLNQVNMT DFQQQQPQQQ QQQQQQQQQQ QQQQQQTQQT L
