GATA1_MOUSE
ID GATA1_MOUSE Reviewed; 413 AA.
AC P17679; Q3UIH9; Q7TMX8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Erythroid transcription factor;
DE AltName: Full=Eryf1;
DE AltName: Full=GATA-binding factor 1;
DE Short=GATA-1;
DE Short=GF-1;
DE AltName: Full=NF-E1 DNA-binding protein;
GN Name=Gata1; Synonyms=Gf-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Erythrocyte;
RX PubMed=2725678; DOI=10.1038/339446a0;
RA Tsai S.-F., Martin D.I.K., Zon L.I., D'Andrea A.D., Wong G.W., Orkin S.H.;
RT "Cloning of cDNA for the major DNA-binding protein of the erythroid lineage
RT through expression in mammalian cells.";
RL Nature 339:446-451(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
RC STRAIN=BALB/cJ;
RA Todokoro K., Chiba T., Kuramochi S., Ikawa Y.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PARTIAL PROTEIN SEQUENCE, INTERACTION WITH BRD3, ACETYLATION AT LYS-308;
RP LYS-312; LYS-314 AND LYS-315, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21536911; DOI=10.1073/pnas.1102140108;
RA Lamonica J.M., Deng W., Kadauke S., Campbell A.E., Gamsjaeger R., Wang H.,
RA Cheng Y., Billin A.N., Hardison R.C., Mackay J.P., Blobel G.A.;
RT "Bromodomain protein Brd3 associates with acetylated GATA1 to promote its
RT chromatin occupancy at erythroid target genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E159-E168(2011).
RN [8]
RP FUNCTION OF ZINC-FINGERS, AND MUTAGENESIS OF CYS-207; LEU-230; CYS-261 AND
RP LEU-284.
RX PubMed=2276623; DOI=10.1101/gad.4.11.1886;
RA Martin D.I.K., Orkin S.H.;
RT "Transcriptional activation and DNA binding by the erythroid factor GF-
RT 1/NF-E1/Eryf 1.";
RL Genes Dev. 4:1886-1898(1990).
RN [9]
RP PHOSPHORYLATION AT SER-26; SER-49; SER-72; SER-142; SER-178; SER-187 AND
RP SER-310, FUNCTION, AND MUTAGENESIS OF SER-26; SER-49; SER-72; SER-142;
RP SER-178; SER-187 AND SER-310.
RX PubMed=8206977; DOI=10.1016/s0021-9258(19)89430-9;
RA Crossley M., Orkin S.H.;
RT "Phosphorylation of the erythroid transcription factor GATA-1.";
RL J. Biol. Chem. 269:16589-16596(1994).
RN [10]
RP ALTERNATIVE INITIATION (ISOFORM 2), FUNCTION, SUBUNIT, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=8524811; DOI=10.1073/pnas.92.25.11598;
RA Calligaris R., Bottardi S., Cogoi S., Apezteguia I., Santoro C.;
RT "Alternative translation initiation site usage results in two functionally
RT distinct forms of the GATA-1 transcription factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11598-11602(1995).
RN [11]
RP MUTAGENESIS OF GLU-203; CYS-204; VAL-205; CYS-207; GLY-208; ASP-218;
RP HIS-222; LEU-224; CYS-225; CYS-228 AND LYS-233.
RX PubMed=10078204; DOI=10.1016/s1097-2765(00)80312-3;
RA Crispino J.D., Lodish M.B., MacKay J.P., Orkin S.H.;
RT "Use of altered specificity mutants to probe a specific protein-protein
RT interaction in differentiation: the GATA-1:FOG complex.";
RL Mol. Cell 3:219-228(1999).
RN [12]
RP INTERACTION WITH CREBBP, ACETYLATION AT LYS-246; LYS-252 AND LYS-312, AND
RP MUTAGENESIS OF 245-LYS-LYS-246 AND 312-LYS--LYS-316.
RX PubMed=10207073; DOI=10.1128/mcb.19.5.3496;
RA Hung H.L., Lau J., Kim A.Y., Weiss M.J., Blobel G.A.;
RT "CREB-Binding protein acetylates hematopoietic transcription factor GATA-1
RT at functionally important sites.";
RL Mol. Cell. Biol. 19:3496-3505(1999).
RN [13]
RP SUMOYLATION AT LYS-137, INTERACTION WITH PIAS4, FUNCTION, AND MUTAGENESIS
RP OF LYS-137.
RX PubMed=15173587; DOI=10.1073/pnas.0308605101;
RA Collavin L., Gostissa M., Avolio F., Secco P., Ronchi A., Santoro C.,
RA Del Sal G.;
RT "Modification of the erythroid transcription factor GATA-1 by SUMO-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8870-8875(2004).
RN [14]
RP INTERACTION WITH GFI1B.
RX PubMed=15920471; DOI=10.1038/sj.emboj.7600702;
RA Rodriguez P., Bonte E., Krijgsveld J., Kolodziej K.E., Guyot B.,
RA Heck A.J.R., Vyas P., de Boer E., Grosveld F., Strouboulis J.;
RT "GATA-1 forms distinct activating and repressive complexes in erythroid
RT cells.";
RL EMBO J. 24:2354-2366(2005).
RN [15]
RP INTERACTION WITH LMCD1.
RX PubMed=16199866; DOI=10.1128/mcb.25.20.8864-8873.2005;
RA Rath N., Wang Z., Lu M.M., Morrisey E.E.;
RT "LMCD1/Dyxin is a novel transcriptional cofactor that restricts GATA6
RT function by inhibiting DNA binding.";
RL Mol. Cell. Biol. 25:8864-8873(2005).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 245-LYS-LYS-246 AND
RP 312-LYS--LYS-316.
RX PubMed=16888089; DOI=10.1182/blood-2006-07-032847;
RA Lamonica J.M., Vakoc C.R., Blobel G.A.;
RT "Acetylation of GATA-1 is required for chromatin occupancy.";
RL Blood 108:3736-3738(2006).
RN [17]
RP INTERACTION WITH MED1; CCAR1 AND CALCOCO1.
RX PubMed=24245781; DOI=10.1111/gtc.12104;
RA Mizuta S., Minami T., Fujita H., Kaminaga C., Matsui K., Ishino R.,
RA Fujita A., Oda K., Kawai A., Hasegawa N., Urahama N., Roeder R.G., Ito M.;
RT "CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel
RT pathway for GATA1 function.";
RL Genes Cells 19:28-51(2014).
RN [18]
RP STRUCTURE BY NMR OF 200-243.
RX PubMed=10212985; DOI=10.1023/a:1008309602929;
RA Kowalski K., Czolij R., King G.F., Crossley M., Mackay J.P.;
RT "The solution structure of the N-terminal zinc finger of GATA-1 reveals a
RT specific binding face for the transcriptional co-factor FOG.";
RL J. Biomol. NMR 13:249-262(1999).
RN [19]
RP STRUCTURE BY NMR OF 308-320 IN COMPLEX WITH BRD3, AND INTERACTION WITH
RP BRD3.
RX PubMed=21555453; DOI=10.1128/mcb.05413-11;
RA Gamsjaeger R., Webb S.R., Lamonica J.M., Billin A., Blobel G.A.,
RA Mackay J.P.;
RT "Structural basis and specificity of acetylated transcription factor GATA1
RT recognition by BET family bromodomain protein Brd3.";
RL Mol. Cell. Biol. 31:2632-2640(2011).
CC -!- FUNCTION: Transcriptional activator or repressor which probably serves
CC as a general switch factor for erythroid development. It binds to DNA
CC sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory
CC regions of globin genes and of other genes expressed in erythroid
CC cells. Activates the transcription of genes involved in erythroid
CC differentiation of K562 erythroleukemia cells, including HBB, HBG1/2,
CC ALAS2 and HMBS (By similarity). {ECO:0000250|UniProtKB:P15976,
CC ECO:0000269|PubMed:15173587, ECO:0000269|PubMed:16888089,
CC ECO:0000269|PubMed:2276623, ECO:0000269|PubMed:8206977,
CC ECO:0000269|PubMed:8524811}.
CC -!- SUBUNIT: May form homodimers or heterodimers with other isoforms.
CC Interacts (via the N-terminal zinc finger) with ZFPM1 (By similarity).
CC Interacts with GFI1B. Interacts with PIAS4; the interaction enhances
CC sumoylation and represses the transactivational activity in a
CC sumoylation-independent manner. Interacts with LMCD1. Interacts with
CC CREBBP; the interaction stimulates acetylation and transcriptional
CC activity in vivo. Interacts with BRD3. Interacts with MED1, CCAR1 and
CC CALCOCO1. Interacts with EP300 (By similarity). Interacts with CEBPE
CC (By similarity). {ECO:0000250|UniProtKB:P15976,
CC ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:15173587,
CC ECO:0000269|PubMed:15920471, ECO:0000269|PubMed:16199866,
CC ECO:0000269|PubMed:21536911, ECO:0000269|PubMed:21555453,
CC ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:8524811}.
CC -!- INTERACTION:
CC P17679; P25801: Lmo2; NbExp=5; IntAct=EBI-3903251, EBI-3903256;
CC P17679; P13405: Rb1; NbExp=3; IntAct=EBI-3903251, EBI-971782;
CC P17679; P22091: Tal1; NbExp=2; IntAct=EBI-3903251, EBI-8006437;
CC P17679; O35615: Zfpm1; NbExp=7; IntAct=EBI-3903251, EBI-4394596;
CC P17679; Q9VPQ6: ush; Xeno; NbExp=2; IntAct=EBI-3903251, EBI-110692;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16888089}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P17679-1; Sequence=Displayed;
CC Name=2; Synonyms=GATA-1s;
CC IsoId=P17679-2; Sequence=VSP_041452;
CC -!- TISSUE SPECIFICITY: Erythrocytes. Expressed (at protein level) in
CC liver. {ECO:0000269|PubMed:2725678, ECO:0000269|PubMed:8524811}.
CC -!- DEVELOPMENTAL STAGE: Detected at 11.5-day fetal livers (at protein
CC level). Isoform 2 detected earlier at 8.5-day embryo.
CC {ECO:0000269|PubMed:8524811}.
CC -!- DOMAIN: The two fingers are functionally distinct and cooperate to
CC achieve specific, stable DNA binding. The first finger is necessary
CC only for full specificity and stability of binding, whereas the second
CC one is required for binding.
CC -!- PTM: Highly phosphorylated on serine residues. Phosphorylation on Ser-
CC 310 is enhanced on erythroid differentiation. Phosphorylation on Ser-
CC 142 promotes sumoylation on Lys-137 (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142
CC and by interaction with PIAS4. Sumoylation with SUMO1 has no effect on
CC transcriptional activity. {ECO:0000269|PubMed:15173587,
CC ECO:0000269|PubMed:8206977}.
CC -!- PTM: Acetylated on Lys-233, Lys-245 Lys-246 by EP300 (By similarity).
CC Acetylated on Lys-246, Lys-252 and Lys-312 by CREBBP in vitro.
CC Acetylation does not affect DNA-binding in vitro but is essential to
CC induce erythroid differentiation and for binding chromatin in vivo.
CC {ECO:0000250, ECO:0000269|PubMed:10207073,
CC ECO:0000269|PubMed:21536911}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 84 of isoform 1. Less effective than isoform 1 in its ability to
CC transactivate target genes. {ECO:0000305}.
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DR EMBL; X15763; CAA33769.1; -; mRNA.
DR EMBL; AK146915; BAE27527.1; -; mRNA.
DR EMBL; AL670169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466638; EDL33938.1; -; Genomic_DNA.
DR EMBL; X57530; CAA40751.1; -; Genomic_DNA.
DR EMBL; BC052653; AAH52653.1; -; mRNA.
DR CCDS; CCDS29981.1; -. [P17679-1]
DR PIR; S04655; S04655.
DR RefSeq; NP_032115.1; NM_008089.2. [P17679-1]
DR RefSeq; XP_011245750.1; XM_011247448.2. [P17679-1]
DR PDB; 1GNF; NMR; -; A=200-243.
DR PDB; 1Y0J; NMR; -; A=200-243.
DR PDB; 2L5E; NMR; -; B=308-320.
DR PDB; 2L6Y; NMR; -; A=200-238.
DR PDB; 2L6Z; NMR; -; A=200-238.
DR PDB; 3VD6; X-ray; 1.98 A; C=200-318.
DR PDB; 3VEK; X-ray; 2.63 A; C/F=200-318.
DR PDBsum; 1GNF; -.
DR PDBsum; 1Y0J; -.
DR PDBsum; 2L5E; -.
DR PDBsum; 2L6Y; -.
DR PDBsum; 2L6Z; -.
DR PDBsum; 3VD6; -.
DR PDBsum; 3VEK; -.
DR AlphaFoldDB; P17679; -.
DR SMR; P17679; -.
DR BioGRID; 199838; 23.
DR CORUM; P17679; -.
DR DIP; DIP-40883N; -.
DR IntAct; P17679; 10.
DR MINT; P17679; -.
DR STRING; 10090.ENSMUSP00000033502; -.
DR iPTMnet; P17679; -.
DR PhosphoSitePlus; P17679; -.
DR PaxDb; P17679; -.
DR PRIDE; P17679; -.
DR ProteomicsDB; 267766; -. [P17679-1]
DR ProteomicsDB; 267767; -. [P17679-2]
DR ABCD; P17679; 35 sequenced antibodies.
DR Antibodypedia; 372; 993 antibodies from 48 providers.
DR DNASU; 14460; -.
DR Ensembl; ENSMUST00000033502; ENSMUSP00000033502; ENSMUSG00000031162. [P17679-1]
DR GeneID; 14460; -.
DR KEGG; mmu:14460; -.
DR UCSC; uc009snl.2; mouse. [P17679-1]
DR CTD; 2623; -.
DR MGI; MGI:95661; Gata1.
DR VEuPathDB; HostDB:ENSMUSG00000031162; -.
DR eggNOG; KOG1601; Eukaryota.
DR GeneTree; ENSGT00940000161156; -.
DR HOGENOM; CLU_027524_1_1_1; -.
DR InParanoid; P17679; -.
DR OMA; YSKTGLY; -.
DR OrthoDB; 807790at2759; -.
DR PhylomeDB; P17679; -.
DR TreeFam; TF315391; -.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 14460; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Gata1; mouse.
DR EvolutionaryTrace; P17679; -.
DR PRO; PR:P17679; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P17679; protein.
DR Bgee; ENSMUSG00000031162; Expressed in fetal liver hematopoietic progenitor cell and 89 other tissues.
DR ExpressionAtlas; P17679; baseline and differential.
DR Genevisible; P17679; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0002039; F:p53 binding; IPI:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:BHF-UCL.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031100; P:animal organ regeneration; ISO:MGI.
DR GO; GO:0030221; P:basophil differentiation; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0048468; P:cell development; IMP:MGI.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IMP:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:MGI.
DR GO; GO:0097028; P:dendritic cell differentiation; IDA:MGI.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR GO; GO:0035854; P:eosinophil fate commitment; ISO:MGI.
DR GO; GO:0048821; P:erythrocyte development; ISO:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IDA:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IGI:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; ISO:MGI.
DR GO; GO:0030219; P:megakaryocyte differentiation; IDA:MGI.
DR GO; GO:0033028; P:myeloid cell apoptotic process; IMP:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; ISO:MGI.
DR GO; GO:0033687; P:osteoblast proliferation; IMP:MGI.
DR GO; GO:0070527; P:platelet aggregation; IMP:BHF-UCL.
DR GO; GO:0030220; P:platelet formation; IMP:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:MGI.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; ISO:MGI.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; IMP:MGI.
DR GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; IDA:BHF-UCL.
DR GO; GO:0010559; P:regulation of glycoprotein biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0010725; P:regulation of primitive erythrocyte differentiation; IGI:MGI.
DR GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR IDEAL; IID50040; -.
DR InterPro; IPR029524; GATA-1.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 1.
DR PANTHER; PTHR10071:SF190; PTHR10071:SF190; 1.
DR Pfam; PF00320; GATA; 2.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00401; ZnF_GATA; 2.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative initiation;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..413
FT /note="Erythroid transcription factor"
FT /id="PRO_0000083398"
FT ZN_FING 204..228
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 258..282
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 29..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..330
FT /note="Interaction with MED1 and CCAR1"
FT /evidence="ECO:0000269|PubMed:24245781"
FT REGION 203..222
FT /note="Required for interaction with ZFPM1"
FT /evidence="ECO:0000250"
FT REGION 249..315
FT /note="Interaction with CALCOCO1"
FT /evidence="ECO:0000269|PubMed:24245781"
FT REGION 297..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8206977"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8206977"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8206977"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8206977"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8206977"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8206977"
FT MOD_RES 233
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:P15976"
FT MOD_RES 245
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:P15976"
FT MOD_RES 246
FT /note="N6-acetyllysine; by CREBBP"
FT /evidence="ECO:0000269|PubMed:10207073"
FT MOD_RES 246
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250"
FT MOD_RES 252
FT /note="N6-acetyllysine; by CREBBP"
FT /evidence="ECO:0000269|PubMed:10207073"
FT MOD_RES 308
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21536911"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8206977"
FT MOD_RES 312
FT /note="N6-acetyllysine; by CREBBP"
FT /evidence="ECO:0000269|PubMed:10207073,
FT ECO:0000269|PubMed:21536911"
FT MOD_RES 314
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21536911"
FT MOD_RES 315
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21536911"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15173587"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041452"
FT MUTAGEN 26
FT /note="S->A: Loss of phosphorylation of the chymotryptic
FT peptide."
FT /evidence="ECO:0000269|PubMed:8206977"
FT MUTAGEN 49
FT /note="S->A: Loss of phosphorylation of the chymotryptic
FT peptide."
FT /evidence="ECO:0000269|PubMed:8206977"
FT MUTAGEN 72
FT /note="S->A: Loss of phosphorylation of the chymotryptic
FT peptide."
FT /evidence="ECO:0000269|PubMed:8206977"
FT MUTAGEN 137
FT /note="K->R: Abolishes sumoylation. No change in PIAS4
FT binding nor on transcriptional activity."
FT /evidence="ECO:0000269|PubMed:15173587"
FT MUTAGEN 142
FT /note="S->A: Loss of phosphorylation of the chymotryptic
FT peptide."
FT /evidence="ECO:0000269|PubMed:8206977"
FT MUTAGEN 178
FT /note="S->A: Loss of phosphorylation of the chymotryptic
FT peptide."
FT /evidence="ECO:0000269|PubMed:8206977"
FT MUTAGEN 187
FT /note="S->A: Loss of phosphorylation of the chymotryptic
FT peptide."
FT /evidence="ECO:0000269|PubMed:8206977"
FT MUTAGEN 203
FT /note="E->V: Disrupts interaction with ZFPM1. Binds
FT normally to DNA."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 204
FT /note="C->R: Disrupts interaction with ZFPM1 and binding to
FT DNA."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 205
FT /note="V->G: Disrupts interaction with ZFPM1. Binds
FT normally to DNA."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 205
FT /note="V->M: Disrupts interaction with ZFPM1. Binds
FT normally to DNA."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 207
FT /note="C->G,R,W: Disrupts interaction with ZFPM1."
FT /evidence="ECO:0000269|PubMed:10078204,
FT ECO:0000269|PubMed:2276623"
FT MUTAGEN 207
FT /note="C->P: Stability of binding to DNA reduced."
FT /evidence="ECO:0000269|PubMed:10078204,
FT ECO:0000269|PubMed:2276623"
FT MUTAGEN 208
FT /note="G->E,V: Disrupts interaction with ZFPM1 and binding
FT to DNA."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 218
FT /note="D->G,V: No effect on interaction with ZFPM1."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 222
FT /note="H->R: Disrupts interaction with ZFPM1. Binds
FT normally to DNA."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 224
FT /note="L->P: Disrupts interaction with ZFPM1 and binding to
FT DNA."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 225
FT /note="C->R,S,Y: Disrupts interaction with ZFPM1."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 228
FT /note="C->R,S: Disrupts interaction with ZFPM1."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 230
FT /note="L->F: Stability of binding to DNA reduced."
FT /evidence="ECO:0000269|PubMed:2276623"
FT MUTAGEN 233
FT /note="K->E: No effect on interaction with ZFPM1."
FT /evidence="ECO:0000269|PubMed:10078204"
FT MUTAGEN 245..246
FT /note="KK->AA: No effect on DNA binding. Reduces
FT acetylation. Reduces ability to induce erythroid
FT differentiation. Abrogates acetylation; when associated
FT with 312-A--A-316. Abrogates ability to induce erythroid
FT differentiation; when associated with 312-A--A-316. Reduces
FT binding to CREBBP; when associated with 312-A--A-316.
FT Disrupts stable association with chromatin; when associated
FT with 312-A--A-316."
FT /evidence="ECO:0000269|PubMed:10207073,
FT ECO:0000269|PubMed:16888089"
FT MUTAGEN 245..246
FT /note="KK->RR: No effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:10207073,
FT ECO:0000269|PubMed:16888089"
FT MUTAGEN 261
FT /note="C->P: Abolishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:2276623"
FT MUTAGEN 284
FT /note="L->F: Binds to DNA with reduced affinity."
FT /evidence="ECO:0000269|PubMed:2276623"
FT MUTAGEN 310
FT /note="S->A: Loss of phosphorylation of the chymotryptic
FT peptide."
FT /evidence="ECO:0000269|PubMed:8206977"
FT MUTAGEN 312..316
FT /note="KGKKK->AGAAA: No effect on DNA binding. Reduces
FT acetylation. Reduces binding to CREBBP. Reduces ability to
FT induce erythroid differentiation. Abrogates acetylation;
FT when associated with 245-A-A-246. Abrogates ability to
FT induce erythroid differentiation; when associated with 245-
FT A-A-246. Reduces binding to CREBBP; when associated with
FT 245-A-A-246. Disrupts stable association with chromatin;
FT when associated with 245-A-A-246."
FT /evidence="ECO:0000269|PubMed:10207073,
FT ECO:0000269|PubMed:16888089"
FT MUTAGEN 312..316
FT /note="KGKKK->RGRRR: No effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:10207073,
FT ECO:0000269|PubMed:16888089"
FT CONFLICT 29
FT /note="D -> G (in Ref. 5; AAH52653)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="N -> S (in Ref. 5; AAH52653)"
FT /evidence="ECO:0000305"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3VD6"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:3VD6"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:3VD6"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:3VD6"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:3VD6"
SQ SEQUENCE 413 AA; 42674 MW; BB627A92700D557A CRC64;
MDFPGLGALG TSEPLPQFVD SALVSSPSDS TGFFSSGPEG LDAASSSTSP NAATAAASAL
AYYREAEAYR HSPVFQVYPL LNSMEGIPGG SPYASWAYGK TALYPASTVC PSHEDAPSQA
LEDQEGKSNN TFLDTLKTER LSPDLLTLGT ALPASLPVTG SAYGGADFPS PFFSPTGSPL
SSAAYSSPKF HGSLPLAPCE ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP
LIRPKKRMIV SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYFKLHQ VNRPLTMRKD
GIQTRNRKAS GKGKKKRGSN LAGAGAAEGP AGGFMVVAGS SSSGNCGEVA SGLALGTAGT
AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TTSFPTGPAP TTSSTSVIAP LSS
