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 14-OCT-2015, entry version 155. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Orkin S.H.; RT "Cloning of cDNA for the major DNA-binding protein of the erythroid RT lineage 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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 RT project: 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/c; 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 RP LYS-308; LYS-312; LYS-314 AND LYS-315, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=21536911; DOI=10.1073/pnas.1102140108; RA Lamonica J.M., Deng W., Kadauke S., Campbell A.E., Gamsjaeger R., RA Wang H., Cheng Y., Billin A.N., Hardison R.C., Mackay J.P., RA Blobel G.A.; RT "Bromodomain protein Brd3 associates with acetylated GATA1 to promote RT its 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 RP AND 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 RT GF-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 RP AND SER-310, FUNCTION, AND MUTAGENESIS OF SER-26; SER-49; SER-72; RP SER-142; SER-178; SER-187 AND SER-310. RX PubMed=8206977; 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 RP SPECIFICITY, 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 RT functionally 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- RT protein 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, RP AND MUTAGENESIS OF 245-LYS-LYS-246 AND 312-LYS--LYS-316. RX PubMed=10207073; RA Hung H.L., Lau J., Kim A.Y., Weiss M.J., Blobel G.A.; RT "CREB-Binding protein acetylates hematopoietic transcription factor RT GATA-1 at functionally important sites."; RL Mol. Cell. Biol. 19:3496-3505(1999). RN [13] RP SUMOYLATION AT LYS-137, INTERACTION WITH PIAS4, FUNCTION, AND RP MUTAGENESIS 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- RT 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 RT erythroid 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., RA 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 RT reveals a specific binding face for the transcriptional co-factor RT 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 RT GATA1 recognition by BET family bromodomain protein Brd3."; RL Mol. Cell. Biol. 31:2632-2640(2011). CC -!- FUNCTION: Transcriptional activator or repressor which probably CC serves as a general switch factor for erythroid development. It CC binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' CC within regulatory regions of globin genes and of other genes CC expressed in erythroid cells. Activates the transcription of genes CC involved in erythroid differentiation of K562 erythroleukemia CC cells, including HBB, HBG1/2, ALAS2 and HMBS (By similarity). CC {ECO:0000250|UniProtKB:P15976, ECO:0000269|PubMed:15173587, CC ECO:0000269|PubMed:16888089, ECO:0000269|PubMed:2276623, CC ECO:0000269|PubMed:8206977, 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 CC similarity). Interacts with GFI1B. Interacts with PIAS4; the CC interaction enhances sumoylation and represses the CC transactivational activity in a sumoylation-independent manner. CC Interacts with LMCD1. Interacts with CREBBP; the interaction CC stimulates acetylation and transcriptional activity in vivo. CC Interacts with BRD3. Interacts with MED1, CCAR1 and CALCOCO1. CC {ECO:0000250|UniProtKB:P15976, ECO:0000269|PubMed:10207073, CC ECO:0000269|PubMed:15173587, ECO:0000269|PubMed:15920471, CC ECO:0000269|PubMed:16199866, ECO:0000269|PubMed:21536911, CC ECO:0000269|PubMed:21555453, ECO:0000269|PubMed:24245781, CC ECO:0000269|PubMed:8524811}. CC -!- INTERACTION: CC P25801:Lmo2; NbExp=5; IntAct=EBI-3903251, EBI-3903256; 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 Note=Produced by alternative initiation at Met-84 of isoform 1. CC Less effective than isoform 1 in its ability to transactivate CC target genes.; 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 CC necessary only for full specificity and stability of binding, CC whereas the second one is required for binding. CC -!- PTM: Highly phosphorylated on serine residues. Phosphorylation on CC Ser-310 is enhanced on erythroid differentiation. Phosphorylation CC on Ser-142 promotes sumoylation on Lys-137 (By similarity). CC {ECO:0000250}. CC -!- PTM: Sumoylation on Lys-137 is enhanced by phosphorylation on Ser- CC 142 and by interaction with PIAS4. Sumoylation with SUMO1 has no CC effect on transcriptional activity. {ECO:0000269|PubMed:15173587, CC ECO:0000269|PubMed:8206977}. CC -!- PTM: Acetylated on Lys-233, Lys-245 Lys-246 by EP300 (By CC similarity). Acetylated on Lys-246, Lys-252 and Lys-312 by CREBBP CC in vitro. Acetylation does not affect DNA-binding in vitro but is CC essential to induce erythroid differentiation and for binding CC chromatin in vivo. {ECO:0000250, ECO:0000269|PubMed:10207073, CC ECO:0000269|PubMed:21536911}. CC -!- SIMILARITY: Contains 2 GATA-type zinc fingers. CC {ECO:0000255|PROSITE-ProRule:PRU00094}. 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; X15763; CAA33769.1; -; mRNA. DR EMBL; AK146915; BAE27527.1; -; mRNA. DR EMBL; AL670169; CAM17247.1; -; 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_011247448.1. [P17679-1] DR UniGene; Mm.335973; -. 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 ProteinModelPortal; P17679; -. DR SMR; P17679; 200-310. DR BioGrid; 199838; 23. DR DIP; DIP-40883N; -. DR IntAct; P17679; 5. DR MINT; MINT-94735; -. DR STRING; 10090.ENSMUSP00000033502; -. DR PhosphoSite; P17679; -. DR PRIDE; P17679; -. 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 eggNOG; COG5641; -. DR GeneTree; ENSGT00760000119221; -. DR HOGENOM; HOG000047701; -. DR HOVERGEN; HBG051705; -. DR InParanoid; P17679; -. DR KO; K09182; -. DR OMA; TPCEARE; -. DR OrthoDB; EOG7CCBRF; -. DR PhylomeDB; P17679; -. DR TreeFam; TF315391; -. DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production. DR EvolutionaryTrace; P17679; -. DR NextBio; 286092; -. DR PRO; PR:P17679; -. DR Proteomes; UP000000589; Chromosome X. DR Bgee; P17679; -. DR CleanEx; MM_GATA1; -. DR ExpressionAtlas; P17679; baseline and differential. DR Genevisible; P17679; MM. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005667; C:transcription factor complex; ISO:MGI. DR GO; GO:0017053; C:transcriptional 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:0001047; F:core promoter binding; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0008301; F:DNA binding, bending; IDA:MGI. DR GO; GO:0001158; F:enhancer sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0002039; F:p53 binding; IPI:MGI. DR GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI. DR GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:MGI. DR GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI. DR GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:MGI. DR GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030221; P:basophil differentiation; IEA:Ensembl. DR GO; GO:0048468; P:cell development; IMP:MGI. DR GO; GO:0007267; P:cell-cell signaling; IMP: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; IMP:BHF-UCL. 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:0030099; P:myeloid cell differentiation; IMP:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI. DR GO; GO:0030502; P:negative regulation of bone mineralization; IMP:MGI. DR GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI. DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI. DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; ISO:MGI. DR GO; GO:0070527; P:platelet aggregation; IMP:BHF-UCL. DR GO; GO:0030220; P:platelet formation; IMP:MGI. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; 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 from RNA polymerase II promoter; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB. 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:0006366; P:transcription from RNA polymerase II promoter; ISO:MGI. DR GO; GO:0071733; P:transcriptional activation by promoter-enhancer looping; IDA:BHF-UCL. DR Gene3D; 3.30.50.10; -; 2. DR InterPro; IPR029524; GATA-1. DR InterPro; IPR000679; Znf_GATA. DR InterPro; IPR013088; Znf_NHR/GATA. DR PANTHER; PTHR10071:SF150; PTHR10071:SF150; 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 Complete proteome; Direct protein sequencing; DNA-binding; KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1 413 Erythroid transcription factor. FT /FTId=PRO_0000083398. FT ZN_FING 204 228 GATA-type 1. {ECO:0000255|PROSITE- FT ProRule:PRU00094}. FT ZN_FING 258 282 GATA-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU00094}. FT REGION 200 330 Interaction with MED1 and CCAR1. FT {ECO:0000269|PubMed:24245781}. FT REGION 203 222 Required for interaction with ZFPM1. FT {ECO:0000250}. FT REGION 249 315 Interaction with CALCOCO1. FT {ECO:0000269|PubMed:24245781}. FT MOD_RES 26 26 Phosphoserine. FT {ECO:0000269|PubMed:8206977}. FT MOD_RES 49 49 Phosphoserine. FT {ECO:0000269|PubMed:8206977}. FT MOD_RES 72 72 Phosphoserine. FT {ECO:0000269|PubMed:8206977}. FT MOD_RES 142 142 Phosphoserine. FT {ECO:0000269|PubMed:8206977}. FT MOD_RES 178 178 Phosphoserine. FT {ECO:0000269|PubMed:8206977}. FT MOD_RES 187 187 Phosphoserine. FT {ECO:0000269|PubMed:8206977}. FT MOD_RES 233 233 N6-acetyllysine; by EP300. {ECO:0000250}. FT MOD_RES 245 245 N6-acetyllysine; by EP300. {ECO:0000250}. FT MOD_RES 246 246 N6-acetyllysine; by CREBBP. FT {ECO:0000269|PubMed:10207073}. FT MOD_RES 246 246 N6-acetyllysine; by EP300. {ECO:0000250}. FT MOD_RES 252 252 N6-acetyllysine; by CREBBP. FT {ECO:0000269|PubMed:10207073}. FT MOD_RES 308 308 N6-acetyllysine. FT {ECO:0000269|PubMed:21536911}. FT MOD_RES 310 310 Phosphoserine. FT {ECO:0000269|PubMed:8206977}. FT MOD_RES 312 312 N6-acetyllysine; by CREBBP. FT {ECO:0000269|PubMed:10207073, FT ECO:0000269|PubMed:21536911}. FT MOD_RES 314 314 N6-acetyllysine. FT {ECO:0000269|PubMed:21536911}. FT MOD_RES 315 315 N6-acetyllysine. FT {ECO:0000269|PubMed:21536911}. FT CROSSLNK 137 137 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT VAR_SEQ 1 83 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_041452. FT MUTAGEN 26 26 S->A: Loss of phosphorylation of the FT chymotryptic peptide. FT {ECO:0000269|PubMed:8206977}. FT MUTAGEN 49 49 S->A: Loss of phosphorylation of the FT chymotryptic peptide. FT {ECO:0000269|PubMed:8206977}. FT MUTAGEN 72 72 S->A: Loss of phosphorylation of the FT chymotryptic peptide. FT {ECO:0000269|PubMed:8206977}. FT MUTAGEN 137 137 K->R: Abolishes sumoylation. No change in FT PIAS4 binding nor on transcriptional FT activity. {ECO:0000269|PubMed:15173587}. FT MUTAGEN 142 142 S->A: Loss of phosphorylation of the FT chymotryptic peptide. FT {ECO:0000269|PubMed:8206977}. FT MUTAGEN 178 178 S->A: Loss of phosphorylation of the FT chymotryptic peptide. FT {ECO:0000269|PubMed:8206977}. FT MUTAGEN 187 187 S->A: Loss of phosphorylation of the FT chymotryptic peptide. FT {ECO:0000269|PubMed:8206977}. FT MUTAGEN 203 203 E->V: Disrupts interaction with ZFPM1. FT Binds normally to DNA. FT {ECO:0000269|PubMed:10078204}. FT MUTAGEN 204 204 C->R: Disrupts interaction with ZFPM1 and FT binding to DNA. FT {ECO:0000269|PubMed:10078204}. FT MUTAGEN 205 205 V->G: Disrupts interaction with ZFPM1. FT Binds normally to DNA. FT {ECO:0000269|PubMed:10078204}. FT MUTAGEN 205 205 V->M: Disrupts interaction with ZFPM1. FT Binds normally to DNA. FT {ECO:0000269|PubMed:10078204}. FT MUTAGEN 207 207 C->G,R,W: Disrupts interaction with FT ZFPM1. {ECO:0000269|PubMed:10078204, FT ECO:0000269|PubMed:2276623}. FT MUTAGEN 207 207 C->P: Stability of binding to DNA FT reduced. {ECO:0000269|PubMed:10078204, FT ECO:0000269|PubMed:2276623}. FT MUTAGEN 208 208 G->E,V: Disrupts interaction with ZFPM1 FT and binding to DNA. FT {ECO:0000269|PubMed:10078204}. FT MUTAGEN 218 218 D->G,V: No effect on interaction with FT ZFPM1. {ECO:0000269|PubMed:10078204}. FT MUTAGEN 222 222 H->R: Disrupts interaction with ZFPM1. FT Binds normally to DNA. FT {ECO:0000269|PubMed:10078204}. FT MUTAGEN 224 224 L->P: Disrupts interaction with ZFPM1 and FT binding to DNA. FT {ECO:0000269|PubMed:10078204}. FT MUTAGEN 225 225 C->R,S,Y: Disrupts interaction with FT ZFPM1. {ECO:0000269|PubMed:10078204}. FT MUTAGEN 228 228 C->R,S: Disrupts interaction with ZFPM1. FT {ECO:0000269|PubMed:10078204}. FT MUTAGEN 230 230 L->F: Stability of binding to DNA FT reduced. {ECO:0000269|PubMed:2276623}. FT MUTAGEN 233 233 K->E: No effect on interaction with FT ZFPM1. {ECO:0000269|PubMed:10078204}. FT MUTAGEN 245 246 KK->AA: No effect on DNA binding. Reduces FT acetylation. Reduces ability to induce FT erythroid differentiation. Abrogates FT acetylation; when associated with 312-A-- FT A-316. Abrogates ability to induce FT erythroid differentiation; when FT associated with 312-A--A-316. Reduces FT binding to CREBBP; when associated with FT 312-A--A-316. Disrupts stable association FT with chromatin; when associated with 312- FT A--A-316. {ECO:0000269|PubMed:10207073, FT ECO:0000269|PubMed:16888089}. FT MUTAGEN 245 246 KK->RR: No effect on DNA binding. FT {ECO:0000269|PubMed:10207073, FT ECO:0000269|PubMed:16888089}. FT MUTAGEN 261 261 C->P: Abolishes DNA-binding. FT {ECO:0000269|PubMed:2276623}. FT MUTAGEN 284 284 L->F: Binds to DNA with reduced affinity. FT {ECO:0000269|PubMed:2276623}. FT MUTAGEN 310 310 S->A: Loss of phosphorylation of the FT chymotryptic peptide. FT {ECO:0000269|PubMed:8206977}. FT MUTAGEN 312 316 KGKKK->AGAAA: No effect on DNA binding. FT Reduces acetylation. Reduces binding to FT CREBBP. Reduces ability to induce FT erythroid differentiation. Abrogates FT acetylation; when associated with 245-A- FT A-246. Abrogates ability to induce FT erythroid differentiation; when FT associated with 245-A-A-246. Reduces FT binding to CREBBP; when associated with FT 245-A-A-246. Disrupts stable association FT with chromatin; when associated with 245- FT A-A-246. {ECO:0000269|PubMed:10207073, FT ECO:0000269|PubMed:16888089}. FT MUTAGEN 312 316 KGKKK->RGRRR: No effect on DNA binding. FT {ECO:0000269|PubMed:10207073, FT ECO:0000269|PubMed:16888089}. FT CONFLICT 29 29 D -> G (in Ref. 5; AAH52653). FT {ECO:0000305}. FT CONFLICT 129 129 N -> S (in Ref. 5; AAH52653). FT {ECO:0000305}. FT TURN 205 207 {ECO:0000244|PDB:3VD6}. FT HELIX 226 235 {ECO:0000244|PDB:3VD6}. FT TURN 259 261 {ECO:0000244|PDB:3VD6}. FT HELIX 280 289 {ECO:0000244|PDB:3VD6}. FT HELIX 295 297 {ECO:0000244|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 //