ID GATA1_HUMAN Reviewed; 413 AA. AC P15976; Q96GB8; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 11-NOV-2015, entry version 172. 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=ERYF1, GF1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=2104960; DOI=10.1038/343092a0; RA Trainor C.D., Evans T., Felsenfeld G., Boguski M.S.; RT "Structure and evolution of a human erythroid transcription factor."; RL Nature 343:92-96(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Erythrocyte; RX PubMed=2300555; DOI=10.1073/pnas.87.2.668; RA Zon L.I., Tsai S.-F., Burgess S., Matsudaira P., Bruns G.A.P., RA Orkin S.H.; RT "The major human erythroid DNA-binding protein (GF-1): primary RT sequence and localization of the gene to the X chromosome."; RL Proc. Natl. Acad. Sci. U.S.A. 87:668-672(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow; 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 [5] RP ALTERNATIVE INITIATION (ISOFORM 3), SUBUNIT, AND TISSUE SPECIFICITY. 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 [6] RP INTERACTION WITH EP300, AND ACETYLATION AT LYS-233; LYS-245 AND RP LYS-246. RX PubMed=9859997; DOI=10.1038/25166; RA Boyes J., Byfield P., Nakatani Y., Ogryzko V.; RT "Regulation of activity of the transcription factor GATA-1 by RT acetylation."; RL Nature 396:594-598(1998). RN [7] RP INVOLVEMENT IN XLAWT. RX PubMed=16783379; DOI=10.1038/ng1825; RA Hollanda L.M., Lima C.S., Cunha A.F., Albuquerque D.M., Vassallo J., RA Ozelo M.C., Joazeiro P.P., Saad S.T., Costa F.F.; RT "An inherited mutation leading to production of only the short isoform RT of GATA-1 is associated with impaired erythropoiesis."; RL Nat. Genet. 38:807-812(2006). RN [8] RP SUMOYLATION AT LYS-137, PHOSPHORYLATION AT SER-142, AND MUTAGENESIS OF RP LYS-137 AND SER-142. RX PubMed=16371476; DOI=10.1073/pnas.0503698102; RA Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J., RA Nakai A., Sistonen L.; RT "PDSM, a motif for phosphorylation-dependent SUMO modification."; RL Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006). RN [9] RP INTERACTION WITH GFI1B. RX PubMed=17420275; DOI=10.1128/MCB.02212-06; RA Kuo Y.-Y., Chang Z.-F.; RT "GATA-1 and Gfi-1B interplay to regulate Bcl-xL transcription."; RL Mol. Cell. Biol. 27:4261-4272(2007). RN [10] RP FUNCTION, AND DNA-BINDING. RX PubMed=22235304; DOI=10.1371/journal.pone.0029518; RA Zeng Y., Wang W., Ma J., Wang X., Guo M., Li W.; RT "Knockdown of ZNF268, which is transcriptionally downregulated by RT GATA-1, promotes proliferation of K562 cells."; RL PLoS ONE 7:E29518-E29518(2012). RN [11] RP FUNCTION, AND 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 [12] RP VARIANT XDAT MET-205, INTERACTION WITH ZFPM1, CHARACTERIZATION OF RP VARIANT XDAT MET-205, AND MUTAGENESIS OF CYS-204. RC TISSUE=Peripheral blood; RX PubMed=10700180; DOI=10.1038/73480; RA Nichols K.E., Crispino J.D., Poncz M., White J.G., Orkin S.H., RA Maris J.M., Weiss M.J.; RT "Familial dyserythropoietic anaemia and thrombocytopenia due to an RT inherited mutation in GATA1."; RL Nat. Genet. 24:266-270(2000). RN [13] RP VARIANT XDAT GLY-218, INTERACTION WITH ZFPM1, AND CHARACTERIZATION OF RP VARIANT XDAT GLY-218. RX PubMed=11418466; DOI=10.1182/blood.V98.1.85; RA Freson K., Devriendt K., Matthijs G., Van Hoof A., De Vos R., Thys C., RA Minner K., Hoylaerts M.F., Vermylen J., Van Geet C.; RT "Platelet characteristics in patients with X-linked RT macrothrombocytopenia because of a novel GATA1 mutation."; RL Blood 98:85-92(2001). RN [14] RP VARIANT XDAT SER-208, INTERACTION WITH ZFPM1, AND CHARACTERIZATION OF RP VARIANT XDAT SER-208. RX PubMed=11675338; DOI=10.1182/blood.V98.9.2681; RA Mehaffey M.G., Newton A.L., Gandhi M.J., Crossley M., Drachman J.G.; RT "X-linked thrombocytopenia caused by a novel mutation of GATA-1."; RL Blood 98:2681-2688(2001). RN [15] RP VARIANT XLTT GLN-216, INTERACTION WITH ZFPM1, AND CHARACTERIZATION OF RP VARIANT XLTT GLN-216. RX PubMed=12200364; DOI=10.1182/blood-2002-02-0387; RA Yu C., Niakan K.K., Matsushita M., Stamatoyannopoulos G., Orkin S.H., RA Raskind W.H.; RT "X-linked thrombocytopenia with thalassemia from a mutation in the RT amino finger of GATA-1 affecting DNA binding rather than FOG-1 RT interaction."; RL Blood 100:2040-2045(2002). RN [16] RP VARIANT XDAT TYR-218, INTERACTION WITH ZFPM1, AND CHARACTERIZATION OF RP VARIANT XDAT TYR-218. RX PubMed=11809723; DOI=10.1093/hmg/11.2.147; RA Freson K., Matthijs G., Thys C., Marieen P., Hoylaerts M.F., RA Vermylen J., Van Geet C.; RT "Different substitutions at residue D218 of the X-linked transcription RT factor GATA1 lead to altered clinical severity of RT macrothrombocytopenia and anemia and are associated with variable RT skewed X inactivation."; RL Hum. Mol. Genet. 11:147-152(2002). 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 (PubMed:24245781). CC {ECO:0000269|PubMed:22235304, ECO:0000269|PubMed:24245781}. CC -!- SUBUNIT: May form homodimers or heterodimers with other isoforms. CC Interacts (via the N-terminal zinc finger) with ZFPM1. Interacts CC 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 CC with BRD3 (By similarity). Interacts with CREBBP; the interaction CC stimulates acetylation and transcriptional activity in vivo (By CC similarity). Interacts with EP300. Interacts with MED1, CCAR1 and CC CALCOCO1. {ECO:0000250|UniProtKB:P17679, CC ECO:0000269|PubMed:10700180, ECO:0000269|PubMed:11418466, CC ECO:0000269|PubMed:11675338, ECO:0000269|PubMed:11809723, CC ECO:0000269|PubMed:12200364, ECO:0000269|PubMed:17420275, CC ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:8524811, CC ECO:0000269|PubMed:9859997}. CC -!- INTERACTION: CC Q8N4L8:CCDC24; NbExp=3; IntAct=EBI-3909284, EBI-1104933; CC Q8TES7-6:FBF1; NbExp=3; IntAct=EBI-3909284, EBI-10244131; CC O43559:FRS3; NbExp=3; IntAct=EBI-3909284, EBI-725515; CC Q96MH2:HEXIM2; NbExp=3; IntAct=EBI-3909284, EBI-5460660; CC P49639:HOXA1; NbExp=3; IntAct=EBI-3909284, EBI-740785; CC P08107:HSPA1B; NbExp=5; IntAct=EBI-3909284, EBI-629985; CC P60370:KRTAP10-5; NbExp=3; IntAct=EBI-3909284, EBI-10172150; CC Q9BYQ4:KRTAP9-2; NbExp=3; IntAct=EBI-3909284, EBI-1044640; CC O43741:PRKAB2; NbExp=3; IntAct=EBI-3909284, EBI-1053424; CC Q96JH8:RADIL; NbExp=3; IntAct=EBI-3909284, EBI-744267; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=3; CC Name=1; CC IsoId=P15976-1; Sequence=Displayed; CC Name=2; CC IsoId=P15976-2; Sequence=VSP_014782; CC Note=No experimental confirmation available.; CC Name=3; Synonyms=GATA-1s; CC IsoId=P15976-3; Sequence=VSP_041451; CC Note=Produced by alternative initiation at Met-84 of isoform 1.; CC -!- TISSUE SPECIFICITY: Erythrocytes. {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 (By similarity). CC {ECO:0000250}. 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 (By similarity). {ECO:0000250}. CC -!- PTM: Acetylated at 2 conserved lysine-rich motifs by CREBBP in CC vitro. Acetylation does not affect DNA-binding in vitro but is CC essential to induce erythroid differentiation and for binding CC chromatin in vivo (By similarity). Acetylated on Lys-233, Lys-245 CC Lys-246 by EP300. {ECO:0000250, ECO:0000269|PubMed:9859997}. CC -!- DISEASE: X-linked dyserythropoietic anemia and thrombocytopenia CC (XDAT) [MIM:300367]: Disorder characterized by erythrocytes with CC abnormal size and shape, and paucity of platelets in peripheral CC blood. The bone marrow contains abundant and abnormally small CC megakaryocytes. {ECO:0000269|PubMed:10700180, CC ECO:0000269|PubMed:11418466, ECO:0000269|PubMed:11675338, CC ECO:0000269|PubMed:11809723}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Thrombocytopenia with beta-thalassemia, X-linked (XLTT) CC [MIM:314050]: An unusual form of thrombocytopenia associated with CC beta-thalassemia. Patients have splenomegaly and petechiae, CC moderate thrombocytopenia, prolonged bleeding time due to platelet CC dysfunction, reticulocytosis and unbalanced (hemo)globin chain CC synthesis resembling that of beta-thalassemia minor. CC {ECO:0000269|PubMed:12200364}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Anemia without thrombocytopenia, X-linked (XLAWT) CC [MIM:300835]: A form of anemia characterized by abnormal CC morphology of erythrocytes and granulocytes in peripheral blood, CC bone marrow dysplasia with hypocellularity of erythroid and CC granulocytic lineages, and normal or increased number of CC megakaryocytes. Neutropenia of a variable degree is present in CC affected individuals. {ECO:0000269|PubMed:16783379}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- SIMILARITY: Contains 2 GATA-type zinc fingers. CC {ECO:0000255|PROSITE-ProRule:PRU00094}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/GATA1ID40689chXp11.html"; 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; X17254; CAA35120.1; -; mRNA. DR EMBL; M30601; AAA35885.1; -; mRNA. DR EMBL; AF196971; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009797; AAH09797.1; -; mRNA. DR CCDS; CCDS14305.1; -. [P15976-1] DR PIR; A34888; A34888. DR RefSeq; NP_002040.1; NM_002049.3. [P15976-1] DR UniGene; Hs.765; -. DR ProteinModelPortal; P15976; -. DR SMR; P15976; 200-310. DR BioGrid; 108893; 55. DR DIP; DIP-41431N; -. DR IntAct; P15976; 17. DR MINT; MINT-247486; -. DR STRING; 9606.ENSP00000365858; -. DR PhosphoSite; P15976; -. DR BioMuta; GATA1; -. DR DMDM; 120956; -. DR MaxQB; P15976; -. DR PaxDb; P15976; -. DR PRIDE; P15976; -. DR DNASU; 2623; -. DR Ensembl; ENST00000376670; ENSP00000365858; ENSG00000102145. [P15976-1] DR GeneID; 2623; -. DR KEGG; hsa:2623; -. DR UCSC; uc004dkq.4; human. [P15976-1] DR CTD; 2623; -. DR GeneCards; GATA1; -. DR GeneReviews; GATA1; -. DR HGNC; HGNC:4170; GATA1. DR HPA; CAB009195; -. DR HPA; HPA000232; -. DR HPA; HPA000233; -. DR MIM; 300367; phenotype. DR MIM; 300835; phenotype. DR MIM; 305371; gene. DR MIM; 314050; phenotype. DR neXtProt; NX_P15976; -. DR Orphanet; 86849; Acute basophilic leukemia. DR Orphanet; 231393; Beta-thalassemia - X-linked thrombocytopenia. DR Orphanet; 124; Blackfan-Diamond anemia. DR Orphanet; 79277; Congenital erythropoietic porphyria. DR Orphanet; 67044; Thrombocytopenia with congenital dyserythropoietic anemia. DR Orphanet; 363727; X-linked dyserythropoetic anemia with abnormal platelets and neutropenia. DR PharmGKB; PA28584; -. DR eggNOG; KOG1601; Eukaryota. DR eggNOG; COG5641; LUCA. DR GeneTree; ENSGT00760000119221; -. DR HOGENOM; HOG000047701; -. DR HOVERGEN; HBG051705; -. DR InParanoid; P15976; -. DR KO; K09182; -. DR OMA; TPCEARE; -. DR PhylomeDB; P15976; -. DR TreeFam; TF315391; -. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; P15976; -. DR ChiTaRS; GATA1; human. DR GeneWiki; GATA1; -. DR GenomeRNAi; 2623; -. DR NextBio; 10331; -. DR PMAP-CutDB; P15976; -. DR PRO; PR:P15976; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; P15976; -. DR CleanEx; HS_GATA1; -. DR ExpressionAtlas; P15976; baseline and differential. DR Genevisible; P15976; HS. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL. DR GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL. DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:BHF-UCL. DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB. DR GO; GO:0001047; F:core promoter binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0008301; F:DNA binding, bending; IEA:Ensembl. DR GO; GO:0001158; F:enhancer sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IMP:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL. DR GO; GO:0043565; F:sequence-specific DNA binding; IMP:BHF-UCL. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IMP:BHF-UCL. DR GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl. DR GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IBA:GO_Central. DR GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:BHF-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030221; P:basophil differentiation; IEP:BHF-UCL. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl. DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IDA:UniProtKB. DR GO; GO:0097028; P:dendritic cell differentiation; IEA:Ensembl. DR GO; GO:0048565; P:digestive tract development; IBA:GO_Central. DR GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl. DR GO; GO:0030222; P:eosinophil differentiation; IEP:BHF-UCL. DR GO; GO:0035854; P:eosinophil fate commitment; IDA:BHF-UCL. DR GO; GO:0048821; P:erythrocyte development; IMP:BHF-UCL. DR GO; GO:0030218; P:erythrocyte differentiation; IEP:BHF-UCL. DR GO; GO:0007507; P:heart development; IBA:GO_Central. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0008584; P:male gonad development; IMP:BHF-UCL. DR GO; GO:0030219; P:megakaryocyte differentiation; IMP:BHF-UCL. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0030502; P:negative regulation of bone mineralization; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB. DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IDA:BHF-UCL. DR GO; GO:0009887; P:organ morphogenesis; IBA:GO_Central. DR GO; GO:0070527; P:platelet aggregation; IMP:BHF-UCL. DR GO; GO:0030220; P:platelet formation; IMP:BHF-UCL. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB. DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl. 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:0009888; P:tissue development; IBA:GO_Central. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:BHF-UCL. DR GO; GO:0071733; P:transcriptional activation by promoter-enhancer looping; ISS: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: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 Acetylation; Activator; Alternative initiation; Alternative splicing; KW Complete proteome; Direct protein sequencing; Disease mutation; KW DNA-binding; 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_0000083397. 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 REGION 249 315 Interaction with CALCOCO1. FT {ECO:0000269|PubMed:24245781}. FT MOD_RES 26 26 Phosphoserine. FT {ECO:0000250|UniProtKB:P17679}. FT MOD_RES 72 72 Phosphoserine. FT {ECO:0000250|UniProtKB:P17679}. FT MOD_RES 142 142 Phosphoserine. FT {ECO:0000269|PubMed:16371476}. FT MOD_RES 178 178 Phosphoserine. FT {ECO:0000250|UniProtKB:P17679}. FT MOD_RES 187 187 Phosphoserine. FT {ECO:0000250|UniProtKB:P17679}. FT MOD_RES 233 233 N6-acetyllysine; by EP300. FT {ECO:0000305|PubMed:9859997}. FT MOD_RES 245 245 N6-acetyllysine; by EP300. FT {ECO:0000305|PubMed:9859997}. FT MOD_RES 246 246 N6-acetyllysine; by CREBBP. FT {ECO:0000250}. FT MOD_RES 246 246 N6-acetyllysine; by EP300. FT {ECO:0000305|PubMed:9859997}. FT MOD_RES 252 252 N6-acetyllysine; by CREBBP. FT {ECO:0000250}. FT MOD_RES 308 308 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P17679}. FT MOD_RES 310 310 Phosphoserine. FT {ECO:0000250|UniProtKB:P17679}. FT MOD_RES 312 312 N6-acetyllysine; by CREBBP. FT {ECO:0000250}. FT MOD_RES 314 314 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P17679}. FT MOD_RES 315 315 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P17679}. FT CROSSLNK 137 137 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT VAR_SEQ 1 83 Missing (in isoform 3). {ECO:0000305}. FT /FTId=VSP_041451. FT VAR_SEQ 290 413 QVNRPLTMRKDGIQTRNRKASGKGKKKRGSSLGGTGAAEGP FT AGGFMVVAGGSGSGNCGEVASGLTLGPPGTAHLYQGLGPVV FT LSGPVSHLMPFPGPLLGSPTGSFPTGPMPPTTSTTVVAPLS FT S -> HQHYCGGSAQLMRAQSMASRGGVVSFSSCSQNSGQP FT KSLGPRHPLA (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_014782. FT VARIANT 205 205 V -> M (in XDAT; severe impairment of FT ZFPM1 binding and erythroid FT differentiation in vitro). FT {ECO:0000269|PubMed:10700180}. FT /FTId=VAR_010115. FT VARIANT 208 208 G -> S (in XDAT; partially disrupts the FT interaction with ZFPM1). FT {ECO:0000269|PubMed:11675338}. FT /FTId=VAR_012706. FT VARIANT 216 216 R -> Q (in XLTT; does not affect ZFPM1 FT binding; reduced affinity to palindromic FT GATA sites; supports erythroid maturation FT less efficiently than wild-type GATA1). FT {ECO:0000269|PubMed:12200364}. FT /FTId=VAR_033114. FT VARIANT 218 218 D -> G (in XDAT; partially disrupts the FT interaction with ZFPM1). FT {ECO:0000269|PubMed:11418466}. FT /FTId=VAR_012707. FT VARIANT 218 218 D -> Y (in XDAT; stronger loss of FT affinity than of G-218-GATA1 for ZFPM1 FT and disturbed GATA1 self-association). FT {ECO:0000269|PubMed:11809723}. FT /FTId=VAR_033115. FT MUTAGEN 137 137 K->R: Abolishes sumoylation. FT {ECO:0000269|PubMed:16371476}. FT MUTAGEN 142 142 S->A: Loss of sumoylation. FT {ECO:0000269|PubMed:16371476}. FT MUTAGEN 142 142 S->D: Increased sumoylation in vitro. FT {ECO:0000269|PubMed:16371476}. FT MUTAGEN 204 204 C->R: Increase of dissociation rate from FT bound DNA. {ECO:0000269|PubMed:10700180}. SQ SEQUENCE 413 AA; 42751 MW; 822BD2DE14B908AD CRC64; MEFPGLGSLG TSEPLPQFVD PALVSSTPES GVFFPSGPEG LDAAASSTAP STATAAAAAL AYYRDAEAYR HSPVFQVYPL LNCMEGIPGG SPYAGWAYGK TGLYPASTVC PTREDSPPQA VEDLDGKGST SFLETLKTER LSPDLLTLGP ALPSSLPVPN SAYGGPDFSS TFFSPTGSPL NSAAYSSPKL RGTLPLPPCE ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP LIRPKKRLIV SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYYKLHQ VNRPLTMRKD GIQTRNRKAS GKGKKKRGSS LGGTGAAEGP AGGFMVVAGG SGSGNCGEVA SGLTLGPPGT AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TGSFPTGPMP PTTSTTVVAP LSS //