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 24-JAN-2024, entry version 229. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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., Orkin S.H.; RT "The major human erythroid DNA-binding protein (GF-1): primary sequence and RT 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., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., 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., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., 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., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., 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., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., 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., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA 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 project: RT 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 functionally RT 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 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 of RT 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 GATA-1, RT promotes proliferation of K562 cells."; RL PLoS ONE 7:E29518-E29518(2012). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-131, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] 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., 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 [13] RP INTERACTION WITH CEBPE. RX PubMed=26019275; DOI=10.4049/jimmunol.1402222; RA Wada T., Akagi T., Muraoka M., Toma T., Kaji K., Agematsu K., RA Koeffler H.P., Yokota T., Yachie A.; RT "A novel in-frame deletion in the leucine zipper domain of C/EBPepsilon RT leads to neutrophil-specific granule deficiency."; RL J. Immunol. 195:80-86(2015). RN [14] RP VARIANT XDAT MET-205, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT RP 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., Maris J.M., RA 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 [15] 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 macrothrombocytopenia RT because of a novel GATA1 mutation."; RL Blood 98:85-92(2001). RN [16] 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 [17] 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 amino RT finger of GATA-1 affecting DNA binding rather than FOG-1 interaction."; RL Blood 100:2040-2045(2002). RN [18] 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., Vermylen J., RA Van Geet C.; RT "Different substitutions at residue D218 of the X-linked transcription RT factor GATA1 lead to altered clinical severity of macrothrombocytopenia and RT anemia and are associated with variable skewed X inactivation."; RL Hum. Mol. Genet. 11:147-152(2002). RN [19] RP INVOLVEMENT IN HAEADA, VARIANTS HAEADA CYS-307 AND HIS-307, RP CHARACTERIZATION OF VARIANTS HAEADA CYS-307 AND HIS-307, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=35030251; DOI=10.1182/blood.2021013753; RA Ludwig L.S., Lareau C.A., Bao E.L., Liu N., Utsugisawa T., Tseng A.M., RA Myers S.A., Verboon J.M., Ulirsch J.C., Luo W., Muus C., Fiorini C., RA Olive M.E., Vockley C.M., Munschauer M., Hunter A., Ogura H., Yamamoto T., RA Inada H., Nakagawa S., Ohzono S., Subramanian V., Chiarle R., Glader B., RA Carr S.A., Aryee M.J., Kundaje A., Orkin S.H., Regev A., McCavit T.L., RA Kanno H., Sankaran V.G.; RT "Congenital anemia reveals distinct targeting mechanisms for master RT transcription factor GATA1."; RL Blood 139:2534-2546(2022). CC -!- FUNCTION: Transcriptional activator or repressor which serves as a CC general switch factor for erythroid development (PubMed:35030251). 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 expressed CC in erythroid cells. Activates the transcription of genes involved in CC erythroid differentiation of K562 erythroleukemia cells, including HBB, CC HBG1/2, ALAS2 and HMBS (PubMed:24245781). {ECO:0000269|PubMed:22235304, CC ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:35030251}. CC -!- SUBUNIT: May form homodimers or heterodimers with other isoforms. CC Interacts (via the N-terminal zinc finger) with ZFPM1. Interacts with CC GFI1B. Interacts with PIAS4; the interaction enhances sumoylation and CC represses the transactivational activity in a sumoylation-independent CC manner. Interacts with LMCD1. Interacts with BRD3 (By similarity). CC Interacts with CREBBP; the interaction stimulates acetylation and CC transcriptional activity in vivo (By similarity). Interacts with EP300. CC Interacts with MED1, CCAR1 and CALCOCO1. Interacts with CEBPE CC (PubMed:26019275). {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:26019275, CC ECO:0000269|PubMed:8524811, ECO:0000269|PubMed:9859997}. CC -!- INTERACTION: CC P15976; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-3909284, EBI-1104933; CC P15976; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-3909284, EBI-10244131; CC P15976; O43559: FRS3; NbExp=3; IntAct=EBI-3909284, EBI-725515; CC P15976; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-3909284, EBI-5460660; CC P15976; P49639: HOXA1; NbExp=3; IntAct=EBI-3909284, EBI-740785; CC P15976; P08107: HSPA1B; NbExp=5; IntAct=EBI-3909284, EBI-629985; CC P15976; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-3909284, EBI-10172150; CC P15976; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-3909284, EBI-1044640; CC P15976; Q15648: MED1; NbExp=6; IntAct=EBI-3909284, EBI-394459; CC P15976; Q16236: NFE2L2; NbExp=2; IntAct=EBI-3909284, EBI-2007911; CC P15976; O43741: PRKAB2; NbExp=3; IntAct=EBI-3909284, EBI-1053424; CC P15976; Q96JH8: RADIL; NbExp=3; IntAct=EBI-3909284, EBI-744267; CC P15976; P06400: RB1; NbExp=2; IntAct=EBI-3909284, EBI-491274; CC P15976; Q8IX07: ZFPM1; NbExp=2; IntAct=EBI-3909284, EBI-3942619; CC P15976; P13405: Rb1; Xeno; NbExp=2; IntAct=EBI-3909284, EBI-971782; CC P15976; O35615: Zfpm1; Xeno; NbExp=5; IntAct=EBI-3909284, EBI-4394596; CC P15976-2; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-9090198, EBI-742909; CC P15976-2; Q86V38: ATN1; NbExp=3; IntAct=EBI-9090198, EBI-11954292; CC P15976-2; P46379-2: BAG6; NbExp=3; IntAct=EBI-9090198, EBI-10988864; CC P15976-2; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-9090198, EBI-1104933; CC P15976-2; Q9H2X0: CHRD; NbExp=3; IntAct=EBI-9090198, EBI-947551; CC P15976-2; P02489: CRYAA; NbExp=3; IntAct=EBI-9090198, EBI-6875961; CC P15976-2; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-9090198, EBI-742953; CC P15976-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-9090198, EBI-10976677; CC P15976-2; Q9NW38: FANCL; NbExp=3; IntAct=EBI-9090198, EBI-2339898; CC P15976-2; P22607: FGFR3; NbExp=3; IntAct=EBI-9090198, EBI-348399; CC P15976-2; Q13643: FHL3; NbExp=4; IntAct=EBI-9090198, EBI-741101; CC P15976-2; O43559: FRS3; NbExp=5; IntAct=EBI-9090198, EBI-725515; CC P15976-2; P28799: GRN; NbExp=3; IntAct=EBI-9090198, EBI-747754; CC P15976-2; P06396: GSN; NbExp=3; IntAct=EBI-9090198, EBI-351506; CC P15976-2; P49639: HOXA1; NbExp=3; IntAct=EBI-9090198, EBI-740785; CC P15976-2; P04792: HSPB1; NbExp=3; IntAct=EBI-9090198, EBI-352682; CC P15976-2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-9090198, EBI-2556193; CC P15976-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9090198, EBI-10975473; CC P15976-2; O14901: KLF11; NbExp=3; IntAct=EBI-9090198, EBI-948266; CC P15976-2; Q92876: KLK6; NbExp=3; IntAct=EBI-9090198, EBI-2432309; CC P15976-2; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-9090198, EBI-751260; CC P15976-2; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-9090198, EBI-10302392; CC P15976-2; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-9090198, EBI-11993254; CC P15976-2; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-9090198, EBI-741037; CC P15976-2; P31153: MAT2A; NbExp=3; IntAct=EBI-9090198, EBI-1050743; CC P15976-2; Q99750: MDFI; NbExp=5; IntAct=EBI-9090198, EBI-724076; CC P15976-2; Q13064: MKRN3; NbExp=3; IntAct=EBI-9090198, EBI-2340269; CC P15976-2; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-9090198, EBI-473160; CC P15976-2; P78337: PITX1; NbExp=3; IntAct=EBI-9090198, EBI-748265; CC P15976-2; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-9090198, EBI-769257; CC P15976-2; O43741: PRKAB2; NbExp=6; IntAct=EBI-9090198, EBI-1053424; CC P15976-2; P60891: PRPS1; NbExp=3; IntAct=EBI-9090198, EBI-749195; CC P15976-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-9090198, EBI-396669; CC P15976-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-9090198, EBI-5235340; CC P15976-2; Q8WW24: TEKT4; NbExp=5; IntAct=EBI-9090198, EBI-750487; CC P15976-2; Q08117-2: TLE5; NbExp=5; IntAct=EBI-9090198, EBI-11741437; CC P15976-2; Q13077: TRAF1; NbExp=3; IntAct=EBI-9090198, EBI-359224; CC P15976-2; Q15654: TRIP6; NbExp=4; IntAct=EBI-9090198, EBI-742327; CC P15976-2; O76024: WFS1; NbExp=3; IntAct=EBI-9090198, EBI-720609; CC P15976-2; Q9Y649; NbExp=3; IntAct=EBI-9090198, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35030251}. 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 Name=3; Synonyms=GATA-1s; CC IsoId=P15976-3; Sequence=VSP_041451; 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 necessary CC only for full specificity and stability of binding, whereas the second CC one is required for binding (By similarity). {ECO:0000250}. 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 (By similarity). {ECO:0000250}. CC -!- PTM: Acetylated at 2 conserved lysine-rich motifs 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 (By CC similarity). Acetylated on Lys-233, Lys-245 Lys-246 by EP300. CC {ECO:0000250, ECO:0000269|PubMed:9859997}. CC -!- DISEASE: X-linked dyserythropoietic anemia and thrombocytopenia (XDAT) CC [MIM:300367]: Disorder characterized by erythrocytes with abnormal size CC and shape, and paucity of platelets in peripheral blood. The bone CC marrow contains abundant and abnormally small megakaryocytes. CC {ECO:0000269|PubMed:10700180, ECO:0000269|PubMed:11418466, CC ECO:0000269|PubMed:11675338, ECO:0000269|PubMed:11809723}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Thrombocytopenia with beta-thalassemia, X-linked (XLTT) CC [MIM:314050]: An unusual form of thrombocytopenia associated with beta- CC thalassemia. Patients have splenomegaly and petechiae, moderate CC thrombocytopenia, prolonged bleeding time due to platelet dysfunction, CC reticulocytosis and unbalanced (hemo)globin chain synthesis resembling CC that of beta-thalassemia minor. {ECO:0000269|PubMed:12200364}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Anemia without thrombocytopenia, X-linked (XLAWT) CC [MIM:300835]: A form of anemia characterized by abnormal morphology of CC erythrocytes and granulocytes in peripheral blood, bone marrow CC dysplasia with hypocellularity of erythroid and granulocytic lineages, CC and normal or increased number of megakaryocytes. Neutropenia of a CC variable degree is present in affected individuals. CC {ECO:0000269|PubMed:16783379}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Hemolytic anemia due to elevated adenosine deaminase (HAEADA) CC [MIM:301083]: An X-linked disorder characterized by onset of mild to CC moderate red cell anemia soon after birth or in childhood. The anemia CC is associated with significantly increased adenosine deaminase CC activity, specifically in erythrocyte precursors. CC {ECO:0000269|PubMed:35030251}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation at Met- CC 84 of isoform 1. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40689/GATA1"; 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 PDB; 6G0Q; X-ray; 1.40 A; B=309-319. DR PDBsum; 6G0Q; -. DR AlphaFoldDB; P15976; -. DR SMR; P15976; -. DR BioGRID; 108893; 146. DR DIP; DIP-41431N; -. DR IntAct; P15976; 137. DR MINT; P15976; -. DR STRING; 9606.ENSP00000365858; -. DR iPTMnet; P15976; -. DR PhosphoSitePlus; P15976; -. DR BioMuta; GATA1; -. DR DMDM; 120956; -. DR MassIVE; P15976; -. DR MaxQB; P15976; -. DR PaxDb; 9606-ENSP00000365858; -. DR PeptideAtlas; P15976; -. DR ProteomicsDB; 53260; -. [P15976-1] DR ProteomicsDB; 53261; -. [P15976-2] DR ProteomicsDB; 53262; -. [P15976-3] DR Pumba; P15976; -. DR Antibodypedia; 372; 1089 antibodies from 48 providers. DR DNASU; 2623; -. DR Ensembl; ENST00000376670.9; ENSP00000365858.3; ENSG00000102145.16. [P15976-1] DR Ensembl; ENST00000651144.2; ENSP00000498550.1; ENSG00000102145.16. [P15976-3] DR GeneID; 2623; -. DR KEGG; hsa:2623; -. DR MANE-Select; ENST00000376670.9; ENSP00000365858.3; NM_002049.4; NP_002040.1. DR UCSC; uc004dkq.5; human. [P15976-1] DR AGR; HGNC:4170; -. DR CTD; 2623; -. DR DisGeNET; 2623; -. DR GeneCards; GATA1; -. DR GeneReviews; GATA1; -. DR HGNC; HGNC:4170; GATA1. DR HPA; ENSG00000102145; Tissue enriched (bone). DR MalaCards; GATA1; -. DR MIM; 300367; phenotype. DR MIM; 300835; phenotype. DR MIM; 301083; phenotype. DR MIM; 305371; gene. DR MIM; 314050; phenotype. DR neXtProt; NX_P15976; -. DR OpenTargets; ENSG00000102145; -. DR Orphanet; 86849; Acute basophilic leukemia. DR Orphanet; 99887; Acute megakaryoblastic leukemia in Down syndrome. DR Orphanet; 231393; Beta-thalassemia-X-linked thrombocytopenia syndrome. DR Orphanet; 79277; Congenital erythropoietic porphyria. DR Orphanet; 124; Diamond-Blackfan anemia. DR Orphanet; 67044; Thrombocytopenia with congenital dyserythropoietic anemia. DR Orphanet; 420611; Transient myeloproliferative syndrome. DR Orphanet; 363727; X-linked dyserythropoietic anemia with abnormal platelets and neutropenia. DR PharmGKB; PA28584; -. DR VEuPathDB; HostDB:ENSG00000102145; -. DR eggNOG; KOG1601; Eukaryota. DR GeneTree; ENSGT00940000161156; -. DR HOGENOM; CLU_027524_1_1_1; -. DR InParanoid; P15976; -. DR OMA; YSKTGLY; -. DR OrthoDB; 685518at2759; -. DR PhylomeDB; P15976; -. DR TreeFam; TF315391; -. DR PathwayCommons; P15976; -. DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; P15976; -. DR SIGNOR; P15976; -. DR BioGRID-ORCS; 2623; 39 hits in 810 CRISPR screens. DR ChiTaRS; GATA1; human. DR GeneWiki; GATA1; -. DR GenomeRNAi; 2623; -. DR Pharos; P15976; Tbio. DR PRO; PR:P15976; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P15976; Protein. DR Bgee; ENSG00000102145; Expressed in trabecular bone tissue and 93 other cell types or tissues. DR ExpressionAtlas; P15976; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032993; C:protein-DNA complex; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL. DR GO; GO:0017053; C:transcription 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:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0002039; F:p53 binding; IEA:Ensembl. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL. 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; IMP:BHF-UCL. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:BHF-UCL. DR GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0030221; P:basophil differentiation; IEP:BHF-UCL. DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl. DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central. DR GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0097028; P:dendritic cell differentiation; 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:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl. 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:0033028; P:myeloid cell apoptotic process; IEA:Ensembl. 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 population 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:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IDA:BHF-UCL. DR GO; GO:0033687; P:osteoblast proliferation; IEA:Ensembl. DR GO; GO:0070527; P:platelet aggregation; IMP:BHF-UCL. DR GO; GO:0030220; P:platelet formation; IMP:BHF-UCL. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB. DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl. 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 by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0060319; P:primitive erythrocyte differentiation; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR CDD; cd00202; ZnF_GATA; 2. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 2. DR InterPro; IPR039355; Transcription_factor_GATA. DR InterPro; IPR000679; Znf_GATA. DR InterPro; IPR013088; Znf_NHR/GATA. DR PANTHER; PTHR10071:SF190; ERYTHROID TRANSCRIPTION FACTOR; 1. DR PANTHER; PTHR10071; TRANSCRIPTION FACTOR GATA FAMILY MEMBER; 1. DR Pfam; PF00320; GATA; 2. DR PRINTS; PR00619; GATAZNFINGER. DR SMART; SM00401; ZnF_GATA; 2. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2. DR PROSITE; PS00344; GATA_ZN_FINGER_1; 2. DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2. DR Genevisible; P15976; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative initiation; KW Alternative splicing; Direct protein sequencing; Disease variant; KW DNA-binding; Hereditary hemolytic anemia; 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_0000083397" 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 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 REGION 249..315 FT /note="Interaction with CALCOCO1" FT /evidence="ECO:0000269|PubMed:24245781" FT REGION 297..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 26 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P17679" FT MOD_RES 72 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P17679" FT MOD_RES 116 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 131 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 142 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16371476" FT MOD_RES 178 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P17679" FT MOD_RES 187 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P17679" FT MOD_RES 233 FT /note="N6-acetyllysine; by EP300" FT /evidence="ECO:0000305|PubMed:9859997" FT MOD_RES 245 FT /note="N6-acetyllysine; by EP300" FT /evidence="ECO:0000305|PubMed:9859997" FT MOD_RES 246 FT /note="N6-acetyllysine; by CREBBP" FT /evidence="ECO:0000250|UniProtKB:P17679" FT MOD_RES 246 FT /note="N6-acetyllysine; by EP300" FT /evidence="ECO:0000305|PubMed:9859997" FT MOD_RES 252 FT /note="N6-acetyllysine; by CREBBP" FT /evidence="ECO:0000250|UniProtKB:P17679" FT MOD_RES 308 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P17679" FT MOD_RES 310 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P17679" FT MOD_RES 312 FT /note="N6-acetyllysine; by CREBBP" FT /evidence="ECO:0000250|UniProtKB:P17679" FT MOD_RES 314 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P17679" FT MOD_RES 315 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P17679" FT CROSSLNK 137 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:16371476" FT VAR_SEQ 1..83 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_041451" FT VAR_SEQ 290..413 FT /note="QVNRPLTMRKDGIQTRNRKASGKGKKKRGSSLGGTGAAEGPAGGFMVVAGGS FT GSGNCGEVASGLTLGPPGTAHLYQGLGPVVLSGPVSHLMPFPGPLLGSPTGSFPTGPMP FT PTTSTTVVAPLSS -> HQHYCGGSAQLMRAQSMASRGGVVSFSSCSQNSGQPKSLGPR FT HPLA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014782" FT VARIANT 205 FT /note="V -> M (in XDAT; severe impairment of ZFPM1 binding FT and erythroid differentiation in vitro; dbSNP:rs104894815)" FT /evidence="ECO:0000269|PubMed:10700180" FT /id="VAR_010115" FT VARIANT 208 FT /note="G -> S (in XDAT; partially disrupts the interaction FT with ZFPM1; dbSNP:rs137852312)" FT /evidence="ECO:0000269|PubMed:11675338" FT /id="VAR_012706" FT VARIANT 216 FT /note="R -> Q (in XLTT; does not affect ZFPM1 binding; FT reduced affinity to palindromic GATA sites; supports FT erythroid maturation less efficiently than wild-type GATA1; FT dbSNP:rs104894809)" FT /evidence="ECO:0000269|PubMed:12200364" FT /id="VAR_033114" FT VARIANT 218 FT /note="D -> G (in XDAT; partially disrupts the interaction FT with ZFPM1; dbSNP:rs104894816)" FT /evidence="ECO:0000269|PubMed:11418466" FT /id="VAR_012707" FT VARIANT 218 FT /note="D -> Y (in XDAT; stronger loss of affinity than of FT G-218-GATA1 for ZFPM1 and disturbed GATA1 self-association; FT dbSNP:rs104894808)" FT /evidence="ECO:0000269|PubMed:11809723" FT /id="VAR_033115" FT VARIANT 307 FT /note="R -> C (in HAEADA; altered transcriptional activity FT at canonical GATA1 target genes, affecting both silencing FT and activation of select genes necessary for effective FT terminal red cell production; may affect binding to FT specific genomic loci; partial loss of nuclear FT localization; dbSNP:rs1057518396)" FT /evidence="ECO:0000269|PubMed:35030251" FT /id="VAR_087448" FT VARIANT 307 FT /note="R -> H (in HAEADA; altered transcriptional activity FT at canonical GATA1 target genes, affecting both silencing FT and activation of select genes necessary for effective FT terminal red cell production; partial loss of nuclear FT localization)" FT /evidence="ECO:0000269|PubMed:35030251" FT /id="VAR_087449" FT MUTAGEN 137 FT /note="K->R: Abolishes sumoylation." FT /evidence="ECO:0000269|PubMed:16371476" FT MUTAGEN 142 FT /note="S->A: Loss of sumoylation." FT /evidence="ECO:0000269|PubMed:16371476" FT MUTAGEN 142 FT /note="S->D: Increased sumoylation in vitro." FT /evidence="ECO:0000269|PubMed:16371476" FT MUTAGEN 204 FT /note="C->R: Increase of dissociation rate from bound DNA." FT /evidence="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 //