GATA1_HUMAN
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 03-AUG-2022, entry version 222.
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).
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 (PubMed:24245781). {ECO:0000269|PubMed:22235304,
CC 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 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.
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 -!- 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="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 PDB; 6G0Q; X-ray; 1.40 A; B=309-319.
DR PDBsum; 6G0Q; -.
DR AlphaFoldDB; P15976; -.
DR SMR; P15976; -.
DR BioGRID; 108893; 143.
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; P15976; -.
DR PeptideAtlas; P15976; -.
DR PRIDE; P15976; -.
DR ProteomicsDB; 53260; -. [P15976-1]
DR ProteomicsDB; 53261; -. [P15976-2]
DR ProteomicsDB; 53262; -. [P15976-3]
DR Antibodypedia; 372; 993 antibodies from 48 providers.
DR DNASU; 2623; -.
DR Ensembl; ENST00000376670.9; ENSP00000365858.3; ENSG00000102145.15. [P15976-1]
DR Ensembl; ENST00000651144.1; ENSP00000498550.1; ENSG00000102145.15. [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 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; 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; 124; Blackfan-Diamond anemia.
DR Orphanet; 79277; Congenital erythropoietic porphyria.
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; 807790at2759; -.
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; 34 hits in 730 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 92 other tissues.
DR ExpressionAtlas; P15976; baseline and differential.
DR Genevisible; P15976; HS.
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:0097067; P:cellular response to thyroid hormone stimulus; IDA:UniProtKB.
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: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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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; -; 2.
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 Alternative splicing; Direct protein sequencing; Disease variant;
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
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 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
