P15976 (GATA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Erythroid transcription factor

Alternative name(s):
Eryf1
GATA-binding factor 1
Short name=GATA-1
Short name=GF-1
NF-E1 DNA-binding protein

Gene names

Name:	GATA1
Synonyms:	ERYF1, GF1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells.
Subunit structure	May form homodimers or heterodimers with other isoforms. Interacts (via the N-terminal zinc finger) with ZFPM1. Interacts with GFI1B. Interacts with PIAS4; the interaction enhances sumoylation and represses the transactivational activity in a sumoylation-independent manner. Interacts with LMCD1 By similarity. Ref.5 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Nucleus.
Tissue specificity	Erythrocytes. Ref.5
Domain	The two fingers are functionally distinct and cooperate to achieve specific, stable DNA binding. The first finger is necessary only for full specificity and stability of binding, whereas the second one is required for binding By similarity.
Post-translational modification	Highly phosphorylated on serine residues. Phosphorylation on Ser-310 is enhanced on erythroid differentiation. Phosphorylation on Ser-142 promotes sumoylation on Lys-137 By similarity. Ref.7 Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4. Sumoylation by SUMO1 has no effect on transcriptional activity By similarity.
Involvement in disease	Defects in GATA1 are the cause of X-linked dyserythropoietic anemia and thrombocytopenia (XDAT) [MIM:300367]. XDAT is a disorder characterized by erythrocytes with abnormal size and shape, and paucity of platelets in peripheral blood. The bone marrow contains abundant and abnormally small megakaryocytes. Ref.9 Ref.10 Ref.11 Ref.13 Defects in GATA1 are the cause of X-linked thrombocytopenia with beta-thalassemia (XLTT) [MIM:314050]; also knwon as thrombocytopenia, platelet dysfunction, hemolysis, and imbalanced globin synthesis. XLTT consists of an unusual form of thrombocytopenia with beta-thalassemia. Patients have splenomegaly and petechiae, moderate thrombocytopenia, prolonged bleeding time due to platelet dysfunction, reticulocytosis and unbalanced hemoglobin chain synthesis resembling that of beta-thalassemia minor. Defects in GATA1 are the cause of anemia without thrombocytopenia X-linked (XLAWT) [MIM:300835]. XLAWT is a form of anemia characterized by abnormal morphology of erythrocytes and granulocytes in peripheral blood, bone marrow dysplasia with hypocellularity of erythroid and granulocytic lineages, and normal or increased number of megakaryocytes. Neutropenia of a variable degree is present in affected individuals. Ref.6
Sequence similarities	Contains 2 GATA-type zinc fingers.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative initiation Alternative splicing
Disease	Disease mutation
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	basophil differentiation Inferred from expression pattern. Source: BHF-UCL cellular response to thyroid hormone stimulus Inferred from direct assay. Source: UniProtKB eosinophil fate commitment Inferred from direct assay. Source: BHF-UCL erythrocyte development Inferred from mutant phenotype Ref.9. Source: BHF-UCL megakaryocyte differentiation Inferred from mutant phenotype Ref.9. Source: BHF-UCL negative regulation of transcription regulatory region DNA binding Inferred from direct assay. Source: BHF-UCL platelet aggregation Inferred from mutant phenotype. Source: BHF-UCL platelet formation Inferred from mutant phenotype Ref.9Ref.11. Source: BHF-UCL positive regulation of anti-apoptosis Traceable author statement. Source: BHF-UCL positive regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype. Source: BHF-UCL regulation of definitive erythrocyte differentiation Inferred from direct assay Ref.12. Source: BHF-UCL regulation of glycoprotein biosynthetic process Inferred from mutant phenotype. Source: BHF-UCL transcriptional activation by promoter-enhancer looping Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	nuclear membrane Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA transcription factor complex Inferred from direct assay. Source: BHF-UCL transcriptional repressor complex Inferred from direct assay. Source: BHF-UCL
Molecular function	C2H2 zinc finger domain binding Inferred from physical interaction. Source: BHF-UCL RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Inferred from direct assay. Source: BHF-UCL RNA polymerase II transcription factor binding Inferred from physical interaction Ref.11. Source: BHF-UCL zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSPA1A	P08107	5	EBI-3909284,EBI-629985

Alternative products

This entry describes 3 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Isoform 1 (identifier: P15976-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P15976-2)

The sequence of this isoform differs from the canonical sequence as follows:
     290-413: QVNRPLTMRK...STTVVAPLSS → HQHYCGGSAQ...KSLGPRHPLA

Note: No experimental confirmation available.

Isoform 3 (identifier: P15976-3)

Also known as: GATA-1s;

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: Missing.

Note: Produced by alternative initiation at Met-84 of isoform 1.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 413	413	Erythroid transcription factor		PRO_0000083397
Regions
	Zinc finger	204 – 228	25	GATA-type 1
	Zinc finger	258 – 282	25	GATA-type 2
	Region	203 – 222	20	Required for interaction with ZFPM1
Amino acid modifications
	Modified residue	26	1	Phosphoserine By similarity
	Modified residue	72	1	Phosphoserine By similarity
	Modified residue	142	1	Phosphoserine Ref.7
	Modified residue	178	1	Phosphoserine By similarity
	Modified residue	187	1	Phosphoserine By similarity
	Modified residue	310	1	Phosphoserine By similarity
	Cross-link	137		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7
Natural variations
	Alternative sequence	1 – 83	83	Missing in isoform 3.		VSP_041451
	Alternative sequence	290 – 413	124	QVNRP…APLSS → HQHYCGGSAQLMRAQSMASR GGVVSFSSCSQNSGQPKSLG PRHPLA in isoform 2.		VSP_014782
	Natural variant	205	1	V → M in XDAT; severe impairment of ZFPM1 binding and erythroid differentiation in vitro. Ref.9		VAR_010115
	Natural variant	208	1	G → S in XDAT; partially disrupts the interaction with ZFPM1. Ref.11		VAR_012706
	Natural variant	216	1	R → Q in XLTT; does not affect ZFPM1 binding; reduced affinity to palindromic GATA sites; supports erythroid maturation less efficiently than wild-type GATA1. Ref.12		VAR_033114
	Natural variant	218	1	D → G in XDAT; partially disrupts the interaction with ZFPM1. Ref.10		VAR_012707
	Natural variant	218	1	D → Y in XDAT; stronger loss of affinity than of G-218-GATA1 for ZFPM1 and disturbed GATA1 self-association. Ref.13		VAR_033115
Experimental info
	Mutagenesis	137	1	K → R: Abolishes sumoylation. Ref.7
	Mutagenesis	142	1	S → A: Loss of sumoylation. Ref.7
	Mutagenesis	142	1	S → D: Increased sumoylation in vitro. Ref.7
	Mutagenesis	204	1	C → R: Increase of dissociation rate from bound DNA. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 822BD2DE14B908AD	FASTA	413	42,751
	10 20 30 40 50 60 MEFPGLGSLG TSEPLPQFVD PALVSSTPES GVFFPSGPEG LDAAASSTAP STATAAAAAL 70 80 90 100 110 120 AYYRDAEAYR HSPVFQVYPL LNCMEGIPGG SPYAGWAYGK TGLYPASTVC PTREDSPPQA 130 140 150 160 170 180 VEDLDGKGST SFLETLKTER LSPDLLTLGP ALPSSLPVPN SAYGGPDFSS TFFSPTGSPL 190 200 210 220 230 240 NSAAYSSPKL RGTLPLPPCE ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP 250 260 270 280 290 300 LIRPKKRLIV SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYYKLHQ VNRPLTMRKD 310 320 330 340 350 360 GIQTRNRKAS GKGKKKRGSS LGGTGAAEGP AGGFMVVAGG SGSGNCGEVA SGLTLGPPGT 370 380 390 400 410 AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TGSFPTGPMP PTTSTTVVAP LSS
	Isoform 2 [UniParc]. Checksum: 9CE44220E09F69D7	FASTA	335	35,430
	10 20 30 40 50 60 MEFPGLGSLG TSEPLPQFVD PALVSSTPES GVFFPSGPEG LDAAASSTAP STATAAAAAL 70 80 90 100 110 120 AYYRDAEAYR HSPVFQVYPL LNCMEGIPGG SPYAGWAYGK TGLYPASTVC PTREDSPPQA 130 140 150 160 170 180 VEDLDGKGST SFLETLKTER LSPDLLTLGP ALPSSLPVPN SAYGGPDFSS TFFSPTGSPL 190 200 210 220 230 240 NSAAYSSPKL RGTLPLPPCE ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP 250 260 270 280 290 300 LIRPKKRLIV SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYYKLHH QHYCGGSAQL 310 320 330 MRAQSMASRG GVVSFSSCSQ NSGQPKSLGP RHPLA
	Isoform 3 (GATA-1s) [UniParc]. Checksum: E5ACD72BCBDB40B1	FASTA	330	34,232
	10 20 30 40 50 60 MEGIPGGSPY AGWAYGKTGL YPASTVCPTR EDSPPQAVED LDGKGSTSFL ETLKTERLSP 70 80 90 100 110 120 DLLTLGPALP SSLPVPNSAY GGPDFSSTFF SPTGSPLNSA AYSSPKLRGT LPLPPCEARE 130 140 150 160 170 180 CVNCGATATP LWRRDRTGHY LCNACGLYHK MNGQNRPLIR PKKRLIVSKR AGTQCTNCQT 190 200 210 220 230 240 TTTTLWRRNA SGDPVCNACG LYYKLHQVNR PLTMRKDGIQ TRNRKASGKG KKKRGSSLGG 250 260 270 280 290 300 TGAAEGPAGG FMVVAGGSGS GNCGEVASGL TLGPPGTAHL YQGLGPVVLS GPVSHLMPFP 310 320 330 GPLLGSPTGS FPTGPMPPTT STTVVAPLSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and evolution of a human erythroid transcription factor." Trainor C.D., Evans T., Felsenfeld G., Boguski M.S. Nature 343:92-96(1990) [PubMed: 2104960] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Bone marrow.
[2]	"The major human erythroid DNA-binding protein (GF-1): primary sequence and localization of the gene to the X chromosome." Zon L.I., Tsai S.-F., Burgess S., Matsudaira P., Bruns G.A.P., Orkin S.H. Proc. Natl. Acad. Sci. U.S.A. 87:668-672(1990) [PubMed: 2300555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE. Tissue: Erythrocyte.
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Bone marrow.
[5]	"Alternative translation initiation site usage results in two functionally distinct forms of the GATA-1 transcription factor." Calligaris R., Bottardi S., Cogoi S., Apezteguia I., Santoro C. Proc. Natl. Acad. Sci. U.S.A. 92:11598-11602(1995) [PubMed: 8524811] [Abstract] Cited for: ALTERNATIVE INITIATION (ISOFORM 3), SUBUNIT, TISSUE SPECIFICITY.
[6]	"An inherited mutation leading to production of only the short isoform of GATA-1 is associated with impaired erythropoiesis." Hollanda L.M., Lima C.S., Cunha A.F., Albuquerque D.M., Vassallo J., Ozelo M.C., Joazeiro P.P., Saad S.T., Costa F.F. Nat. Genet. 38:807-812(2006) [PubMed: 16783379] [Abstract] Cited for: INVOLVEMENT IN XLAWT.
[7]	"PDSM, a motif for phosphorylation-dependent SUMO modification." Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J., Nakai A., Sistonen L. Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006) [PubMed: 16371476] [Abstract] Cited for: SUMOYLATION AT LYS-137, PHOSPHORYLATION AT SER-142, MUTAGENESIS OF LYS-137 AND SER-142.
[8]	"GATA-1 and Gfi-1B interplay to regulate Bcl-xL transcription." Kuo Y.-Y., Chang Z.-F. Mol. Cell. Biol. 27:4261-4272(2007) [PubMed: 17420275] [Abstract] Cited for: INTERACTION WITH GFI1B.
[9]	"Familial dyserythropoietic anaemia and thrombocytopenia due to an inherited mutation in GATA1." Nichols K.E., Crispino J.D., Poncz M., White J.G., Orkin S.H., Maris J.M., Weiss M.J. Nat. Genet. 24:266-270(2000) [PubMed: 10700180] [Abstract] Cited for: VARIANT XDAT MET-205, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT XDAT MET-205, MUTAGENESIS OF CYS-204. Tissue: Peripheral blood.
[10]	"Platelet characteristics in patients with X-linked macrothrombocytopenia because of a novel GATA1 mutation." Freson K., Devriendt K., Matthijs G., Van Hoof A., De Vos R., Thys C., Minner K., Hoylaerts M.F., Vermylen J., Van Geet C. Blood 98:85-92(2001) [PubMed: 11418466] [Abstract] Cited for: VARIANT XDAT GLY-218, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT XDAT GLY-218.
[11]	"X-linked thrombocytopenia caused by a novel mutation of GATA-1." Mehaffey M.G., Newton A.L., Gandhi M.J., Crossley M., Drachman J.G. Blood 98:2681-2688(2001) [PubMed: 11675338] [Abstract] Cited for: VARIANT XDAT SER-208, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT XDAT SER-208.
[12]	"X-linked thrombocytopenia with thalassemia from a mutation in the amino finger of GATA-1 affecting DNA binding rather than FOG-1 interaction." Yu C., Niakan K.K., Matsushita M., Stamatoyannopoulos G., Orkin S.H., Raskind W.H. Blood 100:2040-2045(2002) [PubMed: 12200364] [Abstract] Cited for: VARIANT XLTT GLN-216, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT XLTT GLN-216.
[13]	"Different substitutions at residue D218 of the X-linked transcription factor GATA1 lead to altered clinical severity of macrothrombocytopenia and anemia and are associated with variable skewed X inactivation." Freson K., Matthijs G., Thys C., Marieen P., Hoylaerts M.F., Vermylen J., Van Geet C. Hum. Mol. Genet. 11:147-152(2002) [PubMed: 11809723] [Abstract] Cited for: VARIANT XDAT TYR-218, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT XDAT TYR-218.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	X17254 mRNA. Translation: CAA35120.1. M30601 mRNA. Translation: AAA35885.1. AF196971 Genomic DNA. No translation available. BC009797 mRNA. Translation: AAH09797.1.
IPI	IPI00013999. IPI01014333. IPI01018734.
PIR	A34888.
RefSeq	NP_002040.1. NM_002049.3.
UniGene	Hs.765.
3D structure databases
ProteinModelPortal	P15976.
SMR	P15976. Positions 200-243, 252-310.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-41431N.
IntAct	P15976. 3 interactions.
MINT	MINT-247486.
STRING	P15976.
PTM databases
PhosphoSite	P15976.
Polymorphism databases
DMDM	120956.
Proteomic databases
PRIDE	P15976.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000376670; ENSP00000365858; ENSG00000102145.
GeneID	2623.
KEGG	hsa:2623.
UCSC	uc004dkq.2. human.
Organism-specific databases
CTD	2623.
GeneCards	GC0XP048644.
H-InvDB	HIX0203296.
HGNC	HGNC:4170. GATA1.
HPA	CAB009195. HPA000232. HPA000233.
MIM	300367. phenotype. 300835. phenotype. 305371. gene. 314050. phenotype.
neXtProt	NX_P15976.
Orphanet	231393. Beta-thalassemia - X-linked thrombocytopenia. 67044. Dyserythropoietic anemia with thrombocytopenia.
PharmGKB	PA28584.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16265.
GeneTree	ENSGT00550000074470.
HOGENOM	HBG716943.
HOVERGEN	HBG051705.
InParanoid	P15976.
OMA	FPTGPVP.
OrthoDB	EOG4QNMWM.
PhylomeDB	P15976.
Enzyme and pathway databases
Pathway_Interaction_DB	hdac_classi_pathway. Signaling events mediated by HDAC Class I. hdac_classii_pathway. Signaling events mediated by HDAC Class II.
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P15976.
Bgee	P15976.
CleanEx	HS_GATA1.
Genevestigator	P15976.
GermOnline	ENSG00000102145. Homo sapiens.
Family and domain databases
InterPro	IPR016374. TF_GATA-1/2/3. IPR000679. Znf_GATA. IPR013088. Znf_NHR/GATA. [Graphical view]
Gene3D	G3DSA:3.30.50.10. Znf_NHR/GATA. 2 hits.
KO	K09182.
Pfam	PF00320. GATA. 2 hits. [Graphical view]
PIRSF	PIRSF003027. TF_GATA-1/2/3. 1 hit.
PRINTS	PR00619. GATAZNFINGER.
SMART	SM00401. ZnF_GATA. 2 hits. [Graphical view]
PROSITE	PS00344. GATA_ZN_FINGER_1. 2 hits. PS50114. GATA_ZN_FINGER_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	10331.
PMAP-CutDB	P15976.
SOURCE	Search...

Entry information

Entry name

GATA1_HUMAN

Accession

Primary (citable) accession number: P15976
Secondary accession number(s): Q96GB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.