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P15976 (GATA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Ref.10

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. Interacts with BRD3 By similarity. Interacts with CREBBP; the interaction stimulates acetylation and transcriptional activity in vivo By similarity. Interacts with EP300. Ref.5 Ref.6 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

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.8

Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4. Sumoylation with SUMO1 has no effect on transcriptional activity By similarity. Ref.8

Acetylated at 2 conserved lysine-rich motifs by CREBBP in vitro. Acetylation does not affect DNA-binding in vitro but is essential to induce erythroid differentiation and for binding chromatin in vivo By similarity. Acetylated on Lys-233, Lys-245 Lys-246 by EP300. Ref.6

Involvement in disease

X-linked dyserythropoietic anemia and thrombocytopenia (XDAT) [MIM:300367]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13 Ref.15

Thrombocytopenia with beta-thalassemia, X-linked (XLTT) [MIM:314050]: An unusual form of thrombocytopenia associated with beta-thalassemia. Patients have splenomegaly and petechiae, moderate thrombocytopenia, prolonged bleeding time due to platelet dysfunction, reticulocytosis and unbalanced (hemo)globin chain synthesis resembling that of beta-thalassemia minor.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Anemia without thrombocytopenia, X-linked (XLAWT) [MIM:300835]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Contains 2 GATA-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
   DiseaseDisease mutation
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbasophil differentiation

Inferred from expression pattern PubMed 7678994. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

cell-cell signaling

Inferred from electronic annotation. Source: Ensembl

cellular response to thyroid hormone stimulus

Inferred from direct assay PubMed 19375645. Source: UniProtKB

dendritic cell differentiation

Inferred from electronic annotation. Source: Ensembl

embryonic hemopoiesis

Inferred from electronic annotation. Source: Ensembl

eosinophil differentiation

Inferred from expression pattern PubMed 8507862. Source: BHF-UCL

eosinophil fate commitment

Inferred from direct assay PubMed 12045236. Source: BHF-UCL

erythrocyte development

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

erythrocyte differentiation

Inferred from expression pattern PubMed 7678994. Source: BHF-UCL

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

megakaryocyte differentiation

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 17167422. Source: UniProtKB

negative regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from mutant phenotype PubMed 17167422. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of transcription regulatory region DNA binding

Inferred from direct assay PubMed 15920471. Source: BHF-UCL

platelet aggregation

Inferred from mutant phenotype PubMed 15701726. Source: BHF-UCL

platelet formation

Inferred from mutant phenotype Ref.11Ref.13PubMed 12483298. Source: BHF-UCL

positive regulation of erythrocyte differentiation

Inferred from mutant phenotype PubMed 17167422. Source: UniProtKB

positive regulation of osteoblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 15701726. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.14. Source: BHF-UCL

regulation of definitive erythrocyte differentiation

Inferred from direct assay Ref.14PubMed 15920471. Source: BHF-UCL

regulation of glycoprotein biosynthetic process

Inferred from mutant phenotype PubMed 15701726. Source: BHF-UCL

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 2467208. Source: BHF-UCL

transcriptional activation by promoter-enhancer looping

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17167422. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 15920471. Source: BHF-UCL

transcriptional repressor complex

Inferred from direct assay PubMed 15920471. Source: BHF-UCL

   Molecular_functionC2H2 zinc finger domain binding

Inferred from physical interaction PubMed 12483298. Source: BHF-UCL

DNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

DNA binding, bending

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 15920471. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 2467208. Source: BHF-UCL

RNA polymerase II transcription factor binding

Inferred from physical interaction Ref.13PubMed 15920471. Source: BHF-UCL

chromatin DNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

enhancer sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding

Inferred from mutant phenotype Ref.14. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 2467208. Source: BHF-UCL

transcription regulatory region sequence-specific DNA binding

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSPA1BP081075EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Erythroid transcription factor
PRO_0000083397

Regions

Zinc finger204 – 22825GATA-type 1
Zinc finger258 – 28225GATA-type 2
Region203 – 22220Required for interaction with ZFPM1

Amino acid modifications

Modified residue261Phosphoserine By similarity
Modified residue721Phosphoserine By similarity
Modified residue1421Phosphoserine Ref.8
Modified residue1781Phosphoserine By similarity
Modified residue1871Phosphoserine By similarity
Modified residue2331N6-acetyllysine; by EP300 Probable
Modified residue2451N6-acetyllysine; by EP300 Probable
Modified residue2461N6-acetyllysine; by CREBBP; alternate By similarity
Modified residue2461N6-acetyllysine; by EP300; alternate Probable
Modified residue2521N6-acetyllysine; by CREBBP By similarity
Modified residue3081N6-acetyllysine By similarity
Modified residue3101Phosphoserine By similarity
Modified residue3121N6-acetyllysine; by CREBBP By similarity
Modified residue3141N6-acetyllysine By similarity
Modified residue3151N6-acetyllysine By similarity
Cross-link137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8

Natural variations

Alternative sequence1 – 8383Missing in isoform 3.
VSP_041451
Alternative sequence290 – 413124QVNRP…APLSS → HQHYCGGSAQLMRAQSMASR GGVVSFSSCSQNSGQPKSLG PRHPLA in isoform 2.
VSP_014782
Natural variant2051V → M in XDAT; severe impairment of ZFPM1 binding and erythroid differentiation in vitro. Ref.11
VAR_010115
Natural variant2081G → S in XDAT; partially disrupts the interaction with ZFPM1. Ref.13
VAR_012706
Natural variant2161R → Q in XLTT; does not affect ZFPM1 binding; reduced affinity to palindromic GATA sites; supports erythroid maturation less efficiently than wild-type GATA1. Ref.14
VAR_033114
Natural variant2181D → G in XDAT; partially disrupts the interaction with ZFPM1. Ref.12
VAR_012707
Natural variant2181D → Y in XDAT; stronger loss of affinity than of G-218-GATA1 for ZFPM1 and disturbed GATA1 self-association. Ref.15
VAR_033115

Experimental info

Mutagenesis1371K → R: Abolishes sumoylation. Ref.8
Mutagenesis1421S → A: Loss of sumoylation. Ref.8
Mutagenesis1421S → D: Increased sumoylation in vitro. Ref.8
Mutagenesis2041C → R: Increase of dissociation rate from bound DNA. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 822BD2DE14B908AD

FASTA41342,751
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 9CE44220E09F69D7
Show »

FASTA33535,430
Isoform 3 (GATA-1s) [UniParc].

Checksum: E5ACD72BCBDB40B1
Show »

FASTA33034,232

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION (ISOFORM 3), SUBUNIT, TISSUE SPECIFICITY.
[6]"Regulation of activity of the transcription factor GATA-1 by acetylation."
Boyes J., Byfield P., Nakatani Y., Ogryzko V.
Nature 396:594-598(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EP300, ACETYLATION AT LYS-233; LYS-245 AND LYS-246.
[7]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN XLAWT.
[8]"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] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-137, PHOSPHORYLATION AT SER-142, MUTAGENESIS OF LYS-137 AND SER-142.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GFI1B.
[10]"Knockdown of ZNF268, which is transcriptionally downregulated by GATA-1, promotes proliferation of K562 cells."
Zeng Y., Wang W., Ma J., Wang X., Guo M., Li W.
PLoS ONE 7:E29518-E29518(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING.
[11]"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] [Europe PMC] [Abstract]
Cited for: VARIANT XDAT MET-205, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT XDAT MET-205, MUTAGENESIS OF CYS-204.
Tissue: Peripheral blood.
[12]"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] [Europe PMC] [Abstract]
Cited for: VARIANT XDAT GLY-218, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT XDAT GLY-218.
[13]"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] [Europe PMC] [Abstract]
Cited for: VARIANT XDAT SER-208, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT XDAT SER-208.
[14]"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] [Europe PMC] [Abstract]
Cited for: VARIANT XLTT GLN-216, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT XLTT GLN-216.
[15]"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] [Europe PMC] [Abstract]
Cited for: VARIANT XDAT TYR-218, INTERACTION WITH ZFPM1, CHARACTERIZATION OF VARIANT XDAT TYR-218.
+Additional computationally mapped references.

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.
PIRA34888.
RefSeqNP_002040.1. NM_002049.3.
UniGeneHs.765.

3D structure databases

ProteinModelPortalP15976.
SMRP15976. Positions 200-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108893. 44 interactions.
DIPDIP-41431N.
IntActP15976. 5 interactions.
MINTMINT-247486.
STRING9606.ENSP00000365858.

PTM databases

PhosphoSiteP15976.

Polymorphism databases

DMDM120956.

Proteomic databases

PaxDbP15976.
PRIDEP15976.

Protocols and materials databases

DNASU2623.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376670; ENSP00000365858; ENSG00000102145. [P15976-1]
ENST00000596667; ENSP00000469059; ENSG00000267841. [P15976-1]
GeneID2623.
KEGGhsa:2623.
UCSCuc004dkq.4. human. [P15976-1]

Organism-specific databases

CTD2623.
GeneCardsGC0XP048644.
HGNCHGNC:4170. GATA1.
HPACAB009195.
HPA000232.
HPA000233.
MIM300367. phenotype.
300835. phenotype.
305371. gene.
314050. phenotype.
neXtProtNX_P15976.
Orphanet86849. Acute basophilic leukemia.
231393. Beta-thalassemia - X-linked thrombocytopenia.
79277. Congenital erythropoietic porphyria.
67044. Thrombocytopenia with congenital dyserythropoietic anemia.
363727. X-linked dyserythropoetic anemia with abnormal platelets and neutropenia.
PharmGKBPA28584.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5641.
HOGENOMHOG000047701.
HOVERGENHBG051705.
InParanoidP15976.
KOK09182.
OMAPLLNCVE.
PhylomeDBP15976.
TreeFamTF315391.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
SignaLinkP15976.

Gene expression databases

ArrayExpressP15976.
BgeeP15976.
CleanExHS_GATA1.
GenevestigatorP15976.

Family and domain databases

Gene3D3.30.50.10. 2 hits.
InterProIPR016374. TF_GATA-1/2/3.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00320. GATA. 2 hits.
[Graphical view]
PIRSFPIRSF003027. TF_GATA-1/2/3. 1 hit.
PRINTSPR00619. GATAZNFINGER.
SMARTSM00401. ZnF_GATA. 2 hits.
[Graphical view]
PROSITEPS00344. GATA_ZN_FINGER_1. 2 hits.
PS50114. GATA_ZN_FINGER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGATA1.
GenomeRNAi2623.
NextBio10331.
PMAP-CutDBP15976.
PROP15976.
SOURCESearch...

Entry information

Entry nameGATA1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM