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Protein

Erythroid transcription factor

Gene

GATA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS (PubMed:24245781).2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri204 – 22825GATA-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri258 – 28225GATA-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • basophil differentiation Source: BHF-UCL
  • blood coagulation Source: Reactome
  • cell-cell signaling Source: Ensembl
  • cellular response to thyroid hormone stimulus Source: UniProtKB
  • dendritic cell differentiation Source: Ensembl
  • embryonic hemopoiesis Source: Ensembl
  • eosinophil differentiation Source: BHF-UCL
  • eosinophil fate commitment Source: BHF-UCL
  • erythrocyte development Source: BHF-UCL
  • erythrocyte differentiation Source: BHF-UCL
  • in utero embryonic development Source: Ensembl
  • male gonad development Source: BHF-UCL
  • megakaryocyte differentiation Source: BHF-UCL
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of bone mineralization Source: Ensembl
  • negative regulation of cell proliferation Source: Ensembl
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of transcription regulatory region DNA binding Source: BHF-UCL
  • platelet aggregation Source: BHF-UCL
  • platelet formation Source: BHF-UCL
  • positive regulation of erythrocyte differentiation Source: UniProtKB
  • positive regulation of osteoblast proliferation Source: Ensembl
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of definitive erythrocyte differentiation Source: BHF-UCL
  • regulation of glycoprotein biosynthetic process Source: BHF-UCL
  • transcriptional activation by promoter-enhancer looping Source: BHF-UCL
  • transcription from RNA polymerase II promoter Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP15976.

Names & Taxonomyi

Protein namesi
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 namesi
Name:GATA1
Synonyms:ERYF1, GF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:4170. GATA1.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • transcriptional repressor complex Source: BHF-UCL
  • transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

X-linked dyserythropoietic anemia and thrombocytopenia (XDAT)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionDisorder characterized by erythrocytes with abnormal size and shape, and paucity of platelets in peripheral blood. The bone marrow contains abundant and abnormally small megakaryocytes.

See also OMIM:300367
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti205 – 2051V → M in XDAT; severe impairment of ZFPM1 binding and erythroid differentiation in vitro. 1 Publication
VAR_010115
Natural varianti208 – 2081G → S in XDAT; partially disrupts the interaction with ZFPM1. 1 Publication
VAR_012706
Natural varianti218 – 2181D → G in XDAT; partially disrupts the interaction with ZFPM1. 1 Publication
VAR_012707
Natural varianti218 – 2181D → Y in XDAT; stronger loss of affinity than of G-218-GATA1 for ZFPM1 and disturbed GATA1 self-association. 1 Publication
VAR_033115
Thrombocytopenia with beta-thalassemia, X-linked (XLTT)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:314050
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti216 – 2161R → Q in XLTT; does not affect ZFPM1 binding; reduced affinity to palindromic GATA sites; supports erythroid maturation less efficiently than wild-type GATA1. 1 Publication
VAR_033114
Anemia without thrombocytopenia, X-linked (XLAWT)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:300835

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi137 – 1371K → R: Abolishes sumoylation. 1 Publication
Mutagenesisi142 – 1421S → A: Loss of sumoylation. 1 Publication
Mutagenesisi142 – 1421S → D: Increased sumoylation in vitro. 1 Publication
Mutagenesisi204 – 2041C → R: Increase of dissociation rate from bound DNA. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi300367. phenotype.
300835. phenotype.
314050. phenotype.
Orphaneti86849. Acute basophilic leukemia.
231393. Beta-thalassemia - X-linked thrombocytopenia.
124. Blackfan-Diamond anemia.
79277. Congenital erythropoietic porphyria.
67044. Thrombocytopenia with congenital dyserythropoietic anemia.
363727. X-linked dyserythropoetic anemia with abnormal platelets and neutropenia.
PharmGKBiPA28584.

Polymorphism and mutation databases

BioMutaiGATA1.
DMDMi120956.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 413413Erythroid transcription factorPRO_0000083397Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei72 – 721PhosphoserineBy similarity
Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei142 – 1421Phosphoserine1 Publication
Modified residuei178 – 1781PhosphoserineBy similarity
Modified residuei187 – 1871PhosphoserineBy similarity
Modified residuei233 – 2331N6-acetyllysine; by EP3001 Publication
Modified residuei245 – 2451N6-acetyllysine; by EP3001 Publication
Modified residuei246 – 2461N6-acetyllysine; by CREBBP; alternateBy similarity
Modified residuei246 – 2461N6-acetyllysine; by EP300; alternate1 Publication
Modified residuei252 – 2521N6-acetyllysine; by CREBBPBy similarity
Modified residuei308 – 3081N6-acetyllysineBy similarity
Modified residuei310 – 3101PhosphoserineBy similarity
Modified residuei312 – 3121N6-acetyllysine; by CREBBPBy similarity
Modified residuei314 – 3141N6-acetyllysineBy similarity
Modified residuei315 – 3151N6-acetyllysineBy similarity

Post-translational modificationi

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).By similarity
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).By similarity
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.By similarity1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP15976.
PaxDbiP15976.
PRIDEiP15976.

PTM databases

PhosphoSiteiP15976.

Miscellaneous databases

PMAP-CutDBP15976.

Expressioni

Tissue specificityi

Erythrocytes.1 Publication

Gene expression databases

BgeeiP15976.
CleanExiHS_GATA1.
ExpressionAtlasiP15976. baseline and differential.
GenevisibleiP15976. HS.

Organism-specific databases

HPAiCAB009195.
HPA000232.
HPA000233.

Interactioni

Subunit structurei

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. Interacts with MED1, CCAR1 and CALCOCO1.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC24Q8N4L83EBI-3909284,EBI-1104933
FBF1Q8TES7-63EBI-3909284,EBI-10244131
FRS3O435593EBI-3909284,EBI-725515
HEXIM2Q96MH23EBI-3909284,EBI-5460660
HOXA1P496393EBI-3909284,EBI-740785
HSPA1BP081075EBI-3909284,EBI-629985
KRTAP10-5P603703EBI-3909284,EBI-10172150
KRTAP9-2Q9BYQ43EBI-3909284,EBI-1044640
PRKAB2O437413EBI-3909284,EBI-1053424
RADILQ96JH83EBI-3909284,EBI-744267

Protein-protein interaction databases

BioGridi108893. 56 interactions.
DIPiDIP-41431N.
IntActiP15976. 17 interactions.
MINTiMINT-247486.

Structurei

3D structure databases

ProteinModelPortaliP15976.
SMRiP15976. Positions 200-310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 330131Interaction with MED1 and CCAR11 PublicationAdd
BLAST
Regioni203 – 22220Required for interaction with ZFPM1Add
BLAST
Regioni249 – 31567Interaction with CALCOCO11 PublicationAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Contains 2 GATA-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri204 – 22825GATA-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri258 – 28225GATA-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5641.
GeneTreeiENSGT00760000119221.
HOGENOMiHOG000047701.
HOVERGENiHBG051705.
InParanoidiP15976.
KOiK09182.
OMAiTPCEARE.
PhylomeDBiP15976.
TreeFamiTF315391.

Family and domain databases

Gene3Di3.30.50.10. 2 hits.
InterProiIPR029524. GATA-1.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PANTHERiPTHR10071:SF150. PTHR10071:SF150. 1 hit.
PfamiPF00320. GATA. 2 hits.
[Graphical view]
PRINTSiPR00619. GATAZNFINGER.
SMARTiSM00401. ZnF_GATA. 2 hits.
[Graphical view]
PROSITEiPS00344. GATA_ZN_FINGER_1. 2 hits.
PS50114. GATA_ZN_FINGER_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P15976-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEFPGLGSLG TSEPLPQFVD PALVSSTPES GVFFPSGPEG LDAAASSTAP
60 70 80 90 100
STATAAAAAL AYYRDAEAYR HSPVFQVYPL LNCMEGIPGG SPYAGWAYGK
110 120 130 140 150
TGLYPASTVC PTREDSPPQA VEDLDGKGST SFLETLKTER LSPDLLTLGP
160 170 180 190 200
ALPSSLPVPN SAYGGPDFSS TFFSPTGSPL NSAAYSSPKL RGTLPLPPCE
210 220 230 240 250
ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP LIRPKKRLIV
260 270 280 290 300
SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYYKLHQ VNRPLTMRKD
310 320 330 340 350
GIQTRNRKAS GKGKKKRGSS LGGTGAAEGP AGGFMVVAGG SGSGNCGEVA
360 370 380 390 400
SGLTLGPPGT AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TGSFPTGPMP
410
PTTSTTVVAP LSS
Length:413
Mass (Da):42,751
Last modified:April 1, 1990 - v1
Checksum:i822BD2DE14B908AD
GO
Isoform 2 (identifier: P15976-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:335
Mass (Da):35,430
Checksum:i9CE44220E09F69D7
GO
Isoform 3 (identifier: P15976-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:330
Mass (Da):34,232
Checksum:iE5ACD72BCBDB40B1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti205 – 2051V → M in XDAT; severe impairment of ZFPM1 binding and erythroid differentiation in vitro. 1 Publication
VAR_010115
Natural varianti208 – 2081G → S in XDAT; partially disrupts the interaction with ZFPM1. 1 Publication
VAR_012706
Natural varianti216 – 2161R → Q in XLTT; does not affect ZFPM1 binding; reduced affinity to palindromic GATA sites; supports erythroid maturation less efficiently than wild-type GATA1. 1 Publication
VAR_033114
Natural varianti218 – 2181D → G in XDAT; partially disrupts the interaction with ZFPM1. 1 Publication
VAR_012707
Natural varianti218 – 2181D → Y in XDAT; stronger loss of affinity than of G-218-GATA1 for ZFPM1 and disturbed GATA1 self-association. 1 Publication
VAR_033115

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8383Missing in isoform 3. CuratedVSP_041451Add
BLAST
Alternative sequencei290 – 413124QVNRP…APLSS → HQHYCGGSAQLMRAQSMASR GGVVSFSSCSQNSGQPKSLG PRHPLA in isoform 2. 1 PublicationVSP_014782Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17254 mRNA. Translation: CAA35120.1.
M30601 mRNA. Translation: AAA35885.1.
AF196971 Genomic DNA. No translation available.
BC009797 mRNA. Translation: AAH09797.1.
CCDSiCCDS14305.1. [P15976-1]
PIRiA34888.
RefSeqiNP_002040.1. NM_002049.3. [P15976-1]
UniGeneiHs.765.

Genome annotation databases

EnsembliENST00000376670; ENSP00000365858; ENSG00000102145. [P15976-1]
GeneIDi2623.
KEGGihsa:2623.
UCSCiuc004dkq.4. human. [P15976-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17254 mRNA. Translation: CAA35120.1.
M30601 mRNA. Translation: AAA35885.1.
AF196971 Genomic DNA. No translation available.
BC009797 mRNA. Translation: AAH09797.1.
CCDSiCCDS14305.1. [P15976-1]
PIRiA34888.
RefSeqiNP_002040.1. NM_002049.3. [P15976-1]
UniGeneiHs.765.

3D structure databases

ProteinModelPortaliP15976.
SMRiP15976. Positions 200-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108893. 56 interactions.
DIPiDIP-41431N.
IntActiP15976. 17 interactions.
MINTiMINT-247486.

PTM databases

PhosphoSiteiP15976.

Polymorphism and mutation databases

BioMutaiGATA1.
DMDMi120956.

Proteomic databases

MaxQBiP15976.
PaxDbiP15976.
PRIDEiP15976.

Protocols and materials databases

DNASUi2623.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376670; ENSP00000365858; ENSG00000102145. [P15976-1]
GeneIDi2623.
KEGGihsa:2623.
UCSCiuc004dkq.4. human. [P15976-1]

Organism-specific databases

CTDi2623.
GeneCardsiGC0XP048644.
GeneReviewsiGATA1.
HGNCiHGNC:4170. GATA1.
HPAiCAB009195.
HPA000232.
HPA000233.
MIMi300367. phenotype.
300835. phenotype.
305371. gene.
314050. phenotype.
neXtProtiNX_P15976.
Orphaneti86849. Acute basophilic leukemia.
231393. Beta-thalassemia - X-linked thrombocytopenia.
124. Blackfan-Diamond anemia.
79277. Congenital erythropoietic porphyria.
67044. Thrombocytopenia with congenital dyserythropoietic anemia.
363727. X-linked dyserythropoetic anemia with abnormal platelets and neutropenia.
PharmGKBiPA28584.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5641.
GeneTreeiENSGT00760000119221.
HOGENOMiHOG000047701.
HOVERGENiHBG051705.
InParanoidiP15976.
KOiK09182.
OMAiTPCEARE.
PhylomeDBiP15976.
TreeFamiTF315391.

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP15976.

Miscellaneous databases

ChiTaRSiGATA1. human.
GeneWikiiGATA1.
GenomeRNAii2623.
NextBioi10331.
PMAP-CutDBP15976.
PROiP15976.
SOURCEiSearch...

Gene expression databases

BgeeiP15976.
CleanExiHS_GATA1.
ExpressionAtlasiP15976. baseline and differential.
GenevisibleiP15976. HS.

Family and domain databases

Gene3Di3.30.50.10. 2 hits.
InterProiIPR029524. GATA-1.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PANTHERiPTHR10071:SF150. PTHR10071:SF150. 1 hit.
PfamiPF00320. GATA. 2 hits.
[Graphical view]
PRINTSiPR00619. GATAZNFINGER.
SMARTiSM00401. ZnF_GATA. 2 hits.
[Graphical view]
PROSITEiPS00344. GATA_ZN_FINGER_1. 2 hits.
PS50114. GATA_ZN_FINGER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. "CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel pathway for GATA1 function."
    Mizuta S., Minami T., Fujita H., Kaminaga C., Matsui K., Ishino R., Fujita A., Oda K., Kawai A., Hasegawa N., Urahama N., Roeder R.G., Ito M.
    Genes Cells 19:28-51(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MED1; CCAR1 AND CALCOCO1.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.

Entry informationi

Entry nameiGATA1_HUMAN
AccessioniPrimary (citable) accession number: P15976
Secondary accession number(s): Q96GB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 24, 2015
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.