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P15976

- GATA1_HUMAN

UniProt

P15976 - GATA1_HUMAN

Protein

Erythroid transcription factor

Gene

GATA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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.1 Publication

    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

    1. C2H2 zinc finger domain binding Source: BHF-UCL
    2. chromatin DNA binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. DNA binding, bending Source: Ensembl
    5. enhancer sequence-specific DNA binding Source: Ensembl
    6. protein binding Source: UniProtKB
    7. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
    10. RNA polymerase II regulatory region sequence-specific DNA binding Source: BHF-UCL
    11. RNA polymerase II transcription factor binding Source: BHF-UCL
    12. sequence-specific DNA binding Source: BHF-UCL
    13. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    14. transcription regulatory region sequence-specific DNA binding Source: BHF-UCL
    15. zinc ion binding Source: InterPro

    GO - Biological processi

    1. basophil differentiation Source: BHF-UCL
    2. blood coagulation Source: Reactome
    3. cell-cell signaling Source: Ensembl
    4. cellular response to thyroid hormone stimulus Source: UniProtKB
    5. dendritic cell differentiation Source: Ensembl
    6. embryonic hemopoiesis Source: Ensembl
    7. eosinophil differentiation Source: BHF-UCL
    8. eosinophil fate commitment Source: BHF-UCL
    9. erythrocyte development Source: BHF-UCL
    10. erythrocyte differentiation Source: BHF-UCL
    11. in utero embryonic development Source: Ensembl
    12. male gonad development Source: BHF-UCL
    13. megakaryocyte differentiation Source: BHF-UCL
    14. negative regulation of apoptotic process Source: UniProtKB
    15. negative regulation of bone mineralization Source: Ensembl
    16. negative regulation of cell proliferation Source: Ensembl
    17. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
    18. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    19. negative regulation of transcription regulatory region DNA binding Source: BHF-UCL
    20. platelet aggregation Source: BHF-UCL
    21. platelet formation Source: BHF-UCL
    22. positive regulation of erythrocyte differentiation Source: UniProtKB
    23. positive regulation of osteoblast proliferation Source: Ensembl
    24. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    25. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    26. regulation of definitive erythrocyte differentiation Source: BHF-UCL
    27. regulation of glycoprotein biosynthetic process Source: BHF-UCL
    28. transcriptional activation by promoter-enhancer looping Source: BHF-UCL
    29. transcription from RNA polymerase II promoter Source: BHF-UCL

    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: Chromosome X

    Organism-specific databases

    HGNCiHGNC:4170. GATA1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: UniProtKB
    3. transcriptional repressor complex Source: BHF-UCL
    4. transcription factor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    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.
    79277. Congenital erythropoietic porphyria.
    67044. Thrombocytopenia with congenital dyserythropoietic anemia.
    363727. X-linked dyserythropoetic anemia with abnormal platelets and neutropenia.
    PharmGKBiPA28584.

    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

    ArrayExpressiP15976.
    BgeeiP15976.
    CleanExiHS_GATA1.
    GenevestigatoriP15976.

    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.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSPA1BP081075EBI-3909284,EBI-629985

    Protein-protein interaction databases

    BioGridi108893. 44 interactions.
    DIPiDIP-41431N.
    IntActiP15976. 6 interactions.
    MINTiMINT-247486.
    STRINGi9606.ENSP00000365858.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni203 – 22220Required for interaction with ZFPM1Add
    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.
    HOGENOMiHOG000047701.
    HOVERGENiHBG051705.
    InParanoidiP15976.
    KOiK09182.
    OMAiPLLNCVE.
    PhylomeDBiP15976.
    TreeFamiTF315391.

    Family and domain databases

    Gene3Di3.30.50.10. 2 hits.
    InterProiIPR029524. GATA-1.
    IPR016374. TF_GATA-1/2/3.
    IPR000679. Znf_GATA.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PANTHERiPTHR10071:SF150. PTHR10071:SF150. 1 hit.
    PfamiPF00320. GATA. 2 hits.
    [Graphical view]
    PIRSFiPIRSF003027. TF_GATA-1/2/3. 1 hit.
    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. Align

    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

    MEFPGLGSLG TSEPLPQFVD PALVSSTPES GVFFPSGPEG LDAAASSTAP    50
    STATAAAAAL AYYRDAEAYR HSPVFQVYPL LNCMEGIPGG SPYAGWAYGK 100
    TGLYPASTVC PTREDSPPQA VEDLDGKGST SFLETLKTER LSPDLLTLGP 150
    ALPSSLPVPN SAYGGPDFSS TFFSPTGSPL NSAAYSSPKL RGTLPLPPCE 200
    ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP LIRPKKRLIV 250
    SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYYKLHQ VNRPLTMRKD 300
    GIQTRNRKAS GKGKKKRGSS LGGTGAAEGP AGGFMVVAGG SGSGNCGEVA 350
    SGLTLGPPGT AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TGSFPTGPMP 400
    PTTSTTVVAP LSS 413
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi120956.

    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17254 mRNA. Translation: CAA35120.1 .
    M30601 mRNA. Translation: AAA35885.1 .
    AF196971 Genomic DNA. No translation available.
    BC009797 mRNA. Translation: AAH09797.1 .
    CCDSi CCDS14305.1. [P15976-1 ]
    PIRi A34888.
    RefSeqi NP_002040.1. NM_002049.3. [P15976-1 ]
    UniGenei Hs.765.

    3D structure databases

    ProteinModelPortali P15976.
    SMRi P15976. Positions 200-310.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108893. 44 interactions.
    DIPi DIP-41431N.
    IntActi P15976. 6 interactions.
    MINTi MINT-247486.
    STRINGi 9606.ENSP00000365858.

    PTM databases

    PhosphoSitei P15976.

    Polymorphism databases

    DMDMi 120956.

    Proteomic databases

    MaxQBi P15976.
    PaxDbi P15976.
    PRIDEi P15976.

    Protocols and materials databases

    DNASUi 2623.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376670 ; ENSP00000365858 ; ENSG00000102145 . [P15976-1 ]
    GeneIDi 2623.
    KEGGi hsa:2623.
    UCSCi uc004dkq.4. human. [P15976-1 ]

    Organism-specific databases

    CTDi 2623.
    GeneCardsi GC0XP048644.
    GeneReviewsi GATA1.
    HGNCi HGNC:4170. GATA1.
    HPAi CAB009195.
    HPA000232.
    HPA000233.
    MIMi 300367. phenotype.
    300835. phenotype.
    305371. gene.
    314050. phenotype.
    neXtProti NX_P15976.
    Orphaneti 86849. 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.
    PharmGKBi PA28584.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5641.
    HOGENOMi HOG000047701.
    HOVERGENi HBG051705.
    InParanoidi P15976.
    KOi K09182.
    OMAi PLLNCVE.
    PhylomeDBi P15976.
    TreeFami TF315391.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.
    SignaLinki P15976.

    Miscellaneous databases

    GeneWikii GATA1.
    GenomeRNAii 2623.
    NextBioi 10331.
    PMAP-CutDB P15976.
    PROi P15976.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15976.
    Bgeei P15976.
    CleanExi HS_GATA1.
    Genevestigatori P15976.

    Family and domain databases

    Gene3Di 3.30.50.10. 2 hits.
    InterProi IPR029524. GATA-1.
    IPR016374. TF_GATA-1/2/3.
    IPR000679. Znf_GATA.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    PANTHERi PTHR10071:SF150. PTHR10071:SF150. 1 hit.
    Pfami PF00320. GATA. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF003027. TF_GATA-1/2/3. 1 hit.
    PRINTSi PR00619. GATAZNFINGER.
    SMARTi SM00401. ZnF_GATA. 2 hits.
    [Graphical view ]
    PROSITEi PS00344. GATA_ZN_FINGER_1. 2 hits.
    PS50114. GATA_ZN_FINGER_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.

    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: October 1, 2014
    This is version 159 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