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P17679

- GATA1_MOUSE

UniProt

P17679 - GATA1_MOUSE

Protein

Erythroid transcription factor

Gene

Gata1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Aug 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.5 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

    1. chromatin binding Source: MGI
    2. chromatin DNA binding Source: UniProtKB
    3. DNA binding Source: MGI
    4. DNA binding, bending Source: MGI
    5. enhancer sequence-specific DNA binding Source: UniProtKB
    6. p53 binding Source: MGI
    7. protein binding Source: IntAct
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: MGI
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: Ensembl
    10. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    11. RNA polymerase II transcription factor binding Source: BHF-UCL
    12. sequence-specific DNA binding Source: MGI
    13. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
    14. zinc ion binding Source: InterPro

    GO - Biological processi

    1. basophil differentiation Source: Ensembl
    2. cell-cell signaling Source: MGI
    3. cell development Source: MGI
    4. cellular response to thyroid hormone stimulus Source: Ensembl
    5. dendritic cell differentiation Source: MGI
    6. embryonic hemopoiesis Source: MGI
    7. eosinophil fate commitment Source: Ensembl
    8. erythrocyte development Source: Ensembl
    9. erythrocyte differentiation Source: BHF-UCL
    10. in utero embryonic development Source: MGI
    11. male gonad development Source: Ensembl
    12. megakaryocyte differentiation Source: MGI
    13. myeloid cell differentiation Source: MGI
    14. negative regulation of apoptotic process Source: MGI
    15. negative regulation of bone mineralization Source: MGI
    16. negative regulation of cell proliferation Source: MGI
    17. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    18. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    19. negative regulation of transcription regulatory region DNA binding Source: Ensembl
    20. platelet aggregation Source: BHF-UCL
    21. platelet formation Source: MGI
    22. positive regulation of erythrocyte differentiation Source: Ensembl
    23. positive regulation of osteoblast proliferation Source: MGI
    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

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.

    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:Gf-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:95661. Gata1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nuclear membrane Source: Ensembl
    2. nucleolus Source: Ensembl
    3. nucleus Source: MGI
    4. transcriptional repressor complex Source: Ensembl
    5. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi26 – 261S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication
    Mutagenesisi49 – 491S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication
    Mutagenesisi72 – 721S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication
    Mutagenesisi137 – 1371K → R: Abolishes sumoylation. No change in PIAS4 binding nor on transcriptional activity. 1 Publication
    Mutagenesisi142 – 1421S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication
    Mutagenesisi178 – 1781S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication
    Mutagenesisi187 – 1871S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication
    Mutagenesisi203 – 2031E → V: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication
    Mutagenesisi204 – 2041C → R: Disrupts interaction with ZFPM1 and binding to DNA. 1 Publication
    Mutagenesisi205 – 2051V → G: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication
    Mutagenesisi205 – 2051V → M: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication
    Mutagenesisi207 – 2071C → G, R or W: Disrupts interaction with ZFPM1. 2 Publications
    Mutagenesisi207 – 2071C → P: Stability of binding to DNA reduced. 2 Publications
    Mutagenesisi208 – 2081G → E or V: Disrupts interaction with ZFPM1 and binding to DNA. 1 Publication
    Mutagenesisi218 – 2181D → G or V: No effect on interaction with ZFPM1. 1 Publication
    Mutagenesisi222 – 2221H → R: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication
    Mutagenesisi224 – 2241L → P: Disrupts interaction with ZFPM1 and binding to DNA. 1 Publication
    Mutagenesisi225 – 2251C → R, S or Y: Disrupts interaction with ZFPM1. 1 Publication
    Mutagenesisi228 – 2281C → R or S: Disrupts interaction with ZFPM1. 1 Publication
    Mutagenesisi230 – 2301L → F: Stability of binding to DNA reduced. 1 Publication
    Mutagenesisi233 – 2331K → E: No effect on interaction with ZFPM1. 1 Publication
    Mutagenesisi245 – 2462KK → AA: No effect on DNA binding. Reduces acetylation. Reduces ability to induce erythroid differentiation. Abrogates acetylation; when associated with 312-A--A-316. Abrogates ability to induce erythroid differentiation; when associated with 312-A--A-316. Reduces binding to CREBBP; when associated with 312-A--A-316. Disrupts stable association with chromatin; when associated with 312-A--A-316.
    Mutagenesisi245 – 2462KK → RR: No effect on DNA binding.
    Mutagenesisi261 – 2611C → P: Abolishes DNA-binding. 1 Publication
    Mutagenesisi284 – 2841L → F: Binds to DNA with reduced affinity. 1 Publication
    Mutagenesisi310 – 3101S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication
    Mutagenesisi312 – 3165KGKKK → AGAAA: No effect on DNA binding. Reduces acetylation. Reduces binding to CREBBP. Reduces ability to induce erythroid differentiation. Abrogates acetylation; when associated with 245-A-A-246. Abrogates ability to induce erythroid differentiation; when associated with 245-A-A-246. Reduces binding to CREBBP; when associated with 245-A-A-246. Disrupts stable association with chromatin; when associated with 245-A-A-246.
    Mutagenesisi312 – 3165KGKKK → RGRRR: No effect on DNA binding.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 413413Erythroid transcription factorPRO_0000083398Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei26 – 261Phosphoserine1 Publication
    Modified residuei49 – 491Phosphoserine1 Publication
    Modified residuei72 – 721Phosphoserine1 Publication
    Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei142 – 1421Phosphoserine1 Publication
    Modified residuei178 – 1781Phosphoserine1 Publication
    Modified residuei187 – 1871Phosphoserine1 Publication
    Modified residuei233 – 2331N6-acetyllysine; by EP300By similarity
    Modified residuei245 – 2451N6-acetyllysine; by EP300By similarity
    Modified residuei246 – 2461N6-acetyllysine; by CREBBP1 Publication
    Modified residuei246 – 2461N6-acetyllysine; by EP300By similarity
    Modified residuei252 – 2521N6-acetyllysine; by CREBBP1 Publication
    Modified residuei308 – 3081N6-acetyllysine1 Publication
    Modified residuei310 – 3101Phosphoserine1 Publication
    Modified residuei312 – 3121N6-acetyllysine; by CREBBP2 Publications
    Modified residuei314 – 3141N6-acetyllysine1 Publication
    Modified residuei315 – 3151N6-acetyllysine1 Publication

    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.2 Publications
    Acetylated on Lys-233, Lys-245 Lys-246 by EP300 By similarity. Acetylated on Lys-246, Lys-252 and Lys-312 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 similarity2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP17679.

    PTM databases

    PhosphoSiteiP17679.

    Expressioni

    Tissue specificityi

    Erythrocytes. Expressed (at protein level) in liver.2 Publications

    Developmental stagei

    Detected at 11.5-day fetal livers (at protein level). Isoform 2 detected earlier at 8.5-day embryo.1 Publication

    Gene expression databases

    BgeeiP17679.
    CleanExiMM_GATA1.
    GenevestigatoriP17679.

    Interactioni

    Subunit structurei

    May form homodimers or heterodimers with other isoforms. Interacts (via the N-terminal zinc finger) with ZFPM1 By similarity. 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 CREBBP; the interaction stimulates acetylation and transcriptional activity in vivo. Interacts with BRD3.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Lmo2P258015EBI-3903251,EBI-3903256

    Protein-protein interaction databases

    BioGridi199838. 22 interactions.
    DIPiDIP-40883N.
    IntActiP17679. 5 interactions.
    MINTiMINT-94735.
    STRINGi10090.ENSMUSP00000033502.

    Structurei

    Secondary structure

    1
    413
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni205 – 2073
    Helixi226 – 23510
    Turni259 – 2613
    Helixi280 – 28910
    Helixi295 – 2973

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GNFNMR-A200-243[»]
    1Y0JNMR-A200-243[»]
    2L5ENMR-B308-320[»]
    2L6YNMR-A200-238[»]
    2L6ZNMR-A200-238[»]
    3VD6X-ray1.98C200-318[»]
    3VEKX-ray2.63C/F200-318[»]
    ProteinModelPortaliP17679.
    SMRiP17679. Positions 200-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17679.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni203 – 22220Required for interaction with ZFPM1By similarityAdd
    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.

    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.
    GeneTreeiENSGT00750000117454.
    HOGENOMiHOG000047701.
    HOVERGENiHBG051705.
    InParanoidiP17679.
    KOiK09182.
    OMAiPLLNCVE.
    OrthoDBiEOG7CCBRF.
    PhylomeDBiP17679.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: P17679-1) [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

    MDFPGLGALG TSEPLPQFVD SALVSSPSDS TGFFSSGPEG LDAASSSTSP    50
    NAATAAASAL AYYREAEAYR HSPVFQVYPL LNSMEGIPGG SPYASWAYGK 100
    TALYPASTVC PSHEDAPSQA LEDQEGKSNN TFLDTLKTER LSPDLLTLGT 150
    ALPASLPVTG SAYGGADFPS PFFSPTGSPL SSAAYSSPKF HGSLPLAPCE 200
    ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP LIRPKKRMIV 250
    SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYFKLHQ VNRPLTMRKD 300
    GIQTRNRKAS GKGKKKRGSN LAGAGAAEGP AGGFMVVAGS SSSGNCGEVA 350
    SGLALGTAGT AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TTSFPTGPAP 400
    TTSSTSVIAP LSS 413
    Length:413
    Mass (Da):42,674
    Last modified:August 1, 1990 - v1
    Checksum:iBB627A92700D557A
    GO
    Isoform 2 (identifier: P17679-2) [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. Less effective than isoform 1 in its ability to transactivate target genes.

    Show »
    Length:330
    Mass (Da):34,188
    Checksum:i8BF1F251EB8E47A1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291D → G in AAH52653. (PubMed:15489334)Curated
    Sequence conflicti129 – 1291N → S in AAH52653. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8383Missing in isoform 2. CuratedVSP_041452Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15763 mRNA. Translation: CAA33769.1.
    AK146915 mRNA. Translation: BAE27527.1.
    AL670169 Genomic DNA. Translation: CAM17247.1.
    CH466638 Genomic DNA. Translation: EDL33938.1.
    X57530 Genomic DNA. Translation: CAA40751.1.
    BC052653 mRNA. Translation: AAH52653.1.
    CCDSiCCDS29981.1. [P17679-1]
    PIRiS04655.
    RefSeqiNP_032115.1. NM_008089.2. [P17679-1]
    UniGeneiMm.335973.

    Genome annotation databases

    EnsembliENSMUST00000033502; ENSMUSP00000033502; ENSMUSG00000031162. [P17679-1]
    GeneIDi14460.
    KEGGimmu:14460.
    UCSCiuc009snl.1. mouse. [P17679-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15763 mRNA. Translation: CAA33769.1 .
    AK146915 mRNA. Translation: BAE27527.1 .
    AL670169 Genomic DNA. Translation: CAM17247.1 .
    CH466638 Genomic DNA. Translation: EDL33938.1 .
    X57530 Genomic DNA. Translation: CAA40751.1 .
    BC052653 mRNA. Translation: AAH52653.1 .
    CCDSi CCDS29981.1. [P17679-1 ]
    PIRi S04655.
    RefSeqi NP_032115.1. NM_008089.2. [P17679-1 ]
    UniGenei Mm.335973.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GNF NMR - A 200-243 [» ]
    1Y0J NMR - A 200-243 [» ]
    2L5E NMR - B 308-320 [» ]
    2L6Y NMR - A 200-238 [» ]
    2L6Z NMR - A 200-238 [» ]
    3VD6 X-ray 1.98 C 200-318 [» ]
    3VEK X-ray 2.63 C/F 200-318 [» ]
    ProteinModelPortali P17679.
    SMRi P17679. Positions 200-310.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199838. 22 interactions.
    DIPi DIP-40883N.
    IntActi P17679. 5 interactions.
    MINTi MINT-94735.
    STRINGi 10090.ENSMUSP00000033502.

    PTM databases

    PhosphoSitei P17679.

    Proteomic databases

    PRIDEi P17679.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033502 ; ENSMUSP00000033502 ; ENSMUSG00000031162 . [P17679-1 ]
    GeneIDi 14460.
    KEGGi mmu:14460.
    UCSCi uc009snl.1. mouse. [P17679-1 ]

    Organism-specific databases

    CTDi 2623.
    MGIi MGI:95661. Gata1.

    Phylogenomic databases

    eggNOGi COG5641.
    GeneTreei ENSGT00750000117454.
    HOGENOMi HOG000047701.
    HOVERGENi HBG051705.
    InParanoidi P17679.
    KOi K09182.
    OMAi PLLNCVE.
    OrthoDBi EOG7CCBRF.
    PhylomeDBi P17679.
    TreeFami TF315391.

    Enzyme and pathway databases

    Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    EvolutionaryTracei P17679.
    NextBioi 286092.
    PROi P17679.
    SOURCEi Search...

    Gene expression databases

    Bgeei P17679.
    CleanExi MM_GATA1.
    Genevestigatori P17679.

    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. "Cloning of cDNA for the major DNA-binding protein of the erythroid lineage through expression in mammalian cells."
      Tsai S.-F., Martin D.I.K., Zon L.I., D'Andrea A.D., Wong G.W., Orkin S.H.
      Nature 339:446-451(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
      Tissue: Erythrocyte.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Strain: C57BL/6NCr.
      Tissue: Hematopoietic stem cell.
    6. Todokoro K., Chiba T., Kuramochi S., Ikawa Y.
      Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
      Strain: BALB/c.
    7. "Bromodomain protein Brd3 associates with acetylated GATA1 to promote its chromatin occupancy at erythroid target genes."
      Lamonica J.M., Deng W., Kadauke S., Campbell A.E., Gamsjaeger R., Wang H., Cheng Y., Billin A.N., Hardison R.C., Mackay J.P., Blobel G.A.
      Proc. Natl. Acad. Sci. U.S.A. 108:E159-E168(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH BRD3, ACETYLATION AT LYS-308; LYS-312; LYS-314 AND LYS-315, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Transcriptional activation and DNA binding by the erythroid factor GF-1/NF-E1/Eryf 1."
      Martin D.I.K., Orkin S.H.
      Genes Dev. 4:1886-1898(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ZINC-FINGERS, MUTAGENESIS OF CYS-207; LEU-230; CYS-261 AND LEU-284.
    9. "Phosphorylation of the erythroid transcription factor GATA-1."
      Crossley M., Orkin S.H.
      J. Biol. Chem. 269:16589-16596(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-26; SER-49; SER-72; SER-142; SER-178; SER-187 AND SER-310, FUNCTION, MUTAGENESIS OF SER-26; SER-49; SER-72; SER-142; SER-178; SER-187 AND SER-310.
    10. "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 2), FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    11. "Use of altered specificity mutants to probe a specific protein-protein interaction in differentiation: the GATA-1:FOG complex."
      Crispino J.D., Lodish M.B., MacKay J.P., Orkin S.H.
      Mol. Cell 3:219-228(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-203; CYS-204; VAL-205; CYS-207; GLY-208; ASP-218; HIS-222; LEU-224; CYS-225; CYS-228 AND LYS-233.
    12. "CREB-Binding protein acetylates hematopoietic transcription factor GATA-1 at functionally important sites."
      Hung H.L., Lau J., Kim A.Y., Weiss M.J., Blobel G.A.
      Mol. Cell. Biol. 19:3496-3505(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CREBBP, ACETYLATION AT LYS-246; LYS-252 AND LYS-312, MUTAGENESIS OF 245-LYS-LYS-246 AND 312-LYS--LYS-316.
    13. Cited for: SUMOYLATION AT LYS-137, INTERACTION WITH PIAS4, FUNCTION, MUTAGENESIS OF LYS-137.
    14. "GATA-1 forms distinct activating and repressive complexes in erythroid cells."
      Rodriguez P., Bonte E., Krijgsveld J., Kolodziej K.E., Guyot B., Heck A.J.R., Vyas P., de Boer E., Grosveld F., Strouboulis J.
      EMBO J. 24:2354-2366(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GFI1B.
    15. "LMCD1/Dyxin is a novel transcriptional cofactor that restricts GATA6 function by inhibiting DNA binding."
      Rath N., Wang Z., Lu M.M., Morrisey E.E.
      Mol. Cell. Biol. 25:8864-8873(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LMCD1.
    16. "Acetylation of GATA-1 is required for chromatin occupancy."
      Lamonica J.M., Vakoc C.R., Blobel G.A.
      Blood 108:3736-3738(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 245-LYS-LYS-246 AND 312-LYS--LYS-316.
    17. "The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG."
      Kowalski K., Czolij R., King G.F., Crossley M., Mackay J.P.
      J. Biomol. NMR 13:249-262(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 200-243.
    18. "Structural basis and specificity of acetylated transcription factor GATA1 recognition by BET family bromodomain protein Brd3."
      Gamsjaeger R., Webb S.R., Lamonica J.M., Billin A., Blobel G.A., Mackay J.P.
      Mol. Cell. Biol. 31:2632-2640(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 308-320 IN COMPLEX WITH BRD3, INTERACTION WITH BRD3.

    Entry informationi

    Entry nameiGATA1_MOUSE
    AccessioniPrimary (citable) accession number: P17679
    Secondary accession number(s): Q3UIH9, Q7TMX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3