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P17679 (GATA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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:Gf-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.8 Ref.9 Ref.10 Ref.13 Ref.16

Subunit structure

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. Ref.7 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18

Subcellular location

Nucleus Ref.16.

Tissue specificity

Erythrocytes. Expressed (at protein level) in liver. Ref.1 Ref.10

Developmental stage

Detected at 11.5-day fetal livers (at protein level). Isoform 2 detected earlier at 8.5-day embryo. Ref.10

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.

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.9

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. Ref.13

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. Ref.7 Ref.12

Sequence similarities

Contains 2 GATA-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative initiation
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbasophil differentiation

Inferred from electronic annotation. Source: Ensembl

cell development

Inferred from mutant phenotype PubMed 9233806. Source: MGI

cell-cell signaling

Inferred from mutant phenotype PubMed 15005853. Source: MGI

cellular response to thyroid hormone stimulus

Inferred from electronic annotation. Source: Ensembl

dendritic cell differentiation

Inferred from direct assay PubMed 17505015. Source: MGI

embryonic hemopoiesis

Inferred from mutant phenotype PubMed 9576834. Source: MGI

eosinophil fate commitment

Inferred from electronic annotation. Source: Ensembl

erythrocyte development

Inferred from electronic annotation. Source: Ensembl

erythrocyte differentiation

Inferred from direct assay PubMed 9427697. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 9576834. Source: MGI

male gonad development

Inferred from electronic annotation. Source: Ensembl

megakaryocyte differentiation

Inferred from direct assay PubMed 9427697. Source: MGI

myeloid cell differentiation

Inferred from mutant phenotype PubMed 8901585PubMed 9139715. Source: MGI

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of bone mineralization

Inferred from mutant phenotype PubMed 15005853. Source: MGI

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 9233806. Source: MGI

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17505015. Source: MGI

negative regulation of transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

platelet aggregation

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

platelet formation

Inferred from electronic annotation. Source: Ensembl

positive regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast proliferation

Inferred from mutant phenotype PubMed 15005853. Source: MGI

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 PubMed 12200364. Source: BHF-UCL

regulation of definitive erythrocyte differentiation

Inferred from direct assay PubMed 12200364. 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 Ref.10. Source: GOC

transcriptional activation by promoter-enhancer looping

Inferred from direct assay PubMed 15644435. Source: BHF-UCL

   Cellular_componentnuclear membrane

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 15613485PubMed 17505015PubMed 7924983Ref.10PubMed 9787185. Source: MGI

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

transcriptional repressor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from direct assay PubMed 10773455PubMed 12023274PubMed 15613485. Source: MGI

DNA binding, bending

Inferred from direct assay PubMed 21436399. Source: MGI

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

Inferred from direct assay PubMed 7896801. Source: MGI

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

Inferred from electronic annotation. Source: Ensembl

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

Inferred from direct assay PubMed 19398553PubMed 8195185PubMed 9230307PubMed 9427697. Source: MGI

RNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 18063754. Source: BHF-UCL

chromatin DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 17505015PubMed 19011221. Source: MGI

enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 20855530. Source: UniProtKB

p53 binding

Inferred from physical interaction PubMed 19411634. Source: MGI

sequence-specific DNA binding

Inferred from direct assay PubMed 8195185Ref.10PubMed 9787185. Source: MGI

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay Ref.10. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Lmo2P258015EBI-3903251,EBI-3903256

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P17679-1)

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: P17679-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Erythroid transcription factor
PRO_0000083398

Regions

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

Amino acid modifications

Modified residue261Phosphoserine Ref.9
Modified residue491Phosphoserine Ref.9
Modified residue721Phosphoserine Ref.9
Modified residue1421Phosphoserine Ref.9
Modified residue1781Phosphoserine Ref.9
Modified residue1871Phosphoserine
Modified residue2331N6-acetyllysine; by EP300 By similarity
Modified residue2451N6-acetyllysine; by EP300 By similarity
Modified residue2461N6-acetyllysine; by CREBBP Ref.12
Modified residue2461N6-acetyllysine; by EP300 By similarity
Modified residue2521N6-acetyllysine; by CREBBP Ref.12
Modified residue3081N6-acetyllysine Ref.7
Modified residue3101Phosphoserine Ref.9
Modified residue3121N6-acetyllysine; by CREBBP Ref.7 Ref.12
Modified residue3141N6-acetyllysine Ref.7
Modified residue3151N6-acetyllysine Ref.7
Cross-link137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Natural variations

Alternative sequence1 – 8383Missing in isoform 2.
VSP_041452

Experimental info

Mutagenesis261S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9
Mutagenesis491S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9
Mutagenesis721S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9
Mutagenesis1371K → R: Abolishes sumoylation. No change in PIAS4 binding nor on transcriptional activity. Ref.13
Mutagenesis1421S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9
Mutagenesis1781S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9
Mutagenesis1871S → A: Loss of phosphorylation of the chymotryptic peptide.
Mutagenesis2031E → V: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.11
Mutagenesis2041C → R: Disrupts interaction with ZFPM1 and binding to DNA. Ref.11
Mutagenesis2051V → G: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.11
Mutagenesis2051V → M: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.11
Mutagenesis2071C → G, R or W: Disrupts interaction with ZFPM1. Ref.8 Ref.11
Mutagenesis2071C → P: Stability of binding to DNA reduced. Ref.8 Ref.11
Mutagenesis2081G → E or V: Disrupts interaction with ZFPM1 and binding to DNA. Ref.11
Mutagenesis2181D → G or V: No effect on interaction with ZFPM1. Ref.11
Mutagenesis2221H → R: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.11
Mutagenesis2241L → P: Disrupts interaction with ZFPM1 and binding to DNA. Ref.11
Mutagenesis2251C → R, S or Y: Disrupts interaction with ZFPM1. Ref.11
Mutagenesis2281C → R or S: Disrupts interaction with ZFPM1. Ref.11
Mutagenesis2301L → F: Stability of binding to DNA reduced. Ref.8
Mutagenesis2331K → E: No effect on interaction with ZFPM1. Ref.11
Mutagenesis245 – 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.
Mutagenesis245 – 2462KK → RR: No effect on DNA binding.
Mutagenesis2611C → P: Abolishes DNA-binding. Ref.8
Mutagenesis2841L → F: Binds to DNA with reduced affinity. Ref.8
Mutagenesis3101S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.9
Mutagenesis312 – 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. Ref.12 Ref.16
Mutagenesis312 – 3165KGKKK → RGRRR: No effect on DNA binding. Ref.12 Ref.16
Sequence conflict291D → G in AAH52653. Ref.5
Sequence conflict1291N → S in AAH52653. Ref.5

Secondary structure

........... 413
Helix Strand Turn

Details...

Sequences

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

Last modified August 1, 1990. Version 1.
Checksum: BB627A92700D557A

FASTA41342,674
        10         20         30         40         50         60 
MDFPGLGALG TSEPLPQFVD SALVSSPSDS TGFFSSGPEG LDAASSSTSP NAATAAASAL 

        70         80         90        100        110        120 
AYYREAEAYR HSPVFQVYPL LNSMEGIPGG SPYASWAYGK TALYPASTVC PSHEDAPSQA 

       130        140        150        160        170        180 
LEDQEGKSNN TFLDTLKTER LSPDLLTLGT ALPASLPVTG SAYGGADFPS PFFSPTGSPL 

       190        200        210        220        230        240 
SSAAYSSPKF HGSLPLAPCE ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP 

       250        260        270        280        290        300 
LIRPKKRMIV SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYFKLHQ VNRPLTMRKD 

       310        320        330        340        350        360 
GIQTRNRKAS GKGKKKRGSN LAGAGAAEGP AGGFMVVAGS SSSGNCGEVA SGLALGTAGT 

       370        380        390        400        410 
AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TTSFPTGPAP TTSSTSVIAP LSS 

« Hide

Isoform 2 (GATA-1s) [UniParc].

Checksum: 8BF1F251EB8E47A1
Show »

FASTA33034,188

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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 AND SER-310, FUNCTION, MUTAGENESIS OF SER-26; SER-49; SER-72; SER-142; SER-178 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]"Modification of the erythroid transcription factor GATA-1 by SUMO-1."
Collavin L., Gostissa M., Avolio F., Secco P., Ronchi A., Santoro C., Del Sal G.
Proc. Natl. Acad. Sci. U.S.A. 101:8870-8875(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS04655.
RefSeqNP_032115.1. NM_008089.2.
UniGeneMm.335973.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP17679.
SMRP17679. Positions 200-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199838. 22 interactions.
DIPDIP-40883N.
IntActP17679. 5 interactions.
MINTMINT-94735.
STRING10090.ENSMUSP00000033502.

PTM databases

PhosphoSiteP17679.

Proteomic databases

PRIDEP17679.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033502; ENSMUSP00000033502; ENSMUSG00000031162. [P17679-1]
GeneID14460.
KEGGmmu:14460.
UCSCuc009snl.1. mouse. [P17679-1]

Organism-specific databases

CTD2623.
MGIMGI:95661. Gata1.

Phylogenomic databases

eggNOGCOG5641.
GeneTreeENSGT00750000117454.
HOGENOMHOG000047701.
HOVERGENHBG051705.
InParanoidP17679.
KOK09182.
OMAPLLNCVE.
OrthoDBEOG7CCBRF.
PhylomeDBP17679.
TreeFamTF315391.

Gene expression databases

BgeeP17679.
CleanExMM_GATA1.
GenevestigatorP17679.

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

EvolutionaryTraceP17679.
NextBio286092.
PROP17679.
SOURCESearch...

Entry information

Entry nameGATA1_MOUSE
AccessionPrimary (citable) accession number: P17679
Secondary accession number(s): Q3UIH9, Q7TMX8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot