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P17679

- GATA1_MOUSE

UniProt

P17679 - GATA1_MOUSE

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Protein

Erythroid transcription factor

Gene

Gata1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.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. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: MGI
  8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: Ensembl
  9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  10. RNA polymerase II transcription factor binding Source: BHF-UCL
  11. sequence-specific DNA binding Source: MGI
  12. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
  13. 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
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_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. nucleus Source: MGI
  2. transcriptional repressor complex Source: Ensembl
  3. transcription factor complex Source: Ensembl
Complete GO annotation...

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. 2 Publications
Mutagenesisi245 – 2462KK → RR: No effect on DNA binding. 2 Publications
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. 2 Publications
Mutagenesisi312 – 3165KGKKK → RGRRR: No effect on DNA binding. 2 Publications

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.
ExpressionAtlasiP17679. baseline and differential.
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.
GeneTreeiENSGT00760000119221.
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

        10         20         30         40         50
MDFPGLGALG TSEPLPQFVD SALVSSPSDS TGFFSSGPEG LDAASSSTSP
60 70 80 90 100
NAATAAASAL AYYREAEAYR HSPVFQVYPL LNSMEGIPGG SPYASWAYGK
110 120 130 140 150
TALYPASTVC PSHEDAPSQA LEDQEGKSNN TFLDTLKTER LSPDLLTLGT
160 170 180 190 200
ALPASLPVTG SAYGGADFPS PFFSPTGSPL SSAAYSSPKF HGSLPLAPCE
210 220 230 240 250
ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP LIRPKKRMIV
260 270 280 290 300
SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYFKLHQ VNRPLTMRKD
310 320 330 340 350
GIQTRNRKAS GKGKKKRGSN LAGAGAAEGP AGGFMVVAGS SSSGNCGEVA
360 370 380 390 400
SGLALGTAGT AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TTSFPTGPAP
410
TTSSTSVIAP LSS
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 ENSGT00760000119221.
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.
ExpressionAtlasi P17679. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 145 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