Reviewed,
UniProtKB/Swiss-Prot P17679 (GATA1_MOUSE)
Last modified
January 19, 2010.
Version 97.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | 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 names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 413 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells. Ref.3 Ref.4 Ref.6 |
| Subunit structure | 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. Ref.6 Ref.7 |
| Subcellular location | |
| Tissue specificity | Erythrocytes. Ref.1 |
| 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.4 Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4. Sumoylation by SUMO1 has no effect on transcriptional activity. |
| Sequence similarities | Contains 2 GATA-type zinc fingers. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Domain | Zinc-finger |
| Ligand | DNA-binding Metal-binding Zinc |
| Molecular function | Activator |
| PTM | Isopeptide bond Phosphoprotein Ubl conjugation |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro transcriptionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | protein binding Inferred from physical interaction. Source: MGI sequence-specific DNA bindingInferred from direct assay. Source: MGI transcription factor activityInferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||
Molecule processing | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 413 | 413 | Erythroid transcription factor | PRO_0000083398 | |||||||||
Regions | |||||||||||||
| Zinc finger | 204 – 228 | 25 | GATA-type 1 | ||||||||||
| Zinc finger | 258 – 282 | 25 | GATA-type 2 | ||||||||||
| Region | 203 – 222 | 20 | Required for interaction with ZFPM1 By similarity | ||||||||||
Amino acid modifications | |||||||||||||
| Modified residue | 26 | 1 | Phosphoserine Ref.4 | ||||||||||
| Modified residue | 49 | 1 | Phosphoserine Ref.4 | ||||||||||
| Modified residue | 72 | 1 | Phosphoserine Ref.4 | ||||||||||
| Modified residue | 142 | 1 | Phosphoserine Ref.4 | ||||||||||
| Modified residue | 178 | 1 | Phosphoserine Ref.4 | ||||||||||
| Modified residue | 187 | 1 | Phosphoserine | ||||||||||
| Modified residue | 310 | 1 | Phosphoserine Ref.4 | ||||||||||
| Cross-link | 137 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.6 | |||||||||||
Experimental info | |||||||||||||
| Mutagenesis | 26 | 1 | S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.4 | ||||||||||
| Mutagenesis | 49 | 1 | S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.4 | ||||||||||
| Mutagenesis | 72 | 1 | S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.4 | ||||||||||
| Mutagenesis | 137 | 1 | K → R: Abolishes sumoylation. No change in PIAS4 binding nor on transcriptional activity. Ref.6 | ||||||||||
| Mutagenesis | 142 | 1 | S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.4 | ||||||||||
| Mutagenesis | 178 | 1 | S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.4 | ||||||||||
| Mutagenesis | 187 | 1 | S → A: Loss of phosphorylation of the chymotryptic peptide. | ||||||||||
| Mutagenesis | 203 | 1 | E → V: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.5 | ||||||||||
| Mutagenesis | 204 | 1 | C → R: Disrupts interaction with ZFPM1 and binding to DNA. Ref.5 | ||||||||||
| Mutagenesis | 205 | 1 | V → G: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.5 | ||||||||||
| Mutagenesis | 205 | 1 | V → M: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.5 | ||||||||||
| Mutagenesis | 207 | 1 | C → G, R or W: Disrupts interaction with ZFPM1. Ref.3 Ref.5 | ||||||||||
| Mutagenesis | 207 | 1 | C → P: Stability of binding to DNA reduced. Ref.3 Ref.5 | ||||||||||
| Mutagenesis | 208 | 1 | G → E or V: Disrupts interaction with ZFPM1 and binding to DNA. Ref.5 | ||||||||||
| Mutagenesis | 218 | 1 | D → G or V: No effect on interaction with ZFPM1. Ref.5 | ||||||||||
| Mutagenesis | 222 | 1 | H → R: Disrupts interaction with ZFPM1. Binds normally to DNA. Ref.5 | ||||||||||
| Mutagenesis | 224 | 1 | L → P: Disrupts interaction with ZFPM1 and binding to DNA. Ref.5 | ||||||||||
| Mutagenesis | 225 | 1 | C → R, S or Y: Disrupts interaction with ZFPM1. Ref.5 | ||||||||||
| Mutagenesis | 228 | 1 | C → R or S: Disrupts interaction with ZFPM1. Ref.5 | ||||||||||
| Mutagenesis | 230 | 1 | L → F: Stability of binding to DNA reduced. Ref.3 | ||||||||||
| Mutagenesis | 233 | 1 | K → E: No effect on interaction with ZFPM1. Ref.5 | ||||||||||
| Mutagenesis | 261 | 1 | C → P: Abolishes DNA-binding. Ref.3 | ||||||||||
| Mutagenesis | 284 | 1 | L → F: Binds to DNA with reduced affinity. Ref.3 | ||||||||||
| Mutagenesis | 310 | 1 | S → A: Loss of phosphorylation of the chymotryptic peptide. Ref.4 | ||||||||||
Secondary structure | |||||||||||||
Helix Strand Turn | |||||||||||||
| Beta strand | 205 – 207 | 3 | |||||||||||
| Helix | 228 – 234 | 7 | |||||||||||
Sequences
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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: 2725678] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY. Tissue: Erythrocyte. |
| [2] | 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. |
| [3] | "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: 2276623] [Abstract] Cited for: FUNCTION OF ZINC FINGERS, MUTAGENESIS OF CYS-207; LEU-230; CYS-261 AND LEU-284. |
| [4] | "Phosphorylation of the erythroid transcription factor GATA-1." Crossley M., Orkin S.H. J. Biol. Chem. 269:16589-16596(1994) [PubMed: 8206977] [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. |
| [5] | "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: 10078204] [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. |
| [6] | "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: 15173587] [Abstract] Cited for: SUMOYLATION AT LYS-137, INTERACTION WITH PIAS4, FUNCTION, MUTAGENESIS OF LYS-137. |
| [7] | "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: 15920471] [Abstract] Cited for: INTERACTION WITH GFI1B. |
| [8] | "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: 10212985] [Abstract] Cited for: STRUCTURE BY NMR OF 200-243. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X15763 mRNA. Translation: CAA33769.1. X57530 Genomic DNA. Translation: CAA40751.1. | ||||||||||||||||||
| IPI | IPI00111277. | ||||||||||||||||||
| PIR | S04655. | ||||||||||||||||||
| RefSeq | NP_032115.1. | ||||||||||||||||||
| UniGene | Mm.335973 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| SMR | P17679. Positions 252-317. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | P17679. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P17679. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | P17679. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSMUST00000033502; ENSMUSP00000033502; ENSMUSG00000031162; Mus musculus. [Genome view] | ||||||||||||||||||
| GeneID | 14460. | ||||||||||||||||||
| KEGG | mmu:14460. | ||||||||||||||||||
| UCSC | uc009snl.1. mouse. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 14460. | ||||||||||||||||||
| MGI | MGI:95661. Gata1. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | roNOG05410. | ||||||||||||||||||
| HOGENOM | HBG716943. | ||||||||||||||||||
| HOVERGEN | P17679. | ||||||||||||||||||
| InParanoid | P17679. | ||||||||||||||||||
| OMA | FPTGPVP. | ||||||||||||||||||
| PhylomeDB | P17679. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P17679. | ||||||||||||||||||
| Bgee | P17679. | ||||||||||||||||||
| CleanEx | MM_GATA1. | ||||||||||||||||||
| Genevestigator | P17679. | ||||||||||||||||||
| GermOnline | ENSMUSG00000031162. Mus musculus. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR016374. TF_GATA-1/2/3. IPR000679. Znf_GATA. IPR013088. Znf_NHR/GATA. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.30.50.10. Znf_NHR/GATA. 2 hits. | ||||||||||||||||||
| Pfam | PF00320. GATA. 2 hits. [Graphical view] | ||||||||||||||||||
| PIRSF | PIRSF003027. TF_GATA-1/2/3. 1 hit. | ||||||||||||||||||
| PRINTS | PR00619. GATAZNFINGER. | ||||||||||||||||||
| SMART | SM00401. ZnF_GATA. 2 hits. [Graphical view] | ||||||||||||||||||
| PROSITE | PS00344. GATA_ZN_FINGER_1. 2 hits. PS50114. GATA_ZN_FINGER_2. 2 hits. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| NextBio | 286092. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | GATA1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P17679 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


