P17679 · GATA1_MOUSE
- ProteinErythroid transcription factor
- GeneGata1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids413 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameErythroid transcription factor
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP17679
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 26 | Loss of phosphorylation of the chymotryptic peptide. | ||||
Sequence: S → A | ||||||
Mutagenesis | 49 | Loss of phosphorylation of the chymotryptic peptide. | ||||
Sequence: S → A | ||||||
Mutagenesis | 72 | Loss of phosphorylation of the chymotryptic peptide. | ||||
Sequence: S → A | ||||||
Mutagenesis | 137 | Abolishes sumoylation. No change in PIAS4 binding nor on transcriptional activity. | ||||
Sequence: K → R | ||||||
Mutagenesis | 142 | Loss of phosphorylation of the chymotryptic peptide. | ||||
Sequence: S → A | ||||||
Mutagenesis | 178 | Loss of phosphorylation of the chymotryptic peptide. | ||||
Sequence: S → A | ||||||
Mutagenesis | 187 | Loss of phosphorylation of the chymotryptic peptide. | ||||
Sequence: S → A | ||||||
Mutagenesis | 203 | Disrupts interaction with ZFPM1. Binds normally to DNA. | ||||
Sequence: E → V | ||||||
Mutagenesis | 204 | Disrupts interaction with ZFPM1 and binding to DNA. | ||||
Sequence: C → R | ||||||
Mutagenesis | 205 | Disrupts interaction with ZFPM1. Binds normally to DNA. | ||||
Sequence: V → G | ||||||
Mutagenesis | 205 | Disrupts interaction with ZFPM1. Binds normally to DNA. | ||||
Sequence: V → M | ||||||
Mutagenesis | 207 | Disrupts interaction with ZFPM1. | ||||
Sequence: C → G, R, or W | ||||||
Mutagenesis | 207 | Stability of binding to DNA reduced. | ||||
Sequence: C → P | ||||||
Mutagenesis | 208 | Disrupts interaction with ZFPM1 and binding to DNA. | ||||
Sequence: G → E or V | ||||||
Mutagenesis | 218 | No effect on interaction with ZFPM1. | ||||
Sequence: D → G or V | ||||||
Mutagenesis | 222 | Disrupts interaction with ZFPM1. Binds normally to DNA. | ||||
Sequence: H → R | ||||||
Mutagenesis | 224 | Disrupts interaction with ZFPM1 and binding to DNA. | ||||
Sequence: L → P | ||||||
Mutagenesis | 225 | Disrupts interaction with ZFPM1. | ||||
Sequence: C → R, S, or Y | ||||||
Mutagenesis | 228 | Disrupts interaction with ZFPM1. | ||||
Sequence: C → R or S | ||||||
Mutagenesis | 230 | Stability of binding to DNA reduced. | ||||
Sequence: L → F | ||||||
Mutagenesis | 233 | No effect on interaction with ZFPM1. | ||||
Sequence: K → E | ||||||
Mutagenesis | 245-246 | 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. | ||||
Sequence: KK → AA | ||||||
Mutagenesis | 245-246 | No effect on DNA binding. | ||||
Sequence: KK → RR | ||||||
Mutagenesis | 261 | Abolishes DNA-binding. | ||||
Sequence: C → P | ||||||
Mutagenesis | 284 | Binds to DNA with reduced affinity. | ||||
Sequence: L → F | ||||||
Mutagenesis | 310 | Loss of phosphorylation of the chymotryptic peptide. | ||||
Sequence: S → A | ||||||
Mutagenesis | 312-316 | 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. | ||||
Sequence: KGKKK → AGAAA | ||||||
Mutagenesis | 312-316 | No effect on DNA binding. | ||||
Sequence: KGKKK → RGRRR |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 29 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000083398 | 1-413 | Erythroid transcription factor | |||
Sequence: MDFPGLGALGTSEPLPQFVDSALVSSPSDSTGFFSSGPEGLDAASSSTSPNAATAAASALAYYREAEAYRHSPVFQVYPLLNSMEGIPGGSPYASWAYGKTALYPASTVCPSHEDAPSQALEDQEGKSNNTFLDTLKTERLSPDLLTLGTALPASLPVTGSAYGGADFPSPFFSPTGSPLSSAAYSSPKFHGSLPLAPCEARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRMIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYFKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSNLAGAGAAEGPAGGFMVVAGSSSSGNCGEVASGLALGTAGTAHLYQGLGPVVLSGPVSHLMPFPGPLLGSPTTSFPTGPAPTTSSTSVIAPLSS | ||||||
Modified residue | 26 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 49 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 72 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 137 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | ||||||
Modified residue | 142 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 178 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 187 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 233 | N6-acetyllysine; by EP300 | ||||
Sequence: K | ||||||
Modified residue | 245 | N6-acetyllysine; by EP300 | ||||
Sequence: K | ||||||
Modified residue | 246 | N6-acetyllysine; by CREBBP | ||||
Sequence: K | ||||||
Modified residue | 246 | N6-acetyllysine; by EP300 | ||||
Sequence: K | ||||||
Modified residue | 252 | N6-acetyllysine; by CREBBP | ||||
Sequence: K | ||||||
Modified residue | 308 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 310 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 312 | N6-acetyllysine; by CREBBP | ||||
Sequence: K | ||||||
Modified residue | 314 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 315 | N6-acetyllysine | ||||
Sequence: K |
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).
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.
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
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
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Erythrocytes. Expressed (at protein level) in liver.
Developmental stage
Detected at 11.5-day fetal livers (at protein level). Isoform 2 detected earlier at 8.5-day embryo.
Gene expression databases
Interaction
Subunit
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. Interacts with MED1, CCAR1 and CALCOCO1. Interacts with EP300 (By similarity).
Interacts with CEBPE (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. Interacts with MED1, CCAR1 and CALCOCO1. Interacts with EP300 (By similarity).
Interacts with CEBPE (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P17679 | Lmo2 P25801 | 5 | EBI-3903251, EBI-3903256 | |
BINARY | P17679 | Rb1 P13405 | 3 | EBI-3903251, EBI-971782 | |
BINARY | P17679 | Tal1 P22091 | 2 | EBI-3903251, EBI-8006437 | |
XENO | P17679 | ush Q9VPQ6 | 2 | EBI-3903251, EBI-110692 | |
BINARY | P17679 | Zfpm1 O35615 | 7 | EBI-3903251, EBI-4394596 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 29-49 | Disordered | ||||
Sequence: DSTGFFSSGPEGLDAASSSTS | ||||||
Region | 200-330 | Interaction with MED1 and CCAR1 | ||||
Sequence: EARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRMIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYFKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSNLAGAGAAEGP | ||||||
Region | 203-222 | Required for interaction with ZFPM1 | ||||
Sequence: ECVNCGATATPLWRRDRTGH | ||||||
Zinc finger | 204-228 | GATA-type 1 | ||||
Sequence: CVNCGATATPLWRRDRTGHYLCNAC | ||||||
Region | 249-315 | Interaction with CALCOCO1 | ||||
Sequence: IVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYFKLHQVNRPLTMRKDGIQTRNRKASGKGKK | ||||||
Zinc finger | 258-282 | GATA-type 2 | ||||
Sequence: CTNCQTTTTTLWRRNASGDPVCNAC | ||||||
Region | 297-325 | Disordered | ||||
Sequence: MRKDGIQTRNRKASGKGKKKRGSNLAGAG | ||||||
Region | 391-413 | Disordered | ||||
Sequence: TTSFPTGPAPTTSSTSVIAPLSS |
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.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative initiation.
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.
- Name1
- Length413
- Mass (Da)42,674
- Last updated1990-08-01 v1
- ChecksumBB627A92700D557A
P17679-2
- Name2
- SynonymsGATA-1s
- Differences from canonical
- 1-83: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_041452 | 1-83 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 29 | in Ref. 5; AAH52653 | ||||
Sequence: D → G | ||||||
Sequence conflict | 129 | in Ref. 5; AAH52653 | ||||
Sequence: N → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X15763 EMBL· GenBank· DDBJ | CAA33769.1 EMBL· GenBank· DDBJ | mRNA | ||
AK146915 EMBL· GenBank· DDBJ | BAE27527.1 EMBL· GenBank· DDBJ | mRNA | ||
AL670169 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466638 EMBL· GenBank· DDBJ | EDL33938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X57530 EMBL· GenBank· DDBJ | CAA40751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC052653 EMBL· GenBank· DDBJ | AAH52653.1 EMBL· GenBank· DDBJ | mRNA |