GATA1
entrez
2623
canonical
uniprot
P15976
canonical
ensembl
ENSG00000102145
resolver
ensp
ENSP00000365858
resolver
genesymbol
GATA1
resolver
genesymbol_syn
ERYF1
resolver
genesymbol_syn
GF1
resolver
hgnc
HGNC:4170
resolver
uniprot
Q96GB8
resolver
uniprot_entry
GATA1_HUMAN
resolver
uniprot_sec
Q96GB8
resolver
amino_acid_sequence
MEFPGLGSLGTSEPLPQFVDPALVSSTPESGVFFPSGPEGLDAAASSTAPSTATAAAAALAYYRDAEAYRHSPVFQVYPLLNCMEGIPGGSPYAGWAYGKTGLYPASTVCPTREDSPPQAVEDLDGKGSTSFLETLKTERLSPDLLTLGPALPSSLPVPNSAYGGPDFSSTFFSPTGSPLNSAAYSSPKLRGTLPLPPCEARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRLIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYYKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSSLGGTGAAEGPAGGFMVVAGGSGSGNCGEVASGLTLGPPGTAHLYQGLGPVVLSGPVSHLMPFPGPLLGSPTGSFPTGPMPPTTSTTVVAPLSS
uniprot
proteins
disease_involvement
DISEASE: X-linked dyserythropoietic anemia and thrombocytopenia (XDAT) [MIM:300367]: Disorder characterized by erythrocytes with abnormal size and shape, and paucity of platelets in peripheral blood. The bone marrow contains abundant and abnormally small megakaryocytes. {ECO:0000269|PubMed:10700180, ECO:0000269|PubMed:11418466, ECO:0000269|PubMed:11675338, ECO:0000269|PubMed:11809723}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Thrombocytopenia with beta-thalassemia, X-linked (XLTT) [MIM:314050]: An unusual form of thrombocytopenia associated with beta-thalassemia. Patients have splenomegaly and petechiae, moderate thrombocytopenia, prolonged bleeding time due to platelet dysfunction, reticulocytosis and unbalanced (hemo)globin chain synthesis resembling that of beta-thalassemia minor. {ECO:0000269|PubMed:12200364}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Anemia without thrombocytopenia, X-linked (XLAWT) [MIM:300835]: A form of anemia characterized by abnormal morphology of erythrocytes and granulocytes in peripheral blood, bone marrow dysplasia with hypocellularity of erythroid and granulocytic lineages, and normal or increased number of megakaryocytes. Neutropenia of a variable degree is present in affected individuals. {ECO:0000269|PubMed:16783379}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Anemia, congenital, non-spherocytic hemolytic, 9 (CNSHA9) [MIM:301083]: An X-linked disorder characterized by onset of mild to moderate red cell anemia soon after birth or in childhood. The anemia is associated with significantly increased adenosine deaminase activity, specifically in erythrocyte precursors. {ECO:0000269|PubMed:35030251}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Transcriptional activator or repressor which serves as a general switch factor for erythroid development (PubMed:35030251). 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 (PubMed:24245781). {ECO:0000269|PubMed:22235304, ECO:0000269|PubMed:24245781, ECO:0000269|PubMed:35030251}.
uniprot
proteins
mass_dalton
42751
uniprot
proteins
mutagenesis
MUTAGEN 137; /note="K->R: Abolishes sumoylation."; /evidence="ECO:0000269|PubMed:16371476"; MUTAGEN 142; /note="S->A: Loss of sumoylation."; /evidence="ECO:0000269|PubMed:16371476"; MUTAGEN 142; /note="S->D: Increased sumoylation in vitro."; /evidence="ECO:0000269|PubMed:16371476"; MUTAGEN 204; /note="C->R: Increase of dissociation rate from bound DNA."; /evidence="ECO:0000269|PubMed:10700180
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000250}.; PTM: 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 (By similarity). {ECO:0000250}.; PTM: Acetylated at 2 conserved lysine-rich motifs 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 similarity). Acetylated on Lys-233, Lys-245 Lys-246 by EP300. {ECO:0000250, ECO:0000269|PubMed:9859997}.
uniprot
proteins
pubmed
10700180
uniprot
proteins
pubmed
11418466
uniprot
proteins
pubmed
11675338
uniprot
proteins
pubmed
11809723
uniprot
proteins
pubmed
12200364
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16371476
uniprot
proteins
pubmed
16783379
uniprot
proteins
pubmed
17420275
uniprot
proteins
pubmed
2104960
uniprot
proteins
pubmed
22235304
uniprot
proteins
pubmed
2300555
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24245781
uniprot
proteins
pubmed
26019275
uniprot
proteins
pubmed
35030251
uniprot
proteins
pubmed
8524811
uniprot
proteins
pubmed
9859997
uniprot
proteins
sequence_length
413
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35030251}.
uniprot
proteins