Gata1
entrez
14460
canonical
uniprot
P17679
canonical
ensembl
ENSMUSG00000031162
resolver
ensp
ENSMUSP00000033502
resolver
genesymbol
Gata1
resolver
genesymbol_syn
Gf-1
resolver
uniprot
Q3UIH9
resolver
uniprot
Q7TMX8
resolver
uniprot_entry
GATA1_MOUSE
resolver
uniprot_sec
Q3UIH9
resolver
uniprot_sec
Q7TMX8
resolver
amino_acid_sequence
MDFPGLGALGTSEPLPQFVDSALVSSPSDSTGFFSSGPEGLDAASSSTSPNAATAAASALAYYREAEAYRHSPVFQVYPLLNSMEGIPGGSPYASWAYGKTALYPASTVCPSHEDAPSQALEDQEGKSNNTFLDTLKTERLSPDLLTLGTALPASLPVTGSAYGGADFPSPFFSPTGSPLSSAAYSSPKFHGSLPLAPCEARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRMIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYFKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSNLAGAGAAEGPAGGFMVVAGSSSSGNCGEVASGLALGTAGTAHLYQGLGPVVLSGPVSHLMPFPGPLLGSPTTSFPTGPAPTTSSTSVIAPLSS
uniprot
proteins
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). {ECO:0000250|UniProtKB:P15976, ECO:0000269|PubMed:15173587, ECO:0000269|PubMed:16888089, ECO:0000269|PubMed:2276623, ECO:0000269|PubMed:8206977, ECO:0000269|PubMed:8524811}.
uniprot
proteins
mass_dalton
42674
uniprot
proteins
mutagenesis
MUTAGEN 26; /note="S->A: Loss of phosphorylation of the chymotryptic peptide."; /evidence="ECO:0000269|PubMed:8206977"; MUTAGEN 49; /note="S->A: Loss of phosphorylation of the chymotryptic peptide."; /evidence="ECO:0000269|PubMed:8206977"; MUTAGEN 72; /note="S->A: Loss of phosphorylation of the chymotryptic peptide."; /evidence="ECO:0000269|PubMed:8206977"; MUTAGEN 137; /note="K->R: Abolishes sumoylation. No change in PIAS4 binding nor on transcriptional activity."; /evidence="ECO:0000269|PubMed:15173587"; MUTAGEN 142; /note="S->A: Loss of phosphorylation of the chymotryptic peptide."; /evidence="ECO:0000269|PubMed:8206977"; MUTAGEN 178; /note="S->A: Loss of phosphorylation of the chymotryptic peptide."; /evidence="ECO:0000269|PubMed:8206977"; MUTAGEN 187; /note="S->A: Loss of phosphorylation of the chymotryptic peptide."; /evidence="ECO:0000269|PubMed:8206977"; MUTAGEN 203; /note="E->V: Disrupts interaction with ZFPM1. Binds normally to DNA."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 204; /note="C->R: Disrupts interaction with ZFPM1 and binding to DNA."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 205; /note="V->G: Disrupts interaction with ZFPM1. Binds normally to DNA."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 205; /note="V->M: Disrupts interaction with ZFPM1. Binds normally to DNA."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 207; /note="C->G,R,W: Disrupts interaction with ZFPM1."; /evidence="ECO:0000269|PubMed:10078204, ECO:0000269|PubMed:2276623"; MUTAGEN 207; /note="C->P: Stability of binding to DNA reduced."; /evidence="ECO:0000269|PubMed:10078204, ECO:0000269|PubMed:2276623"; MUTAGEN 208; /note="G->E,V: Disrupts interaction with ZFPM1 and binding to DNA."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 218; /note="D->G,V: No effect on interaction with ZFPM1."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 222; /note="H->R: Disrupts interaction with ZFPM1. Binds normally to DNA."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 224; /note="L->P: Disrupts interaction with ZFPM1 and binding to DNA."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 225; /note="C->R,S,Y: Disrupts interaction with ZFPM1."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 228; /note="C->R,S: Disrupts interaction with ZFPM1."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 230; /note="L->F: Stability of binding to DNA reduced."; /evidence="ECO:0000269|PubMed:2276623"; MUTAGEN 233; /note="K->E: No effect on interaction with ZFPM1."; /evidence="ECO:0000269|PubMed:10078204"; MUTAGEN 245..246; /note="KK->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."; /evidence="ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:16888089"; MUTAGEN 245..246; /note="KK->RR: No effect on DNA binding."; /evidence="ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:16888089"; MUTAGEN 261; /note="C->P: Abolishes DNA-binding."; /evidence="ECO:0000269|PubMed:2276623"; MUTAGEN 284; /note="L->F: Binds to DNA with reduced affinity."; /evidence="ECO:0000269|PubMed:2276623"; MUTAGEN 310; /note="S->A: Loss of phosphorylation of the chymotryptic peptide."; /evidence="ECO:0000269|PubMed:8206977"; MUTAGEN 312..316; /note="KGKKK->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."; /evidence="ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:16888089"; MUTAGEN 312..316; /note="KGKKK->RGRRR: No effect on DNA binding."; /evidence="ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:16888089
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. {ECO:0000269|PubMed:15173587, ECO:0000269|PubMed:8206977}.; PTM: 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. {ECO:0000250, ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:21536911}.
uniprot
proteins
pubmed
10078204
uniprot
proteins
pubmed
10207073
uniprot
proteins
pubmed
10212985
uniprot
proteins
pubmed
15173587
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15920471
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16199866
uniprot
proteins
pubmed
16888089
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21536911
uniprot
proteins
pubmed
21555453
uniprot
proteins
pubmed
2276623
uniprot
proteins
pubmed
24245781
uniprot
proteins
pubmed
2725678
uniprot
proteins
pubmed
8206977
uniprot
proteins
pubmed
8524811
uniprot
proteins
sequence_length
413
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16888089}.
uniprot
proteins