P46099
uniprot
P46099
canonical
amino_acid_sequence
MASAETVLPSISTLTTLGQFLDTQEDFLKWWRSEETQDLGPGPPNPTGPSLHVSLKSEDPSGEDDERDVTCAWDPDLFLTNFPGSESPGTSRTCALAPSVGPVAQFEPPESLGAYAGGPGLVTGPLGSEEHTSWAHPTPRPPAPEPFVAPALAPGLAPKAQPSYSDSRAGSVGGFFPRAGLAVPAAPGAPYGLLSGYPALYPAPQYQGHFQLFRGLAAPSAGGTAPPSFLNCLGPGTVATELGATAIAGDAGLSPGTAPPKRSRRTLAPKRQAAHTCGHEGCGKSYSKSSHLKAHLRTHTGEKPYACSWDGCDWRFARSDELTRHYRKHTGHRPFCCGLCPRAFSRSDHLALHMKRHL
uniprot
proteins
function
FUNCTION: Transcription regulator of erythrocyte development. Binds to the CACCC box in the beta-globin gene promoter and activates transcription. Probably serves as a general switch factor for erythroid development. When sumoylated, acts as a transcriptional repressor by promoting interaction with CDH2/MI2beta and also represses megakaryocytic differentiation. {ECO:0000269|PubMed:11259590, ECO:0000269|PubMed:15542849, ECO:0000269|PubMed:17938210, ECO:0000269|PubMed:9722526}.
uniprot
proteins
mass_dalton
37757
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="T->A: Greatly reduced transactivation activity."; /evidence="ECO:0000269|PubMed:9722526"; MUTAGEN 23; /note="T->D: No change in transactivation activity."; /evidence="ECO:0000269|PubMed:9722526"; MUTAGEN 25..26; /note="ED->AG: Abolishes most of transactivation activity."; /evidence="ECO:0000269|PubMed:9722526"; MUTAGEN 56; /note="K->R: Abolishes sumoylation. No change in nuclear localization but no colocalization with SUMO1. Reduces inhibition of megakaryocytic differentiation. No decrease in bone marrow precursors to form megakaryocytic colonies. No effect on erythroid differentiation."; /evidence="ECO:0000269|PubMed:17938210"; MUTAGEN 270; /note="K->A,R: No effect on DNA binding. Transactivation activity reduced by 50%. Loss of superactivation by CBP of EP300."; /evidence="ECO:0000269|PubMed:11259590"; MUTAGEN 284; /note="K->A,R: No effect on DNA binding. No change in transactivation activity. No loss of superactivation by CBP or EP300."; /evidence="ECO:0000269|PubMed:11259590, ECO:0000269|PubMed:15542849"; MUTAGEN 295; /note="H->N: Loss of DNA binding and transactivation activity. No change in interaction with SIN3A nor with HDAC1. No effect on repressive activity."; /evidence="ECO:0000269|PubMed:15542849"; MUTAGEN 321; /note="E->K: Alters DNA-binding specificity resulting in ectopic transcription of non-erythroid genes."; /evidence="ECO:0000269|PubMed:31126231, ECO:0000269|PubMed:31818881"; MUTAGEN 325; /note="H->N: Loss of DNA binding and transactivation activity. No change in interaction with SIN3A nor with HDAC1. No effect on repressive activity."; /evidence="ECO:0000269|PubMed:15542849"; MUTAGEN 353; /note="H->N: Loss of DNA binding and transactivation activity. No change in interaction with SIN3A nor with HDAC1. No effect on repressive activity."; /evidence="ECO:0000269|PubMed:15542849
uniprot
proteins
post_translational_modification
PTM: Acetylated; can be acetylated on both Lys-270 and Lys-288. Acetylation on Lys-270 (by CBP) appears to be the major site affecting EKLF transactivation activity. {ECO:0000269|PubMed:11259590}.; PTM: Sumoylated; sumoylation, promoted by PIAS1, leads to repression of megakaryocyte differentiation. Also promotes the interaction with the CDH4 subunit of the NuRD repression complex. {ECO:0000269|PubMed:17938210}.; PTM: Phosphorylated primarily on serine residues in the transactivation domain. Phosphorylation on Thr-23 is critical for the transactivation activity. {ECO:0000269|PubMed:9722526}.
uniprot
proteins
protein_family
Krueppel C2H2-type zinc-finger protein family
uniprot
proteins
pubmed
11259590
uniprot
proteins
pubmed
15542849
uniprot
proteins
pubmed
17938210
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
31126231
uniprot
proteins
pubmed
31818881
uniprot
proteins
pubmed
7565748
uniprot
proteins
pubmed
7682653
uniprot
proteins
pubmed
9722526
uniprot
proteins
sequence_length
358
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with SUMO1 in nuclear speckles.
uniprot
proteins