CEBPA
entrez
1050
canonical
uniprot
P49715
canonical
ensembl
ENSG00000245848
resolver
ensp
ENSP00000427514
resolver
genesymbol
CEBPA
resolver
genesymbol_syn
CEBP
resolver
hgnc
HGNC:1833
resolver
uniprot
A7LNP2
resolver
uniprot
P78319
resolver
uniprot
Q05CA4
resolver
uniprot_entry
CEBPA_HUMAN
resolver
uniprot_sec
A7LNP2
resolver
uniprot_sec
P78319
resolver
uniprot_sec
Q05CA4
resolver
amino_acid_sequence
MESADFYEAEPRPPMSSHLQSPPHAPSSAAFGFPRGAGPAQPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAVGPTGGGGGGDFDYPGAPAGPGGAVMPGGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPSHPHPHPPPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHPAPALGAAGLPGPGSALKGLGAAHPDLRASGGSGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELDTLRGIFRQLPESSLVKAMGNCA
uniprot
proteins
disease_involvement
DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:11242107, ECO:0000269|PubMed:12661007, ECO:0000269|PubMed:15575056}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta. Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes (PubMed:11242107). During early embryogenesis, plays essential and redundant functions with CEBPB. Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP). Critical for the proper development of the liver and the lung (By similarity). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (By similarity). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Down-regulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters. Proliferation arrest also depends on a functional binding to SWI/SNF complex (PubMed:14660596). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC1. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity). {ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P53566, ECO:0000269|PubMed:11242107, ECO:0000269|PubMed:14660596}.; FUNCTION: [Isoform 3]: Can act as dominant-negative. Binds DNA and have transactivation activity, even if much less efficiently than isoform 2. Does not inhibit cell proliferation (PubMed:14660596). {ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P53566, ECO:0000269|PubMed:14660596}.; FUNCTION: [Isoform 4]: Directly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation. {ECO:0000269|PubMed:20075868}.
uniprot
proteins
mass_dalton
37561
uniprot
proteins
mutagenesis
MUTAGEN 55; /note="I->A: Decreased interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 57; /note="E->T: No effect on interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 58; /note="H->D: No effect on interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 59; /note="E->A: Decreased interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 61; /note="S->A: Decreased interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 62; /note="I->A: Decreased interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 63; /note="D->A: No effect on interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 64; /note="I->A: Decreased interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 65; /note="S->A: No effect on interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 67; /note="Y->A: Decreased interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 67; /note="Y->F: No effect on interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 68; /note="I->A: Decreased interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797"; MUTAGEN 69; /note="D->A: No effect on interaction with TRIB1."; /evidence="ECO:0000269|PubMed:26455797
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-190 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibition. Dephosphorylated at Ser-190 by protein phosphatase 2A (PP2A) through PI3K/AKT signaling pathway regulation (PubMed:15107404). Phosphorylation at Thr-226 and Thr-230 by GSK3 is constitutive in adipose tissue and lung. In liver, both Thr-226 and Thr-230 are phosphorylated only during feeding but not during fasting. Phosphorylation of the GSK3 consensus sites selectively decreases transactivation activity on IRE-controlled promoters. {ECO:0000250|UniProtKB:P53566}.; PTM: Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2. {ECO:0000250|UniProtKB:P05554}.; PTM: Ubiquitinated by COP1 upon interaction with TRIB1. {ECO:0000303|PubMed:27041596}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
protein_family
C/EBP subfamily
uniprot
proteins
pubmed
10725330
uniprot
proteins
pubmed
11242107
uniprot
proteins
pubmed
12661007
uniprot
proteins
pubmed
14660596
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15078966
uniprot
proteins
pubmed
15107404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15575056
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20075868
uniprot
proteins
pubmed
20176812
uniprot
proteins
pubmed
20410507
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
26455797
uniprot
proteins
pubmed
27041596
uniprot
proteins
pubmed
27923061
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
7575576
uniprot
proteins
pubmed
9915821
uniprot
proteins
sequence_length
358
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11242107}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleolus {ECO:0000269|PubMed:20075868}.
uniprot
proteins