Cebpa
entrez
24252
canonical
uniprot
P05554
canonical
ensembl
ENSRNOG00000010918
resolver
ensp
ENSRNOP00000104202
resolver
genesymbol
Cebpa
resolver
uniprot_entry
CEBPA_RAT
resolver
amino_acid_sequence
MESADFYEAEPRPPMSSHLQSPPHAPSNAAFGFPRGAGPAPPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAAGPAGGGGDFDYPGAPAGPGGAVMSAGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPPHPHASPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHPAPAMGAAGLPGPGGSLKGLAGPHPDLRTGGGGGGGAGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELDTLRGIFRQLPESSLVKAMGNCA
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 (PubMed:11672531, PubMed:16735515, PubMed:20176812, PubMed:8367486). Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes. During early embryogenesis, plays essential and redundant functions with CEBPB (By similarity). Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP) (PubMed:11672531). 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 (PubMed:11672531). 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 (PubMed:11672531). Proliferation arrest also depends on a functional binding to SWI/SNF complex (By similarity). 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:P49715, ECO:0000250|UniProtKB:P53566, ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:16735515, ECO:0000269|PubMed:20176812, ECO:0000269|PubMed:8367486}.; 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. {ECO:0000250|UniProtKB:P49715, ECO:0000250|UniProtKB:P53566, ECO:0000269|PubMed:8367486}.; FUNCTION: [Isoform 4]: Directly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation. {ECO:0000250|UniProtKB:P49715}.
uniprot
proteins
mass_dalton
37371
uniprot
proteins
mutagenesis
MUTAGEN 159; /note="K->A,R: Not sumoylated. No effect of sumoylation on cell cycle inhibition."; /evidence="ECO:0000269|PubMed:16735515"; MUTAGEN 285; /note="Y->A: Decreased transcription factor activity. Strongly decreased transcription factor activity; when associated with R-293."; /evidence="ECO:0000269|PubMed:12578822"; MUTAGEN 285; /note="Y->A: Increases interaction with TFDP1 and TFDP2, reduces DNA-binding, transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction."; /evidence="ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:20176812"; MUTAGEN 287; /note="V->A: No effect on repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-290."; /evidence="ECO:0000269|PubMed:11672531"; MUTAGEN 289; /note="R->A: Loss of DNA-binding and transcription factor activity."; /evidence="ECO:0000269|PubMed:12578822"; MUTAGEN 290; /note="E->A: No effect on repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-287."; /evidence="ECO:0000269|PubMed:11672531"; MUTAGEN 293; /note="N->R: Decreased transcription factor activity. Strongly decreased transcription factor activity; when associated with A-285."; /evidence="ECO:0000269|PubMed:12578822"; MUTAGEN 294; /note="I->A: Increases interaction with TFDP1 and TFDP2, reduces transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction, no effect on DNA-binding; when associated with A-297."; /evidence="ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:20176812"; MUTAGEN 296; /note="V->A: No effect on DNA-binding and transcription factor activity, but modified sequence specificity."; /evidence="ECO:0000269|PubMed:12578822"; MUTAGEN 297; /note="R->A: Increases interaction with TFDP1 and TFDP2, reduces transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction, no effect on DNA-binding; when associated with A-294."; /evidence="ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:20176812"; MUTAGEN 299; /note="S->D: Isoform 4: Stimulates nucleolar retention of isoform 4. No effect on interaction with NPM1, TAF1A and UBTF."; /evidence="ECO:0000269|PubMed:20075868"; MUTAGEN 301; /note="D->A: No effect neither on interaction with TFDP1 or TFDP2 nor on transactivation activity or repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-304."; /evidence="ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:20176812"; MUTAGEN 304; /note="K->A: No effect neither on interaction with TFDP1 or TFDP2 nor on transactivation activity or repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-301."; /evidence="ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:20176812
uniprot
proteins
post_translational_modification
PTM: Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2. {ECO:0000269|PubMed:16735515}.; PTM: Phosphorylation at Ser-193 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibition. Dephosphorylated at Ser-193 by protein phosphatase 2A (PP2A) through PI3K/AKT signaling pathway regulation. Phosphorylation at Thr-222 and Thr-226 by GSK3 is constitutive in adipose tissue and lung. In liver, both Thr-222 and Thr-226 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: Ubiquitinated by COP1 upon interaction with TRIB1. {ECO:0000250|UniProtKB:P49715}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
protein_family
C/EBP subfamily
uniprot
proteins
pubmed
11672531
uniprot
proteins
pubmed
12578822
uniprot
proteins
pubmed
1377818
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
16735515
uniprot
proteins
pubmed
1884998
uniprot
proteins
pubmed
20075868
uniprot
proteins
pubmed
20176812
uniprot
proteins
pubmed
2850264
uniprot
proteins
pubmed
7926792
uniprot
proteins
pubmed
8367486
uniprot
proteins
sequence_length
358
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8367486}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleolus {ECO:0000269|PubMed:20075868}.
uniprot
proteins