Cebpa
entrez
12606
canonical
uniprot
P53566
canonical
ensembl
ENSMUSG00000034957
resolver
ensp
ENSMUSP00000096129
resolver
genesymbol
Cebpa
resolver
genesymbol_syn
Cebp
resolver
uniprot
Q91XB6
resolver
uniprot_entry
CEBPA_MOUSE
resolver
uniprot_sec
Q91XB6
resolver
amino_acid_sequence
MESADFYEVEPRPPMSSHLQSPPHAPSNAAFGFPRGAGPAPPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAAGPAGGGGDFDYPGAPAGPGGAVMSAGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPPHPHASPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHAAPALGAAGLPGPGSALKGLAGAHPDLRTGGGGGGSGAGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELDTLRGIFRQLPESSLVKAMGNCA
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:15107404, PubMed:15589173, PubMed:36228616, PubMed:8415748). 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 (PubMed:15509779). Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP) (PubMed:24367003). Critical for the proper development of the liver and the lung (PubMed:8798745). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (PubMed:1935900, PubMed:8090719). 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 (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 (PubMed:17627282). To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2 (PubMed:17290224). In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (PubMed:17090532). {ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P49715, ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:14660596, ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:15509779, ECO:0000269|PubMed:15589173, ECO:0000269|PubMed:17090532, ECO:0000269|PubMed:17290224, ECO:0000269|PubMed:17627282, ECO:0000269|PubMed:1935900, ECO:0000269|PubMed:24367003, ECO:0000269|PubMed:36228616, ECO:0000269|PubMed:8090719, ECO:0000269|PubMed:8415748, ECO:0000269|PubMed:8798745}.; 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:P05554, ECO:0000250|UniProtKB:P49715, ECO:0000269|PubMed:8415748}.; 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
37430
uniprot
proteins
mutagenesis
MUTAGEN 182..188; /note="PPPPPPP->APPPAPA: No effect on DNA-binding or interaction with CDK2 and CDK4. No effect on cell cycle inhibition."; /evidence="ECO:0000269|PubMed:15107404"; MUTAGEN 184..186; /note="PPP->AAA: No effect on DNA-binding or interaction with CDK2 and CDK4. No effect on cell cycle inhibition."; /evidence="ECO:0000269|PubMed:15107404"; MUTAGEN 193; /note="S->A: No effect on DNA-binding. Loss of interaction with CDK2 and CDK4 as well as cell cycle inhibition."; /evidence="ECO:0000269|PubMed:15107404"; MUTAGEN 222..230; /note="TPPPTPVPS->APPPAPVPA: Decreases phosphorylated form. Deregulation of hepatic glucose metabolism."; /evidence="ECO:0000269|PubMed:17290224"; MUTAGEN 286; /note="Y->A: No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia."; /evidence="ECO:0000269|PubMed:11672531"; MUTAGEN 288; /note="V->A: No effect on DNA-binding, no effect on repression of E2F1:TFDP1-mediated transcription and no effect on adipogenesis and granulopoiesis; when associated with A-291."; /evidence="ECO:0000269|PubMed:11672531"; MUTAGEN 291; /note="E->A: No effect on DNA-binding, no effect on repression of E2F1:TFDP1-mediated transcription and no effect on adipogenesis and granulopoiesis; when associated with A-288."; /evidence="ECO:0000269|PubMed:11672531"; MUTAGEN 295; /note="I->A: No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia; when associated with A-298."; /evidence="ECO:0000269|PubMed:11672531"; MUTAGEN 298; /note="R->A: No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia; when associated with A-295."; /evidence="ECO:0000269|PubMed:11672531
uniprot
proteins
post_translational_modification
PTM: Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2. {ECO:0000250|UniProtKB:P05554}.; 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 (PubMed:15107404). 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 (PubMed:17290224). Phosphorylation of the GSK3 consensus sites selectively decreases transactivation activity on IRE-controlled promoters (PubMed:17290224). {ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:17290224}.; 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
14660596
uniprot
proteins
pubmed
15107404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15509779
uniprot
proteins
pubmed
15589173
uniprot
proteins
pubmed
17090532
uniprot
proteins
pubmed
17290224
uniprot
proteins
pubmed
17627282
uniprot
proteins
pubmed
1935900
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19641492
uniprot
proteins
pubmed
2006196
uniprot
proteins
pubmed
20075868
uniprot
proteins
pubmed
21602272
uniprot
proteins
pubmed
24367003
uniprot
proteins
pubmed
27923061
uniprot
proteins
pubmed
36228616
uniprot
proteins
pubmed
8090719
uniprot
proteins
pubmed
8415748
uniprot
proteins
pubmed
8798745
uniprot
proteins
sequence_length
359
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:36228616, ECO:0000269|PubMed:8415748}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleolus {ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P49715}.
uniprot
proteins