Cebpb
entrez
24253
canonical
uniprot
P21272
canonical
ensembl
ENSRNOG00000078148
resolver
ensp
ENSRNOP00000099899
resolver
genesymbol
Cebpb
resolver
genesymbol_syn
Crp2
resolver
genesymbol_syn
Nf-il6
resolver
genesymbol_syn
Sfb
resolver
uniprot
A2VD03
resolver
uniprot_entry
CEBPB_RAT
resolver
uniprot_sec
A2VD03
resolver
amino_acid_sequence
MHRLLAWDAACLPPPPAAFRPMEVANFYYEPDCLAYGAKAARAAPRAPAAEPAIGEHERAIDFSPYLEPLAPAAADFAAPAPAHHDFLSDLFADDYGAKPSKKPSDYGYVSLGRAGAKAAPPACFPPPPPAALKAEPGFEPADCKRADDAPAMAAGFPFALRAYLGYQATPSGSSGSLSTSSSSSPPGTPSPADAKAAPAACFAGPPAAPAKAKAKKAVDKLSDEYKMRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASAGHC
uniprot
proteins
function
FUNCTION: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:8336793). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis (PubMed:10635333). The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA (By similarity). Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage (PubMed:10635333). Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (By similarity). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (PubMed:15308669). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:10635333, ECO:0000269|PubMed:15308669, ECO:0000269|PubMed:1934061, ECO:0000269|PubMed:8336793}.; FUNCTION: [Isoform 2]: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4(+) T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing. {ECO:0000250|UniProtKB:P28033}.; FUNCTION: [Isoform 3]: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:1934061). Promotes osteoblast differentiation and osteoclastogenesis (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:1934061}.
uniprot
proteins
mass_dalton
31503
uniprot
proteins
mutagenesis
MUTAGEN 105; /note="S->A: No effect on DNA-binding. Loss of transactivation activity. Loss of hepatocyte proliferation induction by TGFA."; /evidence="ECO:0000269|PubMed:10635333, ECO:0000269|PubMed:8336793"; MUTAGEN 105; /note="S->D: No effect on DNA-binding. Increases transactivation activity."; /evidence="ECO:0000269|PubMed:8336793
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Thr-189 by MAPK and CDK2, serves to prime phosphorylation at Thr-180 and Ser-185 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-189 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation (By similarity). Phosphorylation at Ser-105 enhances transactivation activity (PubMed:8336793). Phosphorylation at Ser-277 in response to calcium increases transactivation activity. Phosphorylated at Thr-189 by RPS6KA1 (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:8336793}.; PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2 inhibit transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-189. {ECO:0000250|UniProtKB:P17676}.; PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3 (By similarity). Sumoylation at Lys-134 is required for inhibition of T-cells proliferation. In adipocytes, sumoylation at Lys-134 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation. Desumoylated by SENP2, which abolishes ubiquitination and stabilizes protein levels (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P28033}.; PTM: O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program. {ECO:0000250|UniProtKB:P28033}.; PTM: Acetylated. Acetylation at Lys-39 is an important and dynamic regulatory event that contributes to its ability to transactivate target genes, including those associated with adipogenesis and adipocyte function. Deacetylation by HDAC1 represses its transactivation activity. Acetylated by KAT2A and KAT2B within a cluster of lysine residues between amino acids 99-103, this acetylation is strongly induced by glucocorticoid treatment and enhances transactivation activity. {ECO:0000250|UniProtKB:P28033}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
protein_family
C/EBP subfamily
uniprot
proteins
pubmed
10635333
uniprot
proteins
pubmed
1377818
uniprot
proteins
pubmed
15308669
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1884998
uniprot
proteins
pubmed
1934061
uniprot
proteins
pubmed
2171780
uniprot
proteins
pubmed
2253878
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
8336793
uniprot
proteins
sequence_length
297
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17676}. Cytoplasm {ECO:0000250|UniProtKB:P17676}. Note=Translocates to the nucleus when phosphorylated at Ser-288. In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033}.
uniprot
proteins