Cebpb
entrez
12608
canonical
uniprot
P28033
canonical
ensembl
ENSMUSG00000056501
resolver
ensp
ENSMUSP00000069850
resolver
genesymbol
Cebpb
resolver
uniprot
Q3UPN9
resolver
uniprot_entry
CEBPB_MOUSE
resolver
uniprot_entry
Q3UPN9_MOUSE
resolver
amino_acid_sequence
MHRLLAWDAACLPPPPAAFRPMEVANFYYEPDCLAYGAKAARAAPRAPAAEPAIGEHERAIDFSPYLEPLAPAADFAAPAPAHHDFLSDLFADDYGAKPSKKPADYGYVSLGRAGAKAAPPACFPPPPPAALKAEPGFEPADCKRADDAPAMAAGFPFALRAYLGYQATPSGSSGSLSTSSSSSPPGTPSPADAKAAPAACFAGPPAAPAKAKAKKTVDKLSDEYKMRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASAGHC
uniprot
proteins
function
FUNCTION: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:16585579, PubMed:17911624, PubMed:18486321, PubMed:20111005). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis (PubMed:10635333, PubMed:17301242, PubMed:17601773, PubMed:19478079, PubMed:24061474, PubMed:24216764, PubMed:9727068). 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 (PubMed:15509779). 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, PubMed:16585579, PubMed:9727068). 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 (PubMed:17911624). 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 (PubMed:15985551, PubMed:17301242, PubMed:17601773, PubMed:20194620). Essential for female reproduction because of a critical role in ovarian follicle development (PubMed:9303532). Restricts osteoclastogenesis (PubMed:19440205). Together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P21272, ECO:0000269|PubMed:10635333, ECO:0000269|PubMed:1314426, ECO:0000269|PubMed:15509779, ECO:0000269|PubMed:15985551, ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:17601773, ECO:0000269|PubMed:17911624, ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:19440205, ECO:0000269|PubMed:19478079, ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:24061474, ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:9303532, ECO:0000269|PubMed:9727068, ECO:0000303|PubMed:25451943}.; 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:0000269|PubMed:17911624}.; FUNCTION: [Isoform 3]: Acts as a dominant negative through heterodimerization with isoform 2 (By similarity). Promotes osteoblast differentiation and osteoclastogenesis (PubMed:19440205). {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P21272, ECO:0000269|PubMed:19440205}.
uniprot
proteins
mass_dalton
31446
uniprot
proteins
mutagenesis
MUTAGEN 39; /note="K->A,Q: No effect on interaction with EP300."; /evidence="ECO:0000269|PubMed:18486321"; MUTAGEN 39; /note="K->R: Dominant negative. Loss of transactivation activity. No effect on interaction with EP300."; /evidence="ECO:0000269|PubMed:18486321"; MUTAGEN 98; /note="K->R: No effect on transactivation activity. Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-101 and R-102."; /evidence="ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:18486321"; MUTAGEN 101; /note="K->R: Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-98 and R-102."; /evidence="ECO:0000269|PubMed:17301242"; MUTAGEN 102; /note="K->R: Not acetylated and no increase of transactivation activity after glucocorticoid-stimulation; when associated with R-98 and R-101."; /evidence="ECO:0000269|PubMed:17301242"; MUTAGEN 133; /note="K->R: Not sumoylated. Decreases ubiquitination and increases stability. Loss of proliferation inhibition in T cells. No effect on transactivation activity."; /evidence="ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:24061474"; MUTAGEN 135; /note="E->A: Not sumoylated and not ubiquitinated."; /evidence="ECO:0000269|PubMed:20194620"; MUTAGEN 179; /note="T->A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-184 and A-188."; /evidence="ECO:0000269|PubMed:15985551"; MUTAGEN 180; /note="S->A: Highly increases transactivation activity; when associated with A-181."; /evidence="ECO:0000269|PubMed:19478079"; MUTAGEN 181; /note="S->A: Highly increases transactivation activity; when associated with A-180."; /evidence="ECO:0000269|PubMed:19478079"; MUTAGEN 184; /note="S->A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-188."; /evidence="ECO:0000269|PubMed:15985551"; MUTAGEN 188; /note="T->A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-184."; /evidence="ECO:0000269|PubMed:15985551"; MUTAGEN 215; /note="K->R: No effect on transactivation activity."; /evidence="ECO:0000269|PubMed:18486321"; MUTAGEN 217; /note="T->A: Loss of hepatocyte proliferation induction by TGFA."; /evidence="ECO:0000269|PubMed:10635333"; MUTAGEN 217; /note="T->E: Induces hepatocyte proliferation."; /evidence="ECO:0000269|PubMed:10635333"; MUTAGEN 276; /note="S->A: Reduces phosphorylation in response to calcium."; /evidence="ECO:0000269|PubMed:1314426
uniprot
proteins
post_translational_modification
PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3. Sumoylation at Lys-133 is required for inhibition of T-cells proliferation (PubMed:16585579). In adipocytes, sumoylation at Lys-133 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation (PubMed:24061474). Desumoylated by SENP2, which abolishes ubiquitination and stabilizes protein levels (PubMed:20194620). {ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:24061474}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000269|PubMed:24061474}.; PTM: Phosphorylated at Thr-188 by MAPK and CDK2, serves to prime phosphorylation at Thr-179 and Ser-184 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-188 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation. Phosphorylation at Thr-217 enhances transactivation activity. Phosphorylation at Ser-276 in response to calcium increases transactivation activity (PubMed:1314426). Phosphorylated at Thr-188 by RPS6KA1 (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:1314426, ECO:0000269|PubMed:15985551, ECO:0000269|PubMed:17601773}.; PTM: O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program. {ECO:0000269|PubMed:19478079}.; 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 (PubMed:18486321). Acetylated by KAT2A and KAT2B within a cluster of lysine residues between amino acids 98-102, this acetylation is strongly induced by glucocorticoid treatment and enhances transactivation activity (PubMed:17301242). {ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:18486321}.; PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2, inhibits transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-188. {ECO:0000269|PubMed:20111005, ECO:0000305|PubMed:18647749}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
protein_family
C/EBP subfamily
uniprot
proteins
pubmed
10635333
uniprot
proteins
pubmed
11018027
uniprot
proteins
pubmed
11792321
uniprot
proteins
pubmed
1314426
uniprot
proteins
pubmed
15509779
uniprot
proteins
pubmed
15644333
uniprot
proteins
pubmed
15879117
uniprot
proteins
pubmed
15985551
uniprot
proteins
pubmed
16585579
uniprot
proteins
pubmed
1701020
uniprot
proteins
pubmed
17301242
uniprot
proteins
pubmed
17601773
uniprot
proteins
pubmed
17911624
uniprot
proteins
pubmed
1840554
uniprot
proteins
pubmed
18486321
uniprot
proteins
pubmed
18647749
uniprot
proteins
pubmed
19015024
uniprot
proteins
pubmed
19324970
uniprot
proteins
pubmed
19440205
uniprot
proteins
pubmed
19478079
uniprot
proteins
pubmed
19641492
uniprot
proteins
pubmed
20111005
uniprot
proteins
pubmed
20194620
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21602272
uniprot
proteins
pubmed
22245780
uniprot
proteins
pubmed
24061474
uniprot
proteins
pubmed
24216764
uniprot
proteins
pubmed
25451943
uniprot
proteins
pubmed
27923061
uniprot
proteins
pubmed
7598808
uniprot
proteins
pubmed
9303532
uniprot
proteins
pubmed
9727068
uniprot
proteins
pubmed
9742105
uniprot
proteins
sequence_length
296
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:19015024}. Cytoplasm {ECO:0000250|UniProtKB:P17676}. Note=In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (PubMed:16585579). Translocates to the nucleus when phosphorylated at Ser-288 (By similarity). {ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:16585579}.
uniprot
proteins