CEBPB
entrez
1051
canonical
uniprot
P17676
canonical
ensembl
ENSG00000172216
resolver
ensp
ENSP00000305422
resolver
genesymbol
CEBPB
resolver
genesymbol_syn
TCF5
resolver
hgnc
HGNC:1834
resolver
uniprot
A8K671
resolver
uniprot
Q96IH2
resolver
uniprot
Q9H4Z5
resolver
uniprot_entry
CEBPB_HUMAN
resolver
uniprot_sec
A8K671
resolver
uniprot_sec
Q96IH2
resolver
uniprot_sec
Q9H4Z5
resolver
amino_acid_sequence
MQRLVAWDPACLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPAARPGPRPPAGELGSIGDHERAIDFSPYLEPLGAPQAPAPATATDTFEAAPPAPAPAPASSGQHHDFLSDLFSDDYGGKNCKKPAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKAPPTACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASSGHC
uniprot
proteins
function
FUNCTION: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:12048245, PubMed:1741402, PubMed:18647749, PubMed:9374525). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. 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. 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. 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 (PubMed:20829347). 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 (By similarity). {ECO:0000250|UniProtKB:P21272, ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:12048245, ECO:0000269|PubMed:18647749, ECO:0000269|PubMed:20829347, ECO:0000269|PubMed:9374525, 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:0000250|UniProtKB:P28033}.; FUNCTION: [Isoform 3]: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity). {ECO:0000250|UniProtKB:P21272, ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:11741938}.
uniprot
proteins
mass_dalton
36106
uniprot
proteins
mutagenesis
MUTAGEN 235; /note="T->S: Loss of transactivation activity in response to IFNG."; /evidence="ECO:0000269|PubMed:12048245"; MUTAGEN 288; /note="S->A: Loss of nuclear translocation."; /evidence="ECO:0000269|PubMed:9374525
uniprot
proteins
post_translational_modification
PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-43 by EHMT2 inhibit transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-235. {ECO:0000305|PubMed:18647749, ECO:0000305|PubMed:20111005}.; PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3 (PubMed:12810706). Sumoylation at Lys-174 is required for inhibition of T-cells proliferation. In adipocytes, sumoylation at Lys-174 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation. Desumoylated by SENP2, which abolishes ubiquitination and stabilizes protein levels (By similarity). {ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:12810706}.; PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P28033}.; PTM: Phosphorylated at Thr-235 by MAPK and CDK2, serves to prime phosphorylation at Thr-226 and Ser-231 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-235 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation. Phosphorylation at Thr-266 enhances transactivation activity. Phosphorylation at Ser-325 in response to calcium increases transactivation activity. Phosphorylated at Thr-235 by RPS6KA1 (PubMed:11684016). {ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:11684016}.; PTM: O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program. {ECO:0000250|UniProtKB:P28033}.; PTM: Acetylated. Acetylation at Lys-43 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 129-133, 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
11018027
uniprot
proteins
pubmed
11257229
uniprot
proteins
pubmed
11684016
uniprot
proteins
pubmed
11741938
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
11792321
uniprot
proteins
pubmed
12048245
uniprot
proteins
pubmed
12810706
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15498874
uniprot
proteins
pubmed
1741402
uniprot
proteins
pubmed
17467953
uniprot
proteins
pubmed
18647749
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20111005
uniprot
proteins
pubmed
20829347
uniprot
proteins
pubmed
2112087
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25451943
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
27923061
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
7635140
uniprot
proteins
pubmed
9374525
uniprot
proteins
sequence_length
345
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20829347}. Cytoplasm {ECO:0000269|PubMed:9374525}. 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:P28033, ECO:0000269|PubMed:9374525}.
uniprot
proteins