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Protein

CCAAT/enhancer-binding protein beta

Gene

Cebpb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:16585579, PubMed:17911624, PubMed:18486321, PubMed:20111005). Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis (PubMed:9727068, PubMed:10635333, PubMed:17301242, PubMed:17601773, PubMed:19478079, PubMed:24061474). 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 functions 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:9727068, PubMed:10635333, PubMed:16585579). Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Plays also 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).1 PublicationBy similarity16 Publications
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.1 Publication
Isoform 3: Acts as a dominant negative through heterodimerization with isoform 2 (By similarity). Promotes osteoblast differentiation and osteoclastogenesis (PubMed:19440205).By similarity1 Publication

GO - Molecular functioni

  • chromatin binding Source: MGI
  • DNA binding Source: MGI
  • histone acetyltransferase binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • kinase binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  • RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  • sequence-specific DNA binding Source: MGI
  • ubiquitin-like protein ligase binding Source: UniProtKB

GO - Biological processi

  • brown fat cell differentiation Source: UniProtKB
  • cellular response to amino acid stimulus Source: MGI
  • defense response to bacterium Source: UniProtKB
  • embryonic placenta development Source: MGI
  • fat cell differentiation Source: MGI
  • granuloma formation Source: UniProtKB
  • hepatocyte proliferation Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • liver regeneration Source: UniProtKB
  • mammary gland epithelial cell differentiation Source: MGI
  • mammary gland epithelial cell proliferation Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of T cell proliferation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: MGI
  • neuron differentiation Source: MGI
  • ovarian follicle development Source: UniProtKB
  • positive regulation of fat cell differentiation Source: UniProtKB
  • positive regulation of interleukin-4 production Source: UniProtKB
  • positive regulation of osteoblast differentiation Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: MGI
  • regulation of interleukin-6 biosynthetic process Source: MGI
  • regulation of osteoclast differentiation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription involved in cell fate commitment Source: UniProtKB
  • response to endoplasmic reticulum stress Source: UniProtKB
  • response to lipopolysaccharide Source: BHF-UCL
  • T-helper 1 cell activation Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.
REACT_350665. Senescence-Associated Secretory Phenotype (SASP).

Names & Taxonomyi

Protein namesi
Recommended name:
CCAAT/enhancer-binding protein betaImported
Short name:
C/EBP beta
Alternative name(s):
AGP/EBP
Interleukin-6-dependent-binding protein
Short name:
IL-6DBP
Liver-enriched transcriptional activator
Short name:
LAP
Gene namesi
Name:CebpbImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:88373. Cebpb.

Subcellular locationi

GO - Cellular componenti

  • CHOP-C/EBP complex Source: Ensembl
  • condensed chromosome, centromeric region Source: MGI
  • cytoplasm Source: MGI
  • nuclear chromatin Source: BHF-UCL
  • nuclear matrix Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryos display defects in brown fat tissue development (PubMed:19641492). Females are sterile, ovaries lack corpora lutea (PubMed:9303532). Upon bacterial infection, animals show impaired bactericidal activity and die within 3 days (PubMed:17911624). Posthepatectomy, animals show a reduced regenerative response with DNA synthesis decreased to 25% of normal in hepatocytes and a prolonged period of hypoglycemia (PubMed:9727068). Animals show osteopenia with decreased bone formation and enhanced ostecolastogensis. Long bones have a 1.6 fold diminished bone volume with a reduction of the number and thickness of bone trabeculae (PubMed:19440205). Mutants of isoform 2 show impaired CSF3/G-CSF production by macrophages, IFNG production by CD4+ T-cells and granuloma formation in liver. Upon bacterial infection, mutants of isoform 2 die within 6 days. Resistant to LPS-induced endotoxin shock (PubMed:17911624). Double knockout CEBPA and CEBPB results in embryonic developmental arrest and death at around E10 to E11, associated with a gross placenta failure (PubMed:15509779).6 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391K → A or Q: No effect on interaction with EP300. 1 Publication
Mutagenesisi39 – 391K → R: Dominant negative. Loss of transactivation activity. No effect on interaction with EP300. 1 Publication
Mutagenesisi98 – 981K → 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. 2 Publications
Mutagenesisi101 – 1011K → R: Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-98 and R-102. 1 Publication
Mutagenesisi102 – 1021K → R: Not acetylated and no increase of transactivation activity after glucocorticoid-stimulation; when associated with R-98 and R-101. 1 Publication
Mutagenesisi133 – 1331K → R: Not sumoylated. Decreases ubiquitination and increases stability. Loss of proliferation inhibition in T cells. No effect on transactivation activity. 3 Publications
Mutagenesisi135 – 1351E → A: Not sumoylated and not ubiquitinated. 1 Publication
Mutagenesisi179 – 1791T → A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-184 and A-188. 1 Publication
Mutagenesisi180 – 1801S → A: Highly increases transactivation activity; when associated with A-181. 1 Publication
Mutagenesisi181 – 1811S → A: Highly increases transactivation activity; when associated with A-180. 1 Publication
Mutagenesisi184 – 1841S → A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-188. 1 Publication
Mutagenesisi188 – 1881T → A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-184. 1 Publication
Mutagenesisi215 – 2151K → R: No effect on transactivation activity. 1 Publication
Mutagenesisi217 – 2171T → A: Loss of hepatocyte proliferation induction by TGFA. 1 Publication
Mutagenesisi217 – 2171T → E: Induces hepatoDcyte proliferation. 1 Publication
Mutagenesisi276 – 2761S → A: Reduces phosphorylation in response to calcium. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296CCAAT/enhancer-binding protein betaPRO_0000076618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Omega-N-methylated arginine; by CARM11 Publication
Modified residuei39 – 391N6-acetyllysine1 Publication
Modified residuei39 – 391N6-methylated lysine1 Publication
Modified residuei98 – 981N6-acetyllysine; by KAT2A and KAT2B1 Publication
Modified residuei101 – 1011N6-acetyllysine; by KAT2A and KAT2B1 Publication
Modified residuei102 – 1021N6-acetyllysine; by KAT2A and KAT2B1 Publication
Cross-linki133 – 133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity3 Publications
Modified residuei179 – 1791Phosphothreonine; by GSK3-beta3 Publications
Glycosylationi180 – 1801O-linked (GlcNAc)1 Publication
Glycosylationi181 – 1811O-linked (GlcNAc)1 Publication
Modified residuei184 – 1841Phosphoserine; by GSK3-beta3 Publications
Modified residuei188 – 1881Phosphothreonine; by RPS6KA1, CDK2 and MAPK4 Publications
Modified residuei217 – 2171Phosphothreonine; by RPS6KA1 and PKC/PRKCABy similarity1 Publication
Modified residuei239 – 2391Phosphoserine; by PKC/PRKCABy similarity
Modified residuei276 – 2761Phosphoserine; by CaMK21 Publication

Post-translational modificationi

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).By similarity3 Publications
Ubiquitinated, leading to proteasomal degradation.1 Publication
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).By similarity3 Publications
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.1 Publication
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).2 Publications
Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2, inhibits transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-188.1 Publication1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP28033.
PRIDEiP28033.

PTM databases

PhosphoSiteiP28033.

Expressioni

Tissue specificityi

Abundantly expressed in myoblasts. Enriched in brown adipose tissue (BAT) versus white adipose tissue (WAT). Expressed in hepatocytes (at protein level). Expressed in T lymphocytes (PubMed:16585579). The expression in granulosa cells of antral follicles is induced by luteinizing hormone (PubMed:9303532). Expressed in chondrocytes and osteoblasts (at protein level) (PubMed:19440205).5 Publications

Developmental stagei

At E9.5, expressed in the chorionic plate and ectoplacental cone. From E10.5 to at least E11.5, is also expressed in the trophoblast cells of the three placenta layers (PubMed:15509779). Expressed in monocytic precursors but is vanished during differentiation into osteoclasts. The expression increases during osteoblast differentiation (PubMed:19440205).2 Publications

Inductioni

Up-regulated by cold exposure.1 Publication

Gene expression databases

BgeeiP28033.
CleanExiMM_CEBPB.
ExpressionAtlasiP28033. baseline and differential.
GenevisibleiP28033. MM.

Interactioni

Subunit structurei

Binds DNA as a dimer and can form stable heterodimers with CEBPA, CEBPD and CEBPG. Isoform 2 and isoform 3 also form heterodimers. Interacts with TRIM28 and PTGES2. Interacts with PRDM16. Interacts with CCDC85B. Forms a complex with THOC5. Interacts with ZNF638; this interaction increases transcriptional activation. Interacts with CIDEA and CIDEC. Interaction with CIDEA increases transcriptional activation of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH. Interaction with CIDEC increases transcriptional activation of SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. Interacts with DDIT3/CHOP. Interacts with EP300; recruits EP300 to chromatin. Interacts with RORA; the interaction disrupts interaction with EP300. Interacts (not methylated) with MED23, MED26, SMARCA2, SMARCB1 and SMARCC1 (PubMed:20111005). Interacts with KAT2A and KAT2B (PubMed:17301242).10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Bhlhe41Q99PV55EBI-1029979,EBI-6143801

Protein-protein interaction databases

BioGridi198669. 14 interactions.
DIPiDIP-37539N.
IntActiP28033. 8 interactions.
STRINGi10090.ENSMUSP00000069850.

Structurei

Secondary structure

1
296
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi240 – 28243Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI6X-ray2.60B224-285[»]
ProteinModelPortaliP28033.
SMRiP28033. Positions 239-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28033.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini222 – 28564bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2222Required for Lys-133 sumoylationBy similarityAdd
BLAST
Regioni22 – 10483Required for MYC transcriptional repression1 PublicationAdd
BLAST
Regioni226 – 24621Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni248 – 2558Leucine-zipperPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi120 – 12910Pro-rich
Compositional biasi170 – 19122Pro/Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family. C/EBP subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG299311.
GeneTreeiENSGT00530000063192.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiP28033.
KOiK10048.
OMAiCKKPAEY.
OrthoDBiEOG7R56TQ.
PhylomeDBiP28033.
TreeFamiTF105008.

Family and domain databases

InterProiIPR004827. bZIP.
IPR031106. C/EBP.
IPR016468. C/EBP_chordates.
[Graphical view]
PANTHERiPTHR23334. PTHR23334. 1 hit.
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P28033-1) [UniParc]FASTAAdd to basket

Also known as: a, C/EBPbeta-FL, LAP*

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MHRLLAWDAA CLPPPPAAFR PMEVANFYYE PDCLAYGAKA ARAAPRAPAA
60 70 80 90 100
EPAIGEHERA IDFSPYLEPL APAADFAAPA PAHHDFLSDL FADDYGAKPS
110 120 130 140 150
KKPADYGYVS LGRAGAKAAP PACFPPPPPA ALKAEPGFEP ADCKRADDAP
160 170 180 190 200
AMAAGFPFAL RAYLGYQATP SGSSGSLSTS SSSSPPGTPS PADAKAAPAA
210 220 230 240 250
CFAGPPAAPA KAKAKKTVDK LSDEYKMRRE RNNIAVRKSR DKAKMRNLET
260 270 280 290
QHKVLELTAE NERLQKKVEQ LSRELSTLRN LFKQLPEPLL ASAGHC
Length:296
Mass (Da):31,446
Last modified:August 1, 1992 - v1
Checksum:i827AC4AFC209AE89
GO
Isoform 2 (identifier: P28033-3) [UniParc]FASTAAdd to basket

Also known as: b, C/EBPbeta-LAP

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Note: Major isoform.
Show »
Length:275
Mass (Da):29,133
Checksum:i717E36841E48752D
GO
Isoform 3 (identifier: P28033-2) [UniParc]FASTAAdd to basket

Also known as: c, C/EBPbeta-LIP

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.

Show »
Length:145
Mass (Da):15,597
Checksum:iC7AFEEE4F98F5978
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 151151Missing in isoform 3. CuratedVSP_053976Add
BLAST
Alternative sequencei1 – 2121Missing in isoform 2. CuratedVSP_053977Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61007 mRNA. Translation: AAA37192.1.
X62600 mRNA. Translation: CAA44484.1.
S78572 Genomic DNA. No translation available.
CCDSiCCDS17105.1. [P28033-1]
PIRiA36366.
RefSeqiNP_001274667.1. NM_001287738.1. [P28033-3]
NP_001274668.1. NM_001287739.1. [P28033-2]
NP_034013.1. NM_009883.4. [P28033-1]
UniGeneiMm.439656.

Genome annotation databases

EnsembliENSMUST00000070642; ENSMUSP00000069850; ENSMUSG00000056501. [P28033-1]
GeneIDi12608.
KEGGimmu:12608.
UCSCiuc008oaf.2. mouse. [P28033-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61007 mRNA. Translation: AAA37192.1.
X62600 mRNA. Translation: CAA44484.1.
S78572 Genomic DNA. No translation available.
CCDSiCCDS17105.1. [P28033-1]
PIRiA36366.
RefSeqiNP_001274667.1. NM_001287738.1. [P28033-3]
NP_001274668.1. NM_001287739.1. [P28033-2]
NP_034013.1. NM_009883.4. [P28033-1]
UniGeneiMm.439656.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI6X-ray2.60B224-285[»]
ProteinModelPortaliP28033.
SMRiP28033. Positions 239-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198669. 14 interactions.
DIPiDIP-37539N.
IntActiP28033. 8 interactions.
STRINGi10090.ENSMUSP00000069850.

PTM databases

PhosphoSiteiP28033.

Proteomic databases

MaxQBiP28033.
PRIDEiP28033.

Protocols and materials databases

DNASUi12608.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070642; ENSMUSP00000069850; ENSMUSG00000056501. [P28033-1]
GeneIDi12608.
KEGGimmu:12608.
UCSCiuc008oaf.2. mouse. [P28033-1]

Organism-specific databases

CTDi1051.
MGIiMGI:88373. Cebpb.

Phylogenomic databases

eggNOGiNOG299311.
GeneTreeiENSGT00530000063192.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiP28033.
KOiK10048.
OMAiCKKPAEY.
OrthoDBiEOG7R56TQ.
PhylomeDBiP28033.
TreeFamiTF105008.

Enzyme and pathway databases

ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.
REACT_350665. Senescence-Associated Secretory Phenotype (SASP).

Miscellaneous databases

ChiTaRSiCebpb. mouse.
EvolutionaryTraceiP28033.
NextBioi281758.
PROiP28033.
SOURCEiSearch...

Gene expression databases

BgeeiP28033.
CleanExiMM_CEBPB.
ExpressionAtlasiP28033. baseline and differential.
GenevisibleiP28033. MM.

Family and domain databases

InterProiIPR004827. bZIP.
IPR031106. C/EBP.
IPR016468. C/EBP_chordates.
[Graphical view]
PANTHERiPTHR23334. PTHR23334. 1 hit.
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of a transcription factor, AGP/EBP, that belongs to members of the C/EBP family."
    Chang C.J., Chen T.T., Lei H.Y., Chen D.S., Lee S.C.
    Mol. Cell. Biol. 10:6642-6653(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Liver.
  2. "Regulated expression of three C/EBP isoforms during adipose conversion of 3T3-L1 cells."
    Cao Z., Umek R.M., McKnight S.L.
    Genes Dev. 5:1538-1552(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Autoregulated induction of the acute-phase response transcription factor gene, agp/ebp."
    Chang C.J., Shen B.J., Lee S.C.
    DNA Cell Biol. 14:529-537(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
    Tissue: Liver.
  4. "Calcium-regulated phosphorylation within the leucine zipper of C/EBP beta."
    Wegner M., Cao Z., Rosenfeld M.G.
    Science 256:370-373(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-276, MUTAGENESIS OF SER-276.
  5. "An essential role for C/EBPbeta in female reproduction."
    Sterneck E., Tessarollo L., Johnson P.F.
    Genes Dev. 11:2153-2162(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  6. "CCAAT enhancer- binding protein beta is required for normal hepatocyte proliferation in mice after partial hepatectomy."
    Greenbaum L.E., Li W., Cressman D.E., Peng Y., Ciliberto G., Poli V., Taub R.
    J. Clin. Invest. 102:996-1007(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Coactivator TIF1beta interacts with transcription factor C/EBPbeta and glucocorticoid receptor to induce alpha1-acid glycoprotein gene expression."
    Chang C.J., Chen Y.L., Lee S.C.
    Mol. Cell. Biol. 18:5880-5887(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM28.
  8. "Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP beta is required for hepatocyte proliferation induced by TGF alpha."
    Buck M., Poli V., van der Geer P., Chojkier M., Hunter T.
    Mol. Cell 4:1087-1092(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-217, MUTAGENESIS OF THR-217.
  9. "Essential requirement of CCAAT/enhancer binding proteins in embryogenesis."
    Begay V., Smink J., Leutz A.
    Mol. Cell. Biol. 24:9744-9751(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  10. "Delta-interacting protein A, a new inhibitory partner of CCAAT/enhancer-binding protein beta, implicated in adipocyte differentiation."
    Bezy O., Elabd C., Cochet O., Petersen R.K., Kristiansen K., Dani C., Ailhaud G., Amri E.-Z.
    J. Biol. Chem. 280:11432-11438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCDC85B.
  11. "IFN-gamma-stimulated transcriptional activation by IFN-gamma-activated transcriptional element-binding factor 1 occurs via an inducible interaction with CAAAT/enhancer-binding protein-beta."
    Meng Q., Raha A., Roy S., Hu J., Kalvakolanu D.V.
    J. Immunol. 174:6203-6211(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTGES2.
  12. "Sequential phosphorylation of CCAAT enhancer-binding protein beta by MAPK and glycogen synthase kinase 3beta is required for adipogenesis."
    Tang Q.Q., Gronborg M., Huang H., Kim J.W., Otto T.C., Pandey A., Lane M.D.
    Proc. Natl. Acad. Sci. U.S.A. 102:9766-9771(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-179; SER-184 AND THR-188, DNA-BINDING, MUTAGENESIS OF THR-179; SER-184 AND THR-188, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  13. "SUMOylation interferes with CCAAT/enhancer-binding protein beta-mediated c-myc repression, but not IL-4 activation in T cells."
    Berberich-Siebelt F., Berberich I., Andrulis M., Santner-Nanan B., Jha M.K., Klein-Hessling S., Schimpl A., Serfling E.
    J. Immunol. 176:4843-4851(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUMOYLATION AT LYS-133, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-133, SUBCELLULAR LOCATION.
  14. "The C/EBP beta isoform 34-kDa LAP is responsible for NF-IL-6-mediated gene induction in activated macrophages, but is not essential for intracellular bacteria killing."
    Uematsu S., Kaisho T., Tanaka T., Matsumoto M., Yamakami M., Omori H., Yamamoto M., Yoshimori T., Akira S.
    J. Immunol. 179:5378-5386(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, ALTERNATIVE INITIATION.
  15. "Glucocorticoid-stimulated preadipocyte differentiation is mediated through acetylation of C/EBPbeta by GCN5."
    Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.
    Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ACETYLATION AT LYS-98; LYS-101 AND LYS-102, INTERACTION WITH KAT2A AND KAT2B, MUTAGENESIS OF LYS-98; LYS-101 AND LYS-102.
  16. "Role of cdk2 in the sequential phosphorylation/activation of C/EBPbeta during adipocyte differentiation."
    Li X., Kim J.W., Gronborg M., Urlaub H., Lane M.D., Tang Q.Q.
    Proc. Natl. Acad. Sci. U.S.A. 104:11597-11602(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-179; SER-184 AND THR-188, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "G9a-mediated lysine methylation alters the function of CCAAT/enhancer-binding protein-beta."
    Pless O., Kowenz-Leutz E., Knoblich M., Lausen J., Beyermann M., Walsh M.J., Leutz A.
    J. Biol. Chem. 283:26357-26363(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-39.
  18. "Acetylation and deacetylation regulate CCAAT/enhancer binding protein beta at K39 in mediating gene transcription."
    Cesena T.I., Cui T.X., Subramanian L., Fulton C.T., Iniguez-Lluhi J.A., Kwok R.P., Schwartz J.
    Mol. Cell. Endocrinol. 289:94-101(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EP300, MUTAGENESIS OF LYS-39; LYS-98 AND LYS-215, ACETYLATION AT LYS-39.
  19. "THOC5 couples M-CSF receptor signaling to transcription factor expression."
    Carney L., Pierce A., Rijnen M., Gonzalez Sanchez M.B., Hamzah H.G., Zhang L., Tamura T., Whetton A.D.
    Cell. Signal. 21:309-316(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, COMPLEX FORMATION WITH THOC5.
  20. "Transcription factor C/EBPbeta isoform ratio regulates osteoclastogenesis through MafB."
    Smink J.J., Begay V., Schoenmaker T., Sterneck E., de Vries T.J., Leutz A.
    EMBO J. 28:1769-1781(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1 AND ISOFORM 3), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  21. "O-linked N-acetylglucosamine modification on CCAAT enhancer-binding protein beta: role during adipocyte differentiation."
    Li X., Molina H., Huang H., Zhang Y.Y., Liu M., Qian S.W., Slawson C., Dias W.B., Pandey A., Hart G.W., Lane M.D., Tang Q.Q.
    J. Biol. Chem. 284:19248-19254(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GLYCOSYLATION AT SER-180 AND SER-181, MUTAGENESIS OF SER-180 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-179; SER-184 AND THR-188.
  22. "The orphan nuclear receptor RORalpha restrains adipocyte differentiation through a reduction of C/EBPbeta activity and perilipin gene expression."
    Ohoka N., Kato S., Takahashi Y., Hayashi H., Sato R.
    Mol. Endocrinol. 23:759-771(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ADIPOGENESIS, INTERACTION WITH EP300 AND RORA, ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), PHOSPHORYLATION AT THR-188.
  23. "Initiation of myoblast to brown fat switch by a PRDM16-C/EBP-beta transcriptional complex."
    Kajimura S., Seale P., Kubota K., Lunsford E., Frangioni J.V., Gygi S.P., Spiegelman B.M.
    Nature 460:1154-1158(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PRDM16, INDUCTION BY COLD EXPOSURE, TISSUE SPECIFICITY.
  24. "Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and SWI/SNF/Mediator implies an indexing transcription factor code."
    Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.
    EMBO J. 29:1105-1115(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MED23; MED26; SMARCA2; SMARCB1 AND SMARCC1, IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION AT ARG-3.
  25. Cited for: FUNCTION, SUMOYLATION AT LYS-133, DESUMOYLATION AT LYS-133, MUTAGENESIS OF LYS-133 AND GLU-135, UBIQUITINATION.
  26. "Regulation of adipocyte differentiation by the zinc finger protein ZNF638."
    Meruvu S., Hugendubler L., Mueller E.
    J. Biol. Chem. 286:26516-26523(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF638.
  27. "Cidea is an essential transcriptional coactivator regulating mammary gland secretion of milk lipids."
    Wang W., Lv N., Zhang S., Shui G., Qian H., Zhang J., Chen Y., Ye J., Xie Y., Shen Y., Wenk M.R., Li P.
    Nat. Med. 18:235-243(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIDEA AND CIDEC.
  28. "Protein inhibitor of activated STAT 1 (PIAS1) is identified as the SUMO E3 ligase of CCAAT/enhancer-binding protein beta (C/EBPbeta) during adipogenesis."
    Liu Y., Zhang Y.D., Guo L., Huang H.Y., Zhu H., Huang J.X., Liu Y., Zhou S.R., Dang Y.J., Li X., Tang Q.Q.
    Mol. Cell. Biol. 33:4606-4617(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUMOYLATION AT LYS-133, MUTAGENESIS OF LYS-133, UBIQUITINATION.
  29. "Transcriptional Regulation of Adipocyte Differentiation: A Central Role for CCAAT/Enhancer-binding Protein (C/EBP) beta."
    Guo L., Li X., Tang Q.
    J. Biol. Chem. 290:755-761(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW OF PTMS AND FUNCTION.

Entry informationi

Entry nameiCEBPB_MOUSE
AccessioniPrimary (citable) accession number: P28033
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 22, 2015
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.