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P28033 (CEBPB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CCAAT/enhancer-binding protein beta

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 names
Name:Cebpb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Binds to regulatory regions of several acute-phase and cytokines genes and probably plays a role in the regulation of acute-phase reaction, inflammation and hemopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Plays an important role in adipose tissue differentiation. Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG) as well as other adipogenesis key player genes. Ref.8 Ref.9

Isoform 3:acts as a dominant negative through heterodimerization with isoform 2 By similarity. Ref.8 Ref.9

Subunit structure

Binds DNA as a dimer and can form stable heterodimers with CEBPA, CEBPD and CEBPG. 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. Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11

Subcellular location

Nucleus Ref.7.

Tissue specificity

Abundantly expressed in myoblasts. Enriched in brown adipose tissue (BAT) versus white adipose tissue (WAT). Ref.9

Induction

Up-regulated by cold exposure. Ref.9

Post-translational modification

Sumoylated by polymeric chains of SUMO2 or SUMO3 By similarity.

Disruption phenotype

Mice die in 24 hours after birth. Embryos display defects in brown fat tissue development. Ref.9

Sequence similarities

Belongs to the bZIP family. C/EBP subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative initiation
   LigandDNA-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrown fat cell differentiation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

cellular response to amino acid stimulus

Inferred from direct assay PubMed 20548288. Source: MGI

embryonic placenta development

Inferred from genetic interaction PubMed 15509779. Source: MGI

fat cell differentiation

Inferred from direct assay PubMed 15509789PubMed 17888405. Source: MGI

mammary gland epithelial cell differentiation

Inferred from mutant phenotype PubMed 10707954. Source: MGI

mammary gland epithelial cell proliferation

Inferred from mutant phenotype PubMed 10683373. Source: MGI

negative regulation of neuron apoptotic process

Inferred from direct assay PubMed 11684016. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15175325. Source: MGI

neuron differentiation

Inferred from direct assay PubMed 11733516. Source: MGI

positive regulation of fat cell differentiation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from direct assay PubMed 15175325. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 10859308. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15870285. Source: MGI

regulation of interleukin-6 biosynthetic process

Inferred from direct assay PubMed 11976687. Source: MGI

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

response to lipopolysaccharide

Inferred from mutant phenotype PubMed 17724128. Source: BHF-UCL

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.9. Source: GOC

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11684016PubMed 15870285. Source: MGI

nuclear chromatin

Inferred from direct assay PubMed 15187136. Source: BHF-UCL

nuclear matrix

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10588870PubMed 11733516PubMed 11940593PubMed 12821655PubMed 12871593PubMed 15509789PubMed 15519652PubMed 15870285PubMed 18824566. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 10510303PubMed 11976687PubMed 12821655PubMed 12871593PubMed 15509789PubMed 15870285. Source: MGI

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 10588870. Source: MGI

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.9. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay PubMed 12177065. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 12177065. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 10588870PubMed 15659391. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Bhlhe41Q99PV55EBI-1029979,EBI-6143801

Alternative products

This entry describes 3 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P28033-1)

Also known as: a; C/EBPbeta-FL;

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.
Isoform 2 (identifier: P28033-3)

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.
Isoform 3 (identifier: P28033-2)

Also known as: c; C/EBPbeta-LIP;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296CCAAT/enhancer-binding protein beta
PRO_0000076618

Regions

Domain222 – 28564bZIP
Region1 – 2222Required for Lys-174 sumoylation By similarity
Region226 – 24621Basic motif By similarity
Region248 – 2558Leucine-zipper By similarity
Compositional bias120 – 12910Pro-rich
Compositional bias170 – 19122Pro/Ser-rich

Amino acid modifications

Modified residue1881Phosphothreonine; by RPS6KA1 Ref.8
Cross-link133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 151151Missing in isoform 3.
VSP_053976
Alternative sequence1 – 2121Missing in isoform 2.
VSP_053977

Secondary structure

... 296
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (a) (C/EBPbeta-FL) [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 827AC4AFC209AE89

FASTA29631,446
        10         20         30         40         50         60 
MHRLLAWDAA CLPPPPAAFR PMEVANFYYE PDCLAYGAKA ARAAPRAPAA EPAIGEHERA 

        70         80         90        100        110        120 
IDFSPYLEPL APAADFAAPA PAHHDFLSDL FADDYGAKPS KKPADYGYVS LGRAGAKAAP 

       130        140        150        160        170        180 
PACFPPPPPA ALKAEPGFEP ADCKRADDAP AMAAGFPFAL RAYLGYQATP SGSSGSLSTS 

       190        200        210        220        230        240 
SSSSPPGTPS PADAKAAPAA CFAGPPAAPA KAKAKKTVDK LSDEYKMRRE RNNIAVRKSR 

       250        260        270        280        290 
DKAKMRNLET QHKVLELTAE NERLQKKVEQ LSRELSTLRN LFKQLPEPLL ASAGHC 

« Hide

Isoform 2 (b) (C/EBPbeta-LAP) [UniParc].

Checksum: 717E36841E48752D
Show »

FASTA27529,133
Isoform 3 (c) (C/EBPbeta-LIP) [UniParc].

Checksum: C7AFEEE4F98F5978
Show »

FASTA14515,597

References

[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]"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.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61007 mRNA. Translation: AAA37192.1.
X62600 mRNA. Translation: CAA44484.1.
S78572 Genomic DNA. No translation available.
PIRA36366.
RefSeqNP_034013.1. NM_009883.4.
UniGeneMm.439656.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI6X-ray2.60B224-285[»]
ProteinModelPortalP28033.
SMRP28033. Positions 239-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198669. 12 interactions.
DIPDIP-37539N.
IntActP28033. 6 interactions.
STRING10090.ENSMUSP00000069850.

PTM databases

PhosphoSiteP28033.

Proteomic databases

PRIDEP28033.

Protocols and materials databases

DNASU12608.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070642; ENSMUSP00000069850; ENSMUSG00000056501.
GeneID12608.
KEGGmmu:12608.
UCSCuc008oaf.1. mouse.

Organism-specific databases

CTD1051.
MGIMGI:88373. Cebpb.

Phylogenomic databases

eggNOGNOG299311.
HOGENOMHOG000013112.
HOVERGENHBG050879.
InParanoidP28033.
KOK10048.
OMACKKPAEY.
OrthoDBEOG7R56TQ.
PhylomeDBP28033.
TreeFamTF105008.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Gene expression databases

ArrayExpressP28033.
BgeeP28033.
CleanExMM_CEBPB.
GenevestigatorP28033.

Family and domain databases

InterProIPR004827. bZIP.
IPR016468. CCAAT/enhancer-binding.
[Graphical view]
PfamPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCEBPB. mouse.
EvolutionaryTraceP28033.
NextBio281758.
PROP28033.
SOURCESearch...

Entry information

Entry nameCEBPB_MOUSE
AccessionPrimary (citable) accession number: P28033
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot