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Protein

CCAAT/enhancer-binding protein beta

Gene

CEBPB

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important transcriptional activator 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'. Functions in brown adipose tissue (BAT) differentiation. Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG). Binds to the MGF and MIM-1 promoters and activates the transcription of these genes.1 Publication
Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:8467792). Plays also 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.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-GGA-2559582. Senescence-Associated Secretory Phenotype (SASP).

Names & Taxonomyi

Protein namesi
Recommended name:
CCAAT/enhancer-binding protein beta
Short name:
C/EBP beta
Alternative name(s):
Transcription factor NF-M
Short name:
CCR protein
Gene namesi
Name:CEBPB
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 20

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi3 – 31R → A: Not methylated. Increases interaction with SMARCA2 and MED23. 1 Publication
Mutagenesisi3 – 31R → L: Decreases interaction with SMARCA2 and MED23. 1 Publication
Mutagenesisi39 – 391K → A: Decreases methylation. Increases transactivation activity inhibition. 1 Publication
Mutagenesisi220 – 2201T → D: Decreases methylation by CARM1 and increases transactivation activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328CCAAT/enhancer-binding protein betaPRO_0000076620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Omega-N-methylated arginine; by CARM11 Publication
Modified residuei39 – 391N6-methylated lysine1 Publication
Modified residuei220 – 2201Phosphothreonine; by RPS6KA1, CDK2 and MAPK1 Publication

Post-translational modificationi

Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2, inhibit transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-220.By similarity2 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ05826.

PTM databases

iPTMnetiQ05826.

Expressioni

Tissue specificityi

Specifically expressed in myelomoncytic cells.

Interactioni

Subunit structurei

Binds DNA as a dimer. Interacts (not methylated) with MED23, MED26, SMARCA2, SMARCB1 and SMARCC1 (PubMed:20111005).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CARM1Q86X553EBI-7774198,EBI-2339854From a different organism.

Protein-protein interaction databases

IntActiQ05826. 2 interactions.
MINTiMINT-7895061.
STRINGi9031.ENSGALP00000012991.

Structurei

3D structure databases

ProteinModelPortaliQ05826.
SMRiQ05826. Positions 271-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini254 – 31764bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni258 – 27821Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni280 – 2878Leucine-zipperPROSITE-ProRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3119. Eukaryota.
ENOG410YJ8G. LUCA.
GeneTreeiENSGT00530000063192.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiQ05826.
KOiK10048.
OMAiCKKPAEY.
OrthoDBiEOG7R56TQ.
PhylomeDBiQ05826.
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]

Sequencei

Sequence statusi: Complete.

Q05826-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRLVAWDAA CLPIQPPAFK SMEVANFYYE ADCLAALNKL HPRAAGGRSM
60 70 80 90 100
TELTVGDHER AIDFSPYLDP LAASQQPAQP PPPAAAAGGN FEPACSSGGQ
110 120 130 140 150
DFLSDLFAED YKGSGGGKKP DYTYISLTRH GHPCGSQSHK PGVLPGCFPP
160 170 180 190 200
QIVETKVEPV FETLDSCKGP RKEEGGAGPG PGGMSSPYGS TVRSYLGYQS
210 220 230 240 250
VPSGSSGNLS TSSSSSPPGT PNPSESSKSA AGAGGYSGPP AGKNKPKKCV
260 270 280 290 300
DKHSDEYKLR RERNNIAVRK SRDKAKMRNL ETQHKVLELT AENERLQKKV
310 320
EQLSRELSTL RNLFKQLPEP LLASSPRC
Length:328
Mass (Da):35,030
Last modified:February 1, 1995 - v1
Checksum:i5AAE257F8213671C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21646 mRNA. Translation: CAA79760.1.
X70813 mRNA. Translation: CAA50144.1.
AY212285 Genomic DNA. Translation: AAO39751.1.
PIRiS35336.
RefSeqiNP_990584.1. NM_205253.2.
UniGeneiGga.4285.

Genome annotation databases

EnsembliENSGALT00000013006; ENSGALP00000012991; ENSGALG00000008014.
GeneIDi396185.
KEGGigga:396185.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21646 mRNA. Translation: CAA79760.1.
X70813 mRNA. Translation: CAA50144.1.
AY212285 Genomic DNA. Translation: AAO39751.1.
PIRiS35336.
RefSeqiNP_990584.1. NM_205253.2.
UniGeneiGga.4285.

3D structure databases

ProteinModelPortaliQ05826.
SMRiQ05826. Positions 271-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ05826. 2 interactions.
MINTiMINT-7895061.
STRINGi9031.ENSGALP00000012991.

PTM databases

iPTMnetiQ05826.

Proteomic databases

PaxDbiQ05826.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000013006; ENSGALP00000012991; ENSGALG00000008014.
GeneIDi396185.
KEGGigga:396185.

Organism-specific databases

CTDi1051.

Phylogenomic databases

eggNOGiKOG3119. Eukaryota.
ENOG410YJ8G. LUCA.
GeneTreeiENSGT00530000063192.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiQ05826.
KOiK10048.
OMAiCKKPAEY.
OrthoDBiEOG7R56TQ.
PhylomeDBiQ05826.
TreeFamiTF105008.

Enzyme and pathway databases

ReactomeiR-GGA-2559582. Senescence-Associated Secretory Phenotype (SASP).

Miscellaneous databases

NextBioi20816237.
PROiQ05826.

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. "The NF-M transcription factor is related to C/EBP beta and plays a role in signal transduction, differentiation and leukemogenesis of avian myelomonocytic cells."
    Katz S., Kowenz-Leutz E., Mueller C., Meese K., Ness S.A., Leutz A.
    EMBO J. 12:1321-1332(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "Synergistic activation of the chicken mim-1 gene by v-myb and C/EBP transcription factors."
    Burk O., Mink S., Ringwald M., Klempnauer K.H.
    EMBO J. 12:2027-2038(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Analysis of DNase I-hypersensitive sites in the chromatin of the chicken C/EBPbeta gene reveals multiple cell-type specific cis-regulatory elements."
    Kintscher J.R., Miethe J., Klempnauer K.-H.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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: FUNCTION, METHYLATION AT LYS-39, MUTAGENESIS OF LYS-39.
  5. "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: METHYLATION AT ARG-3, MUTAGENESIS OF ARG-3 AND THR-220, INTERACTION WITH MED23 AND SMARCA2, PHOSPHORYLATION AT THR-220.

Entry informationi

Entry nameiCEBPB_CHICK
AccessioniPrimary (citable) accession number: Q05826
Secondary accession number(s): Q540C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 110 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.