CEBPB_CHICK
ID CEBPB_CHICK Reviewed; 328 AA.
AC Q05826; Q540C6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=CCAAT/enhancer-binding protein beta;
DE Short=C/EBP beta;
DE AltName: Full=Transcription factor NF-M;
DE Short=CCR protein;
GN Name=CEBPB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8467792; DOI=10.1002/j.1460-2075.1993.tb05777.x;
RA Katz S., Kowenz-Leutz E., Mueller C., Meese K., Ness S.A., Leutz A.;
RT "The NF-M transcription factor is related to C/EBP beta and plays a role in
RT signal transduction, differentiation and leukemogenesis of avian
RT myelomonocytic cells.";
RL EMBO J. 12:1321-1332(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8491193; DOI=10.1002/j.1460-2075.1993.tb05852.x;
RA Burk O., Mink S., Ringwald M., Klempnauer K.H.;
RT "Synergistic activation of the chicken mim-1 gene by v-myb and C/EBP
RT transcription factors.";
RL EMBO J. 12:2027-2038(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kintscher J.R., Miethe J., Klempnauer K.-H.;
RT "Analysis of DNase I-hypersensitive sites in the chromatin of the chicken
RT C/EBPbeta gene reveals multiple cell-type specific cis-regulatory
RT elements.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, METHYLATION AT LYS-39, AND MUTAGENESIS OF LYS-39.
RX PubMed=18647749; DOI=10.1074/jbc.m802132200;
RA Pless O., Kowenz-Leutz E., Knoblich M., Lausen J., Beyermann M.,
RA Walsh M.J., Leutz A.;
RT "G9a-mediated lysine methylation alters the function of CCAAT/enhancer-
RT binding protein-beta.";
RL J. Biol. Chem. 283:26357-26363(2008).
RN [5]
RP METHYLATION AT ARG-3, MUTAGENESIS OF ARG-3 AND THR-220, INTERACTION WITH
RP MED23 AND SMARCA2, AND PHOSPHORYLATION AT THR-220.
RX PubMed=20111005; DOI=10.1038/emboj.2010.3;
RA Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
RT "Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and
RT SWI/SNF/Mediator implies an indexing transcription factor code.";
RL EMBO J. 29:1105-1115(2010).
CC -!- FUNCTION: Important transcriptional activator regulating the expression
CC of genes involved in immune and inflammatory responses. Binds to
CC regulatory regions of several acute-phase and cytokines genes and
CC probably plays a role in the regulation of acute-phase reaction,
CC inflammation and hemopoiesis. The consensus recognition site is 5'-
CC T[TG]NNGNAA[TG]-3'. Functions in brown adipose tissue (BAT)
CC differentiation. Regulates the transcriptional induction of peroxisome
CC proliferator-activated receptor gamma (PPARG). Binds to the MGF and
CC MIM-1 promoters and activates the transcription of these genes.
CC {ECO:0000269|PubMed:8467792}.
CC -!- FUNCTION: Important transcription factor regulating the expression of
CC genes involved in immune and inflammatory responses (PubMed:8467792).
CC Also plays a significant role in adipogenesis, as well as in the
CC gluconeogenic pathway, liver regeneration, and hematopoiesis. The
CC consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional
CC capacity is governed by protein interactions and post-translational
CC protein modifications. {ECO:0000250|UniProtKB:P17676,
CC ECO:0000250|UniProtKB:P21272, ECO:0000250|UniProtKB:P28033,
CC ECO:0000269|PubMed:8467792}.
CC -!- SUBUNIT: Binds DNA as a dimer. Interacts (not methylated) with MED23,
CC MED26, SMARCA2, SMARCB1 and SMARCC1 (PubMed:20111005).
CC {ECO:0000269|PubMed:20111005}.
CC -!- INTERACTION:
CC Q05826; Q86X55: CARM1; Xeno; NbExp=3; IntAct=EBI-7774198, EBI-2339854;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in myelomoncytic cells.
CC -!- PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2,
CC inhibit transactivation activity. Methylation is probably inhibited by
CC phosphorylation at Thr-220. {ECO:0000250|UniProtKB:P17676,
CC ECO:0000269|PubMed:18647749, ECO:0000269|PubMed:20111005}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; Z21646; CAA79760.1; -; mRNA.
DR EMBL; X70813; CAA50144.1; -; mRNA.
DR EMBL; AY212285; AAO39751.1; -; Genomic_DNA.
DR PIR; S35336; S35336.
DR RefSeq; NP_990584.1; NM_205253.2.
DR AlphaFoldDB; Q05826; -.
DR SMR; Q05826; -.
DR IntAct; Q05826; 2.
DR MINT; Q05826; -.
DR STRING; 9031.ENSGALP00000012991; -.
DR iPTMnet; Q05826; -.
DR PaxDb; Q05826; -.
DR Ensembl; ENSGALT00000013006; ENSGALP00000012991; ENSGALG00000008014.
DR GeneID; 396185; -.
DR KEGG; gga:396185; -.
DR CTD; 1051; -.
DR VEuPathDB; HostDB:geneid_396185; -.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000162137; -.
DR HOGENOM; CLU_043327_1_0_1; -.
DR InParanoid; Q05826; -.
DR OMA; RLVAWDA; -.
DR OrthoDB; 1284308at2759; -.
DR PhylomeDB; Q05826; -.
DR TreeFam; TF105008; -.
DR Reactome; R-GGA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR PRO; PR:Q05826; -.
DR Proteomes; UP000000539; Chromosome 20.
DR Bgee; ENSGALG00000008014; Expressed in granulocyte and 12 other tissues.
DR GO; GO:1990647; C:C/EBP complex; IEA:Ensembl.
DR GO; GO:0036488; C:CHOP-C/EBP complex; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0072574; P:hepatocyte proliferation; IEA:Ensembl.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0070169; P:positive regulation of biomineral tissue development; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:AgBase.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IDA:AgBase.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:2000120; P:positive regulation of sodium-dependent phosphate transport; IEA:Ensembl.
DR GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:2001198; P:regulation of dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:0032675; P:regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016468; C/EBP_chordates.
DR Pfam; PF07716; bZIP_2; 1.
DR PIRSF; PIRSF005879; CCAAT/enhancer-binding; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..328
FT /note="CCAAT/enhancer-binding protein beta"
FT /id="PRO_0000076620"
FT DOMAIN 254..317
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 165..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..278
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 280..287
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 187..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Asymmetric dimethylarginine; by CARM1"
FT /evidence="ECO:0000269|PubMed:20111005"
FT MOD_RES 39
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000305|PubMed:18647749"
FT MOD_RES 220
FT /note="Phosphothreonine; by RPS6KA1, CDK2 and MAPK"
FT /evidence="ECO:0000305|PubMed:18647749"
FT MUTAGEN 3
FT /note="R->A: Not methylated. Increases interaction with
FT SMARCA2 and MED23."
FT /evidence="ECO:0000269|PubMed:20111005"
FT MUTAGEN 3
FT /note="R->L: Decreases interaction with SMARCA2 and MED23."
FT /evidence="ECO:0000269|PubMed:20111005"
FT MUTAGEN 39
FT /note="K->A: Decreases methylation. Increases
FT transactivation activity inhibition."
FT /evidence="ECO:0000269|PubMed:18647749"
FT MUTAGEN 220
FT /note="T->D: Decreases methylation by CARM1 and increases
FT transactivation activity."
FT /evidence="ECO:0000269|PubMed:20111005"
SQ SEQUENCE 328 AA; 35030 MW; 5AAE257F8213671C CRC64;
MQRLVAWDAA CLPIQPPAFK SMEVANFYYE ADCLAALNKL HPRAAGGRSM TELTVGDHER
AIDFSPYLDP LAASQQPAQP PPPAAAAGGN FEPACSSGGQ DFLSDLFAED YKGSGGGKKP
DYTYISLTRH GHPCGSQSHK PGVLPGCFPP QIVETKVEPV FETLDSCKGP RKEEGGAGPG
PGGMSSPYGS TVRSYLGYQS VPSGSSGNLS TSSSSSPPGT PNPSESSKSA AGAGGYSGPP
AGKNKPKKCV DKHSDEYKLR RERNNIAVRK SRDKAKMRNL ETQHKVLELT AENERLQKKV
EQLSRELSTL RNLFKQLPEP LLASSPRC
