CEBPB_RAT
ID CEBPB_RAT Reviewed; 297 AA.
AC P21272; A2VD03;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=CCAAT/enhancer-binding protein beta {ECO:0000312|RGD:2327};
DE Short=C/EBP beta {ECO:0000312|RGD:2327};
DE AltName: Full=C/EBP-related protein 2;
DE AltName: Full=Interleukin-6-dependent-binding protein;
DE Short=IL-6DBP;
DE AltName: Full=Liver-enriched inhibitory protein;
DE Short=LIP;
DE AltName: Full=Liver-enriched transcriptional activator;
DE Short=LAP;
DE AltName: Full=Silencer factor B;
DE Short=SF-B;
GN Name=Cebpb {ECO:0000312|RGD:2327};
GN Synonyms=Crp2, Nf-il6 {ECO:0000303|PubMed:8336793}, Sfb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2171780; DOI=10.1016/0092-8674(90)90459-r;
RA Poli V., Mancini F.P., Cortese R.;
RT "IL-6DBP, a nuclear protein involved in interleukin-6 signal transduction,
RT defines a new family of leucine zipper proteins related to C/EBP.";
RL Cell 63:643-653(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Lewis; TISSUE=Liver;
RX PubMed=2253878; DOI=10.1101/gad.4.9.1541;
RA Descombes P., Chojkier M., Lichtsteiner S., Falvey E., Schibler U.;
RT "LAP, a novel member of the C/EBP gene family, encodes a liver-enriched
RT transcriptional activator protein.";
RL Genes Dev. 4:1541-1551(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1377818; DOI=10.1093/nar/20.12.3091;
RA Thomassin H., Hamel D., Bernier D., Guertin M., Belanger L.;
RT "Molecular cloning of two C/EBP-related proteins that bind to the promoter
RT and the enhancer of the alpha 1-fetoprotein gene. Further analysis of C/EBP
RT beta and C/EBP gamma.";
RL Nucleic Acids Res. 20:3091-3098(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 77-297 (ISOFORM 1).
RC TISSUE=Liver;
RA Imagawa M., Osada S., Koyama Y., Suzuki T., Hirom P.C., Diccianni M.B.,
RA Morimura S., Muramatsu M.;
RT "SF-B (Silencer Factor B) that binds to a negative element in glutathione
RT transferase P gene is most likely identical to an inducible trans-activator
RT LAP/IL6-DBP.";
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-297, SUBUNIT, AND DNA-BINDING.
RC STRAIN=Sprague-Dawley; TISSUE=Adipose tissue, Liver, and Lung;
RX PubMed=1884998; DOI=10.1101/gad.5.9.1553;
RA Williams S.C., Cantwell C.A., Johnson P.F.;
RT "A family of C/EBP-related proteins capable of forming covalently linked
RT leucine zipper dimers in vitro.";
RL Genes Dev. 5:1553-1567(1991).
RN [7]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), DNA-BINDING,
RP DIMERIZATION, AND SUBUNIT.
RX PubMed=1934061; DOI=10.1016/0092-8674(91)90531-3;
RA Descombes P., Schibler U.;
RT "A liver-enriched transcriptional activator protein, LAP, and a
RT transcriptional inhibitory protein, LIP, are translated from the same
RT mRNA.";
RL Cell 67:569-579(1991).
RN [8]
RP FUNCTION, PHOSPHORYLATION AT SER-105, AND MUTAGENESIS OF SER-105.
RX PubMed=8336793; DOI=10.1038/364544a0;
RA Trautwein C., Caelles C., van der Geer P., Hunter T., Karin M.,
RA Chojkier M.;
RT "Transactivation by NF-IL6/LAP is enhanced by phosphorylation of its
RT activation domain.";
RL Nature 364:544-547(1993).
RN [9]
RP FUNCTION, PHOSPHORYLATION AT SER-105, MUTAGENESIS OF SER-105, AND TISSUE
RP SPECIFICITY.
RX PubMed=10635333; DOI=10.1016/s1097-2765(00)80237-3;
RA Buck M., Poli V., van der Geer P., Chojkier M., Hunter T.;
RT "Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP beta is
RT required for hepatocyte proliferation induced by TGF alpha.";
RL Mol. Cell 4:1087-1092(1999).
RN [10]
RP FUNCTION, AND INTERACTION WITH NFE2L1.
RX PubMed=15308669; DOI=10.1074/jbc.m405031200;
RA Narayanan K., Ramachandran A., Peterson M.C., Hao J., Kolstoe A.B.,
RA Friedman A.D., George A.;
RT "The CCAAT enhancer-binding protein (C/EBP)beta and Nrf1 interact to
RT regulate dentin sialophosphoprotein (DSPP) gene expression during
RT odontoblast differentiation.";
RL J. Biol. Chem. 279:45423-45432(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Important transcription factor regulating the expression of
CC genes involved in immune and inflammatory responses (PubMed:8336793).
CC Also plays a significant role in adipogenesis, as well as in the
CC gluconeogenic pathway, liver regeneration, and hematopoiesis
CC (PubMed:10635333). The consensus recognition site is 5'-
CC T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein
CC interactions and post-translational protein modifications. During early
CC embryogenesis, plays essential and redundant roles with CEBPA (By
CC similarity). Has a promitotic effect on many cell types such as
CC hepatocytes and adipocytes but has an antiproliferative effect on T-
CC cells by repressing MYC expression, facilitating differentiation along
CC the T-helper 2 lineage (PubMed:10635333). Binds to regulatory regions
CC of several acute-phase and cytokines genes and plays a role in the
CC regulation of acute-phase reaction and inflammation. Also plays a role
CC in intracellular bacteria killing (By similarity). During adipogenesis,
CC is rapidly expressed and, after activation by phosphorylation, induces
CC CEBPA and PPARG, which turn on the series of adipocyte genes that give
CC rise to the adipocyte phenotype. The delayed transactivation of the
CC CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic
CC clonal expansion and thereby progression of terminal differentiation
CC (By similarity). Essential for female reproduction because of a
CC critical role in ovarian follicle development (By similarity).
CC Restricts osteoclastogenesis: together with NFE2L1; represses
CC expression of DSPP during odontoblast differentiation
CC (PubMed:15308669). {ECO:0000250|UniProtKB:P17676,
CC ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:10635333,
CC ECO:0000269|PubMed:15308669, ECO:0000269|PubMed:1934061,
CC ECO:0000269|PubMed:8336793}.
CC -!- FUNCTION: [Isoform 2]: Essential for gene expression induction in
CC activated macrophages. Plays a major role in immune responses such as
CC CD4(+) T-cell response, granuloma formation and endotoxin shock. Not
CC essential for intracellular bacteria killing.
CC {ECO:0000250|UniProtKB:P28033}.
CC -!- FUNCTION: [Isoform 3]: Acts as a dominant negative through
CC heterodimerization with isoform 2 (PubMed:1934061). Promotes osteoblast
CC differentiation and osteoclastogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033,
CC ECO:0000269|PubMed:1934061}.
CC -!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer
CC (PubMed:1934061). Interacts with MYB; within the complex, MYB and CEBPB
CC bind to different promoter regions. Interacts with ATF4. Binds DNA as a
CC heterodimer with ATF4 (By similarity). Can form stable heterodimers
CC with CEBPA, CEBPD, CEBPE and CEBPG (PubMed:1377818, PubMed:1884998).
CC Interacts with SIX1 (By similarity). Isoform 2 and isoform 3 also form
CC heterodimers (PubMed:1934061). Interacts with TRIM28 and PTGES2.
CC Interacts with PRDM16. Interacts with CCDC85B. Forms a complex with
CC THOC5. Interacts with ZNF638; this interaction increases
CC transcriptional activation. Interacts with CIDEA and CIDEC; these
CC interactions increase transcriptional activation of a subset of CEBPB
CC downstream target genes. Interacts with DDIT3/CHOP.Interacts with
CC EP300; recruits EP300 to chromatin. Interacts with RORA; the
CC interaction disrupts interaction with EP300. Interacts (not methylated)
CC with MED23, MED26, SMARCA2, SMARCB1 and SMARCC1 (By similarity).
CC Interacts with KAT2A and KAT2B (By similarity). Interacts with ATF5;
CC EP300 is required for ATF5 and CEBPB interaction and DNA binding (By
CC similarity). Interacts with NFE2L1; the heterodimer represses
CC expression of DSPP during odontoblast differentiation
CC (PubMed:15308669). {ECO:0000250|UniProtKB:P17676,
CC ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:1377818,
CC ECO:0000269|PubMed:15308669, ECO:0000269|PubMed:1884998,
CC ECO:0000269|PubMed:1934061}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17676}. Cytoplasm
CC {ECO:0000250|UniProtKB:P17676}. Note=Translocates to the nucleus when
CC phosphorylated at Ser-288. In T-cells when sumoylated drawn to
CC pericentric heterochromatin thereby allowing proliferation (By
CC similarity). {ECO:0000250|UniProtKB:P17676,
CC ECO:0000250|UniProtKB:P28033}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=1; Synonyms=FL;
CC IsoId=P21272-1; Sequence=Displayed;
CC Name=2; Synonyms=LAP;
CC IsoId=P21272-2; Sequence=VSP_053316;
CC Name=3; Synonyms=LIP;
CC IsoId=P21272-3; Sequence=VSP_053315;
CC -!- TISSUE SPECIFICITY: Liver and lung.
CC -!- PTM: Phosphorylated at Thr-189 by MAPK and CDK2, serves to prime
CC phosphorylation at Thr-180 and Ser-185 by GSK3B and acquire DNA-binding
CC as well as transactivation activities, required to induce adipogenesis.
CC MAPK and CDK2 act sequentially to maintain Thr-189 in the primed
CC phosphorylated state during mitotical cloning expansion and thereby
CC progression of terminal differentiation (By similarity).
CC Phosphorylation at Ser-105 enhances transactivation activity
CC (PubMed:8336793). Phosphorylation at Ser-277 in response to calcium
CC increases transactivation activity. Phosphorylated at Thr-189 by
CC RPS6KA1 (By similarity). {ECO:0000250|UniProtKB:P17676,
CC ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:8336793}.
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-189. {ECO:0000250|UniProtKB:P17676}.
CC -!- PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3 (By similarity).
CC Sumoylation at Lys-134 is required for inhibition of T-cells
CC proliferation. In adipocytes, sumoylation at Lys-134 by PIAS1 leads to
CC ubiquitination and subsequent proteasomal degradation. Desumoylated by
CC SENP2, which abolishes ubiquitination and stabilizes protein levels (By
CC similarity). {ECO:0000250|UniProtKB:P17676,
CC ECO:0000250|UniProtKB:P28033}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P28033}.
CC -!- PTM: O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents
CC phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding
CC activity which delays the adipocyte differentiation program.
CC {ECO:0000250|UniProtKB:P28033}.
CC -!- PTM: Acetylated. Acetylation at Lys-39 is an important and dynamic
CC regulatory event that contributes to its ability to transactivate
CC target genes, including those associated with adipogenesis and
CC adipocyte function. Deacetylation by HDAC1 represses its
CC transactivation activity. Acetylated by KAT2A and KAT2B within a
CC cluster of lysine residues between amino acids 99-103, this acetylation
CC is strongly induced by glucocorticoid treatment and enhances
CC transactivation activity. {ECO:0000250|UniProtKB:P28033}.
CC -!- MISCELLANEOUS: [Isoform 1]: Not detected in rat liver.
CC -!- MISCELLANEOUS: [Isoform 2]: Major form in. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; M57235; AAA19669.1; -; mRNA.
DR EMBL; X54626; CAA38443.1; -; Genomic_DNA.
DR EMBL; BC129071; AAI29072.1; -; mRNA.
DR EMBL; X60769; CAA43179.1; -; mRNA.
DR EMBL; AY056052; AAA40972.1; -; Genomic_DNA.
DR PIR; A35914; A35914.
DR RefSeq; NP_001288644.1; NM_001301715.1. [P21272-2]
DR RefSeq; NP_001288649.1; NM_001301720.1. [P21272-3]
DR RefSeq; NP_077039.3; NM_024125.5. [P21272-1]
DR AlphaFoldDB; P21272; -.
DR SMR; P21272; -.
DR BioGRID; 246438; 101.
DR ComplexPortal; CPX-62; bZIP transcription factor complex, Cebpb-Ddit3.
DR ComplexPortal; CPX-63; bZIP transcription factor complex, Cebpb-Cebpb.
DR DIP; DIP-28139N; -.
DR IntAct; P21272; 2.
DR STRING; 10116.ENSRNOP00000065222; -.
DR GlyGen; P21272; 2 sites.
DR iPTMnet; P21272; -.
DR PhosphoSitePlus; P21272; -.
DR PaxDb; P21272; -.
DR PeptideAtlas; P21272; -.
DR GeneID; 24253; -.
DR KEGG; rno:24253; -.
DR UCSC; RGD:2327; rat. [P21272-1]
DR CTD; 1051; -.
DR RGD; 2327; Cebpb.
DR VEuPathDB; HostDB:ENSRNOG00000057347; -.
DR eggNOG; KOG3119; Eukaryota.
DR HOGENOM; CLU_043327_1_0_1; -.
DR InParanoid; P21272; -.
DR OMA; RLVAWDA; -.
DR OrthoDB; 1284308at2759; -.
DR PhylomeDB; P21272; -.
DR TreeFam; TF105008; -.
DR Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR PRO; PR:P21272; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000057347; Expressed in liver and 19 other tissues.
DR Genevisible; P21272; RN.
DR GO; GO:1990647; C:C/EBP complex; ISO:RGD.
DR GO; GO:0036488; C:CHOP-C/EBP complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IPI:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:RGD.
DR GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IDA:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0001892; P:embryonic placenta development; ISO:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR GO; GO:0002432; P:granuloma formation; ISS:UniProtKB.
DR GO; GO:0072574; P:hepatocyte proliferation; IDA:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0097421; P:liver regeneration; ISS:UniProtKB.
DR GO; GO:0060644; P:mammary gland epithelial cell differentiation; ISO:RGD.
DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; ISO:RGD.
DR GO; GO:0007613; P:memory; IEP:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0070169; P:positive regulation of biomineral tissue development; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:2000120; P:positive regulation of sodium-dependent phosphate transport; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:2001198; P:regulation of dendritic cell differentiation; ISO:RGD.
DR GO; GO:0032675; P:regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:1901329; P:regulation of odontoblast differentiation; IDA:UniProtKB.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0035711; P:T-helper 1 cell activation; ISS:UniProtKB.
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 Acetylation; Activator; Alternative initiation; Cytoplasm; Differentiation;
KW DNA-binding; Glycoprotein; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..297
FT /note="CCAAT/enhancer-binding protein beta"
FT /id="PRO_0000076619"
FT DOMAIN 223..286
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..22
FT /note="Required for Lys-134 sumoylation"
FT /evidence="ECO:0000250|UniProtKB:P17676"
FT REGION 22..105
FT /note="Required for MYC transcriptional repression"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT REGION 172..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..247
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 249..256
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 172..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Asymmetric dimethylarginine; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT MOD_RES 39
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT MOD_RES 39
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT MOD_RES 99
FT /note="N6-acetyllysine; by KAT2A and KAT2B"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT MOD_RES 102
FT /note="N6-acetyllysine; by KAT2A and KAT2B"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT MOD_RES 103
FT /note="N6-acetyllysine; by KAT2A and KAT2B; alternate"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT MOD_RES 105
FT /note="Phosphoserine; by RPS6KA1 and PKC/PRKCA"
FT /evidence="ECO:0000269|PubMed:10635333,
FT ECO:0000269|PubMed:8336793"
FT MOD_RES 180
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT MOD_RES 185
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT MOD_RES 189
FT /note="Phosphothreonine; by RPS6KA1, CDK2 and MAPK"
FT /evidence="ECO:0000250|UniProtKB:P17676"
FT MOD_RES 240
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P17676"
FT MOD_RES 277
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT CARBOHYD 181
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT CARBOHYD 182
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:P28033"
FT CROSSLNK 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17676"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17676,
FT ECO:0000250|UniProtKB:P28033"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17676"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17676"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17676"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17676"
FT CROSSLNK 284
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17676"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053315"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053316"
FT MUTAGEN 105
FT /note="S->A: No effect on DNA-binding. Loss of
FT transactivation activity. Loss of hepatocyte proliferation
FT induction by TGFA."
FT /evidence="ECO:0000269|PubMed:10635333,
FT ECO:0000269|PubMed:8336793"
FT MUTAGEN 105
FT /note="S->D: No effect on DNA-binding. Increases
FT transactivation activity."
FT /evidence="ECO:0000269|PubMed:8336793"
SQ SEQUENCE 297 AA; 31503 MW; C2511FDB65527789 CRC64;
MHRLLAWDAA CLPPPPAAFR PMEVANFYYE PDCLAYGAKA ARAAPRAPAA EPAIGEHERA
IDFSPYLEPL APAAADFAAP APAHHDFLSD LFADDYGAKP SKKPSDYGYV SLGRAGAKAA
PPACFPPPPP AALKAEPGFE PADCKRADDA PAMAAGFPFA LRAYLGYQAT PSGSSGSLST
SSSSSPPGTP SPADAKAAPA ACFAGPPAAP AKAKAKKAVD KLSDEYKMRR ERNNIAVRKS
RDKAKMRNLE TQHKVLELTA ENERLQKKVE QLSRELSTLR NLFKQLPEPL LASAGHC
