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CCAAT/enhancer-binding protein beta (C/EBP beta) (C/EBP-related protein 2) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched inhibitory protein) (LIP) (Liver-enriched transcriptional activator) (LAP) (Silencer factor B) (SF-B)

 CEBPB_RAT               Reviewed;         297 AA.
P21272; A2VD03;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
02-JUN-2021, entry version 177.
RecName: Full=CCAAT/enhancer-binding protein beta {ECO:0000312|RGD:2327};
Short=C/EBP beta {ECO:0000312|RGD:2327};
AltName: Full=C/EBP-related protein 2;
AltName: Full=Interleukin-6-dependent-binding protein;
Short=IL-6DBP;
AltName: Full=Liver-enriched inhibitory protein;
Short=LIP;
AltName: Full=Liver-enriched transcriptional activator;
Short=LAP;
AltName: Full=Silencer factor B;
Short=SF-B;
Name=Cebpb {ECO:0000312|RGD:2327};
Synonyms=Crp2, Nf-il6 {ECO:0000303|PubMed:8336793}, Sfb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2171780; DOI=10.1016/0092-8674(90)90459-r;
Poli V., Mancini F.P., Cortese R.;
"IL-6DBP, a nuclear protein involved in interleukin-6 signal transduction,
defines a new family of leucine zipper proteins related to C/EBP.";
Cell 63:643-653(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Lewis; TISSUE=Liver;
PubMed=2253878; DOI=10.1101/gad.4.9.1541;
Descombes P., Chojkier M., Lichtsteiner S., Falvey E., Schibler U.;
"LAP, a novel member of the C/EBP gene family, encodes a liver-enriched
transcriptional activator protein.";
Genes Dev. 4:1541-1551(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=1377818; DOI=10.1093/nar/20.12.3091;
Thomassin H., Hamel D., Bernier D., Guertin M., Belanger L.;
"Molecular cloning of two C/EBP-related proteins that bind to the promoter
and the enhancer of the alpha 1-fetoprotein gene. Further analysis of C/EBP
beta and C/EBP gamma.";
Nucleic Acids Res. 20:3091-3098(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 77-297 (ISOFORM 1).
TISSUE=Liver;
Imagawa M., Osada S., Koyama Y., Suzuki T., Hirom P.C., Diccianni M.B.,
Morimura S., Muramatsu M.;
"SF-B (Silencer Factor B) that binds to a negative element in glutathione
transferase P gene is most likely identical to an inducible trans-activator
LAP/IL6-DBP.";
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-297, SUBUNIT, AND DNA-BINDING.
STRAIN=Sprague-Dawley; TISSUE=Adipose tissue, Liver, and Lung;
PubMed=1884998; DOI=10.1101/gad.5.9.1553;
Williams S.C., Cantwell C.A., Johnson P.F.;
"A family of C/EBP-related proteins capable of forming covalently linked
leucine zipper dimers in vitro.";
Genes Dev. 5:1553-1567(1991).
[7]
FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), DNA-BINDING,
DIMERIZATION, AND SUBUNIT.
PubMed=1934061; DOI=10.1016/0092-8674(91)90531-3;
Descombes P., Schibler U.;
"A liver-enriched transcriptional activator protein, LAP, and a
transcriptional inhibitory protein, LIP, are translated from the same
mRNA.";
Cell 67:569-579(1991).
[8]
FUNCTION, PHOSPHORYLATION AT SER-105, AND MUTAGENESIS OF SER-105.
PubMed=8336793; DOI=10.1038/364544a0;
Trautwein C., Caelles C., van der Geer P., Hunter T., Karin M.,
Chojkier M.;
"Transactivation by NF-IL6/LAP is enhanced by phosphorylation of its
activation domain.";
Nature 364:544-547(1993).
[9]
FUNCTION, PHOSPHORYLATION AT SER-105, MUTAGENESIS OF SER-105, AND TISSUE
SPECIFICITY.
PubMed=10635333; DOI=10.1016/s1097-2765(00)80237-3;
Buck M., Poli V., van der Geer P., Chojkier M., Hunter T.;
"Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP beta is
required for hepatocyte proliferation induced by TGF alpha.";
Mol. Cell 4:1087-1092(1999).
[10]
FUNCTION, AND INTERACTION WITH NFE2L1.
PubMed=15308669; DOI=10.1074/jbc.m405031200;
Narayanan K., Ramachandran A., Peterson M.C., Hao J., Kolstoe A.B.,
Friedman A.D., George A.;
"The CCAAT enhancer-binding protein (C/EBP)beta and Nrf1 interact to
regulate dentin sialophosphoprotein (DSPP) gene expression during
odontoblast differentiation.";
J. Biol. Chem. 279:45423-45432(2004).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Important transcription factor regulating the expression of
genes involved in immune and inflammatory responses (PubMed:8336793).
Plays also a significant role in adipogenesis, as well as in the
gluconeogenic pathway, liver regeneration, and hematopoiesis
(PubMed:10635333). 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 (By
similarity). 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:10635333). 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 (By similarity). 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
(By similarity). Essential for female reproduction because of a
critical role in ovarian follicle development (By similarity).
Restricts osteoclastogenesis: together with NFE2L1; represses
expression of DSPP during odontoblast differentiation
(PubMed:15308669). {ECO:0000250|UniProtKB:P17676,
ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:10635333,
ECO:0000269|PubMed:15308669, ECO:0000269|PubMed:1934061,
ECO:0000269|PubMed:8336793}.
-!- FUNCTION: [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.
{ECO:0000250|UniProtKB:P28033}.
-!- FUNCTION: [Isoform 3]: Acts as a dominant negative through
heterodimerization with isoform 2 (PubMed:1934061). Promotes osteoblast
differentiation and osteoclastogenesis (By similarity).
{ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033,
ECO:0000269|PubMed:1934061}.
-!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer
(PubMed:1934061). Interacts with MYB; within the complex, MYB and CEBPB
bind to different promoter regions. Interacts with ATF4. Binds DNA as a
heterodimer with ATF4 (By similarity). Can form stable heterodimers
with CEBPA, CEBPD, CEBPE and CEBPG (PubMed:1377818, PubMed:1884998).
Interacts with SIX1 (By similarity). Isoform 2 and isoform 3 also form
heterodimers (PubMed:1934061). 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; these
interactions increase transcriptional activation of a subset of CEBPB
downstream target genes. 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 (By similarity).
Interacts with KAT2A and KAT2B (By similarity). Interacts with ATF5;
EP300 is required for ATF5 and CEBPB interaction and DNA binding (By
similarity). Interacts with NFE2L1; the heterodimer represses
expression of DSPP during odontoblast differentiation
(PubMed:15308669). {ECO:0000250|UniProtKB:P17676,
ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:1377818,
ECO:0000269|PubMed:15308669, ECO:0000269|PubMed:1884998,
ECO:0000269|PubMed:1934061}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17676}. Cytoplasm
{ECO:0000250|UniProtKB:P17676}. Note=Translocates to the nucleus when
phosphorylated at Ser-288. In T-cells when sumoylated drawn to
pericentric heterochromatin thereby allowing proliferation (By
similarity). {ECO:0000250|UniProtKB:P17676,
ECO:0000250|UniProtKB:P28033}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=1; Synonyms=FL;
IsoId=P21272-1; Sequence=Displayed;
Name=2; Synonyms=LAP;
IsoId=P21272-2; Sequence=VSP_053316;
Name=3; Synonyms=LIP;
IsoId=P21272-3; Sequence=VSP_053315;
-!- TISSUE SPECIFICITY: Liver and lung.
-!- PTM: Phosphorylated at Thr-189 by MAPK and CDK2, serves to prime
phosphorylation at Thr-180 and Ser-185 by GSK3B and acquire DNA-binding
as well as transactivation activities, required to induce adipogenesis.
MAPK and CDK2 act sequentially to maintain Thr-189 in the primed
phosphorylated state during mitotical cloning expansion and thereby
progression of terminal differentiation (By similarity).
Phosphorylation at Ser-105 enhances transactivation activity
(PubMed:8336793). Phosphorylation at Ser-277 in response to calcium
increases transactivation activity. Phosphorylated at Thr-189 by
RPS6KA1 (By similarity). {ECO:0000250|UniProtKB:P17676,
ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:8336793}.
-!- PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2
inhibit transactivation activity. Methylation is probably inhibited by
phosphorylation at Thr-189. {ECO:0000250|UniProtKB:P17676}.
-!- PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3 (By similarity).
Sumoylation at Lys-134 is required for inhibition of T-cells
proliferation. In adipocytes, sumoylation at Lys-134 by PIAS1 leads to
ubiquitination and subsequent proteasomal degradation. Desumoylated by
SENP2, which abolishes ubiquitination and stabilizes protein levels (By
similarity). {ECO:0000250|UniProtKB:P17676,
ECO:0000250|UniProtKB:P28033}.
-!- PTM: Ubiquitinated, leading to proteasomal degradation.
{ECO:0000250|UniProtKB:P28033}.
-!- PTM: O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents
phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding
activity which delays the adipocyte differentiation program.
{ECO:0000250|UniProtKB:P28033}.
-!- PTM: 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. Acetylated by KAT2A and KAT2B within a
cluster of lysine residues between amino acids 99-103, this acetylation
is strongly induced by glucocorticoid treatment and enhances
transactivation activity. {ECO:0000250|UniProtKB:P28033}.
-!- MISCELLANEOUS: [Isoform 1]: Not detected in rat liver.
-!- MISCELLANEOUS: [Isoform 2]: Major form in. {ECO:0000305}.
-!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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EMBL; M57235; AAA19669.1; -; mRNA.
EMBL; X54626; CAA38443.1; -; Genomic_DNA.
EMBL; BC129071; AAI29072.1; -; mRNA.
EMBL; X60769; CAA43179.1; -; mRNA.
EMBL; AY056052; AAA40972.1; -; Genomic_DNA.
PIR; A35914; A35914.
RefSeq; NP_001288644.1; NM_001301715.1. [P21272-2]
RefSeq; NP_001288649.1; NM_001301720.1. [P21272-3]
RefSeq; NP_077039.3; NM_024125.5. [P21272-1]
SMR; P21272; -.
BioGRID; 246438; 101.
ComplexPortal; CPX-62; CHOP-C/EBPbeta complex.
ComplexPortal; CPX-63; C/EBPbeta complex.
DIP; DIP-28139N; -.
IntAct; P21272; 2.
STRING; 10116.ENSRNOP00000065222; -.
GlyGen; P21272; 2 sites.
iPTMnet; P21272; -.
PhosphoSitePlus; P21272; -.
PaxDb; P21272; -.
PeptideAtlas; P21272; -.
PRIDE; P21272; -.
Ensembl; ENSRNOT00000083876; ENSRNOP00000071427; ENSRNOG00000057347. [P21272-1]
GeneID; 24253; -.
KEGG; rno:24253; -.
UCSC; RGD:2327; rat. [P21272-1]
CTD; 1051; -.
RGD; 2327; Cebpb.
eggNOG; KOG3119; Eukaryota.
GeneTree; ENSGT00940000162137; -.
HOGENOM; CLU_043327_1_0_1; -.
InParanoid; P21272; -.
OMA; KNCKKAA; -.
OrthoDB; 1284308at2759; -.
PhylomeDB; P21272; -.
TreeFam; TF105008; -.
Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
PRO; PR:P21272; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000057347; Expressed in liver and 20 other tissues.
Genevisible; P21272; RN.
GO; GO:0036488; C:CHOP-C/EBP complex; IPI:ParkinsonsUK-UCL.
GO; GO:0000785; C:chromatin; ISO:RGD.
GO; GO:0000779; C:condensed chromosome, centromeric region; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0016363; C:nuclear matrix; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
GO; GO:0003682; F:chromatin binding; ISO:RGD.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
GO; GO:0035259; F:glucocorticoid receptor binding; IPI:RGD.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:RGD.
GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0019900; F:kinase binding; ISO:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:RGD.
GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:RGD.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:RGD.
GO; GO:0050873; P:brown fat cell differentiation; ISO:RGD.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
GO; GO:0001892; P:embryonic placenta development; ISO:RGD.
GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
GO; GO:0002432; P:granuloma formation; ISS:UniProtKB.
GO; GO:0072574; P:hepatocyte proliferation; IDA:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0097421; P:liver regeneration; ISS:UniProtKB.
GO; GO:0060644; P:mammary gland epithelial cell differentiation; ISO:RGD.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; ISO:RGD.
GO; GO:0007613; P:memory; IEP:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0030182; P:neuron differentiation; ISO:RGD.
GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
GO; GO:0070169; P:positive regulation of biomineral tissue development; ISO:RGD.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
GO; GO:2000120; P:positive regulation of sodium-dependent phosphate transport; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
GO; GO:2001198; P:regulation of dendritic cell differentiation; ISO:RGD.
GO; GO:0032675; P:regulation of interleukin-6 production; ISO:RGD.
GO; GO:1901329; P:regulation of odontoblast differentiation; IDA:UniProtKB.
GO; GO:0045670; P:regulation of osteoclast differentiation; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
GO; GO:0035711; P:T-helper 1 cell activation; ISS:UniProtKB.
InterPro; IPR004827; bZIP.
InterPro; IPR016468; C/EBP_chordates.
Pfam; PF07716; bZIP_2; 1.
PIRSF; PIRSF005879; CCAAT/enhancer-binding; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative initiation; Cytoplasm; Differentiation;
DNA-binding; Glycoprotein; Isopeptide bond; Methylation; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1..297
/note="CCAAT/enhancer-binding protein beta"
/id="PRO_0000076619"
DOMAIN 223..286
/note="bZIP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
REGION 1..22
/note="Required for Lys-134 sumoylation"
/evidence="ECO:0000250|UniProtKB:P17676"
REGION 22..105
/note="Required for MYC transcriptional repression"
/evidence="ECO:0000250|UniProtKB:P28033"
REGION 172..201
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 227..247
/note="Basic motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
REGION 249..256
/note="Leucine-zipper"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
COMPBIAS 172..190
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 3
/note="Asymmetric dimethylarginine; by CARM1"
/evidence="ECO:0000250|UniProtKB:P28033"
MOD_RES 39
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P28033"
MOD_RES 39
/note="N6-methylated lysine; alternate"
/evidence="ECO:0000250|UniProtKB:P28033"
MOD_RES 99
/note="N6-acetyllysine; by KAT2A and KAT2B"
/evidence="ECO:0000250|UniProtKB:P28033"
MOD_RES 102
/note="N6-acetyllysine; by KAT2A and KAT2B"
/evidence="ECO:0000250|UniProtKB:P28033"
MOD_RES 103
/note="N6-acetyllysine; by KAT2A and KAT2B; alternate"
/evidence="ECO:0000250|UniProtKB:P28033"
MOD_RES 105
/note="Phosphoserine; by RPS6KA1 and PKC/PRKCA"
/evidence="ECO:0000269|PubMed:10635333,
ECO:0000269|PubMed:8336793"
MOD_RES 180
/note="Phosphothreonine; by GSK3-beta"
/evidence="ECO:0000250|UniProtKB:P28033"
MOD_RES 185
/note="Phosphoserine; by GSK3-beta"
/evidence="ECO:0000250|UniProtKB:P28033"
MOD_RES 189
/note="Phosphothreonine; by RPS6KA1, CDK2 and MAPK"
/evidence="ECO:0000250|UniProtKB:P17676"
MOD_RES 240
/note="Phosphoserine; by PKC/PRKCA"
/evidence="ECO:0000250|UniProtKB:P17676"
MOD_RES 277
/note="Phosphoserine; by CaMK2"
/evidence="ECO:0000250|UniProtKB:P28033"
CARBOHYD 181
/note="O-linked (GlcNAc) serine"
/evidence="ECO:0000250|UniProtKB:P28033"
CARBOHYD 182
/note="O-linked (GlcNAc) serine"
/evidence="ECO:0000250|UniProtKB:P28033"
CROSSLNK 103
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P17676"
CROSSLNK 134
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
/evidence="ECO:0000250|UniProtKB:P17676,
ECO:0000250|UniProtKB:P28033"
CROSSLNK 134
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P17676"
CROSSLNK 145
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P17676"
CROSSLNK 212
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P17676"
CROSSLNK 214
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P17676"
CROSSLNK 284
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P17676"
VAR_SEQ 1..152
/note="Missing (in isoform 3)"
/evidence="ECO:0000305"
/id="VSP_053315"
VAR_SEQ 1..21
/note="Missing (in isoform 2)"
/evidence="ECO:0000305"
/id="VSP_053316"
MUTAGEN 105
/note="S->A: No effect on DNA-binding. Loss of
transactivation activity. Loss of hepatocyte proliferation
induction by TGFA."
/evidence="ECO:0000269|PubMed:10635333,
ECO:0000269|PubMed:8336793"
MUTAGEN 105
/note="S->D: No effect on DNA-binding. Increases
transactivation activity."
/evidence="ECO:0000269|PubMed:8336793"
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


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Related Genes :
[Cebpb Crp2 Nf-il6 Sfb] CCAAT/enhancer-binding protein beta (C/EBP beta) (C/EBP-related protein 2) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched inhibitory protein) (LIP) (Liver-enriched transcriptional activator) (LAP) (Silencer factor B) (SF-B)
[Cebpb] CCAAT/enhancer-binding protein beta (C/EBP beta) (AGP/EBP) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched transcriptional activator) (LAP)
[CEBPB TCF5 PP9092] CCAAT/enhancer-binding protein beta (C/EBP beta) (Liver activator protein) (LAP) (Liver-enriched inhibitory protein) (LIP) (Nuclear factor NF-IL6) (Transcription factor 5) (TCF-5)
[Cebpa Cebp] CCAAT/enhancer-binding protein alpha (C/EBP alpha)
[Ddit3 Chop Chop10 Gadd153] DNA damage-inducible transcript 3 protein (DDIT-3) (C/EBP zeta) (C/EBP-homologous protein) (CHOP) (C/EBP-homologous protein 10) (CHOP-10) (CCAAT/enhancer-binding protein homologous protein) (Growth arrest and DNA-damage-inducible protein GADD153)
[Atf4 Creb2] Cyclic AMP-dependent transcription factor ATF-4 (cAMP-dependent transcription factor ATF-4) (Activating transcription factor 4) (C/EBP-related ATF) (C/ATF) (Cyclic AMP-responsive element-binding protein 2) (CREB-2) (cAMP-responsive element-binding protein 2)
[Cebpa] CCAAT/enhancer-binding protein alpha (C/EBP alpha)
[CEBPA CEBP] CCAAT/enhancer-binding protein alpha (C/EBP alpha)
[Nfkb1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (NF-kappa-B1 p84/NF-kappa-B1 p98) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[DDIT3 CHOP CHOP10 GADD153] DNA damage-inducible transcript 3 protein (DDIT-3) (C/EBP zeta) (C/EBP-homologous protein) (CHOP) (C/EBP-homologous protein 10) (CHOP-10) (CCAAT/enhancer-binding protein homologous protein) (Growth arrest and DNA damage-inducible protein GADD153)
[Runx1 Aml1 Cbfa2 Pebp2ab] Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B subunit)
[CEBPB] CCAAT/enhancer-binding protein beta (C/EBP beta)
[RUNX1 AML1 CBFA2] Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B subunit)
[NFKB1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[Cbfb Pebp2b Pebpb2] Core-binding factor subunit beta (CBF-beta) (Polyomavirus enhancer-binding protein 2 beta subunit) (PEA2-beta) (PEBP2-beta) (SL3-3 enhancer factor 1 subunit beta) (SL3/AKV core-binding factor beta subunit)
[Runx3 Aml2 Cbfa3 Pebp2a3] Runt-related transcription factor 3 (Acute myeloid leukemia 2 protein) (Core-binding factor subunit alpha-3) (CBF-alpha-3) (Oncogene AML-2) (Polyomavirus enhancer-binding protein 2 alpha C subunit) (PEA2-alpha C) (PEBP2-alpha C) (SL3-3 enhancer factor 1 alpha C subunit) (SL3/AKV core-binding factor alpha C subunit)
[Smarca4 Baf190a Brg1 Snf2b Snf2l4] Transcription activator BRG1 (EC 3.6.4.-) (ATP-dependent helicase SMARCA4) (BRG1-associated factor 190A) (BAF190A) (Protein brahma homolog 1) (SNF2-beta) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4)
[NR5A2 B1F CPF FTF] Nuclear receptor subfamily 5 group A member 2 (Alpha-1-fetoprotein transcription factor) (B1-binding factor) (hB1F) (CYP7A promoter-binding factor) (Hepatocytic transcription factor) (Liver receptor homolog 1) (LRH-1)
[Smarca2 Baf190b Brm Snf2a Snf2l2] Probable global transcription activator SNF2L2 (EC 3.6.4.-) (ATP-dependent helicase SMARCA2) (BRG1-associated factor 190B) (BAF190B) (Protein brahma homolog) (SNF2-alpha) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2)
[Tfap2b Tcfap2b] Transcription factor AP-2-beta (AP2-beta) (Activating enhancer-binding protein 2-beta)
[Eif4ebp1] Eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) (eIF4E-binding protein 1) (Phosphorylated heat- and acid-stable protein regulated by insulin 1) (PHAS-I)
[Il6 Il-6] Interleukin-6 (IL-6) (B-cell hybridoma growth factor) (Interleukin HP-1)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[Foxa2 Hnf3b Tcf-3b Tcf3b] Hepatocyte nuclear factor 3-beta (HNF-3-beta) (HNF-3B) (Forkhead box protein A2)
[Ybx1 Msy-1 Msy1 Nsep1 Yb1] Y-box-binding protein 1 (YB-1) (CCAAT-binding transcription factor I subunit A) (CBF-A) (DNA-binding protein B) (DBPB) (Enhancer factor I subunit A) (EFI-A) (Nuclease-sensitive element-binding protein 1) (Y-box transcription factor)
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[ATF4 CREB2 TXREB] Cyclic AMP-dependent transcription factor ATF-4 (cAMP-dependent transcription factor ATF-4) (Activating transcription factor 4) (Cyclic AMP-responsive element-binding protein 2) (CREB-2) (cAMP-responsive element-binding protein 2) (Tax-responsive enhancer element-binding protein 67) (TaxREB67)
[Pfkl Pfk-l Pfkb] ATP-dependent 6-phosphofructokinase, liver type (ATP-PFK) (PFK-L) (EC 2.7.1.11) (6-phosphofructokinase type B) (Phosphofructo-1-kinase isozyme B) (PFK-B) (Phosphohexokinase)
[NKX2-1 NKX2A TITF1 TTF1] Homeobox protein Nkx-2.1 (Homeobox protein NK-2 homolog A) (Thyroid nuclear factor 1) (Thyroid transcription factor 1) (TTF-1) (Thyroid-specific enhancer-binding protein) (T/EBP)
[CEBPA] CCAAT/enhancer-binding protein alpha (C/EBP alpha)

Bibliography :
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