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CCAAT/enhancer-binding protein beta (C/EBP beta) (AGP/EBP) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched transcriptional activator) (LAP)

 CEBPB_MOUSE             Reviewed;         296 AA.
P28033;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
11-DEC-2019, entry version 185.
RecName: Full=CCAAT/enhancer-binding protein beta {ECO:0000312|MGI:MGI:88373};
Short=C/EBP beta;
AltName: Full=AGP/EBP;
AltName: Full=Interleukin-6-dependent-binding protein;
Short=IL-6DBP;
AltName: Full=Liver-enriched transcriptional activator;
Short=LAP;
Name=Cebpb {ECO:0000312|MGI:MGI:88373};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=1701020; DOI=10.1128/mcb.10.12.6642;
Chang C.J., Chen T.T., Lei H.Y., Chen D.S., Lee S.C.;
"Molecular cloning of a transcription factor, AGP/EBP, that belongs to
members of the C/EBP family.";
Mol. Cell. Biol. 10:6642-6653(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1840554; DOI=10.1101/gad.5.9.1538;
Cao Z., Umek R.M., McKnight S.L.;
"Regulated expression of three C/EBP isoforms during adipose conversion of
3T3-L1 cells.";
Genes Dev. 5:1538-1552(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
TISSUE=Liver;
PubMed=7598808; DOI=10.1089/dna.1995.14.529;
Chang C.J., Shen B.J., Lee S.C.;
"Autoregulated induction of the acute-phase response transcription factor
gene, agp/ebp.";
DNA Cell Biol. 14:529-537(1995).
[4]
FUNCTION, PHOSPHORYLATION AT SER-276, AND MUTAGENESIS OF SER-276.
PubMed=1314426; DOI=10.1126/science.256.5055.370;
Wegner M., Cao Z., Rosenfeld M.G.;
"Calcium-regulated phosphorylation within the leucine zipper of C/EBP
beta.";
Science 256:370-373(1992).
[5]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=9303532; DOI=10.1101/gad.11.17.2153;
Sterneck E., Tessarollo L., Johnson P.F.;
"An essential role for C/EBPbeta in female reproduction.";
Genes Dev. 11:2153-2162(1997).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9727068; DOI=10.1172/jci3135;
Greenbaum L.E., Li W., Cressman D.E., Peng Y., Ciliberto G., Poli V.,
Taub R.;
"CCAAT enhancer- binding protein beta is required for normal hepatocyte
proliferation in mice after partial hepatectomy.";
J. Clin. Invest. 102:996-1007(1998).
[7]
INTERACTION WITH TRIM28.
PubMed=9742105; DOI=10.1128/mcb.18.10.5880;
Chang C.J., Chen Y.L., Lee S.C.;
"Coactivator TIF1beta interacts with transcription factor C/EBPbeta and
glucocorticoid receptor to induce alpha1-acid glycoprotein gene
expression.";
Mol. Cell. Biol. 18:5880-5887(1998).
[8]
FUNCTION, PHOSPHORYLATION AT THR-217, AND MUTAGENESIS OF THR-217.
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).
[9]
INTERACTION WITH MYB.
PubMed=11792321; DOI=10.1016/s0092-8674(01)00636-5;
Tahirov T.H., Sato K., Ichikawa-Iwata E., Sasaki M., Inoue-Bungo T.,
Shiina M., Kimura K., Takata S., Fujikawa A., Morii H., Kumasaka T.,
Yamamoto M., Ishii S., Ogata K.;
"Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a
promoter.";
Cell 108:57-70(2002).
[10]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=15509779; DOI=10.1128/mcb.24.22.9744-9751.2004;
Begay V., Smink J., Leutz A.;
"Essential requirement of CCAAT/enhancer binding proteins in
embryogenesis.";
Mol. Cell. Biol. 24:9744-9751(2004).
[11]
INTERACTION WITH CCDC85B.
PubMed=15644333; DOI=10.1074/jbc.m411741200;
Bezy O., Elabd C., Cochet O., Petersen R.K., Kristiansen K., Dani C.,
Ailhaud G., Amri E.-Z.;
"Delta-interacting protein A, a new inhibitory partner of CCAAT/enhancer-
binding protein beta, implicated in adipocyte differentiation.";
J. Biol. Chem. 280:11432-11438(2005).
[12]
INTERACTION WITH PTGES2.
PubMed=15879117; DOI=10.4049/jimmunol.174.10.6203;
Meng Q., Raha A., Roy S., Hu J., Kalvakolanu D.V.;
"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.";
J. Immunol. 174:6203-6211(2005).
[13]
FUNCTION, PHOSPHORYLATION AT THR-179; SER-184 AND THR-188, DNA-BINDING,
MUTAGENESIS OF THR-179; SER-184 AND THR-188, IDENTIFICATION BY MASS
SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=15985551; DOI=10.1073/pnas.0503891102;
Tang Q.Q., Gronborg M., Huang H., Kim J.W., Otto T.C., Pandey A.,
Lane M.D.;
"Sequential phosphorylation of CCAAT enhancer-binding protein beta by MAPK
and glycogen synthase kinase 3beta is required for adipogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 102:9766-9771(2005).
[14]
FUNCTION, SUMOYLATION AT LYS-133, TISSUE SPECIFICITY, MUTAGENESIS OF
LYS-133, AND SUBCELLULAR LOCATION.
PubMed=16585579; DOI=10.4049/jimmunol.176.8.4843;
Berberich-Siebelt F., Berberich I., Andrulis M., Santner-Nanan B.,
Jha M.K., Klein-Hessling S., Schimpl A., Serfling E.;
"SUMOylation interferes with CCAAT/enhancer-binding protein beta-mediated
c-myc repression, but not IL-4 activation in T cells.";
J. Immunol. 176:4843-4851(2006).
[15]
FUNCTION, DISRUPTION PHENOTYPE, AND ALTERNATIVE INITIATION.
PubMed=17911624; DOI=10.4049/jimmunol.179.8.5378;
Uematsu S., Kaisho T., Tanaka T., Matsumoto M., Yamakami M., Omori H.,
Yamamoto M., Yoshimori T., Akira S.;
"The C/EBP beta isoform 34-kDa LAP is responsible for NF-IL-6-mediated gene
induction in activated macrophages, but is not essential for intracellular
bacteria killing.";
J. Immunol. 179:5378-5386(2007).
[16]
FUNCTION, ACETYLATION AT LYS-98; LYS-101 AND LYS-102, INTERACTION WITH
KAT2A AND KAT2B, AND MUTAGENESIS OF LYS-98; LYS-101 AND LYS-102.
PubMed=17301242; DOI=10.1073/pnas.0607378104;
Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.;
"Glucocorticoid-stimulated preadipocyte differentiation is mediated through
acetylation of C/EBPbeta by GCN5.";
Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007).
[17]
FUNCTION, PHOSPHORYLATION AT THR-179; SER-184 AND THR-188, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17601773; DOI=10.1073/pnas.0703771104;
Li X., Kim J.W., Gronborg M., Urlaub H., Lane M.D., Tang Q.Q.;
"Role of cdk2 in the sequential phosphorylation/activation of C/EBPbeta
during adipocyte differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 104:11597-11602(2007).
[18]
METHYLATION AT LYS-39.
PubMed=18647749; DOI=10.1074/jbc.m802132200;
Pless O., Kowenz-Leutz E., Knoblich M., Lausen J., Beyermann M.,
Walsh M.J., Leutz A.;
"G9a-mediated lysine methylation alters the function of CCAAT/enhancer-
binding protein-beta.";
J. Biol. Chem. 283:26357-26363(2008).
[19]
FUNCTION, INTERACTION WITH EP300, MUTAGENESIS OF LYS-39; LYS-98 AND
LYS-215, AND ACETYLATION AT LYS-39.
PubMed=18486321; DOI=10.1016/j.mce.2008.03.009;
Cesena T.I., Cui T.X., Subramanian L., Fulton C.T., Iniguez-Lluhi J.A.,
Kwok R.P., Schwartz J.;
"Acetylation and deacetylation regulate CCAAT/enhancer binding protein beta
at K39 in mediating gene transcription.";
Mol. Cell. Endocrinol. 289:94-101(2008).
[20]
SUBCELLULAR LOCATION, AND COMPLEX FORMATION WITH THOC5.
PubMed=19015024; DOI=10.1016/j.cellsig.2008.10.018;
Carney L., Pierce A., Rijnen M., Gonzalez Sanchez M.B., Hamzah H.G.,
Zhang L., Tamura T., Whetton A.D.;
"THOC5 couples M-CSF receptor signaling to transcription factor
expression.";
Cell. Signal. 21:309-316(2009).
[21]
FUNCTION (ISOFORM 1 AND ISOFORM 3), TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
PubMed=19440205; DOI=10.1038/emboj.2009.127;
Smink J.J., Begay V., Schoenmaker T., Sterneck E., de Vries T.J., Leutz A.;
"Transcription factor C/EBPbeta isoform ratio regulates osteoclastogenesis
through MafB.";
EMBO J. 28:1769-1781(2009).
[22]
FUNCTION, GLYCOSYLATION AT SER-180 AND SER-181, MUTAGENESIS OF SER-180 AND
SER-181, IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT
THR-179; SER-184 AND THR-188.
PubMed=19478079; DOI=10.1074/jbc.m109.005678;
Li X., Molina H., Huang H., Zhang Y.Y., Liu M., Qian S.W., Slawson C.,
Dias W.B., Pandey A., Hart G.W., Lane M.D., Tang Q.Q.;
"O-linked N-acetylglucosamine modification on CCAAT enhancer-binding
protein beta: role during adipocyte differentiation.";
J. Biol. Chem. 284:19248-19254(2009).
[23]
FUNCTION IN ADIPOGENESIS, INTERACTION WITH EP300 AND RORA, ALTERNATIVE
SPLICING (ISOFORMS 2 AND 3), AND PHOSPHORYLATION AT THR-188.
PubMed=19324970; DOI=10.1210/me.2008-0277;
Ohoka N., Kato S., Takahashi Y., Hayashi H., Sato R.;
"The orphan nuclear receptor RORalpha restrains adipocyte differentiation
through a reduction of C/EBPbeta activity and perilipin gene expression.";
Mol. Endocrinol. 23:759-771(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, DISRUPTION PHENOTYPE,
INTERACTION WITH PRDM16, INDUCTION BY COLD EXPOSURE, AND TISSUE
SPECIFICITY.
PubMed=19641492; DOI=10.1038/nature08262;
Kajimura S., Seale P., Kubota K., Lunsford E., Frangioni J.V., Gygi S.P.,
Spiegelman B.M.;
"Initiation of myoblast to brown fat switch by a PRDM16-C/EBP-beta
transcriptional complex.";
Nature 460:1154-1158(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND THR-188, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[26]
FUNCTION, INTERACTION WITH MED23; MED26; SMARCA2; SMARCB1 AND SMARCC1,
IDENTIFICATION BY MASS SPECTROMETRY, AND METHYLATION AT ARG-3.
PubMed=20111005; DOI=10.1038/emboj.2010.3;
Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
"Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and
SWI/SNF/Mediator implies an indexing transcription factor code.";
EMBO J. 29:1105-1115(2010).
[27]
FUNCTION, SUMOYLATION AT LYS-133, DESUMOYLATION AT LYS-133, MUTAGENESIS OF
LYS-133 AND GLU-135, AND UBIQUITINATION.
PubMed=20194620; DOI=10.1128/mcb.00852-09;
Chung S.S., Ahn B.Y., Kim M., Choi H.H., Park H.S., Kang S., Park S.G.,
Kim Y.B., Cho Y.M., Lee H.K., Chung C.H., Park K.S.;
"Control of adipogenesis by the SUMO-specific protease SENP2.";
Mol. Cell. Biol. 30:2135-2146(2010).
[28]
INTERACTION WITH ZNF638.
PubMed=21602272; DOI=10.1074/jbc.m110.212506;
Meruvu S., Hugendubler L., Mueller E.;
"Regulation of adipocyte differentiation by the zinc finger protein
ZNF638.";
J. Biol. Chem. 286:26516-26523(2011).
[29]
INTERACTION WITH CIDEA AND CIDEC.
PubMed=22245780; DOI=10.1038/nm.2614;
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.;
"Cidea is an essential transcriptional coactivator regulating mammary gland
secretion of milk lipids.";
Nat. Med. 18:235-243(2012).
[30]
FUNCTION, SUMOYLATION AT LYS-133, MUTAGENESIS OF LYS-133, AND
UBIQUITINATION.
PubMed=24061474; DOI=10.1128/mcb.00723-13;
Liu Y., Zhang Y.D., Guo L., Huang H.Y., Zhu H., Huang J.X., Liu Y.,
Zhou S.R., Dang Y.J., Li X., Tang Q.Q.;
"Protein inhibitor of activated STAT 1 (PIAS1) is identified as the SUMO E3
ligase of CCAAT/enhancer-binding protein beta (C/EBPbeta) during
adipogenesis.";
Mol. Cell. Biol. 33:4606-4617(2013).
[31]
FUNCTION, AND INTERACTION WITH ATF5 AND EP300.
PubMed=24216764; DOI=10.1128/mcb.00956-13;
Zhao Y., Zhang Y.D., Zhang Y.Y., Qian S.W., Zhang Z.C., Li S.F., Guo L.,
Liu Y., Wen B., Lei Q.Y., Tang Q.Q., Li X.;
"p300-dependent acetylation of activating transcription factor 5 enhances
C/EBPbeta transactivation of C/EBPalpha during 3T3-L1 differentiation.";
Mol. Cell. Biol. 34:315-324(2014).
[32]
REVIEW OF PTMS AND FUNCTION.
PubMed=25451943; DOI=10.1074/jbc.r114.619957;
Guo L., Li X., Tang Q.;
"Transcriptional Regulation of Adipocyte Differentiation: A Central Role
for CCAAT/Enhancer-binding Protein (C/EBP) beta.";
J. Biol. Chem. 290:755-761(2015).
[33]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 224-285 IN COMPLEX WITH ATF4,
INTERACTION WITH ATF4, AND DNA-BINDING.
PubMed=11018027; DOI=10.1074/jbc.m005594200;
Podust L.M., Krezel A.M., Kim Y.;
"Crystal structure of the CCAAT box/enhancer-binding protein beta
activating transcription factor-4 basic leucine zipper heterodimer in the
absence of DNA.";
J. Biol. Chem. 276:505-513(2001).
-!- FUNCTION: Important transcription factor regulating the expression of
genes involved in immune and inflammatory responses (PubMed:16585579,
PubMed:17911624, PubMed:18486321, PubMed:20111005). Plays also a
significant role in adipogenesis, as well as in the gluconeogenic
pathway, liver regeneration, and hematopoiesis (PubMed:9727068,
PubMed:10635333, PubMed:17301242, PubMed:17601773, PubMed:19478079,
PubMed:24061474, PubMed:24216764). 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
(PubMed:15509779). 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:9727068, PubMed:10635333,
PubMed:16585579). 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 (PubMed:17911624). 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 (PubMed:15985551,
PubMed:17301242, PubMed:17601773, PubMed:20194620). Essential for
female reproduction because of a critical role in ovarian follicle
development (PubMed:9303532). Restricts osteoclastogenesis
(PubMed:19440205). Together with NFE2L1; represses expression of DSPP
during odontoblast differentiation (By similarity).
{ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P21272,
ECO:0000269|PubMed:10635333, ECO:0000269|PubMed:1314426,
ECO:0000269|PubMed:15509779, ECO:0000269|PubMed:15985551,
ECO:0000269|PubMed:16585579, ECO:0000269|PubMed:17301242,
ECO:0000269|PubMed:17601773, ECO:0000269|PubMed:17911624,
ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:19440205,
ECO:0000269|PubMed:19478079, ECO:0000269|PubMed:20111005,
ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:24061474,
ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:9303532,
ECO:0000269|PubMed:9727068, ECO:0000303|PubMed:25451943}.
-!- 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:0000269|PubMed:17911624}.
-!- FUNCTION: [Isoform 3]: Acts as a dominant negative through
heterodimerization with isoform 2 (By similarity). Promotes osteoblast
differentiation and osteoclastogenesis (PubMed:19440205).
{ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P21272,
ECO:0000269|PubMed:19440205}.
-!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Interacts with
ATF4. Binds DNA as a heterodimer with ATF4 (PubMed:11018027). Interacts
with MYB; within the complex, MYB and CEBPB bind to different promoter
regions (PubMed:11792321). Can form stable heterodimers with CEBPA,
CEBPD and CEBPE (By similarity). Isoform 2 and isoform 3 also form
heterodimers (By similarity). Interacts with TRIM28 and PTGES2
(PubMed:9742105, PubMed:15879117). Interacts with PRDM16
(PubMed:19641492). Interacts with CCDC85B (PubMed:15644333). Forms a
complex with THOC5 (PubMed:19015024). Interacts with ZNF638; this
interaction increases transcriptional activation (PubMed:21602272).
Interacts with CIDEA and CIDEC (PubMed:22245780). 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 (PubMed:19324970).
Interacts (not methylated) with MED23, MED26, SMARCA2, SMARCB1 and
SMARCC1 (PubMed:20111005). Interacts with KAT2A and KAT2B
(PubMed:17301242). Interacts with ATF5; EP300 is required for ATF5 and
CEBPB interaction and DNA binding (PubMed:24216764). Interacts with
NFE2L1; the heterodimer represses expression of DSPP during odontoblast
differentiation (By similarity). {ECO:0000250|UniProtKB:P21272,
ECO:0000269|PubMed:11018027, ECO:0000269|PubMed:11792321,
ECO:0000269|PubMed:15644333, ECO:0000269|PubMed:15879117,
ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:18486321,
ECO:0000269|PubMed:19015024, ECO:0000269|PubMed:19324970,
ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:20111005,
ECO:0000269|PubMed:21602272, ECO:0000269|PubMed:22245780,
ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:9742105}.
-!- INTERACTION:
Q99PV5:Bhlhe41; NbExp=5; IntAct=EBI-1029979, EBI-6143801;
Q9JHD2:Kat2a; NbExp=5; IntAct=EBI-1029979, EBI-2943116;
Q92831:KAT2B (xeno); NbExp=2; IntAct=EBI-1029979, EBI-477430;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16585579,
ECO:0000269|PubMed:19015024}. Cytoplasm {ECO:0000250|UniProtKB:P17676}.
Note=In T-cells when sumoylated drawn to pericentric heterochromatin
thereby allowing proliferation (PubMed:16585579). Translocates to the
nucleus when phosphorylated at Ser-288 (By similarity).
{ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:16585579}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=1; Synonyms=a, C/EBPbeta-FL, LAP*;
IsoId=P28033-1; Sequence=Displayed;
Name=2; Synonyms=b, C/EBPbeta-LAP;
IsoId=P28033-3; Sequence=VSP_053977;
Name=3; Synonyms=c, C/EBPbeta-LIP;
IsoId=P28033-2; Sequence=VSP_053976;
-!- TISSUE SPECIFICITY: Abundantly expressed in myoblasts. Enriched in
brown adipose tissue (BAT) versus white adipose tissue (WAT). Expressed
in hepatocytes (at protein level). Expressed in T lymphocytes
(PubMed:16585579). The expression in granulosa cells of antral
follicles is induced by luteinizing hormone (PubMed:9303532). Expressed
in chondrocytes and osteoblasts (at protein level) (PubMed:19440205).
{ECO:0000269|PubMed:10635333, ECO:0000269|PubMed:16585579,
ECO:0000269|PubMed:19440205, ECO:0000269|PubMed:19641492,
ECO:0000269|PubMed:9303532}.
-!- DEVELOPMENTAL STAGE: At 9.5 dpc, expressed in the chorionic plate and
ectoplacental cone. From 10.5 dpc to at least 11.5 dpc, is also
expressed in the trophoblast cells of the three placenta layers
(PubMed:15509779). Expressed in monocytic precursors but is vanished
during differentiation into osteoclasts. The expression increases
during osteoblast differentiation (PubMed:19440205).
{ECO:0000269|PubMed:15509779, ECO:0000269|PubMed:19440205}.
-!- INDUCTION: Up-regulated by cold exposure.
{ECO:0000269|PubMed:19641492}.
-!- PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3. Sumoylation at
Lys-133 is required for inhibition of T-cells proliferation
(PubMed:16585579). In adipocytes, sumoylation at Lys-133 by PIAS1 leads
to ubiquitination and subsequent proteasomal degradation
(PubMed:24061474). Desumoylated by SENP2, which abolishes
ubiquitination and stabilizes protein levels (PubMed:20194620).
{ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:16585579,
ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:24061474}.
-!- PTM: Ubiquitinated, leading to proteasomal degradation.
{ECO:0000269|PubMed:24061474}.
-!- PTM: Phosphorylated at Thr-188 by MAPK and CDK2, serves to prime
phosphorylation at Thr-179 and Ser-184 by GSK3B and acquire DNA-binding
as well as transactivation activities, required to induce adipogenesis.
MAPK and CDK2 act sequentially to maintain Thr-188 in the primed
phosphorylated state during mitotical cloning expansion and thereby
progression of terminal differentiation. Phosphorylation at Thr-217
enhances transactivation activity. Phosphorylation at Ser-276 in
response to calcium increases transactivation activity
(PubMed:1314426). Phosphorylated at Thr-188 by RPS6KA1 (By similarity).
{ECO:0000250|UniProtKB:P17676, ECO:0000269|PubMed:1314426,
ECO:0000269|PubMed:15985551, ECO:0000269|PubMed:17601773}.
-!- PTM: O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents
phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding
activity which delays the adipocyte differentiation program.
{ECO:0000269|PubMed:19478079}.
-!- 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 (PubMed:18486321). Acetylated by KAT2A and
KAT2B within a cluster of lysine residues between amino acids 98-102,
this acetylation is strongly induced by glucocorticoid treatment and
enhances transactivation activity (PubMed:17301242).
{ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:18486321}.
-!- PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2,
inhibits transactivation activity. Methylation is probably inhibited by
phosphorylation at Thr-188. {ECO:0000269|PubMed:20111005,
ECO:0000305|PubMed:18647749}.
-!- DISRUPTION PHENOTYPE: Embryos display defects in brown fat tissue
development (PubMed:19641492). Females are sterile, ovaries lack
corpora lutea (PubMed:9303532). Upon bacterial infection, animals show
impaired bactericidal activity and die within 3 days (PubMed:17911624).
Posthepatectomy, animals show a reduced regenerative response with DNA
synthesis decreased to 25% of normal in hepatocytes and a prolonged
period of hypoglycemia (PubMed:9727068). Animals show osteopenia with
decreased bone formation and enhanced ostecolastogenesis. Long bones
have a 1.6 fold diminished bone volume with a reduction of the number
and thickness of bone trabeculae (PubMed:19440205). Mutants of isoform
2 show impaired CSF3/G-CSF production by macrophages, IFNG production
by CD4(+) T-cells and granuloma formation in liver. Upon bacterial
infection, mutants of isoform 2 die within 6 days. Resistant to LPS-
induced endotoxin shock (PubMed:17911624). Double knockout CEBPA and
CEBPB results in embryonic developmental arrest and death at around 10
dpc to 11 dpc, associated with a gross placenta failure
(PubMed:15509779). {ECO:0000269|PubMed:15509779,
ECO:0000269|PubMed:17911624, ECO:0000269|PubMed:19440205,
ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:9303532,
ECO:0000269|PubMed:9727068}.
-!- MISCELLANEOUS: [Isoform 2]: Major isoform. {ECO:0000305}.
-!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
---------------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; M61007; AAA37192.1; -; mRNA.
EMBL; X62600; CAA44484.1; -; mRNA.
EMBL; S78572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS17105.1; -. [P28033-1]
PIR; A36366; A36366.
RefSeq; NP_001274667.1; NM_001287738.1. [P28033-3]
RefSeq; NP_001274668.1; NM_001287739.1. [P28033-2]
RefSeq; NP_034013.1; NM_009883.4. [P28033-1]
PDB; 1CI6; X-ray; 2.60 A; B=224-285.
PDBsum; 1CI6; -.
SMR; P28033; -.
BioGrid; 198669; 16.
ComplexPortal; CPX-66; CHOP-C/EBPbeta complex.
ComplexPortal; CPX-68; C/EBPbeta complex.
ComplexPortal; CPX-685; c-Myb-C/EBPbeta complex.
DIP; DIP-37539N; -.
IntAct; P28033; 14.
MINT; P28033; -.
STRING; 10090.ENSMUSP00000069850; -.
iPTMnet; P28033; -.
PhosphoSitePlus; P28033; -.
jPOST; P28033; -.
PaxDb; P28033; -.
PeptideAtlas; P28033; -.
PRIDE; P28033; -.
DNASU; 12608; -.
Ensembl; ENSMUST00000070642; ENSMUSP00000069850; ENSMUSG00000056501. [P28033-1]
GeneID; 12608; -.
KEGG; mmu:12608; -.
UCSC; uc008oaf.2; mouse. [P28033-1]
CTD; 1051; -.
MGI; MGI:88373; Cebpb.
eggNOG; KOG3119; Eukaryota.
eggNOG; ENOG410YJ8G; LUCA.
GeneTree; ENSGT00940000162137; -.
HOGENOM; HOG000013112; -.
InParanoid; P28033; -.
KO; K10048; -.
OMA; KNCKKAA; -.
OrthoDB; 1284308at2759; -.
PhylomeDB; P28033; -.
TreeFam; TF105008; -.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
ChiTaRS; Cebpb; mouse.
EvolutionaryTrace; P28033; -.
PRO; PR:P28033; -.
Proteomes; UP000000589; Chromosome 2.
RNAct; P28033; protein.
Bgee; ENSMUSG00000056501; Expressed in 273 organ(s), highest expression level in adrenal gland.
ExpressionAtlas; P28033; baseline and differential.
Genevisible; P28033; MM.
GO; GO:0036488; C:CHOP-C/EBP complex; ISO:MGI.
GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0016363; C:nuclear matrix; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
GO; GO:0035259; F:glucocorticoid receptor binding; ISO:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB.
GO; GO:0050873; P:brown fat cell differentiation; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0001892; P:embryonic placenta development; IGI:MGI.
GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
GO; GO:0002432; P:granuloma formation; IMP:UniProtKB.
GO; GO:0072574; P:hepatocyte proliferation; IDA:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
GO; GO:0097421; P:liver regeneration; IMP:UniProtKB.
GO; GO:0060644; P:mammary gland epithelial cell differentiation; IMP:MGI.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IMP:MGI.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0030182; P:neuron differentiation; IDA:MGI.
GO; GO:0001541; P:ovarian follicle development; IMP:UniProtKB.
GO; GO:0070169; P:positive regulation of biomineral tissue development; ISO:MGI.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; IGI:ARUK-UCL.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
GO; GO:2000120; P:positive regulation of sodium-dependent phosphate transport; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:2001198; P:regulation of dendritic cell differentiation; IGI:ARUK-UCL.
GO; GO:0045408; P:regulation of interleukin-6 biosynthetic process; IDA:MGI.
GO; GO:1901329; P:regulation of odontoblast differentiation; ISS:UniProtKB.
GO; GO:0045670; P:regulation of osteoclast differentiation; IDA:UniProtKB.
GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; IMP: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; IMP:BHF-UCL.
GO; GO:0035711; P:T-helper 1 cell activation; IMP: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;
3D-structure; Acetylation; Activator; Alternative initiation; Cytoplasm;
Differentiation; DNA-binding; Glycoprotein; Isopeptide bond; Methylation;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1..296
/note="CCAAT/enhancer-binding protein beta"
/id="PRO_0000076618"
DOMAIN 222..285
/note="bZIP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
REGION 1..22
/note="Required for Lys-133 sumoylation"
/evidence="ECO:0000250|UniProtKB:P17676"
REGION 22..104
/note="Required for MYC transcriptional repression"
/evidence="ECO:0000269|PubMed:16585579"
REGION 226..246
/note="Basic motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
REGION 248..255
/note="Leucine-zipper"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
COMPBIAS 120..129
/note="Pro-rich"
COMPBIAS 170..191
/note="Pro/Ser-rich"
MOD_RES 3
/note="Omega-N-methylated arginine; by CARM1"
/evidence="ECO:0000269|PubMed:20111005"
MOD_RES 39
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000269|PubMed:18486321"
MOD_RES 39
/note="N6-methylated lysine; alternate"
/evidence="ECO:0000305|PubMed:18647749"
MOD_RES 98
/note="N6-acetyllysine; by KAT2A and KAT2B"
/evidence="ECO:0000305|PubMed:17301242"
MOD_RES 101
/note="N6-acetyllysine; by KAT2A and KAT2B"
/evidence="ECO:0000305|PubMed:17301242"
MOD_RES 102
/note="N6-acetyllysine; by KAT2A and KAT2B; alternate"
/evidence="ECO:0000305|PubMed:17301242"
MOD_RES 179
/note="Phosphothreonine; by GSK3-beta"
/evidence="ECO:0000269|PubMed:15985551,
ECO:0000269|PubMed:17601773, ECO:0000269|PubMed:19478079"
MOD_RES 184
/note="Phosphoserine; by GSK3-beta"
/evidence="ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15985551, ECO:0000269|PubMed:17601773,
ECO:0000269|PubMed:19478079"
MOD_RES 188
/note="Phosphothreonine; by RPS6KA1, CDK2 and MAPK"
/evidence="ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15985551, ECO:0000269|PubMed:17601773,
ECO:0000269|PubMed:19324970, ECO:0000269|PubMed:19478079"
MOD_RES 217
/note="Phosphothreonine; by RPS6KA1 and PKC/PRKCA"
/evidence="ECO:0000269|PubMed:10635333"
MOD_RES 239
/note="Phosphoserine; by PKC/PRKCA"
/evidence="ECO:0000250|UniProtKB:P17676"
MOD_RES 276
/note="Phosphoserine; by CaMK2"
/evidence="ECO:0000305|PubMed:1314426"
CARBOHYD 180
/note="O-linked (GlcNAc) serine"
/evidence="ECO:0000269|PubMed:19478079"
CARBOHYD 181
/note="O-linked (GlcNAc) serine"
/evidence="ECO:0000269|PubMed:19478079"
CROSSLNK 102
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P17676"
CROSSLNK 133
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
/evidence="ECO:0000269|PubMed:16585579,
ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:24061474"
CROSSLNK 133
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P17676"
CROSSLNK 144
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P17676"
CROSSLNK 211
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P17676"
CROSSLNK 213
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P17676"
CROSSLNK 283
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P17676"
VAR_SEQ 1..151
/note="Missing (in isoform 3)"
/evidence="ECO:0000305"
/id="VSP_053976"
VAR_SEQ 1..21
/note="Missing (in isoform 2)"
/evidence="ECO:0000305"
/id="VSP_053977"
MUTAGEN 39
/note="K->A,Q: No effect on interaction with EP300."
/evidence="ECO:0000269|PubMed:18486321"
MUTAGEN 39
/note="K->R: Dominant negative. Loss of transactivation
activity. No effect on interaction with EP300."
/evidence="ECO:0000269|PubMed:18486321"
MUTAGEN 98
/note="K->R: No effect on transactivation activity. Not
acetylated after glucocorticoid-stimulation and no increase
of transactivation activity; when associated with R-101 and
R-102."
/evidence="ECO:0000269|PubMed:17301242,
ECO:0000269|PubMed:18486321"
MUTAGEN 101
/note="K->R: Not acetylated after glucocorticoid-
stimulation and no increase of transactivation activity;
when associated with R-98 and R-102."
/evidence="ECO:0000269|PubMed:17301242"
MUTAGEN 102
/note="K->R: Not acetylated and no increase of
transactivation activity after glucocorticoid-stimulation;
when associated with R-98 and R-101."
/evidence="ECO:0000269|PubMed:17301242"
MUTAGEN 133
/note="K->R: Not sumoylated. Decreases ubiquitination and
increases stability. Loss of proliferation inhibition in T
cells. No effect on transactivation activity."
/evidence="ECO:0000269|PubMed:16585579,
ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:24061474"
MUTAGEN 135
/note="E->A: Not sumoylated and not ubiquitinated."
/evidence="ECO:0000269|PubMed:20194620"
MUTAGEN 179
/note="T->A: Disruption of phosphorylation by MAPK and
GSK3B, acquisition of DNA-binding activity and
transactivation function; when associated with A-184 and A-
188."
/evidence="ECO:0000269|PubMed:15985551"
MUTAGEN 180
/note="S->A: Highly increases transactivation activity;
when associated with A-181."
/evidence="ECO:0000269|PubMed:19478079"
MUTAGEN 181
/note="S->A: Highly increases transactivation activity;
when associated with A-180."
/evidence="ECO:0000269|PubMed:19478079"
MUTAGEN 184
/note="S->A: Disruption of phosphorylation by MAPK and
GSK3B, acquisition of DNA-binding activity and
transactivation function; when associated with A-179 and A-
188."
/evidence="ECO:0000269|PubMed:15985551"
MUTAGEN 188
/note="T->A: Disruption of phosphorylation by MAPK and
GSK3B, acquisition of DNA-binding activity and
transactivation function; when associated with A-179 and A-
184."
/evidence="ECO:0000269|PubMed:15985551"
MUTAGEN 215
/note="K->R: No effect on transactivation activity."
/evidence="ECO:0000269|PubMed:18486321"
MUTAGEN 217
/note="T->A: Loss of hepatocyte proliferation induction by
TGFA."
/evidence="ECO:0000269|PubMed:10635333"
MUTAGEN 217
/note="T->E: Induces hepatocyte proliferation."
/evidence="ECO:0000269|PubMed:10635333"
MUTAGEN 276
/note="S->A: Reduces phosphorylation in response to
calcium."
/evidence="ECO:0000269|PubMed:1314426"
HELIX 240..282
/evidence="ECO:0000244|PDB:1CI6"
SEQUENCE 296 AA; 31446 MW; 827AC4AFC209AE89 CRC64;
MHRLLAWDAA CLPPPPAAFR PMEVANFYYE PDCLAYGAKA ARAAPRAPAA EPAIGEHERA
IDFSPYLEPL APAADFAAPA PAHHDFLSDL FADDYGAKPS KKPADYGYVS LGRAGAKAAP
PACFPPPPPA ALKAEPGFEP ADCKRADDAP AMAAGFPFAL RAYLGYQATP SGSSGSLSTS
SSSSPPGTPS PADAKAAPAA CFAGPPAAPA KAKAKKTVDK LSDEYKMRRE RNNIAVRKSR
DKAKMRNLET QHKVLELTAE NERLQKKVEQ LSRELSTLRN LFKQLPEPLL ASAGHC


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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)
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[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)
[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)
[CEBPA CEBP] CCAAT/enhancer-binding protein alpha (C/EBP alpha)
[Cebpa] CCAAT/enhancer-binding protein alpha (C/EBP alpha)
[CEBPB] CCAAT/enhancer-binding protein beta (C/EBP beta)
[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]
[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]
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (Interleukin-33 receptot beta chain)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[CEBPA] CCAAT/enhancer-binding protein alpha (C/EBP alpha)
[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)
[NFIL3 E4BP4 IL3BP1] Nuclear factor interleukin-3-regulated protein (E4 promoter-binding protein 4) (Interleukin-3 promoter transcriptional activator) (Interleukin-3-binding protein 1) (Transcriptional activator NF-IL3A)
[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)
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[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)
[ilf3-a ilf3 ubp3] Interleukin enhancer-binding factor 3-A (CCAAT box transcription factor subunit) (Double-stranded RNA-binding protein 4F.1) (DsRNA-binding protein 4F.1)
[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)
[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] (Fragment)
[Il12rb1 Il12rb] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12 receptor beta component) (CD antigen CD212)
[FOXK2 ILF ILF1] Forkhead box protein K2 (G/T-mismatch specific binding protein) (nGTBP) (Interleukin enhancer-binding factor 1)
[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)
[IL6ST] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (CDw130) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[Ilf3] Interleukin enhancer-binding factor 3
[Il4r Il4ra] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[Foxk2 Ilf1] Forkhead box protein K2 (Cellular transcription factor ILF-1) (Interleukin enhancer-binding factor 1)

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