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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)

 CEBPB_HUMAN             Reviewed;         345 AA.
P17676; A8K671; Q96IH2; Q9H4Z5;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
22-AUG-2003, sequence version 2.
12-SEP-2018, entry version 201.
RecName: Full=CCAAT/enhancer-binding protein beta {ECO:0000312|HGNC:HGNC:1834};
Short=C/EBP beta {ECO:0000312|HGNC:HGNC:1834};
AltName: Full=Liver activator protein;
Short=LAP;
AltName: Full=Liver-enriched inhibitory protein;
Short=LIP;
AltName: Full=Nuclear factor NF-IL6 {ECO:0000303|PubMed:1741402};
AltName: Full=Transcription factor 5;
Short=TCF-5;
Name=CEBPB {ECO:0000312|HGNC:HGNC:1834}; Synonyms=TCF5;
ORFNames=PP9092;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
TISSUE=Placenta;
PubMed=2112087;
Akira S., Isshiki H., Sugita T., Tanabe O., Kinoshita S., Nishio Y.,
Nakajima T., Hirano T., Kishimoto T.;
"A nuclear factor for IL-6 expression (NF-IL6) is a member of a C/EBP
family.";
EMBO J. 9:1897-1906(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-195.
SeattleSNPs variation discovery resource;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, and Skin;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 241-323 (ISOFORMS 1/2/3).
PubMed=7635140; DOI=10.1111/j.1432-1033.1995.tb20699.x;
Toda K., Akira S., Kishimoto T., Sasaki H., Hashimoto K., Yamamoto Y.,
Sagara Y., Shizuta Y.;
"Identification of a transcriptional regulatory factor for human
aromatase cytochrome P450 gene expression as nuclear factor
interleukin-6 (NF-IL6), a member of the CCAAT/enhancer-binding protein
family.";
Eur. J. Biochem. 231:292-299(1995).
[9]
FUNCTION, AND INTERACTION WITH CEBPD.
PubMed=1741402; DOI=10.1073/pnas.89.4.1473;
Kinoshita S., Akira S., Kishimoto T.;
"A member of the C/EBP family, NF-IL6 beta, forms a heterodimer and
transcriptionally synergizes with NF-IL6.";
Proc. Natl. Acad. Sci. U.S.A. 89:1473-1476(1992).
[10]
FUNCTION, PHOSPHORYLATION AT SER-288, MUTAGENESIS OF SER-288, AND
SUBCELLULAR LOCATION.
PubMed=9374525; DOI=10.1074/jbc.272.48.30356;
Chinery R., Brockman J.A., Dransfield D.T., Coffey R.J.;
"Antioxidant-induced nuclear translocation of CCAAT/enhancer-binding
protein beta. A critical role for protein kinase A-mediated
phosphorylation of Ser299.";
J. Biol. Chem. 272:30356-30361(1997).
[11]
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).
[12]
PHOSPHORYLATION AT THR-235.
PubMed=11684016; DOI=10.1016/S1097-2765(01)00374-4;
Buck M., Poli V., Hunter T., Chojkier M.;
"C/EBPbeta phosphorylation by RSK creates a functional XEXD caspase
inhibitory box critical for cell survival.";
Mol. Cell 8:807-816(2001).
[13]
FUNCTION (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), AND
DNA-BINDING.
PubMed=11741938; DOI=10.1074/jbc.M108075200;
Zhu Y., Saunders M.A., Yeh H., Deng W.G., Wu K.K.;
"Dynamic regulation of cyclooxygenase-2 promoter activity by isoforms
of CCAAT/enhancer-binding proteins.";
J. Biol. Chem. 277:6923-6928(2002).
[14]
FUNCTION, AND MUTAGENESIS OF THR-235.
PubMed=12048245; DOI=10.1073/pnas.122075799;
Roy S.K., Hu J., Meng Q., Xia Y., Shapiro P.S., Reddy S.P.,
Platanias L.C., Lindner D.J., Johnson P.F., Pritchard C., Pages G.,
Pouyssegur J., Kalvakolanu D.V.;
"MEKK1 plays a critical role in activating the transcription factor
C/EBP-beta-dependent gene expression in response to IFN-gamma.";
Proc. Natl. Acad. Sci. U.S.A. 99:7945-7950(2002).
[15]
SUMOYLATION AT LYS-174.
PubMed=12810706; DOI=10.1074/jbc.M305680200;
Eaton E.M., Sealy L.;
"Modification of CCAAT/enhancer-binding protein-beta by the small
ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3.";
J. Biol. Chem. 278:33416-33421(2003).
[16]
DOMAIN.
PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P.,
Piskacek M.;
"Nine-amino-acid transactivation domain: establishment and prediction
utilities.";
Genomics 89:756-768(2007).
[17]
FUNCTION, AND PHOSPHORYLATION AT THR-235.
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).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
INTERACTION WITH MED23; MED26; SMARCA2; SMARCB1 AND SMARCC1, 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).
[20]
FUNCTION, INTERACTION WITH DDIT3, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=20829347; DOI=10.1074/jbc.M110.136259;
Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y.;
"Endoplasmic reticulum stress-activated C/EBP homologous protein
enhances nuclear factor-kappaB signals via repression of peroxisome
proliferator-activated receptor gamma.";
J. Biol. Chem. 285:35330-35339(2010).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-174; LYS-187 AND
LYS-260, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-174; LYS-187 AND
LYS-260, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[23]
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).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-174, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-174; LYS-185;
LYS-187; LYS-260; LYS-262 AND LYS-332, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[26]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 259-336 IN COMPLEXES WITH
DNA, AND SUBUNIT.
PubMed=11257229; DOI=10.1016/S0092-8674(01)00271-9;
Tahirov T.H., Inoue-Bungo T., Morii H., Fujikawa A., Sasaki M.,
Kimura K., Shiina M., Sato K., Kumasaka T., Yamamoto M., Ishii S.,
Ogata K.;
"Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain
and its allosteric control by CBFbeta.";
Cell 104:755-767(2001).
[27]
X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 259-345 IN COMPLEX WITH
MOUSE MYB, SUBUNIT, INTERACTION WITH MYB, AND DNA-BINDING.
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).
-!- FUNCTION: Important transcription factor regulating the expression
of genes involved in immune and inflammatory responses
(PubMed:1741402, PubMed:9374525, PubMed:12048245,
PubMed:18647749). Plays also a significant role in adipogenesis,
as well as in the gluconeogenic pathway, liver regeneration, and
hematopoiesis. The consensus recognition site is 5'-
T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein
interactions and post-translational protein modifications. During
early embryogenesis, plays essential and redundant functions with
CEBPA. 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. 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 (PubMed:20829347).
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 (By similarity).
{ECO:0000250|UniProtKB:P21272, ECO:0000250|UniProtKB:P28033,
ECO:0000269|PubMed:12048245, ECO:0000269|PubMed:18647749,
ECO:0000269|PubMed:20829347, ECO:0000269|PubMed:9374525,
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:0000250|UniProtKB:P28033}.
-!- FUNCTION: Isoform 3: Acts as a dominant negative through
heterodimerization with isoform 2 (PubMed:11741938). Promotes
osteoblast differentiation and osteoclastogenesis (By similarity).
{ECO:0000250|UniProtKB:P21272, ECO:0000250|UniProtKB:P28033,
ECO:0000269|PubMed:11741938}.
-!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer
(PubMed:11018027, PubMed:11257229, PubMed:11792321). 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 CEBPD (PubMed:1741402). Can form stable
heterodimers with CEBPA and CEBPE (By similarity). Isoform 2 and
isoform 3 also form heterodimers. 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 (By similarity). Interacts
with DDIT3/CHOP (PubMed:20829347). 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 (PubMed:20111005). 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 (By
similarity). {ECO:0000250|UniProtKB:P21272,
ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:11018027,
ECO:0000269|PubMed:11257229, ECO:0000269|PubMed:11792321,
ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:20829347}.
-!- INTERACTION:
P18848:ATF4; NbExp=2; IntAct=EBI-969696, EBI-492498;
Q16520:BATF; NbExp=2; IntAct=EBI-969696, EBI-749503;
Q86X55:CARM1; NbExp=2; IntAct=EBI-969696, EBI-2339854;
P49715:CEBPA; NbExp=2; IntAct=EBI-969696, EBI-1172054;
P53567:CEBPG; NbExp=2; IntAct=EBI-969696, EBI-740209;
P35638:DDIT3; NbExp=2; IntAct=EBI-969696, EBI-742651;
P03120:E2 (xeno); NbExp=2; IntAct=EBI-969696, EBI-1779322;
P03122:E2 (xeno); NbExp=3; IntAct=EBI-969696, EBI-7028618;
P06422:E2 (xeno); NbExp=4; IntAct=EBI-969696, EBI-7136851;
P06790:E2 (xeno); NbExp=4; IntAct=EBI-969696, EBI-7010629;
P15941:MUC1; NbExp=8; IntAct=EBI-969696, EBI-10053698;
P04637:TP53; NbExp=4; IntAct=EBI-969696, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20829347}.
Cytoplasm {ECO:0000269|PubMed:9374525}. 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:P28033,
ECO:0000269|PubMed:9374525}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=1; Synonyms=C/EBPbeta-FL;
IsoId=P17676-1; Sequence=Displayed;
Name=2; Synonyms=C/EBPbeta-LAP;
IsoId=P17676-2; Sequence=VSP_053314;
Name=3; Synonyms=C/EBPbeta-LIP;
IsoId=P17676-3; Sequence=VSP_053313;
-!- TISSUE SPECIFICITY: Expressed at low levels in the lung, kidney
and spleen.
-!- INDUCTION: By ER stress. {ECO:0000269|PubMed:20829347}.
-!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a
large number of yeast and animal transcription factors.
{ECO:0000269|PubMed:17467953}.
-!- PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-43 by
EHMT2 inhibit transactivation activity. Methylation is probably
inhibited by phosphorylation at Thr-235.
{ECO:0000305|PubMed:18647749, ECO:0000305|PubMed:20111005}.
-!- PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3
(PubMed:12810706). Sumoylation at Lys-174 is required for
inhibition of T-cells proliferation. In adipocytes, sumoylation at
Lys-174 by PIAS1 leads to ubiquitination and subsequent
proteasomal degradation. Desumoylated by SENP2, which abolishes
ubiquitination and stabilizes protein levels (By similarity).
{ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:12810706}.
-!- PTM: Ubiquitinated, leading to proteasomal degradation.
{ECO:0000250|UniProtKB:P28033}.
-!- PTM: Phosphorylated at Thr-235 by MAPK and CDK2, serves to prime
phosphorylation at Thr-226 and Ser-231 by GSK3B and acquire DNA-
binding as well as transactivation activities, required to induce
adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-235
in the primed phosphorylated state during mitotical cloning
expansion and thereby progression of terminal differentiation.
Phosphorylation at Thr-266 enhances transactivation activity.
Phosphorylation at Ser-325 in response to calcium increases
transactivation activity. Phosphorylated at Thr-235 by RPS6KA1
(PubMed:11684016). {ECO:0000250|UniProtKB:P28033,
ECO:0000269|PubMed:11684016}.
-!- PTM: O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents
phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding
activity which delays the adipocyte differentiation program.
{ECO:0000250|UniProtKB:P28033}.
-!- PTM: Acetylated. Acetylation at Lys-43 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 129-133, this
acetylation is strongly induced by glucocorticoid treatment and
enhances transactivation activity. {ECO:0000250|UniProtKB:P28033}.
-!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/cebpb/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X52560; CAA36794.1; -; Genomic_DNA.
EMBL; AF289608; AAL55792.1; -; mRNA.
EMBL; AY193834; AAN86350.1; -; Genomic_DNA.
EMBL; AK291536; BAF84225.1; -; mRNA.
EMBL; AL161937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75629.1; -; Genomic_DNA.
EMBL; BC007538; AAH07538.1; -; mRNA.
EMBL; BC021931; AAH21931.1; -; mRNA.
CCDS; CCDS13429.1; -. [P17676-1]
PIR; S12788; S12788.
PIR; S66246; S66246.
RefSeq; NP_001272807.1; NM_001285878.1. [P17676-2]
RefSeq; NP_001272808.1; NM_001285879.1. [P17676-3]
RefSeq; NP_005185.2; NM_005194.3. [P17676-1]
UniGene; Hs.517106; -.
UniGene; Hs.719041; -.
UniGene; Hs.720603; -.
PDB; 1GTW; X-ray; 1.85 A; A/B=259-336.
PDB; 1GU4; X-ray; 1.80 A; A/B=259-336.
PDB; 1GU5; X-ray; 2.10 A; A/B=259-336.
PDB; 1H88; X-ray; 2.80 A; A/B=259-336.
PDB; 1H89; X-ray; 2.45 A; A/B=273-336.
PDB; 1H8A; X-ray; 2.23 A; A/B=259-336.
PDB; 1HJB; X-ray; 3.00 A; A/B/D/E=259-345.
PDB; 1IO4; X-ray; 3.00 A; A/B=259-336.
PDB; 2E42; X-ray; 1.80 A; A/B=259-336.
PDB; 2E43; X-ray; 2.10 A; A/B=259-336.
PDBsum; 1GTW; -.
PDBsum; 1GU4; -.
PDBsum; 1GU5; -.
PDBsum; 1H88; -.
PDBsum; 1H89; -.
PDBsum; 1H8A; -.
PDBsum; 1HJB; -.
PDBsum; 1IO4; -.
PDBsum; 2E42; -.
PDBsum; 2E43; -.
ProteinModelPortal; P17676; -.
SMR; P17676; -.
BioGrid; 107480; 69.
ComplexPortal; CPX-3361; C/EBPbeta complex.
ComplexPortal; CPX-504; c-Myb-C/EBPbeta complex.
ComplexPortal; CPX-70; CHOP-C/EBPbeta complex.
CORUM; P17676; -.
DIP; DIP-35345N; -.
ELM; P17676; -.
IntAct; P17676; 25.
MINT; P17676; -.
STRING; 9606.ENSP00000305422; -.
iPTMnet; P17676; -.
PhosphoSitePlus; P17676; -.
BioMuta; CEBPB; -.
DMDM; 34223718; -.
EPD; P17676; -.
MaxQB; P17676; -.
PaxDb; P17676; -.
PeptideAtlas; P17676; -.
PRIDE; P17676; -.
ProteomicsDB; 53503; -.
DNASU; 1051; -.
Ensembl; ENST00000303004; ENSP00000305422; ENSG00000172216. [P17676-1]
GeneID; 1051; -.
KEGG; hsa:1051; -.
UCSC; uc002xvi.4; human. [P17676-1]
CTD; 1051; -.
DisGeNET; 1051; -.
EuPathDB; HostDB:ENSG00000172216.5; -.
GeneCards; CEBPB; -.
H-InvDB; HIX0174729; -.
HGNC; HGNC:1834; CEBPB.
HPA; CAB004213; -.
HPA; HPA061355; -.
HPA; HPA062267; -.
MIM; 189965; gene.
neXtProt; NX_P17676; -.
OpenTargets; ENSG00000172216; -.
PharmGKB; PA26377; -.
eggNOG; ENOG410ISXW; Eukaryota.
eggNOG; ENOG410XX4P; LUCA.
GeneTree; ENSGT00530000063192; -.
HOGENOM; HOG000013112; -.
HOVERGEN; HBG050879; -.
InParanoid; P17676; -.
KO; K10048; -.
OMA; CKKPAEY; -.
OrthoDB; EOG091G11FC; -.
PhylomeDB; P17676; -.
TreeFam; TF105008; -.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
SignaLink; P17676; -.
SIGNOR; P17676; -.
ChiTaRS; CEBPB; human.
EvolutionaryTrace; P17676; -.
GeneWiki; CEBPB; -.
GenomeRNAi; 1051; -.
PRO; PR:P17676; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000172216; Expressed in 240 organ(s), highest expression level in layer of synovial tissue.
CleanEx; HS_CEBPB; -.
Genevisible; P17676; HS.
GO; GO:0036488; C:CHOP-C/EBP complex; NAS:ParkinsonsUK-UCL.
GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc.
GO; GO:0035259; F:glucocorticoid receptor binding; IEA:Ensembl.
GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; NAS:ParkinsonsUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; ISS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
GO; GO:0006953; P:acute-phase response; TAS:ProtInc.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
GO; GO:0002432; P:granuloma formation; ISS:UniProtKB.
GO; GO:0072574; P:hepatocyte proliferation; ISS:UniProtKB.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL.
GO; GO:0097421; P:liver regeneration; ISS:UniProtKB.
GO; GO:0060644; P:mammary gland epithelial cell differentiation; IEA:Ensembl.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
GO; GO:0070169; P:positive regulation of biomineral tissue development; IDA:MGI.
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:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:2000120; P:positive regulation of sodium-dependent phosphate transport; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0045408; P:regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
GO; GO:1901329; P:regulation of odontoblast differentiation; ISS:UniProtKB.
GO; GO:0045670; P:regulation of osteoclast differentiation; ISS:UniProtKB.
GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:0035711; P:T-helper 1 cell activation; ISS:UniProtKB.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
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;
Complete proteome; Cytoplasm; Differentiation; DNA-binding;
Glycoprotein; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 345 CCAAT/enhancer-binding protein beta.
/FTId=PRO_0000076617.
DOMAIN 271 334 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 24 Required for Lys-174 sumoylation.
REGION 24 135 Required for MYC transcriptional
repression.
{ECO:0000250|UniProtKB:P28033}.
REGION 275 295 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 297 304 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 116 124 9aaTAD.
COMPBIAS 162 170 Poly-Pro.
MOD_RES 3 3 Omega-N-methylated arginine; by CARM1.
{ECO:0000305|PubMed:20111005}.
MOD_RES 43 43 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 43 43 N6-methylated lysine; alternate.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 129 129 N6-acetyllysine; by KAT2A and KAT2B.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 132 132 N6-acetyllysine; by KAT2A and KAT2B.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 133 133 N6-acetyllysine; by KAT2A and KAT2B;
alternate.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 226 226 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 231 231 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 235 235 Phosphothreonine; by RPS6KA1, CDK2 and
MAPK. {ECO:0000269|PubMed:11684016,
ECO:0000269|PubMed:18647749}.
MOD_RES 266 266 Phosphothreonine; by RPS6KA1 and
PKC/PRKCA.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 288 288 Phosphoserine; by PKC/PRKCA.
{ECO:0000305|PubMed:9374525}.
MOD_RES 325 325 Phosphoserine; by CaMK2.
{ECO:0000250|UniProtKB:P28033}.
CARBOHYD 227 227 O-linked (GlcNAc) serine.
{ECO:0000250|UniProtKB:P28033}.
CARBOHYD 228 228 O-linked (GlcNAc) serine.
{ECO:0000250|UniProtKB:P28033}.
CROSSLNK 133 133 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 174 174 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:12810706}.
CROSSLNK 174 174 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 185 185 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 187 187 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 260 260 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 262 262 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 332 332 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 198 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_053313.
VAR_SEQ 1 23 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_053314.
VARIANT 195 195 G -> S (in dbSNP:rs4253440).
{ECO:0000269|Ref.3}.
/FTId=VAR_016300.
MUTAGEN 235 235 T->S: Loss of transactivation activity in
response to IFNG.
{ECO:0000269|PubMed:12048245}.
MUTAGEN 288 288 S->A: Loss of nuclear translocation.
{ECO:0000269|PubMed:9374525}.
CONFLICT 241 241 A -> P (in Ref. 8; no nucleotide entry).
{ECO:0000305}.
CONFLICT 253 253 A -> G (in Ref. 1; CAA36794).
{ECO:0000305}.
STRAND 269 271 {ECO:0000244|PDB:1H8A}.
HELIX 272 328 {ECO:0000244|PDB:1GU4}.
TURN 329 331 {ECO:0000244|PDB:1GU4}.
SEQUENCE 345 AA; 36106 MW; 9B725BD6CCAA771D CRC64;
MQRLVAWDPA CLPLPPPPPA FKSMEVANFY YEADCLAAAY GGKAAPAAPP AARPGPRPPA
GELGSIGDHE RAIDFSPYLE PLGAPQAPAP ATATDTFEAA PPAPAPAPAS SGQHHDFLSD
LFSDDYGGKN CKKPAEYGYV SLGRLGAAKG ALHPGCFAPL HPPPPPPPPP AELKAEPGFE
PADCKRKEEA GAPGGGAGMA AGFPYALRAY LGYQAVPSGS SGSLSTSSSS SPPGTPSPAD
AKAPPTACYA GAAPAPSQVK SKAKKTVDKH SDEYKIRRER NNIAVRKSRD KAKMRNLETQ
HKVLELTAEN ERLQKKVEQL SRELSTLRNL FKQLPEPLLA SSGHC


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