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Database: UniProt
Entry: P17676
LinkDB: P17676
Original site: P17676 
ID   CEBPB_HUMAN             Reviewed;         345 AA.
AC   P17676; A8K671; Q96IH2; Q9H4Z5;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 2.
DT   29-APR-2015, entry version 172.
DE   RecName: Full=CCAAT/enhancer-binding protein beta {ECO:0000312|HGNC:HGNC:1834};
DE            Short=C/EBP beta {ECO:0000312|HGNC:HGNC:1834};
DE   AltName: Full=Liver activator protein;
DE            Short=LAP;
DE   AltName: Full=Liver-enriched inhibitory protein;
DE            Short=LIP;
DE   AltName: Full=Nuclear factor NF-IL6;
DE   AltName: Full=Transcription factor 5;
DE            Short=TCF-5;
GN   Name=CEBPB {ECO:0000312|HGNC:HGNC:1834}; Synonyms=TCF5;
GN   ORFNames=PP9092;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=2112087;
RA   Akira S., Isshiki H., Sugita T., Tanabe O., Kinoshita S., Nishio Y.,
RA   Nakajima T., Hirano T., Kishimoto T.;
RT   "A nuclear factor for IL-6 expression (NF-IL6) is a member of a C/EBP
RT   family.";
RL   EMBO J. 9:1897-1906(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA   Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA   Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA   Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-195.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 241-323 (ISOFORMS 1/2/3).
RX   PubMed=7635140; DOI=10.1111/j.1432-1033.1995.tb20699.x;
RA   Toda K., Akira S., Kishimoto T., Sasaki H., Hashimoto K., Yamamoto Y.,
RA   Sagara Y., Shizuta Y.;
RT   "Identification of a transcriptional regulatory factor for human
RT   aromatase cytochrome P450 gene expression as nuclear factor
RT   interleukin-6 (NF-IL6), a member of the CCAAT/enhancer-binding protein
RT   family.";
RL   Eur. J. Biochem. 231:292-299(1995).
RN   [9]
RP   FUNCTION, PHOSPHORYLATION AT SER-288, MUTAGENESIS OF SER-288, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=9374525; DOI=10.1074/jbc.272.48.30356;
RA   Chinery R., Brockman J.A., Dransfield D.T., Coffey R.J.;
RT   "Antioxidant-induced nuclear translocation of CCAAT/enhancer-binding
RT   protein beta. A critical role for protein kinase A-mediated
RT   phosphorylation of Ser299.";
RL   J. Biol. Chem. 272:30356-30361(1997).
RN   [10]
RP   PHOSPHORYLATION AT THR-235.
RX   PubMed=11684016; DOI=10.1016/S1097-2765(01)00374-4;
RA   Buck M., Poli V., Hunter T., Chojkier M.;
RT   "C/EBPbeta phosphorylation by RSK creates a functional XEXD caspase
RT   inhibitory box critical for cell survival.";
RL   Mol. Cell 8:807-816(2001).
RN   [11]
RP   FUNCTION (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), AND
RP   DNA-BINDING.
RX   PubMed=11741938; DOI=10.1074/jbc.M108075200;
RA   Zhu Y., Saunders M.A., Yeh H., Deng W.G., Wu K.K.;
RT   "Dynamic regulation of cyclooxygenase-2 promoter activity by isoforms
RT   of CCAAT/enhancer-binding proteins.";
RL   J. Biol. Chem. 277:6923-6928(2002).
RN   [12]
RP   FUNCTION, AND MUTAGENESIS OF THR-235.
RX   PubMed=12048245; DOI=10.1073/pnas.122075799;
RA   Roy S.K., Hu J., Meng Q., Xia Y., Shapiro P.S., Reddy S.P.,
RA   Platanias L.C., Lindner D.J., Johnson P.F., Pritchard C., Pages G.,
RA   Pouyssegur J., Kalvakolanu D.V.;
RT   "MEKK1 plays a critical role in activating the transcription factor
RT   C/EBP-beta-dependent gene expression in response to IFN-gamma.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:7945-7950(2002).
RN   [13]
RP   SUMOYLATION AT LYS-174.
RX   PubMed=12810706; DOI=10.1074/jbc.M305680200;
RA   Eaton E.M., Sealy L.;
RT   "Modification of CCAAT/enhancer-binding protein-beta by the small
RT   ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3.";
RL   J. Biol. Chem. 278:33416-33421(2003).
RN   [14]
RP   DOMAIN.
RX   PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA   Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P.,
RA   Piskacek M.;
RT   "Nine-amino-acid transactivation domain: establishment and prediction
RT   utilities.";
RL   Genomics 89:756-768(2007).
RN   [15]
RP   FUNCTION, AND PHOSPHORYLATION AT THR-235.
RX   PubMed=18647749; DOI=10.1074/jbc.M802132200;
RA   Pless O., Kowenz-Leutz E., Knoblich M., Lausen J., Beyermann M.,
RA   Walsh M.J., Leutz A.;
RT   "G9a-mediated lysine methylation alters the function of
RT   CCAAT/enhancer-binding protein-beta.";
RL   J. Biol. Chem. 283:26357-26363(2008).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [17]
RP   INTERACTION WITH MED23; MED26; SMARCA2; SMARCB1 AND SMARCC1, AND
RP   METHYLATION AT ARG-3.
RX   PubMed=20111005; DOI=10.1038/emboj.2010.3;
RA   Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
RT   "Crosstalk between C/EBPbeta phosphorylation, arginine methylation,
RT   and SWI/SNF/Mediator implies an indexing transcription factor code.";
RL   EMBO J. 29:1105-1115(2010).
RN   [18]
RP   FUNCTION, INTERACTION WITH DDIT3, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=20829347; DOI=10.1074/jbc.M110.136259;
RA   Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y.;
RT   "Endoplasmic reticulum stress-activated C/EBP homologous protein
RT   enhances nuclear factor-kappaB signals via repression of peroxisome
RT   proliferator-activated receptor gamma.";
RL   J. Biol. Chem. 285:35330-35339(2010).
RN   [19]
RP   REVIEW OF PTMS AND FUNCTION.
RX   PubMed=25451943; DOI=10.1074/jbc.R114.619957;
RA   Guo L., Li X., Tang Q.;
RT   "Transcriptional Regulation of Adipocyte Differentiation: A Central
RT   Role for CCAAT/Enhancer-binding Protein (C/EBP) beta.";
RL   J. Biol. Chem. 290:755-761(2015).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 259-336 IN COMPLEX WITH
RP   RUNX1; CBFB AND DNA.
RX   PubMed=11257229; DOI=10.1016/S0092-8674(01)00271-9;
RA   Tahirov T.H., Inoue-Bungo T., Morii H., Fujikawa A., Sasaki M.,
RA   Kimura K., Shiina M., Sato K., Kumasaka T., Yamamoto M., Ishii S.,
RA   Ogata K.;
RT   "Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain
RT   and its allosteric control by CBFbeta.";
RL   Cell 104:755-767(2001).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 259-345 IN COMPLEX WITH MOUSE
RP   MYB.
RX   PubMed=11792321; DOI=10.1016/S0092-8674(01)00636-5;
RA   Tahirov T.H., Sato K., Ichikawa-Iwata E., Sasaki M., Inoue-Bungo T.,
RA   Shiina M., Kimura K., Takata S., Fujikawa A., Morii H., Kumasaka T.,
RA   Yamamoto M., Ishii S., Ogata K.;
RT   "Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a
RT   promoter.";
RL   Cell 108:57-70(2002).
CC   -!- FUNCTION: Important transcription factor regulating the expression
CC       of genes involved in immune and inflammatory responses
CC       (PubMed:9374525, PubMed:12048245, PubMed:18647749). Plays also a
CC       significant role in adipogenesis, as well as in the gluconeogenic
CC       pathway, liver regeneration, and hematopoiesis. The consensus
CC       recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity
CC       is governed by protein interactions and post-translational protein
CC       modifications. During early embryogenesis, plays essential and
CC       redundant functions with CEBPA. Has a promitotic effect on many
CC       cell types such as hepatocytes and adipocytes but has an
CC       antiproliferative effect on T-cells by repressing MYC expression,
CC       facilitating differentiation along the T-helper 2 lineage. Binds
CC       to regulatory regions of several acute-phase and cytokines genes
CC       and plays a role in the regulation of acute-phase reaction and
CC       inflammation. Plays also a role in intracellular bacteria killing
CC       (By similarity). During adipogenesis, is rapidly expressed and,
CC       after activation by phosphorylation, induces CEBPA and PPARG,
CC       which turn on the series of adipocyte genes that give rise to the
CC       adipocyte phenotype. The delayed transactivation of the CEBPA and
CC       PPARG genes by CEBPB appears necessary to allow mitotic clonal
CC       expansion and thereby progression of terminal differentiation
CC       (PubMed:20829347). Essential for female reproduction because of a
CC       critical role in ovarian follicle development (By similarity).
CC       Restricts osteoclastogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:12048245,
CC       ECO:0000269|PubMed:18647749, ECO:0000269|PubMed:20829347,
CC       ECO:0000269|PubMed:9374525, ECO:0000303|PubMed:25451943}.
CC   -!- FUNCTION: Isoform 2: Essential for gene expression induction in
CC       activated macrophages. Plays a major role in immune responses such
CC       as CD4(+) T-cell response, granuloma formation and endotoxin
CC       shock. Not essential for intracellular bacteria killing.
CC       {ECO:0000250|UniProtKB:P28033}.
CC   -!- FUNCTION: Isoform 3: Acts as a dominant negative through
CC       heterodimerization with isoform 2 (PubMed:11741938). Promotes
CC       osteoblast differentiation and osteoclastogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:P21272, ECO:0000250|UniProtKB:P28033,
CC       ECO:0000269|PubMed:11741938}.
CC   -!- SUBUNIT: Binds DNA as a dimer and can form stable heterodimers
CC       with CEBPA, CEBPD and CEBPG. Isoform 2 and isoform 3 also form
CC       heterodimers. Interacts with TRIM28 and PTGES2. Interacts with
CC       PRDM16. Interacts with CCDC85B. Forms a complex with THOC5.
CC       Interacts with ZNF638; this interaction increases transcriptional
CC       activation. Interacts with CIDEA and CIDEC; these interactions
CC       increase transcriptional activation of a subset of CEBPB
CC       downstream target genes. Interacts with DDIT3/CHOP.Interacts with
CC       EP300; recruits EP300 to chromatin. Interacts with RORA; the
CC       interaction disrupts interaction with EP300. Interacts (not
CC       methylated) with MED23, MED26, SMARCA2, SMARCB1 and SMARCC1
CC       (PubMed:20111005). Interacts with KAT2A and KAT2B (By similarity).
CC       {ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:11257229,
CC       ECO:0000269|PubMed:11792321, ECO:0000269|PubMed:20111005,
CC       ECO:0000269|PubMed:20829347}.
CC   -!- INTERACTION:
CC       Q86X55:CARM1; NbExp=2; IntAct=EBI-969696, EBI-2339854;
CC       P03120:E2 (xeno); NbExp=2; IntAct=EBI-969696, EBI-1779322;
CC       P03122:E2 (xeno); NbExp=3; IntAct=EBI-969696, EBI-7028618;
CC       P06422:E2 (xeno); NbExp=4; IntAct=EBI-969696, EBI-7136851;
CC       P06790:E2 (xeno); NbExp=4; IntAct=EBI-969696, EBI-7010629;
CC       P15941:MUC1; NbExp=8; IntAct=EBI-969696, EBI-10053698;
CC       P04637:TP53; NbExp=4; IntAct=EBI-969696, EBI-366083;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20829347}.
CC       Cytoplasm {ECO:0000269|PubMed:9374525}. Note=Translocates to the
CC       nucleus when phosphorylated at Ser-288. In T-cells when sumoylated
CC       drawn to pericentric heterochromatin thereby allowing
CC       proliferation (By similarity). {ECO:0000250|UniProtKB:P28033,
CC       ECO:0000269|PubMed:9374525}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=3;
CC       Name=1; Synonyms=C/EBPbeta-FL;
CC         IsoId=P17676-1; Sequence=Displayed;
CC       Name=2; Synonyms=C/EBPbeta-LAP;
CC         IsoId=P17676-2; Sequence=VSP_053314;
CC       Name=3; Synonyms=C/EBPbeta-LIP;
CC         IsoId=P17676-3; Sequence=VSP_053313;
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in the lung, kidney
CC       and spleen.
CC   -!- INDUCTION: By ER stress. {ECO:0000269|PubMed:20829347}.
CC   -!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a
CC       large number of yeast and animal transcription factors.
CC       {ECO:0000269|PubMed:17467953}.
CC   -!- PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-43 by
CC       EHMT2 inhibit transactivation activity. Methylation is probably
CC       inhibited by phosphorylation at Thr-235.
CC       {ECO:0000305|PubMed:18647749, ECO:0000305|PubMed:20111005}.
CC   -!- PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3
CC       (PubMed:12810706). Sumoylation at Lys-174 is required for
CC       inhibition of T-cells proliferation. In adipocytes, sumoylation at
CC       Lys-174 by PIAS1 leads to ubiquitination and subsequent
CC       proteasomal degradation. Desumoylated by SENP2, which abolishes
CC       ubiquitination and stabilizes protein levels (By similarity).
CC       {ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:12810706}.
CC   -!- PTM: Ubiquitinated, leading to proteasomal degradation.
CC       {ECO:0000250|UniProtKB:P28033}.
CC   -!- PTM: Phosphorylated at Thr-235 by MAPK and CDK2, serves to prime
CC       phosphorylation at Thr-226 and Ser-231 by GSK3B and acquire DNA-
CC       binding as well as transactivation activities, required to induce
CC       adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-235
CC       in the primed phosphorylated state during mitotical cloning
CC       expansion and thereby progression of terminal differentiation.
CC       Phosphorylation at Thr-266 enhances transactivation activity.
CC       Phosphorylation at Ser-325 in response to calcium increases
CC       transactivation activity. Phosphorylated at Thr-235 by RPS6KA1
CC       (PubMed:11684016). {ECO:0000250|UniProtKB:P28033,
CC       ECO:0000269|PubMed:11684016}.
CC   -!- PTM: O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents
CC       phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding
CC       activity which delays the adipocyte differentiation program.
CC       {ECO:0000250|UniProtKB:P28033}.
CC   -!- PTM: Acetylated. Acetylation at Lys-43 is an important and dynamic
CC       regulatory event that contributes to its ability to transactivate
CC       target genes, including those associated with adipogenesis and
CC       adipocyte function. Deacetylation by HDAC1 represses its
CC       transactivation activity. Acetylated by KAT2A and KAT2B within a
CC       cluster of lysine residues between amino acids 129-133, this
CC       acetylation is strongly induced by glucocorticoid treatment and
CC       enhances transactivation activity. {ECO:0000250|UniProtKB:P28033}.
CC   -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 bZIP (basic-leucine zipper) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/cebpb/";
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DR   EMBL; X52560; CAA36794.1; -; Genomic_DNA.
DR   EMBL; AF289608; AAL55792.1; -; mRNA.
DR   EMBL; AY193834; AAN86350.1; -; Genomic_DNA.
DR   EMBL; AK291536; BAF84225.1; -; mRNA.
DR   EMBL; AL161937; CAC14276.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75629.1; -; Genomic_DNA.
DR   EMBL; BC007538; AAH07538.1; -; mRNA.
DR   EMBL; BC021931; AAH21931.1; -; mRNA.
DR   CCDS; CCDS13429.1; -. [P17676-1]
DR   PIR; S12788; S12788.
DR   PIR; S66246; S66246.
DR   RefSeq; NP_001272807.1; NM_001285878.1. [P17676-2]
DR   RefSeq; NP_001272808.1; NM_001285879.1. [P17676-3]
DR   RefSeq; NP_005185.2; NM_005194.3. [P17676-1]
DR   UniGene; Hs.517106; -.
DR   UniGene; Hs.719041; -.
DR   UniGene; Hs.720603; -.
DR   PDB; 1GTW; X-ray; 1.85 A; A/B=259-336.
DR   PDB; 1GU4; X-ray; 1.80 A; A/B=259-336.
DR   PDB; 1GU5; X-ray; 2.10 A; A/B=259-336.
DR   PDB; 1H88; X-ray; 2.80 A; A/B=259-336.
DR   PDB; 1H89; X-ray; 2.45 A; A/B=273-336.
DR   PDB; 1H8A; X-ray; 2.23 A; A/B=259-336.
DR   PDB; 1HJB; X-ray; 3.00 A; A/B/D/E=259-345.
DR   PDB; 1IO4; X-ray; 3.00 A; A/B=259-336.
DR   PDB; 2E42; X-ray; 1.80 A; A/B=259-336.
DR   PDB; 2E43; X-ray; 2.10 A; A/B=259-336.
DR   PDBsum; 1GTW; -.
DR   PDBsum; 1GU4; -.
DR   PDBsum; 1GU5; -.
DR   PDBsum; 1H88; -.
DR   PDBsum; 1H89; -.
DR   PDBsum; 1H8A; -.
DR   PDBsum; 1HJB; -.
DR   PDBsum; 1IO4; -.
DR   PDBsum; 2E42; -.
DR   PDBsum; 2E43; -.
DR   ProteinModelPortal; P17676; -.
DR   SMR; P17676; 268-334.
DR   BioGrid; 107480; 68.
DR   DIP; DIP-35345N; -.
DR   IntAct; P17676; 14.
DR   MINT; MINT-230873; -.
DR   STRING; 9606.ENSP00000305422; -.
DR   PhosphoSite; P17676; -.
DR   BioMuta; CEBPB; -.
DR   DMDM; 34223718; -.
DR   MaxQB; P17676; -.
DR   PaxDb; P17676; -.
DR   PeptideAtlas; P17676; -.
DR   PRIDE; P17676; -.
DR   DNASU; 1051; -.
DR   Ensembl; ENST00000303004; ENSP00000305422; ENSG00000172216. [P17676-1]
DR   GeneID; 1051; -.
DR   KEGG; hsa:1051; -.
DR   UCSC; uc002xvi.2; human. [P17676-1]
DR   CTD; 1051; -.
DR   GeneCards; GC20P048807; -.
DR   H-InvDB; HIX0174729; -.
DR   HGNC; HGNC:1834; CEBPB.
DR   HPA; CAB004213; -.
DR   MIM; 189965; gene.
DR   neXtProt; NX_P17676; -.
DR   PharmGKB; PA26377; -.
DR   eggNOG; NOG299311; -.
DR   GeneTree; ENSGT00530000063192; -.
DR   HOGENOM; HOG000013112; -.
DR   HOVERGEN; HBG050879; -.
DR   InParanoid; P17676; -.
DR   KO; K10048; -.
DR   OMA; CKKPAEY; -.
DR   OrthoDB; EOG7R56TQ; -.
DR   PhylomeDB; P17676; -.
DR   TreeFam; TF105008; -.
DR   Reactome; REACT_169168; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; REACT_27161; Transcriptional regulation of white adipocyte differentiation.
DR   SignaLink; P17676; -.
DR   EvolutionaryTrace; P17676; -.
DR   GeneWiki; CEBPB; -.
DR   GenomeRNAi; 1051; -.
DR   NextBio; 4401; -.
DR   PRO; PR:P17676; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   Bgee; P17676; -.
DR   CleanEx; HS_CEBPB; -.
DR   ExpressionAtlas; P17676; baseline and differential.
DR   Genevestigator; P17676; -.
DR   GO; GO:0036488; C:CHOP-C/EBP complex; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
DR   GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0046982; F:protein heterodimerization activity; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IEA:Ensembl.
DR   GO; GO:0003705; F:RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; NAS:ProtInc.
DR   GO; GO:0006953; P:acute-phase response; TAS:ProtInc.
DR   GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR   GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR   GO; GO:0072574; P:hepatocyte proliferation; ISS:UniProtKB.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR   GO; GO:0097421; P:liver regeneration; ISS:UniProtKB.
DR   GO; GO:0060644; P:mammary gland epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0033598; P:mammary gland epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0045408; P:regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; ISS:UniProtKB.
DR   GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR016468; CCAAT/enhancer-binding.
DR   Pfam; PF07716; bZIP_2; 1.
DR   PIRSF; PIRSF005879; CCAAT/enhancer-binding; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   PROSITE; PS50217; BZIP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative initiation;
KW   Complete proteome; Cytoplasm; Differentiation; DNA-binding;
KW   Glycoprotein; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    345       CCAAT/enhancer-binding protein beta.
FT                                /FTId=PRO_0000076617.
FT   DOMAIN      271    334       bZIP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00978}.
FT   REGION        1     24       Required for Lys-174 sumoylation.
FT   REGION       24    135       Required for MYC transcriptional
FT                                repression.
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   REGION      275    295       Basic motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00978}.
FT   REGION      297    304       Leucine-zipper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00978}.
FT   MOTIF       116    124       9aaTAD.
FT   COMPBIAS    162    170       Poly-Pro.
FT   MOD_RES       3      3       Omega-N-methylated arginine; by CARM1.
FT                                {ECO:0000305|PubMed:20111005}.
FT   MOD_RES      43     43       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   MOD_RES      43     43       N6-methylated lysine.
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   MOD_RES     129    129       N6-acetyllysine; by KAT2A and KAT2B.
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   MOD_RES     132    132       N6-acetyllysine; by KAT2A and KAT2B.
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   MOD_RES     133    133       N6-acetyllysine; by KAT2A and KAT2B.
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   MOD_RES     226    226       Phosphothreonine; by GSK3-beta.
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   MOD_RES     231    231       Phosphoserine; by GSK3-beta.
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   MOD_RES     235    235       Phosphothreonine; by RPS6KA1, CDK2 and
FT                                MAPK. {ECO:0000250|UniProtKB:P28033,
FT                                ECO:0000269|PubMed:11684016,
FT                                ECO:0000269|PubMed:18647749}.
FT   MOD_RES     266    266       Phosphothreonine; by RPS6KA1 and
FT                                PKC/PRKCA.
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   MOD_RES     288    288       Phosphoserine; by PKC/PRKCA.
FT                                {ECO:0000305|PubMed:9374525}.
FT   MOD_RES     325    325       Phosphoserine; by CaMK2.
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   CARBOHYD    227    227       O-linked (GlcNAc).
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   CARBOHYD    228    228       O-linked (GlcNAc).
FT                                {ECO:0000250|UniProtKB:P28033}.
FT   CROSSLNK    174    174       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250|UniProtKB:P28033,
FT                                ECO:0000269|PubMed:12810706}.
FT   VAR_SEQ       1    198       Missing (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_053313.
FT   VAR_SEQ       1     23       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_053314.
FT   VARIANT     195    195       G -> S (in dbSNP:rs4253440).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_016300.
FT   MUTAGEN     235    235       T->S: Loss of transactivation activity in
FT                                response to IFNG.
FT                                {ECO:0000269|PubMed:12048245}.
FT   MUTAGEN     288    288       S->A: Loss of nuclear translocation.
FT                                {ECO:0000269|PubMed:9374525}.
FT   CONFLICT    241    241       A -> P (in Ref. 8; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    253    253       A -> G (in Ref. 1; CAA36794).
FT                                {ECO:0000305}.
FT   STRAND      269    271       {ECO:0000244|PDB:1H8A}.
FT   HELIX       272    328       {ECO:0000244|PDB:1GU4}.
FT   TURN        329    331       {ECO:0000244|PDB:1GU4}.
SQ   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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