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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   01-OCT-2014, entry version 166.
DE   RecName: Full=CCAAT/enhancer-binding protein beta;
DE            Short=C/EBP beta;
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; Synonyms=TCF5; 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   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   [10]
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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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. Binds to
CC       regulatory regions of several acute-phase and cytokines genes and
CC       probably plays a role in the regulation of acute-phase reaction,
CC       inflammation and hemopoiesis. The consensus recognition site is
CC       5'-T[TG]NNGNAA[TG]-3'. Plays an important role in adipose tissue
CC       differentiation. Regulates the transcriptional induction of
CC       peroxisome proliferator-activated receptor gamma (PPARG) as well
CC       as other adipogenesis key player genes.
CC       {ECO:0000269|PubMed:20829347}.
CC   -!- FUNCTION: Isoform 3: acts as a dominant negative through
CC       heterodimerization with isoform 2. {ECO:0000269|PubMed:20829347}.
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.
CC       {ECO:0000269|PubMed:11257229, ECO:0000269|PubMed:11792321,
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       P04637:TP53; NbExp=4; IntAct=EBI-969696, EBI-366083;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00978, ECO:0000269|PubMed:20829347}.
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: Sumoylated by polymeric chains of SUMO2 or SUMO3.
CC       {ECO:0000269|PubMed:12810706}.
CC   -!- PTM: Phosphorylated at Thr-235 by RPS6KA1.
CC       {ECO:0000269|PubMed:11684016}.
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; 67.
DR   DIP; DIP-35345N; -.
DR   IntAct; P17676; 9.
DR   MINT; MINT-230873; -.
DR   STRING; 9606.ENSP00000305422; -.
DR   PhosphoSite; P17676; -.
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   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   ArrayExpress; P17676; -.
DR   Bgee; P17676; -.
DR   CleanEx; HS_CEBPB; -.
DR   Genevestigator; P17676; -.
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:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
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:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
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:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
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:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0045408; P:regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
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; Activator; Alternative initiation; Complete proteome;
KW   Differentiation; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; 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      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     235    235       Phosphothreonine; by RPS6KA1.
FT                                {ECO:0000269|PubMed:11684016}.
FT   CROSSLNK    174    174       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
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   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
FT   HELIX       272    328
FT   TURN        329    331
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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