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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-SEP-2021, entry version 223.
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 {ECO:0000303|PubMed:1741402};
DE   AltName: Full=Transcription factor 5;
DE            Short=TCF-5;
GN   Name=CEBPB {ECO:0000312|HGNC:HGNC:1834}; Synonyms=TCF5; ORFNames=PP9092;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   TISSUE=Placenta;
RX   PubMed=2112087; DOI=10.1002/j.1460-2075.1990.tb08316.x;
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., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., 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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., 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., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., 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., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., 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 project:
RT   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 aromatase
RT   cytochrome P450 gene expression as nuclear factor interleukin-6 (NF-IL6), a
RT   member of the CCAAT/enhancer-binding protein family.";
RL   Eur. J. Biochem. 231:292-299(1995).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH CEBPD.
RX   PubMed=1741402; DOI=10.1073/pnas.89.4.1473;
RA   Kinoshita S., Akira S., Kishimoto T.;
RT   "A member of the C/EBP family, NF-IL6 beta, forms a heterodimer and
RT   transcriptionally synergizes with NF-IL6.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:1473-1476(1992).
RN   [10]
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 phosphorylation
RT   of Ser299.";
RL   J. Biol. Chem. 272:30356-30361(1997).
RN   [11]
RP   INTERACTION WITH ATF4, AND DNA-BINDING.
RX   PubMed=11018027; DOI=10.1074/jbc.m005594200;
RA   Podust L.M., Krezel A.M., Kim Y.;
RT   "Crystal structure of the CCAAT box/enhancer-binding protein beta
RT   activating transcription factor-4 basic leucine zipper heterodimer in the
RT   absence of DNA.";
RL   J. Biol. Chem. 276:505-513(2001).
RN   [12]
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   [13]
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 of
RT   CCAAT/enhancer-binding proteins.";
RL   J. Biol. Chem. 277:6923-6928(2002).
RN   [14]
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., Platanias L.C.,
RA   Lindner D.J., Johnson P.F., Pritchard C., Pages G., Pouyssegur J.,
RA   Kalvakolanu D.V.;
RT   "MEKK1 plays a critical role in activating the transcription factor C/EBP-
RT   beta-dependent gene expression in response to IFN-gamma.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:7945-7950(2002).
RN   [15]
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   [16]
RP   DOMAIN.
RX   PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA   Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.;
RT   "Nine-amino-acid transactivation domain: establishment and prediction
RT   utilities.";
RL   Genomics 89:756-768(2007).
RN   [17]
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 CCAAT/enhancer-
RT   binding protein-beta.";
RL   J. Biol. Chem. 283:26357-26363(2008).
RN   [18]
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., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [19]
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, and
RT   SWI/SNF/Mediator implies an indexing transcription factor code.";
RL   EMBO J. 29:1105-1115(2010).
RN   [20]
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 enhances
RT   nuclear factor-kappaB signals via repression of peroxisome proliferator-
RT   activated receptor gamma.";
RL   J. Biol. Chem. 285:35330-35339(2010).
RN   [21]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-174; LYS-187 AND
RP   LYS-260, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [22]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-174; LYS-187 AND
RP   LYS-260, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [23]
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 Role
RT   for CCAAT/Enhancer-binding Protein (C/EBP) beta.";
RL   J. Biol. Chem. 290:755-761(2015).
RN   [24]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-174, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [25]
RP   INTERACTION WITH SIX1.
RX   PubMed=27923061; DOI=10.1371/journal.pgen.1006474;
RA   Brunmeir R., Wu J., Peng X., Kim S.Y., Julien S.G., Zhang Q., Xie W.,
RA   Xu F.;
RT   "Comparative Transcriptomic and Epigenomic Analyses Reveal New Regulators
RT   of Murine Brown Adipogenesis.";
RL   PLoS Genet. 12:E1006474-E1006474(2016).
RN   [26]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-174; LYS-185; LYS-187;
RP   LYS-260; LYS-262 AND LYS-332, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 259-336 IN COMPLEXES WITH DNA,
RP   AND SUBUNIT.
RX   PubMed=11257229; DOI=10.1016/s0092-8674(01)00271-9;
RA   Tahirov T.H., Inoue-Bungo T., Morii H., Fujikawa A., Sasaki M., Kimura K.,
RA   Shiina M., Sato K., Kumasaka T., Yamamoto M., Ishii S., Ogata K.;
RT   "Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and
RT   its allosteric control by CBFbeta.";
RL   Cell 104:755-767(2001).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 259-345 IN COMPLEX WITH MOUSE
RP   MYB, SUBUNIT, INTERACTION WITH MYB, AND DNA-BINDING.
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 of
CC       genes involved in immune and inflammatory responses (PubMed:1741402,
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 is
CC       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 cell
CC       types such as hepatocytes and adipocytes but has an antiproliferative
CC       effect on T-cells by repressing MYC expression, facilitating
CC       differentiation along the T-helper 2 lineage. Binds to regulatory
CC       regions of several acute-phase and cytokines genes and plays a role in
CC       the regulation of acute-phase reaction and inflammation. Plays also a
CC       role in intracellular bacteria killing (By similarity). During
CC       adipogenesis, is rapidly expressed and, after activation by
CC       phosphorylation, induces CEBPA and PPARG, which turn on the series of
CC       adipocyte genes that give rise to the adipocyte phenotype. The delayed
CC       transactivation of the CEBPA and PPARG genes by CEBPB appears necessary
CC       to allow mitotic clonal expansion and thereby progression of terminal
CC       differentiation (PubMed:20829347). Essential for female reproduction
CC       because of a critical role in ovarian follicle development (By
CC       similarity). Restricts osteoclastogenesis: together with NFE2L1;
CC       represses expression of DSPP during odontoblast differentiation (By
CC       similarity). {ECO:0000250|UniProtKB:P21272,
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 as
CC       CD4(+) T-cell response, granuloma formation and endotoxin shock. Not
CC       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 homodimer and as a heterodimer
CC       (PubMed:11018027, PubMed:11257229, PubMed:11792321). Interacts with
CC       ATF4. Binds DNA as a heterodimer with ATF4 (PubMed:11018027). Interacts
CC       with MYB; within the complex, MYB and CEBPB bind to different promoter
CC       regions (PubMed:11792321). Can form stable heterodimers with CEBPD
CC       (PubMed:1741402). Can form stable heterodimers with CEBPA and CEBPE (By
CC       similarity). Interacts with SIX1 (PubMed:27923061). Isoform 2 and
CC       isoform 3 also form heterodimers. Interacts with TRIM28 and PTGES2.
CC       Interacts with PRDM16. Interacts with CCDC85B. Forms a complex with
CC       THOC5. Interacts with ZNF638; this interaction increases
CC       transcriptional activation. Interacts with CIDEA and CIDEC; these
CC       interactions increase transcriptional activation of a subset of CEBPB
CC       downstream target genes (By similarity). Interacts with DDIT3/CHOP
CC       (PubMed:20829347). Interacts with EP300; recruits EP300 to chromatin.
CC       Interacts with RORA; the interaction disrupts interaction with EP300.
CC       Interacts (not methylated) with MED23, MED26, SMARCA2, SMARCB1 and
CC       SMARCC1 (PubMed:20111005). Interacts with KAT2A and KAT2B (By
CC       similarity). Interacts with ATF5; EP300 is required for ATF5 and CEBPB
CC       interaction and DNA binding (By similarity). Interacts with NFE2L1; the
CC       heterodimer represses expression of DSPP during odontoblast
CC       differentiation (By similarity). {ECO:0000250|UniProtKB:P21272,
CC       ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:11018027,
CC       ECO:0000269|PubMed:11257229, ECO:0000269|PubMed:11792321,
CC       ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:20829347,
CC       ECO:0000269|PubMed:27923061}.
CC   -!- INTERACTION:
CC       P17676; P18848: ATF4; NbExp=2; IntAct=EBI-969696, EBI-492498;
CC       P17676; Q16520: BATF; NbExp=2; IntAct=EBI-969696, EBI-749503;
CC       P17676; Q86X55: CARM1; NbExp=2; IntAct=EBI-969696, EBI-2339854;
CC       P17676; P49715: CEBPA; NbExp=2; IntAct=EBI-969696, EBI-1172054;
CC       P17676; P53567: CEBPG; NbExp=2; IntAct=EBI-969696, EBI-740209;
CC       P17676; P35638: DDIT3; NbExp=2; IntAct=EBI-969696, EBI-742651;
CC       P17676; P03372: ESR1; NbExp=2; IntAct=EBI-969696, EBI-78473;
CC       P17676; PRO_0000317447 [P15941]: MUC1; NbExp=8; IntAct=EBI-969696, EBI-10053698;
CC       P17676; P04637: TP53; NbExp=4; IntAct=EBI-969696, EBI-366083;
CC       P17676; P03120: E2; Xeno; NbExp=2; IntAct=EBI-969696, EBI-1779322;
CC       P17676; P03122: E2; Xeno; NbExp=3; IntAct=EBI-969696, EBI-7028618;
CC       P17676; P06422: E2; Xeno; NbExp=4; IntAct=EBI-969696, EBI-7136851;
CC       P17676; P06790: E2; Xeno; NbExp=4; IntAct=EBI-969696, EBI-7010629;
CC       P17676-1; P63165: SUMO1; NbExp=5; IntAct=EBI-9997012, EBI-80140;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20829347}. Cytoplasm
CC       {ECO:0000269|PubMed:9374525}. Note=Translocates to the nucleus when
CC       phosphorylated at Ser-288. In T-cells when sumoylated drawn to
CC       pericentric heterochromatin thereby allowing proliferation (By
CC       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 and
CC       spleen.
CC   -!- INDUCTION: By ER stress. {ECO:0000269|PubMed:20829347}.
CC   -!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a large
CC       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 EHMT2
CC       inhibit transactivation activity. Methylation is probably inhibited by
CC       phosphorylation at Thr-235. {ECO:0000305|PubMed:18647749,
CC       ECO:0000305|PubMed:20111005}.
CC   -!- PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3
CC       (PubMed:12810706). Sumoylation at Lys-174 is required for inhibition of
CC       T-cells proliferation. In adipocytes, sumoylation at Lys-174 by PIAS1
CC       leads to ubiquitination and subsequent proteasomal degradation.
CC       Desumoylated by SENP2, which abolishes ubiquitination and stabilizes
CC       protein levels (By similarity). {ECO:0000250|UniProtKB:P28033,
CC       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-binding
CC       as well as transactivation activities, required to induce adipogenesis.
CC       MAPK and CDK2 act sequentially to maintain Thr-235 in the primed
CC       phosphorylated state during mitotical cloning expansion and thereby
CC       progression of terminal differentiation. Phosphorylation at Thr-266
CC       enhances transactivation activity. Phosphorylation at Ser-325 in
CC       response to calcium increases transactivation activity. Phosphorylated
CC       at Thr-235 by RPS6KA1 (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. {ECO:0000305}.
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; -; NOT_ANNOTATED_CDS; 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   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   PDB; 6MG1; X-ray; 1.75 A; A/B=269-344.
DR   PDB; 6MG2; X-ray; 1.93 A; A/B=269-344.
DR   PDB; 6MG3; X-ray; 2.05 A; A/B=269-344.
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   PDBsum; 6MG1; -.
DR   PDBsum; 6MG2; -.
DR   PDBsum; 6MG3; -.
DR   SMR; P17676; -.
DR   BioGRID; 107480; 83.
DR   ComplexPortal; CPX-3361; bZIP transcription factor complex, CEBPB-CEBPB.
DR   ComplexPortal; CPX-504; c-Myb-C/EBPbeta complex.
DR   ComplexPortal; CPX-6470; bZIP transcription factor complex, ATF3-CEBPB.
DR   ComplexPortal; CPX-6471; bZIP transcription factor complex, ATF3-CEBPG.
DR   ComplexPortal; CPX-6526; bZIP transcription factor complex, ATF4-CEBPB.
DR   ComplexPortal; CPX-70; bZIP transcription factor complex, CEBPB-DDIT3.
DR   CORUM; P17676; -.
DR   DIP; DIP-35345N; -.
DR   ELM; P17676; -.
DR   IntAct; P17676; 28.
DR   MINT; P17676; -.
DR   STRING; 9606.ENSP00000305422; -.
DR   DrugBank; DB04216; Quercetin.
DR   GlyGen; P17676; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P17676; -.
DR   PhosphoSitePlus; P17676; -.
DR   BioMuta; CEBPB; -.
DR   DMDM; 34223718; -.
DR   EPD; P17676; -.
DR   jPOST; P17676; -.
DR   MassIVE; P17676; -.
DR   MaxQB; P17676; -.
DR   PaxDb; P17676; -.
DR   PeptideAtlas; P17676; -.
DR   PRIDE; P17676; -.
DR   ProteomicsDB; 53503; -. [P17676-1]
DR   Antibodypedia; 3782; 681 antibodies.
DR   DNASU; 1051; -.
DR   Ensembl; ENST00000303004; ENSP00000305422; ENSG00000172216. [P17676-1]
DR   GeneID; 1051; -.
DR   KEGG; hsa:1051; -.
DR   UCSC; uc002xvi.4; human. [P17676-1]
DR   CTD; 1051; -.
DR   DisGeNET; 1051; -.
DR   GeneCards; CEBPB; -.
DR   HGNC; HGNC:1834; CEBPB.
DR   HPA; ENSG00000172216; Tissue enhanced (skeletal).
DR   MIM; 189965; gene.
DR   neXtProt; NX_P17676; -.
DR   OpenTargets; ENSG00000172216; -.
DR   PharmGKB; PA26377; -.
DR   VEuPathDB; HostDB:ENSG00000172216; -.
DR   eggNOG; KOG3119; Eukaryota.
DR   GeneTree; ENSGT00940000162137; -.
DR   HOGENOM; CLU_043327_1_0_1; -.
DR   InParanoid; P17676; -.
DR   OMA; KNCKKAA; -.
DR   OrthoDB; 1284308at2759; -.
DR   PhylomeDB; P17676; -.
DR   TreeFam; TF105008; -.
DR   PathwayCommons; P17676; -.
DR   Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress.
DR   Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR   Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR   Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR   Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR   Reactome; R-HSA-9648895; Response of EIF2AK1 (HRI) to heme deficiency.
DR   SignaLink; P17676; -.
DR   SIGNOR; P17676; -.
DR   BioGRID-ORCS; 1051; 50 hits in 1040 CRISPR screens.
DR   ChiTaRS; CEBPB; human.
DR   EvolutionaryTrace; P17676; -.
DR   GeneWiki; CEBPB; -.
DR   GenomeRNAi; 1051; -.
DR   Pharos; P17676; Tbio.
DR   PRO; PR:P17676; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P17676; protein.
DR   Bgee; ENSG00000172216; Expressed in layer of synovial tissue and 255 other tissues.
DR   Genevisible; P17676; HS.
DR   GO; GO:0036488; C:CHOP-C/EBP complex; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0035259; F:glucocorticoid receptor binding; IEA:Ensembl.
DR   GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:ARUK-UCL.
DR   GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
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:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR   GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR   GO; GO:0002432; P:granuloma formation; ISS:UniProtKB.
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:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL.
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:0007613; P:memory; 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:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0070169; P:positive regulation of biomineral tissue development; IDA:MGI.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
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:2000120; P:positive regulation of sodium-dependent phosphate transport; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR   GO; GO:2001198; P:regulation of dendritic cell differentiation; IEA:Ensembl.
DR   GO; GO:0032675; P:regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:1901329; P:regulation of odontoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; 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:0035711; P:T-helper 1 cell activation; ISS:UniProtKB.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR016468; C/EBP_chordates.
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; Cytoplasm;
KW   Differentiation; DNA-binding; Glycoprotein; Isopeptide bond; Methylation;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..345
FT                   /note="CCAAT/enhancer-binding protein beta"
FT                   /id="PRO_0000076617"
FT   DOMAIN          271..334
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..24
FT                   /note="Required for Lys-174 sumoylation"
FT   REGION          24..135
FT                   /note="Required for MYC transcriptional repression"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   REGION          46..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..295
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          297..304
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   MOTIF           116..124
FT                   /note="9aaTAD"
FT   COMPBIAS        157..175
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         3
FT                   /note="Asymmetric dimethylarginine; by CARM1"
FT                   /evidence="ECO:0000305|PubMed:20111005"
FT   MOD_RES         43
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   MOD_RES         43
FT                   /note="N6-methylated lysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   MOD_RES         129
FT                   /note="N6-acetyllysine; by KAT2A and KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   MOD_RES         132
FT                   /note="N6-acetyllysine; by KAT2A and KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   MOD_RES         133
FT                   /note="N6-acetyllysine; by KAT2A and KAT2B; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   MOD_RES         226
FT                   /note="Phosphothreonine; by GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   MOD_RES         231
FT                   /note="Phosphoserine; by GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   MOD_RES         235
FT                   /note="Phosphothreonine; by RPS6KA1, CDK2 and MAPK"
FT                   /evidence="ECO:0000269|PubMed:11684016,
FT                   ECO:0000269|PubMed:18647749"
FT   MOD_RES         266
FT                   /note="Phosphothreonine; by RPS6KA1 and PKC/PRKCA"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   MOD_RES         288
FT                   /note="Phosphoserine; by PKC/PRKCA"
FT                   /evidence="ECO:0000305|PubMed:9374525"
FT   MOD_RES         325
FT                   /note="Phosphoserine; by CaMK2"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   CARBOHYD        227
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   CARBOHYD        228
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P28033"
FT   CROSSLNK        133
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        174
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000269|PubMed:12810706"
FT   CROSSLNK        174
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        185
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        187
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        260
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        262
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        332
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..198
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_053313"
FT   VAR_SEQ         1..23
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_053314"
FT   VARIANT         195
FT                   /note="G -> S (in dbSNP:rs4253440)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_016300"
FT   MUTAGEN         235
FT                   /note="T->S: Loss of transactivation activity in response
FT                   to IFNG."
FT                   /evidence="ECO:0000269|PubMed:12048245"
FT   MUTAGEN         288
FT                   /note="S->A: Loss of nuclear translocation."
FT                   /evidence="ECO:0000269|PubMed:9374525"
FT   CONFLICT        241
FT                   /note="A -> P (in Ref. 8; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253
FT                   /note="A -> G (in Ref. 1; CAA36794)"
FT                   /evidence="ECO:0000305"
FT   STRAND          269..271
FT                   /evidence="ECO:0007829|PDB:1H8A"
FT   HELIX           272..329
FT                   /evidence="ECO:0007829|PDB:6MG1"
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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