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CCAAT/enhancer-binding protein beta (C/EBP beta) (C/EBP-related protein 2) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched inhibitory protein) (LIP) (Liver-enriched transcriptional activator) (LAP) (Silencer factor B) (SF-B)

 CEBPB_RAT               Reviewed;         297 AA.
P21272; A2VD03;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
20-JUN-2018, entry version 159.
RecName: Full=CCAAT/enhancer-binding protein beta {ECO:0000312|RGD:2327};
Short=C/EBP beta {ECO:0000312|RGD:2327};
AltName: Full=C/EBP-related protein 2;
AltName: Full=Interleukin-6-dependent-binding protein;
Short=IL-6DBP;
AltName: Full=Liver-enriched inhibitory protein;
Short=LIP;
AltName: Full=Liver-enriched transcriptional activator;
Short=LAP;
AltName: Full=Silencer factor B;
Short=SF-B;
Name=Cebpb {ECO:0000312|RGD:2327};
Synonyms=Crp2, Nf-il6 {ECO:0000303|PubMed:8336793}, Sfb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2171780; DOI=10.1016/0092-8674(90)90459-R;
Poli V., Mancini F.P., Cortese R.;
"IL-6DBP, a nuclear protein involved in interleukin-6 signal
transduction, defines a new family of leucine zipper proteins related
to C/EBP.";
Cell 63:643-653(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Lewis; TISSUE=Liver;
PubMed=2253878; DOI=10.1101/gad.4.9.1541;
Descombes P., Chojkier M., Lichtsteiner S., Falvey E., Schibler U.;
"LAP, a novel member of the C/EBP gene family, encodes a liver-
enriched transcriptional activator protein.";
Genes Dev. 4:1541-1551(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=1377818; DOI=10.1093/nar/20.12.3091;
Thomassin H., Hamel D., Bernier D., Guertin M., Belanger L.;
"Molecular cloning of two C/EBP-related proteins that bind to the
promoter and the enhancer of the alpha 1-fetoprotein gene. Further
analysis of C/EBP beta and C/EBP gamma.";
Nucleic Acids Res. 20:3091-3098(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 77-297 (ISOFORM 1).
TISSUE=Liver;
Imagawa M., Osada S., Koyama Y., Suzuki T., Hirom P.C.,
Diccianni M.B., Morimura S., Muramatsu M.;
"SF-B (Silencer Factor B) that binds to a negative element in
glutathione transferase P gene is most likely identical to an
inducible trans-activator LAP/IL6-DBP.";
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-297, SUBUNIT, AND DNA-BINDING.
STRAIN=Sprague-Dawley; TISSUE=Adipose tissue, Liver, and Lung;
PubMed=1884998; DOI=10.1101/gad.5.9.1553;
Williams S.C., Cantwell C.A., Johnson P.F.;
"A family of C/EBP-related proteins capable of forming covalently
linked leucine zipper dimers in vitro.";
Genes Dev. 5:1553-1567(1991).
[7]
FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), DNA-BINDING,
DIMERIZATION, AND SUBUNIT.
PubMed=1934061; DOI=10.1016/0092-8674(91)90531-3;
Descombes P., Schibler U.;
"A liver-enriched transcriptional activator protein, LAP, and a
transcriptional inhibitory protein, LIP, are translated from the same
mRNA.";
Cell 67:569-579(1991).
[8]
FUNCTION, PHOSPHORYLATION AT SER-105, AND MUTAGENESIS OF SER-105.
PubMed=8336793; DOI=10.1038/364544a0;
Trautwein C., Caelles C., van der Geer P., Hunter T., Karin M.,
Chojkier M.;
"Transactivation by NF-IL6/LAP is enhanced by phosphorylation of its
activation domain.";
Nature 364:544-547(1993).
[9]
FUNCTION, PHOSPHORYLATION AT SER-105, MUTAGENESIS OF SER-105, AND
TISSUE SPECIFICITY.
PubMed=10635333; DOI=10.1016/S1097-2765(00)80237-3;
Buck M., Poli V., van der Geer P., Chojkier M., Hunter T.;
"Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP
beta is required for hepatocyte proliferation induced by TGF alpha.";
Mol. Cell 4:1087-1092(1999).
[10]
FUNCTION, AND INTERACTION WITH NFE2L1.
PubMed=15308669; DOI=10.1074/jbc.M405031200;
Narayanan K., Ramachandran A., Peterson M.C., Hao J., Kolstoe A.B.,
Friedman A.D., George A.;
"The CCAAT enhancer-binding protein (C/EBP)beta and Nrf1 interact to
regulate dentin sialophosphoprotein (DSPP) gene expression during
odontoblast differentiation.";
J. Biol. Chem. 279:45423-45432(2004).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Important transcription factor regulating the expression
of genes involved in immune and inflammatory responses
(PubMed:8336793). Plays also a significant role in adipogenesis,
as well as in the gluconeogenic pathway, liver regeneration, and
hematopoiesis (PubMed:10635333). The consensus recognition site is
5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by
protein interactions and post-translational protein modifications.
During early embryogenesis, plays essential and redundant
functions with CEBPA (By similarity). Has a promitotic effect on
many cell types such as hepatocytes and adipocytes but has an
antiproliferative effect on T-cells by repressing MYC expression,
facilitating differentiation along the T-helper 2 lineage
(PubMed:10635333). Binds to regulatory regions of several acute-
phase and cytokines genes and plays a role in the regulation of
acute-phase reaction and inflammation. Plays also a role in
intracellular bacteria killing (By similarity). During
adipogenesis, is rapidly expressed and, after activation by
phosphorylation, induces CEBPA and PPARG, which turn on the series
of adipocyte genes that give rise to the adipocyte phenotype. The
delayed transactivation of the CEBPA and PPARG genes by CEBPB
appears necessary to allow mitotic clonal expansion and thereby
progression of terminal differentiation (By similarity). Essential
for female reproduction because of a critical role in ovarian
follicle development (By similarity). Restricts
osteoclastogenesis: together with NFE2L1; represses expression of
DSPP during odontoblast differentiation (PubMed:15308669).
{ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033,
ECO:0000269|PubMed:10635333, ECO:0000269|PubMed:15308669,
ECO:0000269|PubMed:1934061, ECO:0000269|PubMed:8336793}.
-!- FUNCTION: Isoform 2: Essential for gene expression induction in
activated macrophages. Plays a major role in immune responses such
as CD4(+) T-cell response, granuloma formation and endotoxin
shock. Not essential for intracellular bacteria killing.
{ECO:0000250|UniProtKB:P28033}.
-!- FUNCTION: Isoform 3: Acts as a dominant negative through
heterodimerization with isoform 2 (PubMed:1934061). Promotes
osteoblast differentiation and osteoclastogenesis (By similarity).
{ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033,
ECO:0000269|PubMed:1934061}.
-!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer
(PubMed:1934061). Interacts with MYB; within the complex, MYB and
CEBPB bind to different promoter regions. Interacts with ATF4.
Binds DNA as a heterodimer with ATF4 (By similarity). Can form
stable heterodimers with CEBPA, CEBPD, CEBPE and CEBPG
(PubMed:1377818, PubMed:1884998). Isoform 2 and isoform 3 also
form heterodimers (PubMed:1934061). Interacts with TRIM28 and
PTGES2. Interacts with PRDM16. Interacts with CCDC85B. Forms a
complex with THOC5. Interacts with ZNF638; this interaction
increases transcriptional activation. Interacts with CIDEA and
CIDEC; these interactions increase transcriptional activation of a
subset of CEBPB downstream target genes. Interacts with
DDIT3/CHOP.Interacts with EP300; recruits EP300 to chromatin.
Interacts with RORA; the interaction disrupts interaction with
EP300. Interacts (not methylated) with MED23, MED26, SMARCA2,
SMARCB1 and SMARCC1 (By similarity). Interacts with KAT2A and
KAT2B (By similarity). Interacts with ATF5; EP300 is required for
ATF5 and CEBPB interaction and DNA binding (By similarity).
Interacts with NFE2L1; the heterodimer represses expression of
DSPP during odontoblast differentiation (PubMed:15308669).
{ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033,
ECO:0000269|PubMed:1377818, ECO:0000269|PubMed:15308669,
ECO:0000269|PubMed:1884998, ECO:0000269|PubMed:1934061}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17676}.
Cytoplasm {ECO:0000250|UniProtKB:P17676}. Note=Translocates to the
nucleus when phosphorylated at Ser-288. In T-cells when sumoylated
drawn to pericentric heterochromatin thereby allowing
proliferation (By similarity). {ECO:0000250|UniProtKB:P17676,
ECO:0000250|UniProtKB:P28033}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=1; Synonyms=FL;
IsoId=P21272-1; Sequence=Displayed;
Note=Not detected in rat liver.;
Name=2; Synonyms=LAP;
IsoId=P21272-2; Sequence=VSP_053316;
Note=Major form in.;
Name=3; Synonyms=LIP;
IsoId=P21272-3; Sequence=VSP_053315;
-!- TISSUE SPECIFICITY: Liver and lung.
-!- PTM: Phosphorylated at Thr-189 by MAPK and CDK2, serves to prime
phosphorylation at Thr-180 and Ser-185 by GSK3B and acquire DNA-
binding as well as transactivation activities, required to induce
adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-189
in the primed phosphorylated state during mitotical cloning
expansion and thereby progression of terminal differentiation (By
similarity). Phosphorylation at Ser-105 enhances transactivation
activity (PubMed:8336793). Phosphorylation at Ser-277 in response
to calcium increases transactivation activity. Phosphorylated at
Thr-189 by RPS6KA1 (By similarity). {ECO:0000250|UniProtKB:P17676,
ECO:0000250|UniProtKB:P28033, ECO:0000269|PubMed:8336793}.
-!- PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by
EHMT2 inhibit transactivation activity. Methylation is probably
inhibited by phosphorylation at Thr-189.
{ECO:0000250|UniProtKB:P17676}.
-!- PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3 (By
similarity). Sumoylation at Lys-134 is required for inhibition of
T-cells proliferation. In adipocytes, sumoylation at Lys-134 by
PIAS1 leads to ubiquitination and subsequent proteasomal
degradation. Desumoylated by SENP2, which abolishes ubiquitination
and stabilizes protein levels (By similarity).
{ECO:0000250|UniProtKB:P17676, ECO:0000250|UniProtKB:P28033}.
-!- PTM: Ubiquitinated, leading to proteasomal degradation.
{ECO:0000250|UniProtKB:P28033}.
-!- PTM: O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents
phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding
activity which delays the adipocyte differentiation program.
{ECO:0000250|UniProtKB:P28033}.
-!- PTM: Acetylated. Acetylation at Lys-39 is an important and dynamic
regulatory event that contributes to its ability to transactivate
target genes, including those associated with adipogenesis and
adipocyte function. Deacetylation by HDAC1 represses its
transactivation activity. Acetylated by KAT2A and KAT2B within a
cluster of lysine residues between amino acids 99-103, this
acetylation is strongly induced by glucocorticoid treatment and
enhances transactivation activity. {ECO:0000250|UniProtKB:P28033}.
-!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily.
{ECO:0000305}.
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EMBL; M57235; AAA19669.1; -; mRNA.
EMBL; X54626; CAA38443.1; -; Genomic_DNA.
EMBL; BC129071; AAI29072.1; -; mRNA.
EMBL; X60769; CAA43179.1; -; mRNA.
EMBL; AY056052; AAA40972.1; -; Genomic_DNA.
PIR; A35914; A35914.
RefSeq; NP_001288644.1; NM_001301715.1. [P21272-2]
RefSeq; NP_001288649.1; NM_001301720.1. [P21272-3]
RefSeq; NP_077039.3; NM_024125.5. [P21272-1]
UniGene; Rn.6479; -.
ProteinModelPortal; P21272; -.
SMR; P21272; -.
BioGrid; 246438; 53.
ComplexPortal; CPX-62; CHOP-C/EBPbeta complex.
ComplexPortal; CPX-63; C/EBPbeta complex.
DIP; DIP-28139N; -.
IntAct; P21272; 2.
STRING; 10116.ENSRNOP00000065222; -.
iPTMnet; P21272; -.
PhosphoSitePlus; P21272; -.
PaxDb; P21272; -.
PeptideAtlas; P21272; -.
PRIDE; P21272; -.
Ensembl; ENSRNOT00000083876; ENSRNOP00000071427; ENSRNOG00000057347. [P21272-1]
GeneID; 24253; -.
KEGG; rno:24253; -.
UCSC; RGD:2327; rat. [P21272-1]
CTD; 1051; -.
RGD; 2327; Cebpb.
eggNOG; KOG3119; Eukaryota.
eggNOG; ENOG410YJ8G; LUCA.
GeneTree; ENSGT00530000063192; -.
HOGENOM; HOG000013112; -.
HOVERGEN; HBG050879; -.
InParanoid; P21272; -.
KO; K10048; -.
OMA; CKKPAEY; -.
OrthoDB; EOG091G11FC; -.
PhylomeDB; P21272; -.
TreeFam; TF105008; -.
Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
PRO; PR:P21272; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000057347; -.
Genevisible; P21272; RN.
GO; GO:0036488; C:CHOP-C/EBP complex; IPI:ParkinsonsUK-UCL.
GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0035259; F:glucocorticoid receptor binding; IPI:RGD.
GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
GO; GO:0002432; P:granuloma formation; ISS:UniProtKB.
GO; GO:0072574; P:hepatocyte proliferation; IDA:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0097421; P:liver regeneration; ISS:UniProtKB.
GO; GO:0060644; P:mammary gland epithelial cell differentiation; IEA:Ensembl.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IEA:Ensembl.
GO; GO:0007613; P:memory; IEP:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
GO; GO:0070169; P:positive regulation of biomineral tissue development; IEA:Ensembl.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:2000120; P:positive regulation of sodium-dependent phosphate transport; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0045408; P:regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
GO; GO:1901329; P:regulation of odontoblast differentiation; IDA:UniProtKB.
GO; GO:0045670; P:regulation of osteoclast differentiation; ISS:UniProtKB.
GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0035711; P:T-helper 1 cell activation; ISS:UniProtKB.
InterPro; IPR004827; bZIP.
InterPro; IPR016468; C/EBP_chordates.
Pfam; PF07716; bZIP_2; 1.
PIRSF; PIRSF005879; CCAAT/enhancer-binding; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative initiation; Complete proteome;
Cytoplasm; Differentiation; DNA-binding; Glycoprotein;
Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 297 CCAAT/enhancer-binding protein beta.
/FTId=PRO_0000076619.
DOMAIN 223 286 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 22 Required for Lys-134 sumoylation.
{ECO:0000250|UniProtKB:P17676}.
REGION 22 105 Required for MYC transcriptional
repression.
{ECO:0000250|UniProtKB:P28033}.
REGION 227 247 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 249 256 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 121 130 Pro-rich.
COMPBIAS 171 192 Pro/Ser-rich.
MOD_RES 3 3 Omega-N-methylated arginine; by CARM1.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 39 39 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 39 39 N6-methylated lysine; alternate.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 99 99 N6-acetyllysine; by KAT2A and KAT2B.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 102 102 N6-acetyllysine; by KAT2A and KAT2B.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 103 103 N6-acetyllysine; by KAT2A and KAT2B;
alternate.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 105 105 Phosphoserine; by RPS6KA1 and PKC/PRKCA.
{ECO:0000269|PubMed:10635333,
ECO:0000269|PubMed:8336793}.
MOD_RES 180 180 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 185 185 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:P28033}.
MOD_RES 189 189 Phosphothreonine; by RPS6KA1, CDK2 and
MAPK. {ECO:0000250|UniProtKB:P17676}.
MOD_RES 240 240 Phosphoserine; by PKC/PRKCA.
{ECO:0000250|UniProtKB:P17676}.
MOD_RES 277 277 Phosphoserine; by CaMK2.
{ECO:0000250|UniProtKB:P28033}.
CARBOHYD 181 181 O-linked (GlcNAc) serine.
{ECO:0000250|UniProtKB:P28033}.
CARBOHYD 182 182 O-linked (GlcNAc) serine.
{ECO:0000250|UniProtKB:P28033}.
CROSSLNK 103 103 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P17676}.
CROSSLNK 134 134 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250|UniProtKB:P17676,
ECO:0000250|UniProtKB:P28033}.
CROSSLNK 134 134 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P17676}.
CROSSLNK 145 145 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17676}.
CROSSLNK 212 212 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17676}.
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17676}.
CROSSLNK 284 284 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P17676}.
VAR_SEQ 1 152 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_053315.
VAR_SEQ 1 21 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_053316.
MUTAGEN 105 105 S->A: No effect on DNA-binding. Loss of
transactivation activity. Loss of
hepatocyte proliferation induction by
TGFA. {ECO:0000269|PubMed:10635333,
ECO:0000269|PubMed:8336793}.
MUTAGEN 105 105 S->D: No effect on DNA-binding. Increases
transactivation activity.
{ECO:0000269|PubMed:8336793}.
SEQUENCE 297 AA; 31503 MW; C2511FDB65527789 CRC64;
MHRLLAWDAA CLPPPPAAFR PMEVANFYYE PDCLAYGAKA ARAAPRAPAA EPAIGEHERA
IDFSPYLEPL APAAADFAAP APAHHDFLSD LFADDYGAKP SKKPSDYGYV SLGRAGAKAA
PPACFPPPPP AALKAEPGFE PADCKRADDA PAMAAGFPFA LRAYLGYQAT PSGSSGSLST
SSSSSPPGTP SPADAKAAPA ACFAGPPAAP AKAKAKKAVD KLSDEYKMRR ERNNIAVRKS
RDKAKMRNLE TQHKVLELTA ENERLQKKVE QLSRELSTLR NLFKQLPEPL LASAGHC


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E0713m ELISA kit AGP_EBP,C_EBP beta,CCAAT_enhancer-binding protein beta,Cebpb,IL-6DBP,Interleukin-6-dependent-binding protein,LAP,Liver-enriched transcriptional activator,Mouse,Mus musculus 96T
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