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CCAAT/enhancer-binding protein alpha (C/EBP alpha)

 CEBPA_MOUSE             Reviewed;         359 AA.
P53566; Q91XB6;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
22-NOV-2017, entry version 152.
RecName: Full=CCAAT/enhancer-binding protein alpha {ECO:0000312|MGI:MGI:99480};
Short=C/EBP alpha {ECO:0000312|MGI:MGI:99480};
Name=Cebpa {ECO:0000312|MGI:MGI:99480};
Synonyms=Cebp {ECO:0000303|PubMed:1935900};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2006196; DOI=10.1073/pnas.88.6.2593;
Christy R.J., Kaestner K.H., Geiman D.E., Lane M.D.;
"CCAAT/enhancer binding protein gene promoter: binding of nuclear
factors during differentiation of 3T3-L1 preadipocytes.";
Proc. Natl. Acad. Sci. U.S.A. 88:2593-2597(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=FVB/N; TISSUE=Liver;
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).
[4]
FUNCTION.
PubMed=1935900;
Samuelsson L., Stroemberg K., Vikman K., Bjursell G., Enerbaeck S.;
"The CCAAT/enhancer binding protein and its role in adipocyte
differentiation: evidence for direct involvement in terminal adipocyte
development.";
EMBO J. 10:3787-3793(1991).
[5]
FUNCTION, ALTERNATIVE TRANSLATIONAL INITIATION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND DNA-BINDING.
PubMed=8415748; DOI=10.1073/pnas.90.20.9606;
Lin F.T., MacDougald O.A., Diehl A.M., Lane M.D.;
"A 30-kDa alternative translation product of the CCAAT/enhancer
binding protein alpha message: transcriptional activator lacking
antimitotic activity.";
Proc. Natl. Acad. Sci. U.S.A. 90:9606-9610(1993).
[6]
FUNCTION.
PubMed=8090719; DOI=10.1073/pnas.91.19.8757;
Lin F.T., Lane M.D.;
"CCAAT/enhancer binding protein alpha is sufficient to initiate the
3T3-L1 adipocyte differentiation program.";
Proc. Natl. Acad. Sci. U.S.A. 91:8757-8761(1994).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8798745; DOI=10.1074/jbc.271.40.24753;
Flodby P., Barlow C., Kylefjord H., Ahrlund-Richter L.,
Xanthopoulos K.G.;
"Increased hepatic cell proliferation and lung abnormalities in mice
deficient in CCAAT/enhancer binding protein alpha.";
J. Biol. Chem. 271:24753-24760(1996).
[8]
FUNCTION, MUTAGENESIS OF TYR-286; VAL-288; GLU-291; ILE-295 AND
ARG-298, AND DNA-BINDING.
PubMed=11672531; DOI=10.1016/S0092-8674(01)00516-5;
Porse B.T., Pedersen T.A., Xu X., Lindberg B., Wewer U.M.,
Friis-Hansen L., Nerlov C.;
"E2F repression by C/EBPalpha is required for adipogenesis and
granulopoiesis in vivo.";
Cell 107:247-258(2001).
[9]
FUNCTION, MUTAGENESIS OF 182-PRO--PRO-188 AND SER-193, INTERACTION
WITH CDK2; CDK4 AND SMARCA2, AND PHOSPHORYLATION AT SER-193.
PubMed=15107404; DOI=10.1101/gad.1183304;
Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
"Liver tumors escape negative control of proliferation via PI3K/Akt-
mediated block of C/EBP alpha growth inhibitory activity.";
Genes Dev. 18:912-925(2004).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15589173; DOI=10.1016/j.immuni.2004.11.006;
Zhang P., Iwasaki-Arai J., Iwasaki H., Fenyus M.L., Dayaram T.,
Owens B.M., Shigematsu H., Levantini E., Huettner C.S.,
Lekstrom-Himes J.A., Akashi K., Tenen D.G.;
"Enhancement of hematopoietic stem cell repopulating capacity and
self-renewal in the absence of the transcription factor C/EBP alpha.";
Immunity 21:853-863(2004).
[11]
FUNCTION.
PubMed=14660596; DOI=10.1074/jbc.M312709200;
Muller C., Calkhoven C.F., Sha X., Leutz A.;
"The CCAAT enhancer-binding protein alpha (C/EBPalpha) requires a
SWI/SNF complex for proliferation arrest.";
J. Biol. Chem. 279:7353-7358(2004).
[12]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=15509779; DOI=10.1128/MCB.24.22.9744-9751.2004;
Begay V., Smink J., Leutz A.;
"Essential requirement of CCAAT/enhancer binding proteins in
embryogenesis.";
Mol. Cell. Biol. 24:9744-9751(2004).
[13]
FUNCTION, AND INTERACTION WITH FOXO1.
PubMed=17090532; DOI=10.1074/jbc.M607215200;
Qiao L., Shao J.;
"SIRT1 regulates adiponectin gene expression through Foxo1-C/enhancer-
binding protein alpha transcriptional complex.";
J. Biol. Chem. 281:39915-39924(2006).
[14]
FUNCTION, INTERACTION WITH SREBF1, MUTAGENESIS OF 222-THR--SER-230,
AND PHOSPHORYLATION AT THR-222; THR-226 AND SER-230.
PubMed=17290224; DOI=10.1038/sj.emboj.7601563;
Pedersen T.A., Bereshchenko O., Garcia-Silva S., Ermakova O., Kurz E.,
Mandrup S., Porse B.T., Nerlov C.;
"Distinct C/EBPalpha motifs regulate lipogenic and gluconeogenic gene
expression in vivo.";
EMBO J. 26:1081-1093(2007).
[15]
FUNCTION, AND INTERACTION WITH FOXO1.
PubMed=17627282; DOI=10.1038/sj.emboj.7601784;
Sekine K., Chen Y.R., Kojima N., Ogata K., Fukamizu A., Miyajima A.;
"Foxo1 links insulin signaling to C/EBPalpha and regulates
gluconeogenesis during liver development.";
EMBO J. 26:3607-3615(2007).
[16]
INTERACTION WITH PRDM16.
PubMed=19641492; DOI=10.1038/nature08262;
Kajimura S., Seale P., Kubota K., Lunsford E., Frangioni J.V.,
Gygi S.P., Spiegelman B.M.;
"Initiation of myoblast to brown fat switch by a PRDM16-C/EBP-beta
transcriptional complex.";
Nature 460:1154-1158(2009).
[17]
ALTERNATIVE INITIATION, AND IDENTIFICATION OF NON-CANONICAL INITIATION
CODON.
PubMed=20075868; DOI=10.1038/emboj.2009.404;
Muller C., Bremer A., Schreiber S., Eichwald S., Calkhoven C.F.;
"Nucleolar retention of a translational C/EBPalpha isoform stimulates
rDNA transcription and cell size.";
EMBO J. 29:897-909(2010).
[18]
INTERACTION WITH ZNF638.
PubMed=21602272; DOI=10.1074/jbc.M110.212506;
Meruvu S., Hugendubler L., Mueller E.;
"Regulation of adipocyte differentiation by the zinc finger protein
ZNF638.";
J. Biol. Chem. 286:26516-26523(2011).
[19]
FUNCTION.
PubMed=24367003; DOI=10.1084/jem.20130932;
Ohlsson E., Hasemann M.S., Willer A., Lauridsen F.K., Rapin N.,
Jendholm J., Porse B.T.;
"Initiation of MLL-rearranged AML is dependent on C/EBPalpha.";
J. Exp. Med. 211:5-13(2014).
-!- FUNCTION: Transcription factor that coordinates proliferation
arrest and the differentiation of myeloid progenitors, adipocytes,
hepatocytes, and cells of the lung and the placenta
(PubMed:8415748, PubMed:15107404, PubMed:15589173). Binds directly
to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an
activator on distinct target genes. During early embryogenesis,
plays essential and redundant functions with CEBPB
(PubMed:15509779). Essential for the transition from common
myeloid progenitors (CMP) to granulocyte/monocyte progenitors
(GMP) (PubMed:24367003). Critical for the proper development of
the liver and the lung (PubMed:8798745). Necessary for terminal
adipocyte differentiation, is required for postnatal maintenance
of systemic energy homeostasis and lipid storage (PubMed:1935900,
PubMed:8090719). To regulate these different processes at the
proper moment and tissue, interplays with other transcription
factors and modulators. Downregulates the expression of genes that
maintain cells in an undifferentiated and proliferative state
through E2F1 repression, which is critical for its ability to
induce adipocyte and granulocyte terminal differentiation.
Reciprocally E2F1 blocks adipocyte differentiation by binding to
specific promoters and repressing CEBPA binding to its target gene
promoters (PubMed:11672531). Proliferation arrest also depends on
a functional binding to SWI/SNF complex (PubMed:14660596). In
liver, regulates gluconeogenesis and lipogenesis through different
mechanisms. To regulate gluconeogenesis, functionally cooperates
with FOXO1 binding to IRE-controlled promoters and regulating the
expression of target genes such as PCK1 or G6PC (PubMed:17627282).
To modulate lipogenesis, interacts and transcriptionally
synergizes with SREBF1 in promoter activation of specific
lipogenic target genes such as ACAS2 (PubMed:17290224). In adipose
tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ
promoter through FOXO1 binding sites (PubMed:17090532).
{ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P49715,
ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:14660596,
ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:15509779,
ECO:0000269|PubMed:15589173, ECO:0000269|PubMed:17090532,
ECO:0000269|PubMed:17290224, ECO:0000269|PubMed:17627282,
ECO:0000269|PubMed:1935900, ECO:0000269|PubMed:24367003,
ECO:0000269|PubMed:8090719, ECO:0000269|PubMed:8415748,
ECO:0000269|PubMed:8798745}.
-!- FUNCTION: Isoform 3: Can act as dominant-negative. Binds DNA and
have transctivation activity, even if much less efficiently than
isoform 2. Does not inhibit cell proliferation.
{ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P49715,
ECO:0000269|PubMed:8415748}.
-!- FUNCTION: Isoform 4: Directly and specifically enhances ribosomal
DNA transcription interacting with RNA polymerase I-specific
cofactors and inducing histone acetylation.
{ECO:0000250|UniProtKB:P49715}.
-!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Can form
stable heterodimers with CEBPB, CEBPD, CEBPE and CEBPG (By
similarity). Interacts with PRDM16 (PubMed:19641492). Interacts
with UBN1 (By similarity). Interacts with ZNF638; this interaction
increases transcriptional activation (PubMed:21602272). Interacts
with the complex TFDP2:E2F1; the interaction prevents CEBPA
binding to target gene promoters and represses its transcriptional
activity (By similarity). Interacts with RB1 (PubMed:15107404).
Interacts (when phosphorylated at SER-193) with CDK2, CDK4, E2F4
and SMARCA2 (PubMed:15107404). Interacts with SREBPF1
(PubMed:17290224). Interacts with FOXO1 (via the Fork-head
domain); the interaction increases when FOXO1 is deacetylated
(PubMed:17090532, PubMed:17627282). Isoform 1 and isoform 4
interact with TAF1A and UBTF. Isoform 4 interacts with NPM1 (By
similarity). Interacts (via recognition sequence) with TRIB1 (By
similarity). {ECO:0000250|UniProtKB:P05554,
ECO:0000250|UniProtKB:P49715, ECO:0000269|PubMed:15107404,
ECO:0000269|PubMed:17090532, ECO:0000269|PubMed:17290224,
ECO:0000269|PubMed:17627282, ECO:0000269|PubMed:19641492,
ECO:0000269|PubMed:21602272}.
-!- INTERACTION:
Q9R1E0:Foxo1; NbExp=5; IntAct=EBI-2644207, EBI-1371343;
Q6ZQ88:Kdm1a; NbExp=4; IntAct=EBI-2644207, EBI-1216284;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8415748}.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus, nucleolus
{ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P49715}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=4;
Name=1;
IsoId=P53566-1; Sequence=Displayed;
Name=2; Synonyms=C/EBPalpha-p42 {ECO:0000303|PubMed:8415748};
IsoId=P53566-3; Sequence=VSP_057550;
Name=3; Synonyms=C/EBPalpha-p30 {ECO:0000303|PubMed:8415748};
IsoId=P53566-4; Sequence=VSP_057549;
Name=4; Synonyms=extended-C/EBPalpha
{ECO:0000303|PubMed:20075868};
IsoId=P53566-5; Sequence=VSP_057608;
-!- TISSUE SPECIFICITY: Isoform 2 and isoform 3 are expressed in
adipose tissue and liver (at protein level).
{ECO:0000269|PubMed:8415748}.
-!- DEVELOPMENTAL STAGE: At E9.5, expressed in the chorionic plate.
From E10.5 to at least E11.5, is also expressed in the
trophoblasts of the labyrinthine layer.
{ECO:0000269|PubMed:15509779}.
-!- DOMAIN: The recognition sequence (54-72) is required for
interaction with TRIB1. {ECO:0000250|UniProtKB:P49715}.
-!- PTM: Sumoylated, sumoylation blocks the inhibitory effect on cell
proliferation by disrupting the interaction with SMARCA2.
{ECO:0000250|UniProtKB:P05554}.
-!- PTM: Phosphorylation at Ser-193 is required for interaction with
CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibiton.
Dephosphorylated at Ser-193 by protein phosphatase 2A (PP2A)
through PI3K/AKT signaling pathway regulation (PubMed:15107404).
Phosphorylation at Thr-222 and Thr-226 by GSK3 is constitutive in
adipose tissue and lung. In liver, both Thr-222 and Thr-226 are
phosphorylated only during feeding but not during fasting
(PubMed:17290224). Phosphorylation of the GSK3 consensus sites
selectively decreases transactivation activity on IRE-controlled
promoters (PubMed:17290224). {ECO:0000269|PubMed:15107404,
ECO:0000269|PubMed:17290224}.
-!- PTM: Ubiquitinated by RFWD2/COP1 upon interaction with TRIB1.
{ECO:0000250|UniProtKB:P49715}.
-!- DISRUPTION PHENOTYPE: Mutants die of hypoglycemia at 7-10h after
bith. They have defects in the control of hepatic growth and lung
development. The liver architecture is disturbed with acinar
formation. They show hyperproliferation of type II pneumocytes and
disturbed alveolar architecture. At the molecular level,
accumulation of glycogen and lipids in the liver and adipose
tissues is impaired, and the mutant animals are severely
hypoglycemic (PubMed:8798745). In very few cases (less than 1%)
mutants are able to survive up to 4 weeks but they are sevrely
retarded in development. At 2 weeks, they are about half the size
of their littermates, very thin and with skin problems.
Conditional knockout in adults leads to a lack of granulopoiesis
in all hematopoietic organs with no mature peripheral blood
granulocytes and the presence of >30% immature myeloid cells in
the bone marrow, but without anemia or thrombocytopenia. Animals
rarely survive 4 to 5 weeks of age due to sepsis as a result of
granulocytopenia (PubMed:15589173). Double knockout CEBPA and
CEBPB results in embryonic developmental arrest and death at
around E10 to E11, associated with a gross placenta failure
(PubMed:15509779). {ECO:0000269|PubMed:15509779,
ECO:0000269|PubMed:15589173, ECO:0000269|PubMed:8798745}.
-!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily.
{ECO:0000305}.
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EMBL; M62362; AAA37374.1; -; Genomic_DNA.
EMBL; AC150683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011118; AAH11118.1; -; mRNA.
EMBL; BC028890; AAH28890.1; -; mRNA.
EMBL; BC051102; AAH51102.1; -; mRNA.
EMBL; BC058161; AAH58161.1; -; mRNA.
CCDS; CCDS21145.1; -. [P53566-1]
PIR; I49575; I49575.
RefSeq; NP_001274443.1; NM_001287514.1. [P53566-5]
RefSeq; NP_001274444.1; NM_001287515.1. [P53566-3]
RefSeq; NP_001274450.1; NM_001287521.1. [P53566-4]
RefSeq; NP_031704.2; NM_007678.3. [P53566-1]
UniGene; Mm.349667; -.
ProteinModelPortal; P53566; -.
SMR; P53566; -.
BioGrid; 198667; 120.
CORUM; P53566; -.
DIP; DIP-44054N; -.
IntAct; P53566; 11.
MINT; MINT-1529126; -.
STRING; 10090.ENSMUSP00000096129; -.
ChEMBL; CHEMBL3616358; -.
iPTMnet; P53566; -.
PhosphoSitePlus; P53566; -.
MaxQB; P53566; -.
PaxDb; P53566; -.
PRIDE; P53566; -.
Ensembl; ENSMUST00000042985; ENSMUSP00000096129; ENSMUSG00000034957. [P53566-1]
GeneID; 12606; -.
KEGG; mmu:12606; -.
UCSC; uc009gjl.2; mouse. [P53566-1]
CTD; 1050; -.
MGI; MGI:99480; Cebpa.
eggNOG; KOG3119; Eukaryota.
eggNOG; ENOG410YJ8G; LUCA.
GeneTree; ENSGT00530000063192; -.
HOGENOM; HOG000013112; -.
HOVERGEN; HBG050879; -.
InParanoid; P53566; -.
KO; K09055; -.
OMA; QIAHCAQ; -.
OrthoDB; EOG091G11FC; -.
PhylomeDB; P53566; -.
TreeFam; TF105008; -.
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
PRO; PR:P53566; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000034957; -.
CleanEx; MM_CEBPA; -.
ExpressionAtlas; P53566; baseline and differential.
Genevisible; P53566; MM.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0001013; F:RNA polymerase I regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:MGI.
GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
GO; GO:0048469; P:cell maturation; IMP:MGI.
GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0001892; P:embryonic placenta development; IGI:MGI.
GO; GO:0045444; P:fat cell differentiation; IDA:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0030851; P:granulocyte differentiation; IDA:UniProtKB.
GO; GO:0048839; P:inner ear development; IDA:MGI.
GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
GO; GO:0001889; P:liver development; IMP:UniProtKB.
GO; GO:0030324; P:lung development; IMP:UniProtKB.
GO; GO:0030225; P:macrophage differentiation; IMP:MGI.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; ISO:MGI.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0006360; P:transcription from RNA polymerase I promoter; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; ISO:MGI.
GO; GO:0000050; P:urea cycle; IDA:MGI.
GO; GO:0050872; P:white fat cell differentiation; IMP:MGI.
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;
Developmental protein; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 359 CCAAT/enhancer-binding protein alpha.
/FTId=PRO_0000076614.
DOMAIN 283 346 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
DNA_BIND 286 301 {ECO:0000250|UniProtKB:P05554}.
REGION 1 70 Required to repress E2F1:TFDP1-mediated
transcription, to inhibit cell cycle and
to induce adipocyte differentiation.
{ECO:0000250|UniProtKB:P05554}.
REGION 54 72 Required for interaction with TRIB1.
{ECO:0000250|UniProtKB:P49715}.
REGION 126 200 Required to induce adipocyte
differentiation.
{ECO:0000250|UniProtKB:P05554}.
REGION 180 194 Required to functionally cooperate with
SREBF1 in promoter activation.
{ECO:0000269|PubMed:17290224}.
REGION 240 359 Interaction with FOXO1.
{ECO:0000269|PubMed:17627282}.
REGION 287 314 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 318 346 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 99 102 Poly-Gly.
COMPBIAS 181 190 Poly-Pro.
COMPBIAS 262 271 Poly-Gly.
MOD_RES 159 159 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P49715}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000269|PubMed:15107404}.
MOD_RES 222 222 Phosphothreonine; by GSK3.
{ECO:0000269|PubMed:17290224}.
MOD_RES 226 226 Phosphothreonine; by GSK3.
{ECO:0000269|PubMed:17290224}.
MOD_RES 230 230 Phosphoserine; by GSK3.
{ECO:0000305|PubMed:17290224}.
CROSSLNK 159 159 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:P05554}.
CROSSLNK 159 159 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P49715}.
VAR_SEQ 1 117 Missing (in isoform 3).
{ECO:0000269|PubMed:8415748}.
/FTId=VSP_057549.
VAR_SEQ 1 14 Missing (in isoform 2).
{ECO:0000269|PubMed:8415748}.
/FTId=VSP_057550.
VAR_SEQ 1 1 M -> MRGREPVGALGGRRRQRRHAQAGGRRGSPCRENSNS
PM (in isoform 4).
/FTId=VSP_057608.
MUTAGEN 182 188 PPPPPPP->APPPAPA: No effect on DNA-
binding or interaction with CDK2 and
CDK4. No effect on cell cycle inhibition.
{ECO:0000269|PubMed:15107404}.
MUTAGEN 184 186 PPP->AAA: No effect on DNA-binding or
interaction with CDK2 and CDK4. No effect
on cell cycle inhibition.
{ECO:0000269|PubMed:15107404}.
MUTAGEN 193 193 S->A: No effect on DNA-binding. Loss of
interaction with CDK2 and CDK4 as well as
cell cycle inhibition.
{ECO:0000269|PubMed:15107404}.
MUTAGEN 222 230 TPPPTPVPS->APPPAPVPA: Decreases
phosphorylated form. Deregulation of
hepatic glucose metabolism.
{ECO:0000269|PubMed:17290224}.
MUTAGEN 286 286 Y->A: No effect on DNA-binding, represses
E2F1:TFDP1-mediated transcription and
causes adipose hypoplasia and myeloid
dysplasia. {ECO:0000269|PubMed:11672531}.
MUTAGEN 288 288 V->A: No effect on DNA-binding, no effect
on repression of E2F1:TFDP1-mediated
transcription and no effect on
adipogenesis and granulopoiesis; when
associated with A-291.
{ECO:0000269|PubMed:11672531}.
MUTAGEN 291 291 E->A: No effect on DNA-binding, no effect
on repression of E2F1:TFDP1-mediated
transcription and no effect on
adipogenesis and granulopoiesis; when
associated with A-288.
{ECO:0000269|PubMed:11672531}.
MUTAGEN 295 295 I->A: No effect on DNA-binding, represses
E2F1:TFDP1-mediated transcription and
causes adipose hypoplasia and myeloid
dysplasia; when associated with A-298.
{ECO:0000269|PubMed:11672531}.
MUTAGEN 298 298 R->A: No effect on DNA-binding, represses
E2F1:TFDP1-mediated transcription and
causes adipose hypoplasia and myeloid
dysplasia; when associated with A-295.
{ECO:0000269|PubMed:11672531}.
CONFLICT 30 54 AFGFPRGAGPAPPPAPPAAPEPLGG -> RLWLSPGRGPRA
APSPTCRPGAAGR (in Ref. 1; AAA37374).
{ECO:0000305}.
CONFLICT 356 359 GNCA -> ATAREARGCGTALGRPPGWRPRGWFRVAGSLGC
PGRASQD (in Ref. 1; AAA37374).
{ECO:0000305}.
SEQUENCE 359 AA; 37430 MW; 1E6CC09A330BEFEF CRC64;
MESADFYEVE PRPPMSSHLQ SPPHAPSNAA FGFPRGAGPA PPPAPPAAPE PLGGICEHET
SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAAGPAGG GGDFDYPGAP AGPGGAVMSA
GAHGPPPGYG CAAAGYLDGR LEPLYERVGA PALRPLVIKQ EPREEDEAKQ LALAGLFPYQ
PPPPPPPPHP HASPAHLAAP HLQFQIAHCG QTTMHLQPGH PTPPPTPVPS PHAAPALGAA
GLPGPGSALK GLAGAHPDLR TGGGGGGSGA GAGKAKKSVD KNSNEYRVRR ERNNIAVRKS
RDKAKQRNVE TQQKVLELTS DNDRLRKRVE QLSRELDTLR GIFRQLPESS LVKAMGNCA


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