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

 CEBPA_HUMAN             Reviewed;         358 AA.
P49715; A7LNP2; P78319; Q05CA4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 3.
25-OCT-2017, entry version 170.
RecName: Full=CCAAT/enhancer-binding protein alpha {ECO:0000312|HGNC:HGNC:1833};
Short=C/EBP alpha {ECO:0000312|HGNC:HGNC:1833};
Name=CEBPA {ECO:0000312|HGNC:HGNC:1833};
Synonyms=CEBP {ECO:0000312|HGNC:HGNC:1833};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Umbilical cord;
PubMed=7575576; DOI=10.1006/bbrc.1995.2439;
Antonson P., Xanthopoulos K.G.;
"Molecular cloning, sequence, and expression patterns of the human
gene encoding CCAAT/enhancer binding protein alpha (C/EBP alpha).";
Biochem. Biophys. Res. Commun. 215:106-113(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Swart G.W.M., van Groningen J.J.M., van Ruissen F., Bergers M.,
Schalwijk J.;
"Transcription factor C/EBP-alpha: novel sites of expression and
cloning of the human gene.";
Biol. Chem. Hoppe-Seyler 378:373-379(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-133.
TISSUE=Pancreas;
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).
[6]
INTERACTION WITH HBV PROTEIN X.
PubMed=9915821; DOI=10.1074/jbc.274.5.2858;
Choi B.H., Park G.T., Rho H.M.;
"Interaction of hepatitis B viral X protein and CCAAT/enhancer-binding
protein alpha synergistically activates the hepatitis B viral enhancer
II/pregenomic promoter.";
J. Biol. Chem. 274:2858-2865(1999).
[7]
INTERACTION WITH UBN1.
PubMed=10725330; DOI=10.1083/jcb.148.6.1165;
Aho S., Buisson M., Pajunen T., Ryoo Y.W., Giot J.-F., Gruffat H.,
Sergeant A., Uitto J.;
"Ubinuclein, a novel nuclear protein interacting with cellular and
viral transcription factors.";
J. Cell Biol. 148:1165-1176(2000).
[8]
INVOLVEMENT IN AML.
PubMed=12661007; DOI=10.1002/gcc.10185;
Snaddon J., Smith M.L., Neat M., Cambal-Parrales M., Dixon-McIver A.,
Arch R., Amess J.A., Rohatiner A.Z., Lister T.A., Fitzgibbon J.;
"Mutations of CEBPA in acute myeloid leukemia FAB types M1 and M2.";
Genes Chromosomes Cancer 37:72-78(2003).
[9]
INTERACTION WITH CDK2; CDK4; E2F4; RB1 AND SMARCA2, AND
PHOSPHORYLATION AT SER-190.
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 (ISOFORMS 1 AND 3).
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).
[11]
INVOLVEMENT IN AML.
PubMed=15575056; DOI=10.1056/NEJMoa041331;
Smith M.L., Cavenagh J.D., Lister T.A., Fitzgibbon J.;
"Mutation of CEBPA in familial acute myeloid leukemia.";
N. Engl. J. Med. 351:2403-2407(2004).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-161, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
INTERACTION WITH TRIB1.
PubMed=20410507; DOI=10.1182/blood-2009-07-229450;
Dedhia P.H., Keeshan K., Uljon S., Xu L., Vega M.E., Shestova O.,
Zaks-Zilberman M., Romany C., Blacklow S.C., Pear W.S.;
"Differential ability of Tribbles family members to promote
degradation of C/EBPalpha and induce acute myelogenous leukemia.";
Blood 116:1321-1328(2010).
[14]
FUNCTION (ISOFORM 4), ALTERNATIVE INITIATION, IDENTIFICATION OF
NON-CANONICAL INITIATION CODON, SUBCELLULAR LOCATION (ISOFORM 4), AND
INTERACTION WITH NPM1; TAF1A AND UBTF.
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).
[15]
INTERACTION WITH TFDP1; TFDP2 AND E2F1.
PubMed=20176812; DOI=10.1128/MCB.01619-09;
Zaragoza K., Begay V., Schuetz A., Heinemann U., Leutz A.;
"Repression of transcriptional activity of C/EBPalpha by E2F-
dimerization partner complexes.";
Mol. Cell. Biol. 30:2293-2304(2010).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-161, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[17]
INTERACTION WITH TRIB1, DOMAIN, AND MUTAGENESIS OF ILE-55; GLU-57;
HIS-58; GLU-59; SER-61; ILE-62; ASP-63; ILE-64; SER-65; TYR-67; ILE-68
AND ASP-69.
PubMed=26455797; DOI=10.1016/j.str.2015.08.017;
Murphy J.M., Nakatani Y., Jamieson S.A., Dai W., Lucet I.S.,
Mace P.D.;
"Molecular mechanism of CCAAT-enhancer binding protein recruitment by
the TRIB1 pseudokinase.";
Structure 23:2111-2121(2015).
[18]
UBIQUITINATION.
PubMed=27041596; DOI=10.1016/j.str.2016.03.002;
Uljon S., Xu X., Durzynska I., Stein S., Adelmant G., Marto J.A.,
Pear W.S., Blacklow S.C.;
"Structural basis for substrate selectivity of the E3 ligase COP1.";
Structure 24:687-696(2016).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-161, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[20]
VARIANTS AML LEU-84 AND LYS-312 INS, CHARACTERIZATION OF VARIANTS AML
LEU-84 AND LYS-312 INS, INVOLVEMENT IN AML, FUNCTION, SUBCELLULAR
LOCATION, ALTERNATIVE TRANSLATIONAL INITIATION, AND DNA-BINDING.
PubMed=11242107; DOI=10.1038/85820;
Pabst T., Mueller B.U., Zhang P., Radomska H.S., Narravula S.,
Schnittger S., Behre G., Hiddemann W., Tenen D.G.;
"Dominant-negative mutations of CEBPA, encoding CCAAT/enhancer binding
protein-alpha (C/EBPalpha), in acute myeloid leukemia.";
Nat. Genet. 27:263-270(2001).
-!- FUNCTION: Transcription factor that coordinates proliferation
arrest and the differentiation of myeloid progenitors, adipocytes,
hepatocytes, and cells of the lung and the placenta. Binds
directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3'
acting as an activator on distinct target genes (PubMed:11242107).
During early embryogenesis, plays essential and redundant
functions with CEBPB. Essential for the transition from common
myeloid progenitors (CMP) to granulocyte/monocyte progenitors
(GMP). Critical for the proper development of the liver and the
lung (By similarity). Necessary for terminal adipocyte
differentiation, is required for postnatal maintenance of systemic
energy homeostasis and lipid storage (By similarity). 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.
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. To modulate lipogenesis,
interacts and transcriptionally synergizes with SREBF1 in promoter
activation of specific lipogenic target genes such as ACAS2. In
adipose tissue, seems to act as FOXO1 coactivator accessing to
ADIPOQ promoter through FOXO1 binding sites (By similarity).
{ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P53566,
ECO:0000269|PubMed:11242107, ECO:0000269|PubMed:14660596}.
-!- 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 (PubMed:14660596).
{ECO:0000250|UniProtKB:P05554, ECO:0000250|UniProtKB:P53566,
ECO:0000269|PubMed:14660596}.
-!- FUNCTION: Isoform 4: Directly and specifically enhances ribosomal
DNA transcription interacting with RNA polymerase I-specific
cofactors and inducing histone acetylation.
{ECO:0000269|PubMed:20075868}.
-!- 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 (By similarity). Interacts with
UBN1 (PubMed:10725330). Interacts with ZNF638; this interaction
increases transcriptional activation (By similarity). Interacts
with the complex TFDP2:E2F1; the interaction prevents CEBPA
binding to target gene promoters and represses its transcriptional
activity (PubMed:20176812). Interacts with RB1 (PubMed:15107404).
Interacts (when phosphorylated at SER-190) with CDK2, CDK4, E2F4
and SMARCA2 (PubMed:15107404). Interacts with SREBPF1 (By
similarity). Interacts with FOXO1 (via the Fork-head domain); the
interaction increases when FOXO1 is deacetylated (By similarity).
Isoform 1 and isoform 4 interacts with TAF1A and UBTF
(PubMed:20075868). Isoform 4 interacts with NPM1
(PubMed:20075868). Interacts with HBV protein X (PubMed:9915821).
Interacts (via recognition sequence) with TRIB1 (PubMed:20410507,
PubMed:26455797). {ECO:0000250|UniProtKB:P05554,
ECO:0000250|UniProtKB:P53566, ECO:0000269|PubMed:10725330,
ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:20075868,
ECO:0000269|PubMed:20176812, ECO:0000269|PubMed:20410507,
ECO:0000269|PubMed:26455797, ECO:0000269|PubMed:9915821}.
-!- INTERACTION:
P18848:ATF4; NbExp=2; IntAct=EBI-1172054, EBI-492498;
P47902:CDX1; NbExp=3; IntAct=EBI-1172054, EBI-8514176;
P17676:CEBPB; NbExp=2; IntAct=EBI-1172054, EBI-969696;
P49716:CEBPD; NbExp=2; IntAct=EBI-1172054, EBI-7962058;
P53567:CEBPG; NbExp=2; IntAct=EBI-1172054, EBI-740209;
P35638:DDIT3; NbExp=2; IntAct=EBI-1172054, EBI-742651;
P03122:E2 (xeno); NbExp=2; IntAct=EBI-1172054, EBI-7028618;
P06422:E2 (xeno); NbExp=4; IntAct=EBI-1172054, EBI-7136851;
P24001-2:IL32; NbExp=7; IntAct=EBI-1172054, EBI-8800907;
P09874:PARP1; NbExp=2; IntAct=EBI-1172054, EBI-355676;
Q96RU8-1:TRIB1; NbExp=2; IntAct=EBI-16180754, EBI-16180744;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11242107}.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus, nucleolus
{ECO:0000269|PubMed:20075868}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=4;
Name=1;
IsoId=P49715-1; Sequence=Displayed;
Name=2; Synonyms=C/EBPalpha-p42 {ECO:0000303|PubMed:11242107};
IsoId=P49715-2; Sequence=VSP_057548;
Name=3; Synonyms=C/EBPalpha-p30 {ECO:0000303|PubMed:11242107};
IsoId=P49715-3; Sequence=VSP_057547;
Name=4; Synonyms=extended-C/EBPalpha
{ECO:0000303|PubMed:20075868};
IsoId=P49715-4; Sequence=VSP_057607;
-!- DOMAIN: The recognition sequence (54-72) is required for
interaction with TRIB1. {ECO:0000269|PubMed:26455797}.
-!- PTM: Phosphorylation at Ser-190 is required for interaction with
CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibiton.
Dephosphorylated at Ser-190 by protein phosphatase 2A (PP2A)
through PI3K/AKT signaling pathway regulation (PubMed:15107404).
Phosphorylation at Thr-226 and Thr-230 by GSK3 is constitutive in
adipose tissue and lung. In liver, both Thr-226 and Thr-230 are
phosphorylated only during feeding but not during fasting.
Phosphorylation of the GSK3 consensus sites selectively decreases
transactivation activity on IRE-controlled promoters.
{ECO:0000250|UniProtKB:P53566}.
-!- PTM: Sumoylated, sumoylation blocks the inhibitory effect on cell
proliferation by disrupting the interaction with SMARCA2.
{ECO:0000250|UniProtKB:P05554}.
-!- PTM: Ubiquitinated by RFWD2/COP1 upon interaction with TRIB1.
{ECO:0000303|PubMed:27041596}.
-!- DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype
of acute leukemia, a cancer of the white blood cells. AML is a
malignant disease of bone marrow characterized by maturational
arrest of hematopoietic precursors at an early stage of
development. Clonal expansion of myeloid blasts occurs in bone
marrow, blood, and other tissue. Myelogenous leukemias develop
from changes in cells that normally produce neutrophils,
basophils, eosinophils and monocytes.
{ECO:0000269|PubMed:11242107, ECO:0000269|PubMed:12661007,
ECO:0000269|PubMed:15575056}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CEBPAID40050ch19q13.html";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/cebpa/";
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EMBL; U34070; AAC50235.1; -; Genomic_DNA.
EMBL; Y11525; CAA72289.1; -; mRNA.
EMBL; EU048234; ABS82765.1; -; Genomic_DNA.
EMBL; AC008738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC027902; AAH27902.1; -; mRNA.
CCDS; CCDS54243.1; -. [P49715-1]
PIR; JC4311; JC4311.
RefSeq; NP_001272758.1; NM_001285829.1. [P49715-3]
RefSeq; NP_001274353.1; NM_001287424.1. [P49715-4]
RefSeq; NP_001274364.1; NM_001287435.1. [P49715-2]
RefSeq; NP_004355.2; NM_004364.4. [P49715-1]
UniGene; Hs.76171; -.
ProteinModelPortal; P49715; -.
SMR; P49715; -.
BioGrid; 107479; 95.
CORUM; P49715; -.
DIP; DIP-37882N; -.
ELM; P49715; -.
IntAct; P49715; 23.
MINT; MINT-264048; -.
STRING; 9606.ENSP00000427514; -.
iPTMnet; P49715; -.
PhosphoSitePlus; P49715; -.
DMDM; 166898082; -.
EPD; P49715; -.
MaxQB; P49715; -.
PaxDb; P49715; -.
PeptideAtlas; P49715; -.
PRIDE; P49715; -.
DNASU; 1050; -.
Ensembl; ENST00000498907; ENSP00000427514; ENSG00000245848. [P49715-1]
GeneID; 1050; -.
KEGG; hsa:1050; -.
UCSC; uc002nun.4; human. [P49715-1]
CTD; 1050; -.
DisGeNET; 1050; -.
EuPathDB; HostDB:ENSG00000245848.2; -.
GeneCards; CEBPA; -.
GeneReviews; CEBPA; -.
H-InvDB; HIX0040095; -.
HGNC; HGNC:1833; CEBPA.
HPA; HPA052734; -.
HPA; HPA065037; -.
HPA; HPA067937; -.
MalaCards; CEBPA; -.
MIM; 116897; gene.
MIM; 601626; phenotype.
neXtProt; NX_P49715; -.
OpenTargets; ENSG00000245848; -.
Orphanet; 102724; 'Acute myeloid leukemia with t(8;21)(q22;q22) translocation'.
Orphanet; 319480; Acute myeloid leukemia with CEBPA somatic mutations.
Orphanet; 319465; Inherited acute myeloid leukemia.
PharmGKB; PA26376; -.
eggNOG; KOG3119; Eukaryota.
eggNOG; ENOG410YJ8G; LUCA.
GeneTree; ENSGT00530000063192; -.
HOGENOM; HOG000013112; -.
HOVERGEN; HBG050879; -.
InParanoid; P49715; -.
KO; K09055; -.
OMA; QIAHCAQ; -.
OrthoDB; EOG091G11FC; -.
PhylomeDB; P49715; -.
TreeFam; TF105008; -.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
SignaLink; P49715; -.
SIGNOR; P49715; -.
ChiTaRS; CEBPA; human.
GeneWiki; CEBPA; -.
GenomeRNAi; 1050; -.
PRO; PR:P49715; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000245848; -.
CleanEx; HS_CEBPA; -.
Genevisible; P49715; HS.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IMP:BHF-UCL.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0001013; F:RNA polymerase I regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; NAS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IMP:BHF-UCL.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0048469; P:cell maturation; IEA:Ensembl.
GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0030851; P:granulocyte differentiation; ISS:UniProtKB.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
GO; GO:0001889; P:liver development; ISS:UniProtKB.
GO; GO:0030324; P:lung development; ISS:UniProtKB.
GO; GO:0030225; P:macrophage differentiation; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
GO; GO:0030099; P:myeloid cell differentiation; NAS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ParkinsonsUK-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; TAS:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; IDA:UniProtKB.
GO; GO:0006360; P:transcription from RNA polymerase I promoter; IDA:UniProtKB.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0000050; P:urea cycle; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
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; Disease mutation; DNA-binding;
Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 358 CCAAT/enhancer-binding protein alpha.
/FTId=PRO_0000076613.
DOMAIN 282 345 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
DNA_BIND 285 300 {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:0000269|PubMed:26455797}.
REGION 128 204 Required to induce adipocyte
differentiation.
{ECO:0000250|UniProtKB:P05554}.
REGION 182 198 Required to functionally cooperate with
SREBF1 in promoter activation.
{ECO:0000250|UniProtKB:P53566}.
REGION 244 358 Interaction with FOXO1.
{ECO:0000250|UniProtKB:P53566}.
REGION 286 313 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 317 345 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 99 104 Poly-Gly.
COMPBIAS 183 189 Poly-Pro.
MOD_RES 161 161 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000269|PubMed:15107404}.
MOD_RES 226 226 Phosphothreonine; by GSK3.
{ECO:0000250|UniProtKB:P53566}.
MOD_RES 230 230 Phosphothreonine; by GSK3.
{ECO:0000250|UniProtKB:P53566}.
MOD_RES 234 234 Phosphoserine; by GSK3.
{ECO:0000250|UniProtKB:P53566}.
CROSSLNK 161 161 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 119 Missing (in isoform 3).
/FTId=VSP_057547.
VAR_SEQ 1 14 Missing (in isoform 2).
/FTId=VSP_057548.
VAR_SEQ 1 1 M -> MRGRGRAGSPGGRRRRPAQAGGRRGSPCRENSNSPM
(in isoform 4).
/FTId=VSP_057607.
VARIANT 84 84 H -> L (in AML; no effect on expression;
no effect on DNA-binding or
transactivation activity;
dbSNP:rs28931590).
{ECO:0000269|PubMed:11242107}.
/FTId=VAR_072677.
VARIANT 312 312 Q -> QK (in AML; nuclear; no effect on
expression; loss of DNA-binding and
transactivation activity).
{ECO:0000269|PubMed:11242107}.
/FTId=VAR_072678.
MUTAGEN 55 55 I->A: Decreased interaction with TRIB1.
{ECO:0000269|PubMed:26455797}.
MUTAGEN 57 57 E->T: No effect on interaction with
TRIB1. {ECO:0000269|PubMed:26455797}.
MUTAGEN 58 58 H->D: No effect on interaction with
TRIB1. {ECO:0000269|PubMed:26455797}.
MUTAGEN 59 59 E->A: Decreased interaction with TRIB1.
{ECO:0000269|PubMed:26455797}.
MUTAGEN 61 61 S->A: Decreased interaction with TRIB1.
{ECO:0000269|PubMed:26455797}.
MUTAGEN 62 62 I->A: Decreased interaction with TRIB1.
{ECO:0000269|PubMed:26455797}.
MUTAGEN 63 63 D->A: No effect on interaction with
TRIB1. {ECO:0000269|PubMed:26455797}.
MUTAGEN 64 64 I->A: Decreased interaction with TRIB1.
{ECO:0000269|PubMed:26455797}.
MUTAGEN 65 65 S->A: No effect on interaction with
TRIB1. {ECO:0000269|PubMed:26455797}.
MUTAGEN 67 67 Y->A: Decreased interaction with TRIB1.
{ECO:0000269|PubMed:26455797}.
MUTAGEN 67 67 Y->F: No effect on interaction with
TRIB1. {ECO:0000269|PubMed:26455797}.
MUTAGEN 68 68 I->A: Decreased interaction with TRIB1.
{ECO:0000269|PubMed:26455797}.
MUTAGEN 69 69 D->A: No effect on interaction with
TRIB1. {ECO:0000269|PubMed:26455797}.
CONFLICT 40 41 AQ -> PK (in Ref. 1; AAC50235).
{ECO:0000305}.
CONFLICT 95 98 VGPT -> WAH (in Ref. 2; CAA72289).
{ECO:0000305}.
CONFLICT 241 241 L -> V (in Ref. 2; CAA72289).
{ECO:0000305}.
CONFLICT 248 250 GPG -> ALA (in Ref. 2; CAA72289).
{ECO:0000305}.
CONFLICT 269 269 S -> T (in Ref. 1; AAC50235).
{ECO:0000305}.
SEQUENCE 358 AA; 37561 MW; 574C0A049E25BCAC CRC64;
MESADFYEAE PRPPMSSHLQ SPPHAPSSAA FGFPRGAGPA QPPAPPAAPE PLGGICEHET
SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAVGPTGG GGGGDFDYPG APAGPGGAVM
PGGAHGPPPG YGCAAAGYLD GRLEPLYERV GAPALRPLVI KQEPREEDEA KQLALAGLFP
YQPPPPPPPS HPHPHPPPAH LAAPHLQFQI AHCGQTTMHL QPGHPTPPPT PVPSPHPAPA
LGAAGLPGPG SALKGLGAAH PDLRASGGSG AGKAKKSVDK NSNEYRVRRE RNNIAVRKSR
DKAKQRNVET QQKVLELTSD NDRLRKRVEQ LSRELDTLRG IFRQLPESSL VKAMGNCA


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