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CEBPA (CCAAT enhancer binding protein alpha)

Identity

Other namesC/EBPa
HGNC (Hugo) CEBPA
LocusID (NCBI) 1050
Location 19q13.11
Location_base_pair Starts at 33790840 and ends at 33793470 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

Description CEBPA is a single exon gene located on the minus strand of chromosome 19q.
Transcription The mRNA produced consists of a short 5'UTR containing a small 5'ORF, the coding region and a large 3'UTR.

Protein

 
  C/EBPa protein domains
The basic region leucine zipper domain mediates DNA binding, homodimerization of C/EBPa and heterodimerization with other members of the C/EBP family. This region is also involved in mediating protein-protein interactions with other transcription factors involved in lineage determination and growth proliferation. N-terminal region transactivating domains mediate interactions with transcriptional machinery and proteins important in cell cycle control.
The CEBPA mRNA gives rise to two different translational isoforms by using different start codons within the same open reading frame by means of leaky ribosome scanning; the full length 42kDa protein and a 30kDa truncated form. These isoforms display contrasting functions in regards to gene activation and cell proliferation. Both isoforms can be detected within the cell and it is likely that the ratio of isoforms is important in mediating proliferation and differentiation control.
Expression C/EBPa is expressed in many cell types and plays crucial roles in hepatocyte and adipocyte development, with highest concentrations in terminally differentiated cells. In hematopoiesis, C/EBPa is expressed in myeloid cells and drives granulocytic differentiation. C/EBPa is also found expressed in intestine, lung, adrenal gland, breast, ovary and placenta tissues.
Localisation C/EBPa localises to the nucleus
Function C/EBPa and its isoforms play important roles in lineage determination and gene activation in a variety of cell types by activating transcription from lineage-specific promoters. In hematopoiesis, C/EBPa is a key factor in driving the development of myeloid cells interacting with a variety of factors, including c-Myc, PU.1, and microRNAs. The truncated form of C/EBPa has been seen to act in a dominant negative regulatory manner in mice, abolishing normal C/EBPa function and causing a block in differentiation. In humans, the truncated protein selectively inhibits C/EBPa DNA binding but due to variable DNA affinity has a greater range of effects on differentiation.
Several pathways have been implicated as the means by which C/EBPa mediates cell cycle arrest and proliferation, including p21, cyclin-dependent kinases and the E2F complex via c-Myc. The 30kDa isoform of C/EBPa lacks the domains required to mediate cell growth.
Homology C/EBPa belongs to the family of C/EBP proteins and is conserved across a variety of vertebrate species

Mutations

Note Mutations in CEBPA occur in approximately 10% of all acute myeloid leukemias (AMLs)
 
  N-terminal mutations abolish expression of full length 42kDa protein, upregulating production of the 30kDa isoform.
C-terminal mutations result in C/EBPa proteins with decreased DNA binding or dimerization activity.
Germinal Germline mutations in CEBPA have been described in 2 familial cases of AML. The first family contained a heterozygous germline mutation of del (C) at nucleotide 212 which causes the premature termination of the protein at codon 158. The 30kDa isoform is produced. Somatic mutation causing in frame duplication was also found in the C-terminal region of one patient on the other allele, which was not present in remission samples. The second family contained a heterozygous germline mutation of ins (C) at nucleotide 217 which causes the premature termination of the protein. The 30kDa isoform is produced. Somatic mutations in the C-terminal region were found in two of the affected family members.
Somatic Mutations in CEBPA tend to cluster to two regions.
The first group affect the N-terminal region of C/EBPa. These mutations are often insertions or deletions which cause frameshifts which cause premature truncation of the protein. In this case, translation is reinitiated at an internal ATG and the 30kDa protein, which lacks the first transactivating domain, is produced.
Secondly, in-frame or missense mutations occur within the C-terminal region of C/EBPa, disrupting the basic zipper region and thus affecting DNA binding, protein interactions as well as homo and heterodimerization with other C/EBP family members.
Multiple mutations in CEBPA are common and often biallelic, although the allelic frequency of the mutations can change over the course of the disease. Mutations are generally maintained between presentation and replapse and therefore may be useful for monitoring minimal residual disease.

Implicated in

Entity Acute myeloid leukemias
Disease Mutations in CEBPA have been implicated in acute myeloid leukaemia, most often in association with FAB types M1 and M2, although it has also been found in M4 and M5 types. Mutations in CEBPA occur in approximately 10% of all AMLs and are associated with normal karyotype AML.
Prognosis Mutations in CEBPA tend to confer favourable prognosis. Low levels of RNA expression of CEBPA have been noted in AML where it may reflect adverse prognosis.
Oncogenesis CEBPA expression is downregulated in the presence of fusion protein AML1-ETO via inhibition of the CEBPA promoter.
Translation of the C/EBPa protein is suppressed by the fusion gene AML1-MDS1-EVI1 via the activation of calreticulin.
Pericentric inversion of chromosome 16, inv(16)(p13q22), which fuses the CBFB and MYH11 genes, with the latter encoding the smooth muscle myosin heavy chain (SMMHC) suppresses translation of the C/EBPa protein via calreticulin.
BCR-ABL fusion is able to suppress CEBPA protein translation via inhibitory action of the poly(rC)-binding protein hnRNP E2.
The involvement of CEBPA mutations in familial cases of AML, along with evidence of mutations persisting between presentation and relapse indicate that mutations in CEBPA are an early event in leukaemogenesis.
  
Entity Although mutated CEBPA is primarily observed in AML, in rare cases it has been found to be mutated in myelodysplasic syndromes (MDS), lung tumours and prostate tumours. Down-regulation of CEBPA has also been observed in blast crisis chronic myeloid leukaemia, lung cancer, breast cancer and liver cancer.
  
Entity t(14;19)(q32;q13) --> IGH / CEBPA
Disease CEBPA is rarely involved in translocations with other genes. However, in B-cell precursor acute lymphoblastic leukemia (BCP-ALL) the 3'UTR of CEBPA has been found to be translocated to the immunoglobulin heavy chain locus
  

External links

Nomenclature
HGNC (Hugo)CEBPA   1833
Cards
AtlasCEBPAID40050ch19q13
Entrez_Gene (NCBI)CEBPA  1050  CCAAT/enhancer binding protein (C/EBP), alpha
GeneCards (Weizmann)CEBPA
Ensembl (Hinxton)ENSG00000245848 [Gene_View]  chr19:33790840-33793470 [Contig_View]  CEBPA [Vega]
AceView (NCBI)CEBPA
Genatlas (Paris)CEBPA
WikiGenes1050
SOURCE (Princeton)NM_001285829 NM_004364
Genomic and cartography
GoldenPath (UCSC)CEBPA  -  19q13.11   chr19:33790840-33793470 -  19q13.1   [Description]    (hg19-Feb_2009)
EnsemblCEBPA - 19q13.1 [CytoView]
Mapping of homologs : NCBICEBPA [Mapview]
OMIM116897   601626   
Gene and transcription
Genbank (Entrez)BC027902 BC063874 BC160133 X87248 Y11525
RefSeq transcript (Entrez)NM_001285829 NM_004364
RefSeq genomic (Entrez)AC_000151 NC_000019 NC_018930 NG_012022 NT_011109 NW_001838492 NW_004929415
Consensus coding sequences : CCDS (NCBI)CEBPA
Cluster EST : UnigeneHs.76171 [ NCBI ]
CGAP (NCI)Hs.76171
Alternative Splicing GalleryENSG00000245848
Gene ExpressionCEBPA [ NCBI-GEO ]     CEBPA [ SEEK ]   CEBPA [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP49715 (Uniprot)
NextProtP49715  [Medical]
With graphics : InterProP49715
Splice isoforms : SwissVarP49715 (Swissvar)
Domaine pattern : Prosite (Expaxy)BZIP (PS50217)    BZIP_BASIC (PS00036)   
Domains : Interpro (EBI)bZIP    CCAAT/enhancer-binding   
Related proteins : CluSTrP49715
Domain families : Pfam (Sanger)bZIP_2 (PF07716)   
Domain families : Pfam (NCBI)pfam07716   
Domain families : Smart (EMBL)BRLZ (SM00338)  
DMDM Disease mutations1050
Blocks (Seattle)P49715
Human Protein AtlasENSG00000245848
Peptide AtlasP49715
HPRD00296
IPIIPI00292025   
Protein Interaction databases
DIP (DOE-UCLA)P49715
IntAct (EBI)P49715
FunCoupENSG00000245848
BioGRIDCEBPA
InParanoidP49715
Interologous Interaction database P49715
IntegromeDBCEBPA
STRING (EMBL)CEBPA
Ontologies - Pathways
Ontology : AmiGOurea cycle  negative regulation of transcription from RNA polymerase II promoter  liver development  embryonic placenta development  DNA binding  sequence-specific DNA binding transcription factor activity  RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity  protein binding  nucleus  generation of precursor metabolites and energy  transcription, DNA-templated  transcription, DNA-templated  transcription from RNA polymerase II promoter  acute-phase response  mitochondrion organization  transcription factor binding  cholesterol metabolic process  negative regulation of cell proliferation  nuclear matrix  modulation by virus of host morphology or physiology  cytokine-mediated signaling pathway  myeloid cell differentiation  macrophage differentiation  lung development  organ regeneration  protein complex binding  response to vitamin B2  Rb-E2F complex  protein homodimerization activity  sequence-specific DNA binding  transcription regulatory region DNA binding  positive regulation of fat cell differentiation  positive regulation of osteoblast differentiation  positive regulation of transcription from RNA polymerase II promoter  positive regulation of transcription from RNA polymerase III promoter  protein heterodimerization activity  cell maturation  inner ear development  white fat cell differentiation  brown fat cell differentiation  response to glucocorticoid  cellular response to lithium ion  cellular response to organic cyclic compound  HMG box domain binding  
Ontology : EGO-EBIurea cycle  negative regulation of transcription from RNA polymerase II promoter  liver development  embryonic placenta development  DNA binding  sequence-specific DNA binding transcription factor activity  RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity  protein binding  nucleus  generation of precursor metabolites and energy  transcription, DNA-templated  transcription, DNA-templated  transcription from RNA polymerase II promoter  acute-phase response  mitochondrion organization  transcription factor binding  cholesterol metabolic process  negative regulation of cell proliferation  nuclear matrix  modulation by virus of host morphology or physiology  cytokine-mediated signaling pathway  myeloid cell differentiation  macrophage differentiation  lung development  organ regeneration  protein complex binding  response to vitamin B2  Rb-E2F complex  protein homodimerization activity  sequence-specific DNA binding  transcription regulatory region DNA binding  positive regulation of fat cell differentiation  positive regulation of osteoblast differentiation  positive regulation of transcription from RNA polymerase II promoter  positive regulation of transcription from RNA polymerase III promoter  protein heterodimerization activity  cell maturation  inner ear development  white fat cell differentiation  brown fat cell differentiation  response to glucocorticoid  cellular response to lithium ion  cellular response to organic cyclic compound  HMG box domain binding  
Pathways : BIOCARTAMAPKinase Signaling Pathway [Genes]    Keratinocyte Differentiation [Genes]   
Pathways : KEGGNon-alcoholic fatty liver disease (NAFLD)    Pathways in cancer    Transcriptional misregulation in cancer    Acute myeloid leukemia   
REACTOMECEBPA
Protein Interaction DatabaseCEBPA
Wikipedia pathwaysCEBPA
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)CEBPA
SNP (GeneSNP Utah)CEBPA
SNP : HGBaseCEBPA
Genetic variants : HAPMAPCEBPA
1000_GenomesCEBPA 
ICGC programENSG00000245848 
Cancer Gene: CensusCEBPA 
Somatic Mutations in Cancer : COSMICCEBPA 
CONAN: Copy Number AnalysisCEBPA 
Mutations and Diseases : HGMDCEBPA
OMIM116897    601626   
GENETestsCEBPA
Disease Genetic AssociationCEBPA
Huge Navigator CEBPA [HugePedia]  CEBPA [HugeCancerGEM]
Genomic VariantsCEBPA  CEBPA [DGVbeta]
Exome VariantCEBPA
dbVarCEBPA
ClinVarCEBPA
snp3D : Map Gene to Disease1050
General knowledge
Homologs : HomoloGeneCEBPA
Homology/Alignments : Family Browser (UCSC)CEBPA
Phylogenetic Trees/Animal Genes : TreeFamCEBPA
Chemical/Protein Interactions : CTD1050
Chemical/Pharm GKB GenePA26376
Clinical trialCEBPA
Cancer Resource (Charite)ENSG00000245848
Other databases
Probes
Litterature
PubMed317 Pubmed reference(s) in Entrez
CoreMineCEBPA
iHOPCEBPA

Bibliography

The CCAAT/enhancer binding protein (C/EBP alpha) gene (CEBPA) maps to human chromosome 19q13.1 and the related nuclear factor NF-IL6 (C/EBP beta) gene (CEBPB) maps to human chromosome 20q13.1.
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The leukemic fusion gene AML1-MDS1-EVI1 suppresses CEBPA in acute myeloid leukemia by activation of Calreticulin.
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CEBPA point mutations in hematological malignancies.
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C/EBPalpha and the pathophysiology of acute myeloid leukemia.
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CCAAT/enhancer binding protein alpha (C/EBPalpha) and C/EBPalpha myeloid oncoproteins induce bcl-2 via interaction of their basic regions with nuclear factor-kappaB p50.
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Loss of C/EBP alpha cell cycle control increases myeloid progenitor proliferation and transforms the neutrophil granulocyte lineage.
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Further evidence that germline CEBPA mutations cause dominant inheritance of acute myeloid leukaemia.
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PMID 15902292
 
Heterogeneous patterns of CEBPalpha mutation status in the progression of myelodysplastic syndrome and chronic myelomonocytic leukemia to acute myelogenous leukemia.
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AML patients with CEBPalpha mutations mostly retain identical mutant patterns but frequently change in allelic distribution at relapse: a comparative analysis on paired diagnosis and relapse samples.
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PMID 16453003
 
Development of a quantitative real-time polymerase chain reaction method for monitoring CEBPA mutations in normal karyotype acute myeloid leukaemia.
Smith LL, Pearce D, Smith ML, Jenner M, Lister TA, Bonnet D, Goff L, Fitzgibbon J
British journal of haematology. 2006 ; 133 (1) : 103-105.
PMID 16512836
 
Involvement of the CEBP gene family in four IGH@ chromosomal translocations in B-Cell precursor acute lymphoblastic leukemia (BCP-ALL).
Dyer MJS, Akasaka T, Balasas T, Russell L, Sugimoto K, Majid A, Brown DG, Cain K, Strefford JC, Harrison CJ, Siebert R
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Contributor(s)

Written05-2006Lan-Lan Smith
Cancer Research UK Medical Oncology Unit, Charterhouse Square, Barts and the London School of Medicine and Dentistry, London, UK

Citation

This paper should be referenced as such :
Smith LL . CEBPA (CCAAT enhancer binding protein alpha). Atlas Genet Cytogenet Oncol Haematol. May 2006 .
URL : http://AtlasGeneticsOncology.org/Genes/CEBPAID40050ch19q13.html

The various updated versions of this paper are referenced and archived by INIST as such :
http://documents.irevues.inist.fr/bitstream/2042/38341/1/05-2006-CEBPAID40050ch19q13.pdf   [ Bibliographic record ]

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