Gene Detail

Gene Symbol CEBPA
Synonyms C/EBP-alpha | CEBP
Gene Description CEBPA, CCAAT enhancer binding protein alpha, is a transcription factor that regulates the expression of genes involved in cell differentiation (PMID: 26601784). Inactivation of CEBPA is associated with the pathogenesis of leukemia and dysregulation of CEBPA has been identified in various solid tumors (PMID: 28720765, PMID: 28504718).
Entrez Id 1050
Chromosome 19
Map Location 19q13.11
Canonical Transcript NM_004364

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Variant Impact Protein Effect Variant Description Associated with drug Resistance
R288_V296delinsL insertion unknown CEBPA R288_V296delinsL results in the deletion of amino acids 288 to 296 of the Cebpa protein, followed by the insertion of a leucine (L) (UniProt.org). R288_V296delinsL has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
P46Lfs*114 frameshift loss of function - predicted CEBPA P46Lfs*114 likely results in a premature truncation of the 358 aa Cepba protein at aa 46, followed by 114 nonsense amino acids (UniProt.org). P46Lfs*114 has not been characterized, however other frameshifts cause alternate translation and the resulting isoform inhibits Cepba DNA binding (PMID: 11242107), thus P46Lfs*114 is predicted to lead to a loss of Cebpa protein function.
Y67* nonsense loss of function - predicted CEBPA Y67* results in a premature truncation of the Cebpa protein at amino acid 67 of 358 (UniProt.org). Due to the loss of the basic leucine zipper DNA binding domain (UniProt.org), Cebpa is predicted to lead to a loss of Cebpa protein function.
K280N missense unknown CEBPA K280N lies within the FOXO1-interacting region of the Cebpa protein (UniProt.org). K280N has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
E59* nonsense loss of function - predicted CEBPA E59* results in a premature truncation of the Cebpa protein at aminoa acid 59 of 358 (UniProt.org). Due to the loss of the basic leucine zipper DNA binding domain (UniProt.org), E59* is predicted to lead to a loss of protein function.
A111Rfs*59 frameshift loss of function - predicted CEBPA A111Rfs*59 likely results in a truncation of the 358 aa Cebpa protein at aa 111, followed by 59 nonsense amino acids (UniProt.org). A111Rfs*59 has not been characterized, however other frameshifts cause alternate translation and the resulting isoform inhibits Cepba DNA binding (PMID: 11242107), thus A111RPfs*59 is predicted to lead to a loss of Cebpa protein function.
mutant unknown unknown CEBPA mutant indicates an unspecified mutation in the CEBPA gene.
positive unknown unknown CEBPA positive indicates the presence of the CEBPA gene, mRNA, and/or protein.
T310_Q311insKQNP insertion unknown CEBPA T310_Q311insKQNP results in the insertion of four amino acid residues (KQNP) in the Cebpa protein between amino acids 310 and 311 (UniProt.org). T310_Q311insKQNP has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
P197Q missense unknown CEBPA P197Q lies within a transcriptional activation domain of the Cebpa protein (PMID: 11242107). P197Q has been identified in the scientific literature (PMID: 24997986, PMID: 26255870), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
R343Afs*79 frameshift unknown CEBPA R343Afs*79 likely results in a premature truncation of the 358 aa Cebpa protein at aa 343, followed by 79 nonsense amino acids (UniProt.org). R343Afs*79 has been identified in the scientific literature (PMID: 26796102), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
A44Pfs*63 frameshift loss of function - predicted CEBPA A44Pfs*63 likely results in a premature truncation of the 358 aa Cebpa protein at aa 44, followed by 63 nonsense amino acids (UniProt.org). A44Pfs*63 has not been characterized, however other frameshifts cause alternate translation and the resulting isoform inhibits Cepba DNA binding (PMID: 11242107), thus A44Pfs*63 is predicted to lead to a loss of Cebpa protein function.
E347G missense unknown CEBPA E347G does not lie within any known functional domains of the Cebpa protein (UniProt.org). E347G has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
I294K missense unknown CEBPA I294K lies within the bZIP domain of the Cebpa protein (UniProt.org). I294K has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
Q312* nonsense loss of function - predicted CEBPA Q312* results in a premature truncation of the Cebpa protein at amino acid 312 of 358 (UniProt.org). Due to the loss of the leucine zipper region (UniProt.org), Q312* is predicted to lead to a loss of Cebpa protein function.
wild-type none no effect Wild-type CEBPA indicates that no mutation has been detected within the CEBPA gene.
L317_T318insM insertion unknown CEBPA L317_T318insM results in the insertion of one amino acid residue (M) in the Cebpa protein between amino acids 317 and 318 (UniProt.org). L317_T318insM has been identified in the scientific literature (PMID: 15645492, PMID: 29025912), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
T318del deletion unknown CEBPA T318del results in the deletion of a threonine (T) within the basic leucine zipper DNA binding domain of the Cebpa protein domain (UniProt.org). T318del has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
D301H missense unknown CEBPA D301H lies within the bZIP domain of the Cebpa protein (UniProt.org). D301H has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
N293del deletion unknown CEBPA N293del results in the deletion of asparagine (N) within the basic leucine zipper DNA binding domain of the Cebpa protein domain (UniProt.org). N293del has been identified in the scientific literature (PMID: 18729193, PMID: 14726504), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
Q305dup duplication unknown CEBPA Q305dup indicates the insertion of the duplicate amino acid, valine (V)-308 within the basic leucine zipper DNA binding domain of the Cebpa protein (UniProt.org). Q305dup has been identified in the scientific literature (PMID: 25468431), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
E59D missense unknown CEBPA E59D lies within the first transactivation domain of the Cebpa protein (PMID: 11672531). E59D has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
T310_Q311insW insertion unknown CEBPA T310_Q311insW results in the insertion of one amino acid residue (W) in the Cebpa protein between amino acids 310 and 311 (UniProt.org). T310_Q311insW has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
D301N missense unknown CEBPA D301N lies within the bZIP domain of the Cebpa protein (UniProt.org). D301N has been identified in sequencing studies (PMID: 27276561), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
R142Tfs*27 missense loss of function - predicted CEBPA R142Tfs*27 likely results in a premature truncation of the 358 aa Cepba protein at aa 142, followed by 27 nonsense amino acids (UniProt.org). Due to the loss of the basic leucine zipper DNA binding domain (UniProt.org), R142Tfs*27 is predicted to lead to a loss of Cebpa protein function.
amp none no effect CEBPA amplification indicates an increased number of copies of the CEBPA gene. However, the mechanism causing the increase is unspecified.
K304_Q305insL insertion unknown CEBPA K304_Q305insL results in the insertion of one amino acid residue (L) in the Cebpa protein between amino acids 304 and 305 (UniProt.org). K304_Q305insL has been identified in the scientific literature (PMID: 22389883, PMID: 27359055, PMID: 25987038), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Mar 2018).
P23Rfs*137 frameshift loss of function - predicted CEBPA P23Rfs*137 likely results in a premature truncation of the 358 aa Cepba protein at aa 23, followed by 137 nonsense amino acids (UniProt.org). P23Rfs*137 has not been characterized, however other frameshifts cause alternate translation and the resulting isoform inhibits Cepba DNA binding (PMID: 11242107), thus P23Rfs*137 is predicted to lead to a loss of Cebpa protein function.
T318_S319insI insertion unknown CEBPA T318_S319insI results in the insertion of one amino acid residue (I) in the Cebpa protein between amino acids 318 and 319 (UniProt.org). T318_S319insI has been identified in the scientific literature (PMID: 25987038), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
R300C missense unknown CEBPA R300C lies within the bZIP domain of the Cebpa protein (UniProt.org). R300C has been identified in the scientific literature (PMID: 27276561, PMID: 23297133), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
T337M missense unknown CEBPA T337M lies within the bZIP domain of the Cebpa protein (UniProt.org). T337M has been identified in sequencing studies (PMID: 24755471), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
H195_P196dup duplication unknown CEBPA H195_P196dup indicates the insertion of two duplication amino acids, histidine (H)-195 and proline (P)-196 within a transcriptional activation domain of the Cebpa protein (PMID: 11242107). H195_P196dup is a common Cebpa polymorphism, but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PMID: 25468431, PubMed, Jan 2018).
L324P missense unknown CEBPA L324P lies within the bZIP domain of the Cebpa protein (UniProt.org). L324P has been identified in sequencing studies (PMID: 27288520), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
A44P missense unknown CEBPA A44P lies within the first transactivation domain of the Cebpa protein (PMID: 11672531). A44P has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
K326N missense unknown CEBPA K326N lies within the bZIP domain of the Cebpa protein (UniProt.org). K326N has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
R286Pfs*35 frameshift loss of function - predicted CEBPA R286Pfs*35 likely results in a premature truncation of the 358 aa Cebpa protein at aa 286, followed by 35 nonsense amino acids (UniProt.org). Due to the loss of the basic leucine zipper DNA binding domain (UniProt.org), R286Pfs*35 is predicted to lead to a loss of Cebpa protein function.
T337A missense unknown CEBPA T337A lies within the bZIP domain of the Cebpa protein (UniProt.org). T337A has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
V308dup duplication unknown CEBPA V308dup indicates the insertion of the duplicate amino acid, valine (V)-308 within the basic leucine zipper DNA binding domain of the Cebpa protein (UniProt.org). V308dup has been identified in the scientific literature (PMID: 29025912), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
E329Q missense unknown CEBPA E329Q lies within the bZIP domain of the Cebpa protein (UniProt.org). E329Q has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
R339W missense unknown CEBPA R339W lies within the bZIP domain of the Cebpa protein (UniProt.org). R339W has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Jan 2018).
F82S missense unknown CEBPA F82S lies within the first transactivation domain of the Cebpa protein (PMID: 11672531). F82S has been identified in sequencing studies (PMID: 26343386, PMID: 26286987), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
R142Sfs*27 frameshift loss of function - predicted CEBPA R142Sfs*27 likely results in a premature truncation of the 358 aa Cepba protein at aa 142, followed by 27 nonsense amino acids (UniProt.org). Due to the loss of the basic leucine zipper DNA binding domain (UniProt.org), R142Sfs*27 is predicted to lead to a loss of Cebpa protein function.
R306P missense unknown CEBPA R306P lies within the bZIP domain of the Cebpa protein (UniProt.org). R306P has been identified in the scientific literature (PMID: 11830484, PMID: 22649106, PMID: 27288520, PMID: 27276561), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Sep 2018).
Molecular Profile Protein Effect Treatment Approaches
CEBPA R288_V296delinsL unknown
CEBPA P46Lfs*114 loss of function - predicted
CEBPA Y67* loss of function - predicted
CEBPA K280N unknown
CEBPA E59* loss of function - predicted
CEBPA A111Rfs*59 loss of function - predicted
CEBPA mutant unknown
GATA2 T354M CEBPA mutant
CEBPA mutant GATA2 mutant
CEBPA positive unknown
CEBPA T310_Q311insKQNP unknown
CEBPA P197Q unknown
CEBPA R343Afs*79 unknown
CEBPA A44Pfs*63 loss of function - predicted
CEBPA E347G unknown
CEBPA I294K unknown
CEBPA Q312* loss of function - predicted
CEBPA wild-type no effect
CEBPA L317_T318insM unknown
CEBPA T318del unknown
CEBPA D301H unknown
CEBPA N293del unknown
CEBPA Q305dup unknown
CEBPA E59D unknown
CEBPA T310_Q311insW unknown
CEBPA D301N unknown
CEBPA R142Tfs*27 loss of function - predicted
CEBPA amp no effect
CEBPA K304_Q305insL unknown
CEBPA P23Rfs*137 loss of function - predicted
CEBPA T318_S319insI unknown
CEBPA R300C unknown
CEBPA T337M unknown
CEBPA H195_P196dup unknown
CEBPA L324P unknown
CEBPA A44P unknown
CEBPA K326N unknown
CEBPA R286Pfs*35 loss of function - predicted
CEBPA T337A unknown
CEBPA V308dup unknown
CEBPA E329Q unknown
CEBPA R339W unknown
CEBPA F82S unknown
CEBPA R142Sfs*27 loss of function - predicted
CEBPA R306P unknown
Molecular Profile Indication/Tumor Type Response Type Therapy Name Approval Status Evidence Type Efficacy Evidence References
CEBPA mutant acute myeloid leukemia not applicable N/A Clinical Study Prognostic In clinical analyses, biallelic CEBPA mutations were associated with favorable clinical outcome in patients with cytogenetically normal acute myeloid leukemia (PMID: 26601784, PMID: 19171880, PMID: 20038735, PMID: 22915647). 26601784 19171880 20038735
CEBPA mutant acute myeloid leukemia predicted - sensitive Tofacitinib Preclinical - Patient cell culture Actionable In a preclinical study, patient-derived acute myeloid leukemia (AML) cells harboring biallelic CEBPA mutations demonstrated increased sensitivity to Xeljanz (tofacitinib) compared to control AML cells in culture (PMID: 27034432). 27034432
CEBPA mutant acute myeloid leukemia predicted - sensitive Momelotinib Preclinical - Patient cell culture Actionable In a preclinical study, patient-derived acute myeloid leukemia (AML) cells harboring biallelic CEBPA mutations demonstrated increased sensitivity to Momelotinib (CYT387) compared to control AML cells in culture (PMID: 27034432). 27034432
CEBPA mutant acute myeloid leukemia predicted - sensitive AZD1480 Preclinical - Patient cell culture Actionable In a preclinical study, patient-derived acute myeloid leukemia (AML) cells harboring biallelic CEBPA mutations demonstrated increased sensitivity to AZD1480 compared to control AML cells in culture (PMID: 27034432). 27034432
CEBPA mutant acute myeloid leukemia predicted - sensitive Ruxolitinib Preclinical - Patient cell culture Actionable In a preclinical study, patient-derived acute myeloid leukemia (AML) cells harboring biallelic CEBPA mutations demonstrated increased sensitivity to Jakafi (ruxolitinib) compared to control AML cells in culture (PMID: 27034432). 27034432
CEBPA mutant GATA2 mutant acute myeloid leukemia not applicable N/A Clinical Study Prognostic In clinical analyses, mutations in GATA2 were associated with better overall survival in patients with cytogenetically normal acute myeloid leukemia (CN-AML) harboring biallelic CEBPA gene mutations (PMID: 22814295, PMID: 23521373, PMID: 25241285). 25241285 22814295 23521373