Gene Detail

Contact

Missing content? – Request curation!

Request curation for specific Genes, variants, or PubMed publications.

Have questions, comments or suggestions? - Let us know!

Email us at : ckbsupport@jax.org

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, including biallelic CEBPA-mutant AML (PMID: 32086816), and dysregulation of CEBPA has been identified in various solid tumors (PMID: 28720765, PMID: 28504718).

Filtering

  • Case insensitive filtering will display rows where any text in any cell matches the filter term
  • Simple literal full or partial string matches
  • Separate multiple filter terms with a spaces, order doesn't matter (a b c and c b a are equivalent )
  • Filtering will only apply to rows that are already loaded on the page, filtering has no impact on query parameters
  • Use quotes to match a longer phrase which contains spaces "mtor c1483f"

Sorting

  • Generally, the default sort order for tables is set to be first column ascending, however, specific tables may set a different default sort order.
  • Click on any column header arrows to sort by that column
  • Hold down the Shift key and click multiple columns to sort by more than one column, be sure to set ascending or descending order for a given column, before moving on to the next column.

Variant Impact Protein Effect Variant Description Associated with drug Resistance
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.
A44P missense unknown CEBPA A44P lies within a region of the Cebpa protein required to repress E2F1:TFDP1-mediated transcription (UniProt.org). A44P has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
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.
amp none no effect CEBPA amplification indicates an increased number of copies of the CEBPA gene. However, the mechanism causing the increase is unspecified.
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, Apr 2020).
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, Apr 2020).
D63N missense unknown CEBPA D63N lies within the region required to repress E2F1:TFDP1-mediated transcription and TRIB1-interacting region of the Cebpa protein (UniProt.org). D63N is predicted to alter Cebpa protein stability based on structural modeling (PMID: 31621694), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
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, Apr 2020).
E347G missense unknown CEBPA E347G lies within the FOXO1-interacting region 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, Apr 2020).
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.
E59D missense unknown CEBPA E59D lies within the region required to repress E2F1:TFDP1-mediated transcription and TRIB1-interacting region of the Cebpa protein (UniProt.org). E59D has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
F82S missense unknown CEBPA F82S lies within the transactivation domain 1 of the Cebpa protein (PMID: 11242107). 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, Apr 2020).
H195_P196dup duplication unknown CEBPA H195_P196dup indicates the insertion of 2 duplicate amino acids, histidine (H)-195 through proline (P)-196 within the transactivation domain 2 of the Cebpa protein (PMID: 11242107). H195_P196dup is a common polymorphism (PMID: 17190859), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
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, Apr 2020).
inact mut unknown loss of function CEBPA inact mut indicates that this variant results in a loss of function of the Cebpa protein. However, the specific amino acid change has not been identified.
K280N missense unknown CEBPA K280N lies within the FOXO1-interacting region of the Cebpa protein (UniProt.org). K280N has been identified in sequencing studies (PMID: 27322744), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
K304_Q305insL insertion unknown CEBPA K304_Q305insL results in the insertion of a leucine (L) in the bZIP domain of 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, Apr 2020).
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, Apr 2020).
L317_T318insM insertion unknown CEBPA L317_T318insM results in the insertion of a methionine (M) in the bZIP domain of 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, Apr 2020).
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, PMID: 26847745), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
mutant unknown unknown CEBPA mutant indicates an unspecified mutation in the CEBPA gene.
N292S missense unknown CEBPA N292S lies within the bZIP domain the Cebpa protein (UniProt.org). N292S is predicted to destabilize Cebpa protein based on structural modeling (PMID: 31621694), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
N292T missense unknown CEBPA N292T lies within the bZIP domain of the Cebpa protein (UniProt.org). N292T is predicted to alter Cebpa protein stability based on structural modeling (PMID: 31621694), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
N293del deletion unknown CEBPA N293del results in the deletion of an asparagine (N) within the bZIP domain of the Cebpa protein domain at amino acid 293 (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, Apr 2020).
P197Q missense unknown CEBPA P197Q lies within the transactivation domain 2 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, Apr 2020).
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.
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.
positive unknown unknown CEBPA positive indicates the presence of the CEBPA gene, mRNA, and/or protein.
Q305dup duplication unknown CEBPA Q305dup indicates the insertion of the duplicate amino acid, valine (V)-308 within the bZIP domain of the Cebpa protein (UniProt.org). Q305dup has been identified in the scientific literature (PMID: 25468431, PMID: 21403128), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
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.
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.
R142Tfs*27 frameshift 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.
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.
R288P missense unknown CEBPA R288P lies within the bZIP domain of the Cebpa protein (UniProt.org). R288P is predicted to destabilize Cebpa protein based on structural modeling (PMID: 31621694), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
R288_V296delinsL indel unknown CEBPA R288_V296delinsL results in the deletion of 9 amino acids in the bZIP domain of the Cebpa protein from amino acids 288 to 296, combined with the insertion of a leucine (L) at the same site (UniProt.org). R288_V296delinsL has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
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, Apr 2020).
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, Apr 2020).
R339W missense unknown CEBPA R339W lies within the bZIP domain of the Cebpa protein (UniProt.org). R339W has not been characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
R343Afs*79 frameshift unknown CEBPA R343Afs*79 indicates a shift in the reading frame starting at amino acid 343 and terminating 79 residues downstream, resulting in premature truncation of the functional protein, and extension of the 358aa Cebpa protein length by 64 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, Apr 2020).
T310_Q311insKQNP insertion unknown CEBPA T310_Q311insKQNP results in the insertion of four amino acids in the bZIP domain of the Cebpa protein between amino acids 310 and 311 (UniProt.org). T310_Q311insKQNP has not been characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
T310_Q311insW insertion unknown CEBPA T310_Q311insW results in the insertion of a tryptophan (W) in the bZIP domain of the Cebpa protein between amino acids 310 and 311 (UniProt.org). T310_Q311insW has not been characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
T318del deletion unknown CEBPA T318del results in the deletion of a threonine (T) in the bZIP domain of the Cebpa protein at amino acid 318 (UniProt.org). T318del has not been characterized in the scientific literature and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
T318_S319insI insertion unknown CEBPA T318_S319insI results in the insertion of an isoleucine (I) in the bZIP domain of the Cebpa protein between amino acids 318 and 319 (UniProt.org). T318_S319insI has been identified in the scientific literature (PMID: 25987038, PMID: 29025912), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
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, Apr 2020).
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, Apr 2020).
V308dup duplication unknown CEBPA V308dup indicates the insertion of the duplicate amino acid, valine (V)-308 within the bZIP domain of the Cebpa protein (UniProt.org). V308dup has been identified in sequencing studies (PMID: 29025912), but has not been biochemically characterized and therefore, its effect on Cebpa protein function is unknown (PubMed, Apr 2020).
wild-type none no effect Wild-type CEBPA indicates that no mutation has been detected within the CEBPA gene.
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.