Alt. symbols: POLE1

Approved name: DNA polymerase epsilon, catalytic subunit
Alt. names: polymerase (DNA directed), epsilon, polymerase (DNA) epsilon, catalytic subunit | DNA polymerase epsilon catalytic subunit A

Location: 12q24.33: 132623753 - 132687376 (-)
Gene type: protein_coding, 24 transcripts.

Scores: LoFtool: 0.864000 | pLI: 0.00000000 | LOEUF: 0.640

HGNC: 9177

NCBI: 5426, RefSeq: NG_033840.1

Ensembl: ENSG00000177084.19

LRG_789 | Status: public

OMIM: 174762

Expression | ProteinAtlas

POLE encodes the catalytic subunit of DNA polymerase epsilon complex (PubMed:10801849). The enzyme is involved in DNA synthesis during DNA repair (PubMed:20227374, PubMed:27573199). Together with DNA polymerase POLD1 and DNA polymerase POLK, it has a role in excision repair (NER) synthesis following UV irradiation (PubMed:20227374). It has also been suggested that the enzyme could participate in chromosomal DNA replication, and that it might have 3'-5' proofreading exonuclease activity to correct DNA replication errors. During DNA synthesis it is thought to bind at/or near replication origins and move along DNA with the replication fork.

Biallelic mutations in this gene have been associated with the IMAGE-I syndrome [MIM:618336] and the FILS syndrome [MIM:615139]. IMAGEI is an autosomal recessive disorder characterized by intrauterine growth retardation, metaphyseal dysplasia, adrenal hypoplasia congenita, growth hormone deficiency, genital anomalies, and immunodeficiency resulting in increased infections. Biallelic mutations in POLE have been associated with facial dysmorphism, immunodeficiency, livedo, and short stature (FILS) syndrome. The majority of the pathogenic mutations associated with these syndromes are biallelic truncating variants (splice-affecting, nonsense, deletions), with only one homozygous missense variant reported (p.Ala1007Pro). In addition, the monoallelic missense mutation p.Leu424Val has been associated with susceptibility to colorectal cancer (CRCS12; MIM:615083) by different studies (Palles et al., 2013; Valle et al. 2014; Elsayed et al., 2015). Leu424 is highly conserved residue in the exonuclease (proofreading) domain. [Load More]