Aliases for POLH Gene
External Ids for POLH Gene
Previous GeneCards Identifiers for POLH Gene
This gene encodes a member of the Y family of specialized DNA polymerases. It copies undamaged DNA with a lower fidelity than other DNA-directed polymerases. However, it accurately replicates UV-damaged DNA; when thymine dimers are present, this polymerase inserts the complementary nucleotides in the newly synthesized DNA, thereby bypassing the lesion and suppressing the mutagenic effect of UV-induced DNA damage. This polymerase is thought to be involved in hypermutation during immunoglobulin class switch recombination. Mutations in this gene result in XPV, a variant type of xeroderma pigmentosum. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2014]
GeneCards Summary for POLH Gene
POLH (DNA Polymerase Eta) is a Protein Coding gene. Diseases associated with POLH include Xeroderma Pigmentosum, Variant Type and Polh-Related Xeroderma Pigmentosum. Among its related pathways are DNA Damage and DNA Double-Strand Break Repair. GO annotations related to this gene include damaged DNA binding and DNA-directed DNA polymerase activity. An important paralog of this gene is POLK.
UniProtKB/Swiss-Prot for POLH Gene
DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS) (PubMed:10385124, PubMed:11743006, PubMed:24449906). Due to low processivity on both damaged and normal DNA, cooperates with the heterotetrameric (REV3L, REV7, POLD2 and POLD3) POLZ complex for complete bypass of DNA lesions. Inserts one or 2 nucleotide(s) opposite the lesion, the primer is further extended by the tetrameric POLZ complex. In the case of 1,2-intrastrand d(GpG)-cisplatin cross-link, inserts dCTP opposite the 3 guanine (PubMed:24449906). Particularly important for the repair of UV-induced pyrimidine dimers (PubMed:10385124, PubMed:11743006). Although inserts the correct base, may cause base transitions and transversions depending upon the context. May play a role in hypermutation at immunoglobulin genes (PubMed:11376341, PubMed:14734526). Forms a Schiff base with 5-deoxyribose phosphate at abasic sites, but does not have any lyase activity, preventing the release of the 5-deoxyribose phosphate (5-dRP) residue. This covalent trapping of the enzyme by the 5-dRP residue inhibits its DNA synthetic activity during base excision repair, thereby avoiding high incidence of mutagenesis (PubMed:14630940). Targets POLI to replication foci (PubMed:12606586).