POLH report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0006281Biological processDNA repair
GO_0042276Biological processerror-prone translesion synthesis
GO_0009314Biological processresponse to radiation
GO_0010225Biological processresponse to UV-C
GO_0006282Biological processregulation of DNA repair
GO_0006290Biological processpyrimidine dimer repair
GO_0006260Biological processDNA replication
GO_0071494Biological processcellular response to UV-C
GO_0070987Biological processerror-free translesion synthesis
GO_0000731Biological processDNA synthesis involved in DNA repair
GO_0005657Cellular componentreplication fork
GO_0005654Cellular componentnucleoplasm
GO_0005829Cellular componentcytosol
GO_0035861Cellular componentsite of double-strand break
GO_0005634Cellular componentnucleus
GO_0003887Molecular functionDNA-directed DNA polymerase activity
GO_0046872Molecular functionmetal ion binding
GO_0005515Molecular functionprotein binding
GO_0003684Molecular functiondamaged DNA binding

IV. Literature review

[source]
Gene namePOLH
Protein nameDNA polymerase eta
DNA polymerase eta (EC 2.7.7.7) (RAD30 homolog A) (Xeroderma pigmentosum variant type protein)
Truncated DNA polymerase eta
DNA polymerase eta transcript variant
SynonymsXPV
RAD30
RAD30A
DescriptionFUNCTION: DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS) . 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 . Particularly important for the repair of UV-induced pyrimidine dimers . Although inserts the correct base, may cause base transitions and transversions depending upon the context. May play a role in hypermutation at immunoglobulin genes . 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 . Targets POLI to replication foci . .

AccessionsA0A977TKC9
ENST00000372226.1 [Q9Y253-2]
C4P9N5
Q9Y253
ENST00000372236.9 [Q9Y253-1]
ENST00000443535.1
Q5JTF2