Polh
entrez
80905
canonical
uniprot
Q9JJN0
canonical
ensembl
ENSMUSG00000023953
resolver
ensp
ENSMUSP00000024749
resolver
enst
ENSMUST00000024749
resolver
genesymbol
Polh
resolver
genesymbol_syn
Rad30a
resolver
genesymbol_syn
Xpv
resolver
uniprot
Q9JJJ2
resolver
uniprot_entry
POLH_MOUSE
resolver
uniprot_sec
Q9JJJ2
resolver
activity_regulation
ACTIVITY REGULATION: The enzyme in complex with the DNA substrate binds a third divalent metal cation. The binding of this third divalent cation, which is coordinated by water molecules and two oxygen atoms from DNA and dNTP, is essential for catalyzing the DNA synthesis. {ECO:0000250|UniProtKB:Q9Y253}.
uniprot
proteins
amino_acid_sequence
MAPGQNRVVALVDMDCFFVQVEQRQNPHLRNKPCAVVQYKSWKGGGIIAVSYEARAFGVTRNMWADDAKKLCPDLLLAQVRESRGKANLTKYREASVEVMEIMSYFAVIERASIDEAYIDLTSAVQERLQKLQGQPISADLLPSTYIEGLPRGPTVEETVQKEAIRKQGLLQWLDSLQSDDPTSPDLRLTVGAMIVEEMRAAIESKTGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEVLGIEYMGDLTQFTESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATREQVQWWLLQLALELEERLTKDRNDNDRVATQLVVSIRFQGDRRLSSLRRCCALPRYDAHKMSQDAFAAIRNCNTSGIQTEWSPPLTMLFLCATKFSAAAPPACTDITAFLSSDSSCQPKVPIASSETRTQGSGPAVPTSKEAATSLASFFQKAAKKQRMKETSFVPLNTATEKLSSKPSLVFQSSQTTGSQSFFKQKSLLLQHTQLSNSAAPDPPQASPAAQPSCLPAECVDSGPDDGAVKPVSSKAVSTEMNVAGDSPNVLDSPAYNSQEVTQRATEDQVLCEKCDSLVPVWDMPEHTDYHFALELQKSFLQPCTSKPQAIPAVSPQGKRNPKSPSASSSKRLRPHGMQTLESFFKPLTH
uniprot
proteins
ec_number
2.7.7.7
uniprot
proteins
function
FUNCTION: DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS) (PubMed:10871396). 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 (By similarity). Particularly important for the repair of UV-induced pyrimidine dimers (PubMed:10871396). 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 (By similarity). {ECO:0000250|UniProtKB:Q9Y253, ECO:0000269|PubMed:10871396}.
uniprot
proteins
mass_dalton
76167
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated by RCHY1/PIRH2. Ubiquitination depends on integrity of the UBZ3-type zinc finger domain and is enhanced by TRAIP. Ubiquitination inhibits the ability of PolH to interact with PCNA and to bypass UV-induced lesions. {ECO:0000250|UniProtKB:Q9Y253}.
uniprot
proteins
protein_family
DNA polymerase type-Y family
uniprot
proteins
pubmed
10871396
uniprot
proteins
pubmed
14657033
uniprot
proteins
pubmed
16141072
uniprot
proteins
sequence_length
694
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y253}. Note=Binding to ubiquitinated PCNA mediates colocalization to replication foci during DNA replication and persists at sites of stalled replication forks following UV irradiation. After UV irradiation, recruited to DNA damage sites within 1 hour, to a maximum of about 80%; this recruitment may not be not restricted to cells active in DNA replication. Colocalizes with TRAIP to nuclear foci. {ECO:0000250|UniProtKB:Q9Y253}.
uniprot
proteins