UniProt functional annotation for Q6R3M4



	UniProt functional annotation for Q6R3M4

UniProt code: Q6R3M4.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Error-prone DNA polymerase specifically involved in DNA repair (PubMed:15026325, PubMed:16357261). Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls (PubMed:15026325, PubMed:16357261). Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template (By similarity). Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine (By similarity). May play a role in hypermutation of immunogobulin genes (By similarity). Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity (By similarity). {ECO:0000250|UniProtKB:Q9UNA4, ECO:0000269|PubMed:15026325, ECO:0000269|PubMed:16357261}.

Catalytic activity: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:15026325};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UNA4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UNA4}; Note=Binds nucleotide much more tightly and catalyzes nucleotide insertion much more efficiently in the presence of Mg(2+) than in the presence of Mn(2+). {ECO:0000250|UniProtKB:Q9UNA4};

Subunit: Interacts with POLH (By similarity). Interacts with REV1 (PubMed:14657033). Interacts with ubiquitin (PubMed:16357261). {ECO:0000250|UniProtKB:Q9UNA4, ECO:0000269|PubMed:14657033, ECO:0000269|PubMed:16357261}.

Subcellular location: Nucleus {ECO:0000250}. Note=Binding to ubiquitin mediates localization to replication forks after UV-induced DNA damage. {ECO:0000269|PubMed:16357261}.

Tissue specificity: Detected in testis, and at very low levels in spleen, lung and brain. Detected in round spermatids, but not in prophase spermatocytes. {ECO:0000269|PubMed:10458907}.

Domain: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. {ECO:0000250|UniProtKB:Q9UNA4}.

Domain: Ubiquitin-binding motif 1 and ubiquitin-binding motif 2 regulate POLI protein monoubiquitination and localization to nuclear foci after UV-induced DNA damage. {ECO:0000269|PubMed:16357261}.

Ptm: Monoubiquitinated (PubMed:16357261). Protein monoubiquitination prevents POLI binding to ubiquitin via the ubiquitin-binding motif 1 and ubiquitin-binding motif 2 (PubMed:16357261). {ECO:0000269|PubMed:16357261}.

Similarity: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Error-prone DNA polymerase specifically involved in DNA repair (PubMed:15026325, PubMed:16357261). Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls (PubMed:15026325, PubMed:16357261). Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template (By similarity). Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine (By similarity). May play a role in hypermutation of immunogobulin genes (By similarity). Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity (By similarity). {ECO:0000250\|UniProtKB:Q9UNA4, ECO:0000269\|PubMed:15026325, ECO:0000269\|PubMed:16357261}.


Catalytic activity:		Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7; Evidence={ECO:0000269\|PubMed:15026325};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250\|UniProtKB:Q9UNA4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250\|UniProtKB:Q9UNA4}; Note=Binds nucleotide much more tightly and catalyzes nucleotide insertion much more efficiently in the presence of Mg(2+) than in the presence of Mn(2+). {ECO:0000250\|UniProtKB:Q9UNA4};
Subunit:		Interacts with POLH (By similarity). Interacts with REV1 (PubMed:14657033). Interacts with ubiquitin (PubMed:16357261). {ECO:0000250\|UniProtKB:Q9UNA4, ECO:0000269\|PubMed:14657033, ECO:0000269\|PubMed:16357261}.
Subcellular location:		Nucleus {ECO:0000250}. Note=Binding to ubiquitin mediates localization to replication forks after UV-induced DNA damage. {ECO:0000269\|PubMed:16357261}.
Tissue specificity:		Detected in testis, and at very low levels in spleen, lung and brain. Detected in round spermatids, but not in prophase spermatocytes. {ECO:0000269\|PubMed:10458907}.
Domain:		The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. {ECO:0000250\|UniProtKB:Q9UNA4}.
Domain:		Ubiquitin-binding motif 1 and ubiquitin-binding motif 2 regulate POLI protein monoubiquitination and localization to nuclear foci after UV-induced DNA damage. {ECO:0000269\|PubMed:16357261}.
Ptm:		Monoubiquitinated (PubMed:16357261). Protein monoubiquitination prevents POLI binding to ubiquitin via the ubiquitin-binding motif 1 and ubiquitin-binding motif 2 (PubMed:16357261). {ECO:0000269\|PubMed:16357261}.
Similarity:		Belongs to the DNA polymerase type-Y family. {ECO:0000305}.