UniProt functional annotation for Q9UNA4



	UniProt functional annotation for Q9UNA4

UniProt code: Q9UNA4.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Error-prone DNA polymerase specifically involved in DNA repair (PubMed:11013228, PubMed:11387224). Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls (PubMed:11013228, PubMed:11387224, PubMed:14630940, PubMed:15199127). Favors Hoogsteen base-pairing in the active site (PubMed:15254543). Inserts the correct base with high-fidelity opposite an adenosine template (PubMed:15254543). Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine (PubMed:11013228). May play a role in hypermutation of immunogobulin genes (PubMed:12410315). Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity (PubMed:11251121, PubMed:14630940). {ECO:0000269|PubMed:11013228, ECO:0000269|PubMed:11251121, ECO:0000269|PubMed:11387224, ECO:0000269|PubMed:12410315, ECO:0000269|PubMed:14630940, ECO:0000269|PubMed:15199127, ECO:0000269|PubMed:15254543}.

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:11013228, ECO:0000269|PubMed:11387224, ECO:0000269|PubMed:27555320};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27555320}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:27555320}; 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:0000269|PubMed:27555320};

Subunit: Interacts with POLH (PubMed:12606586). Interacts with REV1 (By similarity). Interacts with ubiquitin (By similarity). {ECO:0000250|UniProtKB:Q6R3M4, ECO:0000269|PubMed:12606586}.

Subcellular location: Nucleus {ECO:0000269|PubMed:12606586}. Note=Binding to ubiquitin mediates localization to replication forks after UV-induced DNA damage. {ECO:0000250|UniProtKB:Q6R3M4}.

Tissue specificity: Ubiquitous. Highly expressed in testis. {ECO:0000269|PubMed:10458907, ECO:0000269|PubMed:11387224}.

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:0000269|PubMed:15254543, ECO:0000269|PubMed:27555320}.

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:0000250|UniProtKB:Q6R3M4}.

Ptm: Monoubiquitinated. Protein monoubiquitination prevents POLI binding to ubiquitin via the ubiquitin-binding motif 1 and ubiquitin- binding motif 2. {ECO:0000250|UniProtKB:Q6R3M4}.

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

Sequence caution: Sequence=AAD50381.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAF63383.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAH32662.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAM11872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=CAB66605.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Error-prone DNA polymerase specifically involved in DNA repair (PubMed:11013228, PubMed:11387224). Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls (PubMed:11013228, PubMed:11387224, PubMed:14630940, PubMed:15199127). Favors Hoogsteen base-pairing in the active site (PubMed:15254543). Inserts the correct base with high-fidelity opposite an adenosine template (PubMed:15254543). Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine (PubMed:11013228). May play a role in hypermutation of immunogobulin genes (PubMed:12410315). Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity (PubMed:11251121, PubMed:14630940). {ECO:0000269\|PubMed:11013228, ECO:0000269\|PubMed:11251121, ECO:0000269\|PubMed:11387224, ECO:0000269\|PubMed:12410315, ECO:0000269\|PubMed:14630940, ECO:0000269\|PubMed:15199127, ECO:0000269\|PubMed:15254543}.


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:11013228, ECO:0000269\|PubMed:11387224, ECO:0000269\|PubMed:27555320};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:27555320}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269\|PubMed:27555320}; 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:0000269\|PubMed:27555320};
Subunit:		Interacts with POLH (PubMed:12606586). Interacts with REV1 (By similarity). Interacts with ubiquitin (By similarity). {ECO:0000250\|UniProtKB:Q6R3M4, ECO:0000269\|PubMed:12606586}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:12606586}. Note=Binding to ubiquitin mediates localization to replication forks after UV-induced DNA damage. {ECO:0000250\|UniProtKB:Q6R3M4}.
Tissue specificity:		Ubiquitous. Highly expressed in testis. {ECO:0000269\|PubMed:10458907, ECO:0000269\|PubMed:11387224}.
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:0000269\|PubMed:15254543, ECO:0000269\|PubMed:27555320}.
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:0000250\|UniProtKB:Q6R3M4}.
Ptm:		Monoubiquitinated. Protein monoubiquitination prevents POLI binding to ubiquitin via the ubiquitin-binding motif 1 and ubiquitin- binding motif 2. {ECO:0000250\|UniProtKB:Q6R3M4}.
Similarity:		Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
Sequence caution:		Sequence=AAD50381.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAF63383.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAH32662.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAM11872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=CAB66605.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};