UniProt functional annotation for Q8IW19



	UniProt functional annotation for Q8IW19

UniProt code: Q8IW19.

Organism: Homo sapiens (Human).

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

Function: Nuclease involved in single-strand and double-strand DNA break repair (PubMed:17353262, PubMed:17396150). Recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post- translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions (PubMed:17353262, PubMed:17396150, PubMed:21211721). Displays apurinic- apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro. Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage (PubMed:17353262, PubMed:17396150). Together with PARP3, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (PubMed:21211721). {ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:21211721}.

Subunit: Interacts with LIG4, PARP1, XRCC1, XRCC4 and XRCC5. {ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:17507382, ECO:0000269|PubMed:18077224, ECO:0000269|PubMed:20098424}.

Subcellular location: Nucleus {ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:17507382}. Chromosome {ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:18474613, ECO:0000269|PubMed:21211721}. Cytoplasm, cytosol {ECO:0000269|PubMed:17353262}. Note=Localizes to DNA damage sites (PubMed:18474613, PubMed:18172500, PubMed:21211721). Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers (PubMed:18172500). {ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:18474613, ECO:0000269|PubMed:21211721}.

Domain: The PBZ-type zinc fingers (also named CYR) mediate non-covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the presence of zinc and promotes its recruitment to DNA damage sites. {ECO:0000269|PubMed:18172500}.

Domain: The FHA-like domain mediates interaction with XRCC1 and XRCC4. {ECO:0000269|PubMed:18172500}.

Ptm: Poly-ADP-ribosylated. In addition to binding non covalently poly(ADP-ribose) via its PBZ-type zinc fingers, the protein is also covalently poly-ADP-ribosylated by PARP1. {ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:18172500}.

Ptm: Phosphorylated in an ATM-dependent manner upon double-strand DNA break. {ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:17507382, ECO:0000269|PubMed:18077224}.

Similarity: Belongs to the APLF family. {ECO:0000305}.

Sequence caution: Sequence=AAY14945.1; Type=Erroneous initiation; 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:		Nuclease involved in single-strand and double-strand DNA break repair (PubMed:17353262, PubMed:17396150). Recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post- translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions (PubMed:17353262, PubMed:17396150, PubMed:21211721). Displays apurinic- apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro. Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage (PubMed:17353262, PubMed:17396150). Together with PARP3, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (PubMed:21211721). {ECO:0000269\|PubMed:17353262, ECO:0000269\|PubMed:17396150, ECO:0000269\|PubMed:21211721}.


Subunit:		Interacts with LIG4, PARP1, XRCC1, XRCC4 and XRCC5. {ECO:0000269\|PubMed:17353262, ECO:0000269\|PubMed:17396150, ECO:0000269\|PubMed:17507382, ECO:0000269\|PubMed:18077224, ECO:0000269\|PubMed:20098424}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:17353262, ECO:0000269\|PubMed:17396150, ECO:0000269\|PubMed:17507382}. Chromosome {ECO:0000269\|PubMed:18172500, ECO:0000269\|PubMed:18474613, ECO:0000269\|PubMed:21211721}. Cytoplasm, cytosol {ECO:0000269\|PubMed:17353262}. Note=Localizes to DNA damage sites (PubMed:18474613, PubMed:18172500, PubMed:21211721). Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers (PubMed:18172500). {ECO:0000269\|PubMed:18172500, ECO:0000269\|PubMed:18474613, ECO:0000269\|PubMed:21211721}.
Domain:		The PBZ-type zinc fingers (also named CYR) mediate non-covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the presence of zinc and promotes its recruitment to DNA damage sites. {ECO:0000269\|PubMed:18172500}.
Domain:		The FHA-like domain mediates interaction with XRCC1 and XRCC4. {ECO:0000269\|PubMed:18172500}.
Ptm:		Poly-ADP-ribosylated. In addition to binding non covalently poly(ADP-ribose) via its PBZ-type zinc fingers, the protein is also covalently poly-ADP-ribosylated by PARP1. {ECO:0000269\|PubMed:17396150, ECO:0000269\|PubMed:18172500}.
Ptm:		Phosphorylated in an ATM-dependent manner upon double-strand DNA break. {ECO:0000269\|PubMed:17353262, ECO:0000269\|PubMed:17507382, ECO:0000269\|PubMed:18077224}.
Similarity:		Belongs to the APLF family. {ECO:0000305}.
Sequence caution:		Sequence=AAY14945.1; Type=Erroneous initiation; Evidence={ECO:0000305};