{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8K0Y7","secondaryAccessions":["Q8C6V7"],"uniProtkbId":"PAXX_MOUSE","entryAudit":{"firstPublicDate":"2007-05-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2002-10-01","entryVersion":121,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein PAXX"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29511619"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29511621"}],"value":"Paralog of XRCC4 and XLF"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29511619"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29511621"}],"value":"Paxx"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BUH6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27601299"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27601633"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27798842"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27830975"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28051062"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29077092"}],"value":"Non-essential DNA repair protein involved in DNA non-homologous end joining (NHEJ); participates in double-strand break (DSB) repair and V(D)J recombination (PubMed:27601299, PubMed:27601633, PubMed:27798842, PubMed:27830975, PubMed:28051062, PubMed:29077092). May act as a scaffold required for accumulation of the Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at double-strand break sites and promote the assembly and/or stability of the NHEJ machinery (PubMed:28051062). Involved in NHEJ by promoting the ligation of blunt-ended DNA ends (By similarity). Together with NHEJ1/XLF, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends (By similarity). Constitutes a non-essential component of classical NHEJ: has a complementary but distinct function with NHEJ1/XLF in DNA repair (PubMed:27601299, PubMed:27798842, PubMed:27830975, PubMed:28051062)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BUH6"}],"value":"Homodimer (By similarity). Interacts with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer (Ku complex); the interaction is direct (By similarity). Associated component of the non-homologous end joining (NHEJ) complex, composed of the core proteins PRKDC, LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (By similarity). Interacts with POLL (DNA polymerase lambda); promoting POLL recruitment to double-strand breaks (DSBs) and stimulation of the end-filling activity of POLL (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BUH6"}],"value":"Predominantly localizes to the nucleus. Accumulates at sites of DNA damage generated by laser microirradiation"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BUH6"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BUH6"}],"value":"Chromosome","id":"SL-0468"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BUH6"}],"value":"The N-terminus (residues 1-115) forms a head domain that is structurally related to those of XRCC4, XLF/NHEJ1, and SASS6"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9BUH6"}],"value":"Phosphorylation may inhibit interaction with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer (Ku complex)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27601299"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27601633"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27798842"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27830975"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28051062"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29077092"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29511619"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29511621"}],"value":"No visible phenotype in normal conditions (PubMed:27798842, PubMed:28051062, PubMed:29511619, PubMed:29511621). Mice are viable, grow normally, are fertile and have normal lymphocyte development (PubMed:27798842, PubMed:29511619, PubMed:29511621). They however show mild radiosensitivity (PubMed:29511619, PubMed:29511621). Mice lacking both Paxx and Nhej1/Xlf show embryonic lethality caused by severe defects in classical non-homologous end joining (NHEJ) (PubMed:27601299, PubMed:27601633, PubMed:27798842, PubMed:27830975, PubMed:28051062, PubMed:29077092)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the XRCC4-XLF family. 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