{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q12888","secondaryAccessions":["F8VY86","Q2M1Z7","Q4LE46","Q5FWZ3","Q7Z3U4"],"uniProtkbId":"TP53B_HUMAN","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2000-12-01","entryVersion":246,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"TP53-binding protein 1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9748285"}],"value":"53BP1"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9748285"}],"value":"p53-binding protein 1"},{"value":"p53BP1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:11999"}],"value":"TP53BP1"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P70399"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12364621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17190600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21144835"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22553214"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23727112"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23760478"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27153538"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28241136"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31135337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37696958"}],"value":"Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11877378"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12110597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12364621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12607005"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15525939"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15574327"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16294047"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17190600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19650074"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20347427"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23727112"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23760478"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29651020"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29789392"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31135337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37696958"}],"value":"Homooligomer (PubMed:16294047, PubMed:23345425, PubMed:23760478). Interacts with p53/TP53 (via the central domain) (PubMed:11877378, PubMed:12110597). Interacts with DCLRE1C (PubMed:15574327). Interacts with histone H2AX and this requires phosphorylation of H2AX on 'Ser-139' (PubMed:12607005). Interacts with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2) (PubMed:17190600). Has low affinity for histone H4 containing monomethylated 'Lys-20' (H4K20me1) (PubMed:17190600). Does not bind histone H4 containing unmethylated or trimethylated 'Lys-20' (H4K20me3) (PubMed:17190600). Has low affinity for histone H3 that has been dimethylated on 'Lys-79' (PubMed:15525939). Has very low affinity for histone H3 that has been monomethylated on 'Lys-79' (in vitro) (PubMed:15525939). Does not bind unmethylated histone H3 (PubMed:15525939). Interacts with histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) (PubMed:23760478). Interacts with PWWP3A/EXPAND1 (PubMed:20347427). Interacts with CHEK2; modulates CHEK2 phosphorylation at 'Thr-68' in response to infrared (PubMed:12364621). Interacts with MSL1; this interaction may be required for MSL1 DNA repair activity, but not for histone acetyltransferase activity (PubMed:19650074). Interacts (when phosphorylated by ATM) with RIF1 (PubMed:23333306, PubMed:23727112, PubMed:28241136). Interacts (via the Tudor-like domain) with NUDT16L1/TIRR; interaction masks the Tudor-like domain and prevents recruitment to chromatin (PubMed:28241136). Interacts with PAXIP1 (PubMed:23727112). Interacts with SHLD2 (PubMed:29789392). Interacts (when phosphorylated) with TOPBP1 (PubMed:31135337). Interacts with GFI1; promoting methylation by PRMT1 (PubMed:29651020). Interacts with (phosphorylated) DYNLL1; specifically binds DYNLL1 phosphorylated at 'Ser-88' and promotes its recruitment to double strand breaks (DSBs) (PubMed:37696958)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19656881"}],"value":"(Microbial infection) Interacts (via C-terminus) with Epstein-Barr virus lytic switch protein BZLF1 (via C-terminus); this interaction is involved in the activation of the viral lytic cycle"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q49AR9","geneName":"ANKS1A","intActId":"EBI-11954519"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q13315","geneName":"ATM","intActId":"EBI-495465"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P13637","geneName":"ATP1A3","intActId":"EBI-948169"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P46379-2","geneName":"BAG6","intActId":"EBI-10988864"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P41182","geneName":"BCL6","intActId":"EBI-765407"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P38398","geneName":"BRCA1","intActId":"EBI-349905"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q5SWW7","geneName":"C10orf55","intActId":"EBI-12809220"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P55212","geneName":"CASP6","intActId":"EBI-718729"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q96HB5","geneName":"CCDC120","intActId":"EBI-744556"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q02930-3","geneName":"CREB5","intActId":"EBI-10192698"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"G5E9A7","geneName":"DMWD","intActId":"EBI-10976677"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"O75190-2","geneName":"DNAJB6","intActId":"EBI-12593112"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"O14645","geneName":"DNALI1","intActId":"EBI-395638"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P50570-2","geneName":"DNM2","intActId":"EBI-10968534"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P16104","geneName":"H2AX","intActId":"EBI-494830"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P62807","geneName":"H2BC8","intActId":"EBI-354552"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P68431","geneName":"H3C12","intActId":"EBI-79722"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P62805","geneName":"H4C9","intActId":"EBI-302023"},"numberOfExperiments":14,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"O14964","geneName":"HGS","intActId":"EBI-740220"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P10809","geneName":"HSPD1","intActId":"EBI-352528"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"O14901","geneName":"KLF11","intActId":"EBI-948266"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q96G42","geneName":"KLHDC7B","intActId":"EBI-9478422"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P13473-2","geneName":"LAMP2","intActId":"EBI-21591415"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P50222","geneName":"MEOX2","intActId":"EBI-748397"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q14686","geneName":"NCOA6","intActId":"EBI-78670"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q8TDS5","geneName":"OXER1","intActId":"EBI-12813389"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q6ZW49","geneName":"PAXIP1","intActId":"EBI-743225"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P16284","geneName":"PECAM1","intActId":"EBI-716404"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P78337","geneName":"PITX1","intActId":"EBI-748265"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q13393","geneName":"PLD1","intActId":"EBI-2827556"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P53350","geneName":"PLK1","intActId":"EBI-476768"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"A0A6Q8PF08","geneName":"PMP22","intActId":"EBI-50433196"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P78424","geneName":"POU6F2","intActId":"EBI-12029004"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"O75400-2","geneName":"PRPF40A","intActId":"EBI-5280197"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P62826","geneName":"RAN","intActId":"EBI-286642"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q86V20-2","geneName":"SHLD2","intActId":"EBI-20592761"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q7Z699","geneName":"SPRED1","intActId":"EBI-5235340"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"O43711","geneName":"TLX3","intActId":"EBI-3939165"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P04637","geneName":"TP53","intActId":"EBI-366083"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q5T6F2","geneName":"UBAP2","intActId":"EBI-2514383"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P61086","geneName":"UBE2K","intActId":"EBI-473850"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q08AM6","geneName":"VAC14","intActId":"EBI-2107455"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P23763-3","geneName":"VAMP1","intActId":"EBI-12097582"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P08670","geneName":"VIM","intActId":"EBI-353844"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q99986","geneName":"VRK1","intActId":"EBI-1769146"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"P04275-2","geneName":"VWF","intActId":"EBI-25896548"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"O43257","geneName":"ZNHIT1","intActId":"EBI-347522"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888","intActId":"EBI-396540"},"interactantTwo":{"uniProtKBAccession":"Q6NZQ4","geneName":"Paxip1","intActId":"EBI-1395317"},"numberOfExperiments":5,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q12888-1","intActId":"EBI-8022649"},"interactantTwo":{"uniProtKBAccession":"P62805","geneName":"H4C9","intActId":"EBI-302023"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888-1","intActId":"EBI-8022649"},"interactantTwo":{"uniProtKBAccession":"Q14686","geneName":"NCOA6","intActId":"EBI-78670"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888-1","intActId":"EBI-8022649"},"interactantTwo":{"uniProtKBAccession":"P63165","geneName":"SUMO1","intActId":"EBI-80140"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q12888-1","intActId":"EBI-8022649"},"interactantTwo":{"uniProtKBAccession":"P04637","geneName":"TP53","intActId":"EBI-366083"},"numberOfExperiments":17,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P70399"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17190600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23760478"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28241136"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37696958"}],"value":"Localizes to the nucleus in absence of DNA damage (PubMed:28241136). Following DNA damage, recruited to sites of DNA damage, such as double strand breaks (DSBs): recognizes and binds histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23333306, PubMed:23760478, PubMed:24703952, PubMed:28241136, PubMed:31135337, PubMed:37696958). Associated with kinetochores during mitosis (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11331310"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15525939"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16294045"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16294047"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17190600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19176521"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21144835"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28241136"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9748285"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12824158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15525939"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17190600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23760478"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24703952"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28241136"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31135337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37696958"}],"value":"Chromosome","id":"SL-0468"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P70399"}],"value":"Chromosome, centromere, kinetochore","id":"SL-0149"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q12888-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q12888-2"],"sequenceIds":["VSP_018390"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q12888-3"],"sequenceIds":["VSP_018390","VSP_055062"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17190600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28241136"}],"value":"The Tudor-like region mediates binding to histone H4 dimethylated at 'Lys-20' (H4K20me2) (PubMed:17190600). Interaction with NUDT16L1/TIRR masks the Tudor-like domain and prevents recruitment to chromatin (PubMed:28241136)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23760478"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24703952"}],"value":"The UDR (ubiquitin-dependent recruitment) motif specifically recognizes and binds histone H2A monoubiquitinated at 'Lys-15' (H2AK15ub) (PubMed:23760478, PubMed:24703952). Phosphorylation of the UDR blocks interaction with H2AK15ub (PubMed:24703952)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16294045"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16294047"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29651020"}],"value":"Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11042216"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11331310"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17553757"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19176521"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21144835"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23727112"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24703952"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28241136"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31135337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31527692"}],"value":"Phosphorylated at basal level in the absence of DNA damage (PubMed:11042216, PubMed:11331310). 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In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-29; A-105; A-166; A-176 and A-178.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23727112"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-105; A-166; A-176 and A-178.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23727112"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-166; A-176 and A-178.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23727112"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-176 and A-178.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23727112"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"Loss of phosphorylation site.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17553757"}],"alternativeSequence":{"originalSequence":"SQS","alternativeSequences":["AQA"]}},{"type":"Mutagenesis","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-166 and A-178.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23727112"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-166 and A-176.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23727112"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"Decreased interaction with TOPBP1.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31135337"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":437,"modifier":"EXACT"},"end":{"value":437,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":452,"modifier":"EXACT"},"end":{"value":452,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":523,"modifier":"EXACT"},"end":{"value":523,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":543,"modifier":"EXACT"},"end":{"value":543,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":580,"modifier":"EXACT"},"end":{"value":580,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":625,"modifier":"EXACT"},"end":{"value":625,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":670,"modifier":"EXACT"},"end":{"value":670,"modifier":"EXACT"}},"description":"Decreased interaction with TOPBP1.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31135337"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":674,"modifier":"EXACT"},"end":{"value":674,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":696,"modifier":"EXACT"},"end":{"value":696,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":698,"modifier":"EXACT"},"end":{"value":698,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":784,"modifier":"EXACT"},"end":{"value":784,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":831,"modifier":"EXACT"},"end":{"value":831,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":855,"modifier":"EXACT"},"end":{"value":855,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":892,"modifier":"EXACT"},"end":{"value":892,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":1068,"modifier":"EXACT"},"end":{"value":1068,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1086; A-1104; A-1148; A-1171 and A-1219.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23333306"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23345425"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":1086,"modifier":"EXACT"},"end":{"value":1086,"modifier":"EXACT"}},"description":"In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; 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