TP53BP1
entrez
7158
canonical
uniprot
Q12888
canonical
ensembl
ENSG00000067369
resolver
ensp
ENSP00000263801
resolver
ensp
ENSP00000371470
resolver
ensp
ENSP00000371475
resolver
ensp
ENSP00000388028
resolver
ensp
ENSP00000393497
resolver
ensp
ENSP00000756707
resolver
enst
ENST00000382039
resolver
genesymbol
TP53BP1
resolver
hgnc
HGNC:11999
resolver
uniprot
A6NNK5
resolver
uniprot
F8VY86
resolver
uniprot
Q2M1Z7
resolver
uniprot
Q4LE46
resolver
uniprot
Q5FWZ3
resolver
uniprot
Q7Z3U4
resolver
uniprot_entry
A6NNK5_HUMAN
resolver
uniprot_entry
TP53B_HUMAN
resolver
uniprot_sec
F8VY86
resolver
uniprot_sec
Q2M1Z7
resolver
uniprot_sec
Q4LE46
resolver
uniprot_sec
Q5FWZ3
resolver
uniprot_sec
Q7Z3U4
resolver
amino_acid_sequence
MDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEDDSGSHFSMLSRHLPNLQTHKENPVLDVVSNPEQTAGEERGDGNSGFNEHLKENKVADPVDSSNLDTCGSISQVIEQLPQPNRTSSVLGMSVESAPAVEEEKGEELEQKEKEKEEDTSGNTTHSLGAEDTASSQLGFGVLELSQSQDVEENTVPYEVDKEQLQSVTTNSGYTRLSDVDANTAIKHEEQSNEDIPIAEQSSKDIPVTAQPSKDVHVVKEQNPPPARSEDMPFSPKASVAAMEAKEQLSAQELMESGLQIQKSPEPEVLSTQEDLFDQSNKTVSSDGCSTPSREEGGCSLASTPATTLHLLQLSGQRSLVQDSLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQEGRQDKPMDTSVLSEEGGEPFQKKLQSGEPVELENPPLLPESTVSPQASTPISQSTPVFPPGSLPIPSQPQFSHDIFIPSPSLEEQSNDGKKDGDMHSSSLTVECSKTSEIEPKNSPEDLGLSLTGDSCKLMLSTSEYSQSPKMESLSSHRIDEDGENTQIEDTEPMSPVLNSKFVPAENDSILMNPAQDGEVQLSQNDDKTKGDDTDTRDDISILATGCKGREETVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMEIKEHHPEEGSSGSEVEEIPETPCESQGEELKEENMESVPLHLSLTETQSQGLCLQKEMPKKECSEAMEVETSVISIDSPQKLAILDQELEHKEQEAWEEATSEDSSVVIVDVKEPSPRVDVSCEPLEGVEKCSDSQSWEDIAPEIEPCAENRLDTKEEKSVEYEGDLKSGTAETEPVEQDSSQPSLPLVRADDPLRLDQELQQPQTQEKTSNSLTEDSKMANAKQLSSDAEAQKLGKPSAHASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVMSESMVETHDPILGSGKGDSGAAPDVDDKLCLRMKLVSPETEASEESLQFNLEKPATGERKNGSTAVAESVASPQKTMSVLSCICEARQENEARSEDPPTTPIRGNLLHFPSSQGEEEKEKLEGDHTIRQSQQPMKPISPVKDPVSPASQKMVIQGPSSPQGEAMVTDVLEDQKEGRSTNKENPSKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEFDMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSLHRTSSGTSLSAMHSSGSSGKGAGPLRGKTSGTEPADFALPSSRGGPGKLSPRKGVSQTGTPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETAVPGPLGIEDISPNLSPDDKSFSRVVPRVPDSTRRTDVGAGALRRSDSPEIPFQAAAGPSDGLDASSPGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNVSSPATPTASSSSSTTPTRKITESPRASMGVLSGKRKLITSEEERSPAKRGRKSATVKPGAVGAGEFVSPCESGDNTGEPSALEEQRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLPDGPTGSSEEEEEFLEIPPFNKQYTESQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving TP53BP1 is found in a form of myeloproliferative disorder chronic with eosinophilia. Translocation t(5;15)(q33;q22) with PDGFRB creating a TP53BP1-PDGFRB fusion protein. {ECO:0000269|PubMed:15492236}.
uniprot
proteins
function
FUNCTION: 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). {ECO:0000250|UniProtKB:P70399, ECO:0000269|PubMed:12364621, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:22553214, ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112, ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:31135337, ECO:0000269|PubMed:37696958}.
uniprot
proteins
mass_dalton
213574
uniprot
proteins
mutagenesis
MUTAGEN 6; /note="S->A: In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with 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-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-13; A-25; A-29; A-105; A-166; A-176 and A-178."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112"; MUTAGEN 13; /note="S->A: 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-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-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-25; A-29; A-105; A-166; A-176 and A-178."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112"; MUTAGEN 25; /note="S->A: 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-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-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-29; A-105; A-166; A-176 and A-178."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112"; MUTAGEN 29; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112"; MUTAGEN 105; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112"; MUTAGEN 166; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112"; MUTAGEN 176..178; /note="SQS->AQA: Loss of phosphorylation site."; /evidence="ECO:0000269|PubMed:17553757"; MUTAGEN 176; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112"; MUTAGEN 178; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23727112"; MUTAGEN 302; /note="T->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 366; /note="S->A: Decreased interaction with TOPBP1."; /evidence="ECO:0000269|PubMed:31135337"; MUTAGEN 437; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 452; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 523; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 543; /note="T->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 580; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 625; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 670; /note="T->A: Decreased interaction with TOPBP1."; /evidence="ECO:0000269|PubMed:31135337"; MUTAGEN 674; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 696; /note="T->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 698; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 784; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 831; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 855; /note="T->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 892; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 1068; /note="S->A: 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."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 1086; /note="S->A: 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-1068; A-1104; A-1148; A-1171 and A-1219."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 1104; /note="S->A: 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-1068; A-1086; A-1148; A-1171 and A-1219."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 1148; /note="S->A: 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-1068; A-1086; A-1104; A-1171 and A-1219."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 1171; /note="T->A: 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-1068; A-1086; A-1104; A-1148 and A-1219."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 1219; /note="S->A: 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-1068; A-1086; A-1104; A-1148 and A-1171."; /evidence="ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23345425"; MUTAGEN 1268; /note="K->R: Does not affect monoubiquitination by MSL2."; /evidence="ECO:0000269|PubMed:23874665"; MUTAGEN 1396; /note="R->A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1398; A-1400; A-1401 and A-1403."; /evidence="ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047"; MUTAGEN 1396; /note="R->K: No detectable effect on methylation by PRMT1 (in vitro)."; /evidence="ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047"; MUTAGEN 1398..1401; /note="RGRR->AGAA: No effect on in class-switch recombination (CSR)."; /evidence="ECO:0000269|PubMed:23345425"; MUTAGEN 1398; /note="R->A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1400; A-1401 and A-1403."; /evidence="ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047"; MUTAGEN 1398; /note="R->K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1400. Strongly reduced methylation; when associated with K-1401."; /evidence="ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047"; MUTAGEN 1400; /note="R->A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1401 and A-1403."; /evidence="ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047"; MUTAGEN 1400; /note="R->K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1401."; /evidence="ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047"; MUTAGEN 1401; /note="R->A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1400 and A-1403."; /evidence="ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047"; MUTAGEN 1401; /note="R->K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1400."; /evidence="ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047"; MUTAGEN 1403; /note="R->A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1400 and A-1401."; /evidence="ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047"; MUTAGEN 1403; /note="R->K: No detectable effect on methylation by PRMT1 (in vitro)."; /evidence="ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047"; MUTAGEN 1495; /note="W->A,H: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks. Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks; when associated with A-1521."; /evidence="ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:28241136"; MUTAGEN 1495; /note="W->F: No effect on recruitment to double strand breaks."; /evidence="ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:17190600"; MUTAGEN 1495; /note="W->V: Reduces recruitment to double strand breaks."; /evidence="ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:17190600"; MUTAGEN 1500; /note="Y->A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'."; /evidence="ECO:0000269|PubMed:17190600"; MUTAGEN 1502; /note="Y->A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'."; /evidence="ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:17190600"; MUTAGEN 1502; /note="Y->L,Q: Abolishes recruitment to double strand breaks."; /evidence="ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:17190600"; MUTAGEN 1521; /note="D->A: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks. Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks; when associated with A-1495."; /evidence="ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:28241136"; MUTAGEN 1521; /note="D->R: Abolishes recruitment to double strand breaks and induces defects in class-switch recombination (CSR)."; /evidence="ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:23345425, ECO:0000269|PubMed:23760478"; MUTAGEN 1523; /note="Y->A: Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks."; /evidence="ECO:0000269|PubMed:17190600"; MUTAGEN 1523; /note="Y->S: Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'."; /evidence="ECO:0000269|PubMed:17190600"; MUTAGEN 1563; /note="K->R: Does not affect monoubiquitination by MSL2."; /evidence="ECO:0000269|PubMed:23874665"; MUTAGEN 1609; /note="T->A: Constitutive recruitment to mitotic DNA lesions, leading to mitotic defects; when associated with A-1618."; /evidence="ECO:0000269|PubMed:24703952"; MUTAGEN 1609; /note="T->E: Phosphomimetic mutant that abolishes recruitment to double strand breaks; when associated with D-1618."; /evidence="ECO:0000269|PubMed:24703952"; MUTAGEN 1613; /note="K->A: Does not affect recruitment to double strand breaks."; /evidence="ECO:0000269|PubMed:23760478"; MUTAGEN 1616; /note="D->A: Does not affect recruitment to double strand breaks."; /evidence="ECO:0000269|PubMed:23760478"; MUTAGEN 1617; /note="I->A: Strongly reduced recruitment to double strand breaks. Defects in class-switch recombination (CSR)."; /evidence="ECO:0000269|PubMed:23760478"; MUTAGEN 1618; /note="S->A: Constitutive recruitment to mitotic DNA lesions, leading to mitotic defects; when associated with A-1609."; /evidence="ECO:0000269|PubMed:24703952"; MUTAGEN 1618; /note="S->D: Phosphomimetic mutant that abolishes recruitment to double strand breaks; when associated with E-1609."; /evidence="ECO:0000269|PubMed:24703952"; MUTAGEN 1619; /note="L->A: Strongly reduced recruitment to double strand breaks. Defects in class-switch recombination (CSR). Does not affect interaction with histone H4 dimethylated at 'Lys-20' (H4K20me2). Impaired interaction with histone H2A monoubiquitinated at 'Lys-15' (H2AK15ub)."; /evidence="ECO:0000269|PubMed:23760478"; MUTAGEN 1621; /note="N->A: Reduced recruitment to double strand breaks."; /evidence="ECO:0000269|PubMed:23760478"; MUTAGEN 1622; /note="L->A: Reduced recruitment to double strand breaks."; /evidence="ECO:0000269|PubMed:23760478"; MUTAGEN 1624; /note="E->A: Does not affect recruitment to double strand breaks."; /evidence="ECO:0000269|PubMed:23760478"; MUTAGEN 1627; /note="R->A: Reduced recruitment to double strand breaks."; /evidence="ECO:0000269|PubMed:23760478"; MUTAGEN 1685; /note="K->R: Abolished monoubiquitination by MSL2."; /evidence="ECO:0000269|PubMed:23874665
uniprot
proteins
post_translational_modification
PTM: Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding. {ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047, ECO:0000269|PubMed:29651020}.; PTM: Phosphorylated at basal level in the absence of DNA damage (PubMed:11042216, PubMed:11331310). Phosphorylated by ATM in response to DNA damage: phosphorylation at different sites promotes interaction with different set of proteins: phosphorylation at the N-terminus by ATM (residues from 6-178) promotes interaction with PAXIP1 and non-homologous end joining (NHEJ) of dysfunctional telomeres (PubMed:23727112). Phosphorylation by ATM at residues that are located more C-terminus (residues 300-650) leads to promote interaction with RIF1 (PubMed:23333306, PubMed:23727112, PubMed:28241136). Interaction with RIF1 leads to disrupt interaction with NUDT16L1/TIRR (PubMed:28241136). Phosphorylation at Thr-1609 and Ser-1618 in the UDR motif blocks interaction with H2AK15ub (PubMed:24703952). Dephosphorylated by PPP4C (PubMed:24703952). Hyperphosphorylation during mitosis correlates with its exclusion from chromatin and DNA lesions. Hyperphosphorylated in an ATR-dependent manner in response to DNA damage induced by UV irradiation (PubMed:17553757, PubMed:21144835). Dephosphorylated by PPP5C (PubMed:19176521). Phosphorylation at Ser-366 and Thr-670 promotes interaction with TOPBP1 (PubMed:31135337). Phosphorylated by VRK1 (PubMed:31527692). {ECO:0000269|PubMed:11042216, ECO:0000269|PubMed:11331310, ECO:0000269|PubMed:17553757, ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23727112, ECO:0000269|PubMed:24703952, ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:31135337, ECO:0000269|PubMed:31527692}.; PTM: Monoubiquitinated at Lys-1685 by MSL2 in response to DNA damage, leading to its stabilization. {ECO:0000269|PubMed:23874665}.
uniprot
proteins
pubmed
11042216
uniprot
proteins
pubmed
11331310
uniprot
proteins
pubmed
11877378
uniprot
proteins
pubmed
12110597
uniprot
proteins
pubmed
12364621
uniprot
proteins
pubmed
12607005
uniprot
proteins
pubmed
12824158
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15492236
uniprot
proteins
pubmed
15525939
uniprot
proteins
pubmed
15574327
uniprot
proteins
pubmed
16294045
uniprot
proteins
pubmed
16294047
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17190600
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17553757
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19176521
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19650074
uniprot
proteins
pubmed
19656881
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20347427
uniprot
proteins
pubmed
21144835
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22553214
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23333306
uniprot
proteins
pubmed
23345425
uniprot
proteins
pubmed
23727112
uniprot
proteins
pubmed
23760478
uniprot
proteins
pubmed
23874665
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24703952
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
27153538
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28241136
uniprot
proteins
pubmed
29651020
uniprot
proteins
pubmed
29789392
uniprot
proteins
pubmed
31135337
uniprot
proteins
pubmed
31527692
uniprot
proteins
pubmed
37696958
uniprot
proteins
pubmed
8016121
uniprot
proteins
pubmed
9748285
uniprot
proteins
sequence_length
1972
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11331310, ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16294047, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:9748285}. Chromosome {ECO:0000269|PubMed:12824158, ECO:0000269|PubMed:15525939, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:24703952, ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:31135337, ECO:0000269|PubMed:37696958}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P70399}. Note=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). {ECO:0000250|UniProtKB:P70399, ECO:0000269|PubMed:17190600, ECO:0000269|PubMed:23333306, ECO:0000269|PubMed:23760478, ECO:0000269|PubMed:28241136, ECO:0000269|PubMed:37696958}.
uniprot
proteins