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Q12888 Proteins BRCT domain Repeats
Uniprot ID:Q12888
Protein name: TP53-binding protein 1
Gene : TP53BP1
Protein Family:
Squence Length : 1972
Sequnce
>Q12888 1973 MDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEDDSGSHFSMLSRHLPNLQTHKENPVLDVVSNPEQTAGEERGDGNSGFNEHLKENKVADPVDSSNLDTCGSISQVIEQLPQPNRTSSVLGMSVESAPAVEEEKGEELEQKEKEKEEDTSGNTTHSLGAEDTASSQLGFGVLELSQSQDVEENTVPYEVDKEQLQSVTTNSGYTRLSDVDANTAIKHEEQSNEDIPIAEQSSKDIPVTAQPSKDVHVVKEQNPPPARSEDMPFSPKASVAAMEAKEQLSAQELMESGLQIQKSPEPEVLSTQEDLFDQSNKTVSSDGCSTPSREEGGCSLASTPATTLHLLQLSGQRSLVQDSLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQEGRQDKPMDTSVLSEEGGEPFQKKLQSGEPVELENPPLLPESTVSPQASTPISQSTPVFPPGSLPIPSQPQFSHDIFIPSPSLEEQSNDGKKDGDMHSSSLTVECSKTSEIEPKNSPEDLGLSLTGDSCKLMLSTSEYSQSPKMESLSSHRIDEDGENTQIEDTEPMSPVLNSKFVPAENDSILMNPAQDGEVQLSQNDDKTKGDDTDTRDDISILATGCKGREETVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMEIKEHHPEEGSSGSEVEEIPETPCESQGEELKEENMESVPLHLSLTETQSQGLCLQKEMPKKECSEAMEVETSVISIDSPQKLAILDQELEHKEQEAWEEATSEDSSVVIVDVKEPSPRVDVSCEPLEGVEKCSDSQSWEDIAPEIEPCAENRLDTKEEKSVEYEGDLKSGTAETEPVEQDSSQPSLPLVRADDPLRLDQELQQPQTQEKTSNSLTEDSKMANAKQLSSDAEAQKLGKPSAHASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVMSESMVETHDPILGSGKGDSGAAPDVDDKLCLRMKLVSPETEASEESLQFNLEKPATGERKNGSTAVAESVASPQKTMSVLSCICEARQENEARSEDPPTTPIRGNLLHFPSSQGEEEKEKLEGDHTIRQSQQPMKPISPVKDPVSPASQKMVIQGPSSPQGEAMVTDVLEDQKEGRSTNKENPSKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEFDMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSLHRTSSGTSLSAMHSSGSSGKGAGPLRGKTSGTEPADFALPSSRGGPGKLSPRKGVSQTGTPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETAVPGPLGIEDISPNLSPDDKSFSRVVPRVPDSTRRTDVGAGALRRSDSPEIPFQAAAGPSDGLDASSPGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNVSSPATPTASSSSSTTPTRKITESPRASMGVLSGKRKLITSEEERSPAKRGRKSATVKPGAVGAGEFVSPCESGDNTGEPSALEEQRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLPDGPTGSSEEEEEFLEIPPFNKQYTESQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH
Domains
DOMAIN 1724 1848 BRCT 1 DOMAIN 1864 1964 BRCT 2
BRCT sequence regions
1724 - 1848 KTLFLGYAFLLTMATTSDKLASRSKLPDGPTGSSEEEEEFLEIPPFNKQYTESQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPA 1864 - 1964 ENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYK
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:22553214, PubMed:23333306, PubMed:17190600, PubMed:21144835, PubMed:28241136). 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:23727112, PubMed:23333306). 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:23760478, PubMed:28241136, PubMed:17190600). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates to 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)"
Motifs
MOTIF 1396 1403 GAR. MOTIF 1604 1631 UDR
Mutation
"6 6 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 when associated with A-13 A-25 A-29 A-105 A-166 A-176 and A-178 13 13 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 when associated with A-6 A-25 A-29 A-105 A-166 A-176 and A-178 25 25 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 when associated with A-6 A-13 A-29 A-105 A-166 A-176 and A-178 29 29 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 when associated with A-6 A-13 A-25 A-105 A-166 A-176 and A-178 105 105 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 when associated with A-6 A-13 A-25 A-29 A-166 A-176 and A-178 166 166 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 when associated with A-6 A-13 A-25 A-29 A-105 A-176 and A-178 176 178 SQS->AQA: Loss of phosphorylation site 176 176 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 when associated with A-6 A-13 A-25 A-29 A-105 A-166 and A-178 178 178 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 when associated with A-6 A-13 A-25 A-29 A-105 A-166 and A-176 302 302 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 437 437 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 452 452 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 523 523 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 543 543 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 580 580 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 625 625 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 674 674 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 696 696 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 698 698 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 784 784 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 831 831 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 855 855 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 892 892 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 1068 1068 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 1086 1086 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 1104 1104 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 1148 1148 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 1171 1171 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 1219 1219 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 1396 1396 R->A: No detectable effect on methylation by PRMT1 (in vitro) when associated with A-1398 A-1400 A-1401 and A-1403 1396 1396 R->K: No detectable effect on methylation by PRMT1 (in vitro) 1398 1401 RGRR->AGAA: No effect on in class-switch recombination (CSR) 1398 1398 R->A: No detectable effect on methylation by PRMT1 (in vitro) when associated with A-1396 A-1400 A-1401 and A-1403 1398 1398 R->K: Reduced methylation by PRMT1 (in vitro) when associated with K-1400 when associated with K-1401 1400 1400 R->A: No detectable effect on methylation by PRMT1 (in vitro) when associated with A-1396 A-1398 A-1401 and A-1403 1400 1400 R->K: Reduced methylation by PRMT1 (in vitro) when associated with K-1398 when associated with K-1401 1401 1401 R->A: No detectable effect on methylation by PRMT1 (in vitro) when associated with A-1396 A-1398 A-1400 and A-1403 1401 1401 R->K: Reduced methylation by PRMT1 (in vitro) when associated with K-1398 when associated with K-1400 1403 1403 R->A: No detectable effect on methylation by PRMT1 (in vitro) when associated with A-1396 A-1398 A-1400 and A-1401 1403 1403 R->K: No detectable effect on methylation by PRMT1 (in vitro) 1495 1495 W->A,H: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2) when associated with A-1521 1495 1495 W->F: No effect on recruitment to double strand breaks 1495 1495 W->V: Reduces recruitment to double strand breaks 1500 1500 Y->A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20' 1502 1502 Y->A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20' 1502 1502 Y->L,Q: Abolishes recruitment to double strand breaks 1521 1521 D->A: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2) when associated with A-1495 1521 1521 D->R: Abolishes recruitment to double strand breaks and induces defects in class-switch recombination (CSR) 1523 1523 Y->A: Increases affinity for histone H4 that has been dimethylated at 'Lys-20' 1523 1523 Y->S: Decreases affinity for histone H4 that has been dimethylated at 'Lys-20' 1609 1609 T->A: Constitutive recruitment to mitotic DNA lesions, leading to mitotic defects when associated with A-1618 1609 1609 T->E: Phosphomimetic mutant that abolishes recruitment to double strand breaks when associated with D-1618 1613 1613 K->A: Does not affect recruitment to double strand breaks 1616 1616 D->A: Does not affect recruitment to double strand breaks 1617 1617 I->A: Strongly reduced recruitment to double strand breaks 1618 1618 S->A: Constitutive recruitment to mitotic DNA lesions, leading to mitotic defects when associated with A-1609 1618 1618 S->D: Phosphomimetic mutant that abolishes recruitment to double strand breaks when associated with E-1609 1619 1619 L->A: Strongly reduced recruitment to double strand breaks 1621 1621 N->A: Reduced recruitment to double strand breaks 1622 1622 L->A: Reduced recruitment to double strand breaks 1624 1624 E->A: Does not affect recruitment to double strand breaks 1627 1627 R->A: Reduced recruitment to double strand breaks"
Disease
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