| S.NO | Uniprot ID | Protein Name | Sequence Length | BRCT Region | Mutation | Involvement of Repeats in Mutations |
| 1 | P38398 | Breast cancer type 1 susceptibility protein | 1863 | 26 26 I->A: Disrupts the interaction with E2 enzymes, thereby abolishing the E3 ubiquitin-protein ligase activity 26 26 I->E: No ubiquitination of RBBP8 71 71 R->G: No effect on interaction with BAP1 308 308 S->N: Abolishes phosphorylation by AURKA and interferes with cell cycle progression from G2 to mitosis 1143 1143 S->A: Reduces in vitro phosphorylation by ATR 1239 1239 S->A: No effect on in vitro phosphorylation by ATR 1280 1280 S->A: Reduces in vitro phosphorylation by ATR 1298 1298 S->A: No effect on in vitro phosphorylation by ATR 1330 1330 S->A: No effect on in vitro phosphorylation by ATR 1387 1387 S->A: Loss of IR-induced S-phase checkpoint 1394 1394 T->A: Reduces in vitro phosphorylation by ATR 1423 1423 S->A: Inhibition of the infrared-induced G2 arrest 1457 1457 S->A: Reduces in vitro phosphorylation by ATR 1466 1466 S->A: No effect on in vitro phosphorylation by ATR 1524 1524 S->A: No change in infrared S-phase delay when associated with A-1387 1655 1655 S->A: Abolishes interaction with BRIP1 1656 1656 G->D: No effect on affinity for a BRIP1 phosphopeptide 1662 1662 F->S: Does not abolish ABRAXAS1 binding, but abolishes formation of a heterotetramer with ABRAXAS1 1663 1663 M->K: Does not abolish ABRAXAS1 binding, but abolishes formation of a heterotetramer with ABRAXAS1 1666 1666 Y->A: Does not abolish ABRAXAS1 binding, but impairs formation of a heterotetramer with ABRAXAS1 1670 1670 R->E: Impairs formation of a heterotetramer with ABRAXAS1 1671 1671 K->E: Impairs formation of a heterotetramer with ABRAXAS1 1700 1700 T->A: Strongly reduces affinity for a BRIP1 phosphopeptide 1702 1702 K->M: Abolishes interaction with BRIP1 1738 1738 G->E: Abolishes interaction with BRIP1 1755 1755 S->A: No effect on in vitro phosphorylation by ATR 1835 1835 R->P: Mildly reduces affinity for a BRIP1 phosphopeptide 1836 1836 E->K: Slightly reduces affinity for a BRIP1 phosphopeptide | Y | |
| 2 | Q9H8V3 | Protein ECT2 | 914 | 184 184 T->A: Inhibits interaction with RACGAP1 226 226 K->A: Inhibits interaction with RACGAP1 336 336 W->R: Inhibits homodimerization 359 359 T->A: Inhibits its phosphorylation and anchorage-independent growth and invasion in cancer cells 373 373 T->A: Does not inhibit its Rho exchange activity 373 373 T->D: Does not inhibit subcellular localization or homodimerization 379 381 379 381 KRR->AAA: Shows both nuclear and cytoplasmic localization and activates its transforming activity 402 404 402 404 RKR->AKA: Shows both nuclear and cytoplasmic localization and activates its transforming activity 444 444 T->A: Diminishes its phosphorylation status 444 444 T->D: Does not reduce its interaction with PLK1, change its subcellular localization and Rho exchange activity 596 599 596 599 PVQR->AAAA: Inhibits activation of the transforming activity 846 846 T->A: Diminishes its phosphorylation status | Y | |
| 3 | Q12888 | TP53-binding protein 1 | 1972 | 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-178 176 178 176 178 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 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 | N | |
| 4 | Q14676 | Mediator of DNA damage checkpoint protein 1 | 2089 | 58 58 R->A: Abrogates binding to the MRE11 complex and to CHEK2 72 72 S->A: Abrogates binding to CHEK2 96 96 N->A: Abrogates binding to CHEK2 when associated with A-97 and A-98 97 97 G->A: Abrogates binding to CHEK2 when associated with A-96 and A-98 98 98 T->A: Abrogates binding to CHEK2 when associated with A-96 and A-97 1840 1840 K->R: Suppresses RNF4-mediated ubiquitination, accumulates at sites of DNA damage, defective homologous recombination | N | |
| 5 | Q6ZW49 | PAX-interacting protein 1 | 1069 | 676 676 W->A: Abolishes interaction with TP53BP1 prevents recruitment to DNA damage foci 910 910 R->Q: Abolishes interaction with TP53BP1 impairs intact cellular response to DNA damage 929 929 W->A: Abolishes interaction with TP53BP1 prevents recruitment to DNA damage foci | Y |