HDR through Homologous Recombination or Single Strand Annealing (Homo sapiens)

From WikiPathways

Jump to: navigation, search
5217, 18, 6727, 70, 76, 118, 139...28, 31, 63, 83, 104...13, 15478, 1202, 7, 8, 21, 43...5, 142, 1698282, 93, 12723, 75, 110997857, 73, 13820, 24, 30, 37, 41...3710, 784, 53, 59, 69, 72...2561, 1531315232, 137535, 40, 42, 58, 116...16, 44, 51, 94, 111...52114, 12419, 34, 45, 64, 101...12, 38, 54, 68, 74...57, 13819, 36, 56, 70, 76...1451357, 86, 108, 125, 130...6132, 135, 13757, 13891, 139, 14771, 794, 69, 77, 109, 1284, 22, 48, 15549, 58, 100, 1697, 8, 43, 65, 80...9, 29, 53, 95, 121...nucleoplasmcytosolSPIDRCCNA1 RMI1 RFC3 DNA2 POLD4 p-S990,Ac-K1249-BRIP1 RPA2 SLX1A p-T714,T734-BARD1 p-T3387-BRCA2:p-T309-RAD51 complexRPA3 K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 WRN RMI1 p-T714,T734-BARD1 K6PolyUb,p-T714,T734-BARD1 RAD51C p-S1981,Ac-K3016-ATM RMI1 DNA2 RMI1 SLX1A:SLX4:MUS81:EME1,(MUS81:EME2)EXO1 RAD51C KAT5 p-S327,T847,T859-RBBP8 p-S1981,Ac-K3016-ATM RNF8:Zn2+ATR K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 dsDNA with crossoverp-S343-NBN K63PolyUb-K14,K16,p-S140-H2AFX RAD51B ADPRFC2 RAD50 DNA2 p-S343-NBN MRE11A DNA double-strand break ends RMI1 RHNO1 MRE11A MRE11A CX3 complexp-S1981,Ac-K3016-ATM RAD51:p-Y104-RAD52:p-RPA:ATR:ATRIP:DNA DSBs with annealed 3' ssDNA overhangs and displaced flaps:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1p-Y104-RAD52 BRE HIST1H2BO 3' overhanging DNA at resected DSB ends TOP3A MRE11A RAD1 XRCC2 RAD50 DNA2 K6PolyUb,p-T714,T734-BARD1 RFC5 p-S1981,Ac-K3016-ATM HIST1H2BL TOP3A MRE11A MRE11A p-T714,T734-BARD1 UBC(457-532) ADPRAD50 H2Op-T3387-BRCA2 XRCC3 HUS1 PALB2 RFC5 RPA3 p-S1981,Ac-K3016-ATM p-T714,T734-BARD1 POLD2 RAD51D WRN RMI2 UBA52(1-76) RAD51D UBE2V2 p-S343-NBN p-S343-NBN p-S990,Ac-K1249-BRIP1 p-T714,T734-BARD1 RAD1 p-S988,S1387,S1423,S1524,S1547-BRCA1 MRE11A p-S990,Ac-K1249-BRIP1 3' overhanging DNA at resected DSB ends MRE11A RMI2 POLD3 RMI1 p-S988,S1387,S1423,S1524,S1547-BRCA1 p-S327,T847-RBBP8 RPA3 3' overhanging DNA at resected DSB ends RAD50 p-S343-NBN EXO1 p-T714,T734-BARD1 p-T309-RAD51 RPA1 Zn2+ MRE11A p-T714,T734-BARD1 p-S988,S1387,S1423,S1524,S1547-BRCA1 RAD51C p-S343-NBN p-S1981,Ac-K3016-ATM RFC3 KAT5 RPA1 NAMp-S33-RPA2 DNA2 SLX1A UIMC1HIST1H2BD RAD50 ATRIP KAT53'overhangingssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-T309-RAD51:p-T3387-BRCA2p-S327,T847,T859-RBBP8 K6PolyUb,p-T714,T734-BARD1 RAD9A RMI1 p-T714,T734-BARD1 RAD51BRAD51C ATR KAT5 HIST1H2BN 3' overhanging DNA at resected DSB ends FlapBLM EME1 CX3 complexSUMO1:p-T4827-HERC2p-S990,Ac-K1249-BRIP1 p-S327,T847,T859-RBBP8 MRE11A ATRIP MRE11A EXO1 KAT5K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 DNA2 UBC(381-456) RAD51D DNA double-strand break ends p-S988,S1387,S1423,S1524,S1547-BRCA1 RAD52 heptamerXRCC2 RAD1 WRN TIPIN DNA2 EXO1 RMI2 RAD9B p-S343-NBN HIST1H2BJ RAD1 BLM RPA1 RHNO1 XRCC2 K6PolyUb,p-T714,T734-BARD1 RHNO1 MRE11A p-S988,S1387,S1423,S1524,S1547-BRCA1 p-S1981,Ac-K3016-ATM UBB(1-76) K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 BRCC3 p-T714,T734-BARD1 RAD50 Ac-K432,K526,K604-RBBP8 homotetramerp-S988,S1387,S1423,S1524,S1547-BRCA1 ADPRAD51B UBE2N UBC(381-456) PPP4C:PPP4R2K63PolyUb:K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-NucleosomeNonhomologousEnd-Joining (NHEJ)ERCC4 BLM MUS81:EME1,(MUS81:EME2)p-S327,T847,T859-RBBP8 HIST1H2BN K6PolyUb,p-T714,T734-BARD1 DNA2 RAD51C EXO1 SLX1A:SLX4BLM K6PolyUb,p-T714,T734-BARD1 p-S988,S1387,S1423,S1524,S1547-BRCA1 BLM:TOP3A:RMI1:RMI2RAD51AP1p-S988,S1387,S1423,S1524,S1547-BRCA1 RBBP8 KAT5 RAD50 POLE RAD51C TOPBP1 KAT5 RFC5 PiK63PolyUb-K14,K16,p-S140-H2AFX p-T714,T734-BARD1 UBB(153-228) PALB2 RAD51AP1 K6PolyUb,p-T714,T734-BARD1 RAD50 TOP3A KAT5 K6PolyUb,p-T714,T734-BARD1 p-S1981,Ac-K3016-ATM TOP3A p-S343-NBN K6PolyUb,p-T714,T734-BARD1 TOP3A K6PolyUb,p-T714,T734-BARD1 p-S33-RPA2 p-S102-WHSC1 RFC3 RAD51C UBE2N KAT5 p-S988,S1387,S1423,S1524,S1547-BRCA1 K6PolyUb,p-T714,T734-BARD1 TOP3A Me2K21-HIST1H4 RPA3 H2ORMI2 EXO1,DNA2:BLM,WRNMe2K21-HIST1H4 HIST1H2BJ p-S343-NBN RAD51B p-Y104-RAD52heptamerp-S1981,Ac-K3016-ATMRAD50 BRCC3TOP3A p-S343-NBN K6PolyUb,p-T714,T734-BARD1 RPA3 p-S1981,Ac-K3016-ATM DNA2 K6PolyUb,p-T714,T734-BARD1 WRN p-S327,T847,T859-RBBP8 p-T309-RAD51 KAT5 Heteroduplex DNA with D-loop structure with extended pairing between invading strand and complementary heteroduplex strand RFC3 TOP3A UBC(229-304) p-S1981,Ac-K3016-ATM WRN p-S327,T847,T859-RBBP8 H2BFS MDC1-SUMO2 RFC4 Ac-K432,K526,K604-RBBP8 UBC(229-304) KAT5 RAD17 TOPBP1 RAD51D EXO1 ATRIP EXO1 ATPRPA:3'overhangingssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 RMI1 RFC2 p-S406-FAM175A EXO1 ATR:ATRIP:p-RPA:3'overhangingssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1RAD51AP1 p-S988,S1387,S1423,S1524,S1547-BRCA1 RAD52 BLM p-T714,T734-BARD1 DNADSB:p-MRN:p-S1981,Ac-K3016-ATM:KAT5TOPBP1p-T714,T734-BARD1 POLH UBC(305-380) RMI2 CCNA:p-T160-CDK2p-Y104-RAD52:p-RPA:ATR:ATRIP:3' overhanging ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1BLM p-S343-NBN EXO1,DNA2:BLM,WRNK6PolyUb,p-T714,T734-BARD1 HIST1H2BK DNA2 HollidayJunction:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexUBB(77-152) TOP3A SLX1A UBE2V2 UBC(305-380) p-T4827,SUMO1-HERC2 RMI1 ATRIP p-S990,Ac-K1249-BRIP1 RMI1 p-T714,T734-BARD1 RPA1 TOPBP1BLM RAD51AP1 p-T3387-BRCA2 SIRT6RFC5 WRN p-MRNRAD51D RHNO1 p-T714,T734-BARD1 RFC3 HUS1 RAD17 UBC(609-684) p-S343-NBN PPP4C ATRIP p-S343-NBN H2ORNF8 RAD51:p-Y104-RAD52:p-RPA:ATR:ATRIP:3' overhanging ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1RAD51B p-S988,S1387,S1423,S1524,S1547-BRCA1 HIST1H2BN p-T3387-BRCA2 p-S456-ABL1K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 RHNO1RFC4 p-S343-NBN RMI1 MRE11A p-T160-CDK2 RMI2 3' overhanging DNA at resected DSB ends p-S327,T847,T859-RBBP8 ATR p-S343-NBN SSB-dsDNA withinter-SSA deletionRHNO1 MUS81 ATPRAD50 p-S327,T847,T859-RBBP8 BCDX2 complexp-Y104-RAD52 HIST2H2BE p-T714,T734-BARD1 RAD9B POLE3 RFC5 p-5S-BRCA1:p-2T-BARD1Holliday structure EXO1 RAD51AP1 HUS1 RFC4 DNA double-strand break ends K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 HIST1H2BM p-S1981,Ac-K3016-ATM UBB(1-76) HIST1H2BB p-S406-FAM175AKAT5 BLM 3' overhanging DNA at resected DSB ends p-S327,T847,T859-RBBP8 p-T160-CDK2 p-S327,T847,T859-RBBP8 RAD17 EME1 POLK RFC3 RAD51C TOP3A p-Y104-RAD52heptamerdNTPUBE2N RMI2 WRN DNA double-strand break ends p-S327,T847,T859-RBBP8 ATR:ATRIPK6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 GEN1 MRE11A RAD50 p-S990,Ac-K1249-BRIP1p-S988,S1387,S1423,S1524,S1547-BRCA1 p-S988,S1387,S1423,S1524,S1547-BRCA1 RAD50 PIAS4 RAD9A p-S988,S1387,S1423,S1524,S1547-BRCA1 KAT5 SUMO2-C93-UBE2I dsDNA with inter-SSAdeletionp-S990,Ac-K1249-BRIP1 DNA2 p-S990,Ac-K1249-BRIP1 BLM ATR HIST1H2BL p-S317,S345-CHEK1TIPIN PPP4R2 UBC(533-608) p-T3387-BRCA2 UBC(609-684) EME2 ATRIP XRCC2 RPA2 3' overhanging DNA at resected DSB ends RFC4 HERC2-SUMO1 p-S327,T847,T859-RBBP8 RPA3 HIST1H2BH p-S327,T847,T859-RBBP8 MRE11A p-S327,T847,T859-RBBP8 RAD50 p-T309-RAD51 RAD50 HUS1 RNF4 homodimerRPA3 EXO1 K6PolyUb,p-T714,T734-BARD1 p-T309-RAD51 p-T309-RAD51 RBBP8 K48PolyUb,SUMO2-K1840,p-5T-MDC1 RPA1 RFC2 p-T714,T734-BARD1 RAD9:HUS1:RAD1RTEL1RMI2 RPA3 RAD50 RPS27A(1-76) KAT5 p-S990,Ac-K1249-BRIP1 p-S327,T847,T859-RBBP8 RAD51D H2Op-S988,S1387,S1423,S1524,S1547-BRCA1 p-S343-NBN RAD1 PiRAD50 RAD9A HIST3H3 RMI2 DNA2 CCNA1 TOPBP1 p-S990,Ac-K1249-BRIP1 TOP3A ADPp-S988,S1387,S1423,S1524,S1547-BRCA1 WRN RMI1 TOP3A SLX4 DNA2 MRE11A UBE2IPOLD1 p-S327,T847,T859-RBBP8 p-S1981,Ac-K3016-ATM HIST1H2BK RAD50 RAD50 DNA2 UBC(1-76) HIST1H2BB UBB(153-228) BCDX2 complexK6PolyUb,p-T714,T734-BARD1 BLM RPA1 p-S327,T847,T859-RBBP8 RNF8 EXO1 EXO1 RPA3 K6PolyUb,p-T714,T734-BARD1 p-S343-NBN MRE11A p-T3387-BRCA2 UBE2I-G93-SUMO2 RFC4 RAD17:RFCHUS1 p-T3387-BRCA2:p-T309-RAD51 complexXRCC3 p-S343-NBN WRN SLX4 MRE11A K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 MUS81 RMI2 XRCC3p-T714,T734-BARD1 p-T714,T734-BARD1 TOP3A p-S1981,Ac-K3016-ATM RMI2 RAD51Cp-S102-WHSC1 p-S988,S1387,S1423,S1524,S1547-BRCA1 p-S990,Ac-K1249-BRIP1 p-S33-RPA2 WRN p-Y104-RAD52 RAD9B DNA2 MRE11A p-S343-NBN Sister ChromosomalArmHIST1H2BA XRCC3 p-T309-RAD51 RNF4 K6PolyUb,p-T714,T734-BARD1 K6PolyUb,p-T714,T734-BARD1 MRE11A PALB2RHNO1RFC2 MRE11A DNADSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:CCNA:p-T160-CDK2:RBBP8KAT5 KAT5 p-S990,Ac-K1249-BRIP1 UBB(77-152) RAD1 RAD50 p-T916,S945-CLSPNWRN RMI1 RAD50 BCDX2 complexHIST1H2BH ATR p-S1981,Ac-K3016-ATM TOP3A CCNA2 Me2K21-HIST1H4 K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 TOP3A SUMO2-K1840,p-5T-MDC1 RNF168 HIST1H2BA HIST1H2BD BLM RPA2 BABAM1 p-S343-NBN RAD17 PALB2RPA1 Cleaved D-loop p-S327,T847,T859-RBBP8 PIAS4p-S1981,Ac-K3016-ATM p-S327,T847,T859-RBBP8 HIST1H2BL p-5S-BRCA1:p-2T-BARD1dNTPp-S1981,Ac-K3016-ATM CX3 complexp-S25,S1778-TP53BP1 p-S102-WHSC1ATR:ATRIP:RPA:3'overhangingssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1UbRAD9:HUS1:RAD1Sister ChromosomalArmRAD50 K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 RPA2 dNTPBLM DNA2 BABAM1TOP3A 3'shortoverhangingssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1SUMO2:UBE2IRFC2 RPA1 RAD9B p-S1981,Ac-K3016-ATM Sister Chromatid Armwith CrossoverPALB2 RAD51D RAD9A RAD51 DNADSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:p-BRCA1-C complexp-S327,T847,T859-RBBP8 3'shortoverhangingssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complexRAD9B RMI1 p-S1981,Ac-K3016-ATM TOPBP1 XRCC2 DNA2 RAD52p-5S-BRCA1:p-2T-BARD1EXO1 RAD17 RPS27A(1-76) ATR:ATRIP:p-RPA:3'overhangingssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1:TIMELESS:TIPIN:p-T916,S945-CLSPN:CHEK1RMI2 RAD51D p-S327,T847,T859-RBBP8 homotetramerp-T916,S945-CLSPN RMI2 p-T309-RAD51 HIST1H2BJ RNF8 EME1 RAD51B EXO1,DNA2:BLM,WRNBLM RMI1 RAD17:RFCATRIP DNA DSB with annealed 3' overhanging ssDNA and flaps ATPK6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 RAD9B K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 ATPZn2+ K6PolyUb,p-T714,T734-BARD1 p-S343-NBN RMI2 EME1,EME2MRE11A UIMC1 RAD50 MonoUb-K164-PCNA p-Y104-RAD52 HIST1H2BO ERCC1:ERCC4PALB2 BABAM1 p-S990,Ac-K1249-BRIP1 HERC2-SUMO1 TOP3A RAD51D p-T3387-BRCA2 p-S988,S1387,S1423,S1524,S1547-BRCA1 EME2 p-S988,S1387,S1423,S1524,S1547-BRCA1 RMI1 2'-O-acetyl-ADP-riboseATRIP ATPUBC(533-608) MDC1-SUMO2 RMI1 RFC3 K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 RFC3 DNA double-strand break ends HIST1H2BK ATPRPA1 WRN p-S988,S1387,S1423,S1524,S1547-BRCA1 RPA3 RAD17 PALB2 D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1BLM HIST1H2BA TOP3A DNA2 p-T4827,SUMO1-HERC2 XRCC2 WRN HIST1H2BO p-S343-NBN RAD9A p-S990,Ac-K1249-BRIP1 BLM RPA heterotrimerRMI1 p-T3387-BRCA2 p-T3387-BRCA2 Zn2+ RPA3 UBC(153-228) ADPRAD50 K63PolyUb-K14,K16,p-S140-H2AFX KAT5 CHEK1 RMI1 p-S25,S1778-TP53BP1 p-T714,T734-BARD1 RFC3 K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 ATR p-S33-RPA2 p-T714,T734-BARD1 ATR p-S327,T847,T859-RBBP8 homotetramerBLM p-S33-RPA2 K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 KAT5 ADPEXO1 p-S990,Ac-K1249-BRIP1 DNA2 BLM:TOP3A:RMI1:RMI2:SPIDRKAT5 HIST3H2BB HIST2H2BE K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 RMI1 WRN RAD51C HUS1 RAD51C POLE2 TOP3A UBE2N:UBE2V2RPA1 p-RPA heterotrimerRMI2 CHEK1p-S1981,Ac-K3016-ATM HIST1H2BC HIST1H2BD RAD1 PiRAD51AP1Extended D-loop p-S327,T847,T859-RBBP8 p-T3387-BRCA2 p-S990,Ac-K1249-BRIP1 p-S343-NBN UBE2V2 HIST1H2BH RPA1 HIST1H2BB RAD51C 3' short overhanging ssDNA-DSBs RNF168PPip-S343-NBN RFC4 HERC2-SUMO1 HUS1 K48PolyUb:SUMO2:K1840,p-5T-MDC1 dimerRMI1 p-RPA heterotrimerp-MRNRAD9A RMI2 p-S343-NBN p-S988,S1387,S1423,S1524,S1547-BRCA1 XRCC2 SLX4 TOPBP1 p-S1981,Ac-K3016-ATM WRN RFC5 p-Y104-RAD52 RAD51B RMI2 ATR RAD9A DNA double-strand break ends EME2 DNADNADSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:K63PolyUb-K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-Nucleosome:p-5T-MDC1:p-S102-WHSC1:RNF8:Zn2+:SUMO1:p-T4827-HERC2:UBE2N:UBE2V2:RNF168:PIAS4:p-S25,S1778-TP53BP1:p-5S,2T-BRCA1-A complexPALB2p-S988,S1387,S1423,S1524,S1547-BRCA1 p-S25,S1778-TP53BP1RAD51C POLE4 KAT5 XRCC2 RMI1 3' short overhanging ssDNA-DSBs MRE11A HIST2H2BE K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 HIST1H2BM p-S990,Ac-K1249-BRIP1 TOP3A TIMELESS UIMC1 ATPWRN HIST1H2BC p-S33-RPA2 RFC5 RAD17 MUS81XRCC2 RFC5 p-S988,S1387,S1423,S1524,S1547-BRCA1 ATPMRE11A DNADSBs:p-MRN:p-S327,T847-RBBP8:p-S1981,Ac-K3016-ATM:KAT5UBC(77-152) HIST3H2BB DNA2 DNA Double StrandBreak Response3' overhanging DNA at resected DSB ends RAD1 p-S990,Ac-K1249-BRIP1 KAT5 EME2 BLM RAD51AP1 K6PolyUb,p-T714,T734-BARD1 RAD50 RFC2 p-S327,T847,T859-RBBP8 RAD51B H2ODNA2 CleavedD-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexBRCC3 RFC2 KAT5 CleavedHollidayJunction:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexD-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexp-5T-MDC1 RAD51B TIMELESS:TIPINPCNA K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 KAT5 RBBP8 homotetramerRAD9B p-S343-NBN 3'overhangingssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1ATR K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 EXO1 EXO1 RAD50 PCNA:POLD,POLE,POLH,POLK:RPA:RFCPIAS4 p-S406-FAM175A UBC(457-532) p-S343-NBN p-T714,T734-BARD1 XRCC2ADPATR:ATRIP:RPA:3'overhangingssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1p-S990,Ac-K1249-BRIP1CCNA2 RAD51B TOP3A ADPRAD51 UBC(77-152) RAD51C H2BFS K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 RFC4 p-S1981,Ac-K3016-ATM K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 KAT5 K6PolyUb,p-T714,T734-BARD1 K6PolyUb,p-T714,T734-BARD1 XRCC3 p-S33-RPA2 RAD9B EME1 RPA1 MRE11A p-T309-RAD51K6PolyUb,p-T714,T734-BARD1 p-S1981,Ac-K3016-ATM DNA double-strand break ends MRE11A MUS81 3' overhanging DNA at resected DSB ends TOP3A dsDNARAD50 RMI2 WRN TOP3A RAD51AP1 BRE ATPXRCC3 EXO1 RNF168 MRE11A HIST1H2BM RAD17 p-T3387-BRCA2 EXO1 RPA2 RFC5 UBA52(1-76) p-T714,T734-BARD1 p-T714,T734-BARD1 UBC(1-76) p-S988,S1387,S1423,S1524,S1547-BRCA1 BLM p-S327,T847,T859-RBBP8 Heteroduplex DNA with D-loop structure with extended pairing between invading strand and complementary heteroduplex strand WRN RPA3 XRCC3 RAD51D cleaved Holliday structure RFC4 3'overhangingssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-T309-RAD51:p-T3387-BRCA2:BCDX2 complexXRCC3 RFC2 ExtendedD-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexRAD50 p-S343-NBN RAD51p-T3387-BRCA2p-T714,T734-BARD1 KAT5 3' overhanging DNA at resected DSB ends SPIDR XRCC3 BLM TIMELESS H2BFS p-T309-RAD51 RMI1 BRCA2RMI2 RAD50 p-S1981,Ac-K3016-ATMK6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 RMI2 p-T309-RAD51 p-S1981,Ac-K3016-ATM K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 WRN RFC1 RAD9A PALB2 BLM KAT5 BLM RHNO1 WRN BREHIST3H2BB DNADNADSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:K63PolyUb-K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-Nucleosome:SUMO2:K1840,p-5T-MDC1:p-S102-WHSC1:RNF8:Zn2+:SUMO1:p-T4827-HERC2:UBE2N:UBE2V2:RNF168:PIAS4:p-S25,S1778-TP53BP1:p-5S,2T-BRCA1-A complexp-T4827,SUMO1-HERC2 HIST3H3 K6PolyUb,p-T714,T734-BARD1 RFC2 p-S990,Ac-K1249-BRIP1 NAD+p-S1981,Ac-K3016-ATM p-S988,S1387,S1423,S1524,S1547-BRCA1 p-T714,T734-BARD1 UBC(153-228) XRCC2 DNADSBs:p-MRN:p-S327,T847,T859-RBBP8:p-S1981,Ac-K3016-ATM:KAT5EXO1 HIST1H2BC RAD51DBLM RMI2 SLX1A:SLX4:MUS81:EME1,(MUS81:EME2),GEN1RMI2 ADPHUS1 p-T309-RAD51 p-S990,Ac-K1249-BRIP1KAT5 MRE11A TOPBP1 p-S1981,Ac-K3016-ATM RAD51B ss-gap-reannealedDNAWRN RFC4 p-S1981,Ac-K3016-ATM ATR:ATRIPHIST3H3 RMI2 BLM ATRIP EXO1 EXO1 KAT5 ERCC1 RAD51AP157, 13839, 166991513310, 7815110, 781516112457, 1381950, 12650, 1263315157, 13852103611251915316716757, 13813891531256115657, 13857, 1381, 3, 6, 11, 14...57, 138


Description

Homology directed repair (HDR) of replication-independent DNA double strand breaks (DSBs) via homologous recombination repair (HRR) or single strand annealing (SSA) requires the activation of ATM followed by ATM-mediated phosphorylation of DNA repair proteins. ATM coordinates the recruitment of DNA repair and signaling proteins to DSBs and formation of the so-called ionizing radiation induced foci (IRIF). While IRIFs include chromatin regions kilobases away from the actual DSB, this Reactome pathway represents simplified foci and shows events that happen at the very ends of the broken DNA.

For both HRR and SSA to occur, the ends of the DNA DSB must be processed (resected) to generate lengthy 3' ssDNA tails, and the resulting ssDNA coated with RPA complexes, triggering ATR activation and signaling.<p>After the resection step, BRCA2 and RAD51 trigger HRR, a very accurate process in which the 3'-ssDNA overhang invades a sister chromatid, base pairs with the complementary strand of the sister chromatid DNA duplex, creating a D-loop, and uses the complementary sister chromatid strand as a template for DNA repair synthesis that bridges the DSB.<p>The SSA is triggered when 3'-ssDNA overhangs created in the resection step contain highly homologous direct repeats. In a process involving RAD52, the direct repeats in each 3'-ssDNA overhang become annealed, the unannealed 3'-flaps excised, and structures then processed by DNA repair synthesis. SSA results in the loss of one of the annealed repeats and the DNA sequence between the two repeats. Therefore, SSA is error-prone and is probably used as a backup for HRR, with RAD52 loss-of-function mutations being synthetically lethal with mutations in HRR genes, such as BRCA2 (reviewed by Ciccia and Elledge 2010). View original pathway at Reactome.</div>

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 5693567
Reactome-version 
Reactome version: 75
Reactome Author 
Reactome Author: Thompson, L

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Lee JW, Blanco L, Zhou T, Garcia-Diaz M, Bebenek K, Kunkel TA, Wang Z, Povirk LF.; ''Implication of DNA polymerase lambda in alignment-based gap filling for nonhomologous DNA end joining in human nuclear extracts.''; PubMed Europe PMC Scholia
  2. Sarkies P, Murat P, Phillips LG, Patel KJ, Balasubramanian S, Sale JE.; ''FANCJ coordinates two pathways that maintain epigenetic stability at G-quadruplex DNA.''; PubMed Europe PMC Scholia
  3. Hsu HL, Yannone SM, Chen DJ.; ''Defining interactions between DNA-PK and ligase IV/XRCC4.''; PubMed Europe PMC Scholia
  4. Singleton MR, Wentzell LM, Liu Y, West SC, Wigley DB.; ''Structure of the single-strand annealing domain of human RAD52 protein.''; PubMed Europe PMC Scholia
  5. Sartori AA, Lukas C, Coates J, Mistrik M, Fu S, Bartek J, Baer R, Lukas J, Jackson SP.; ''Human CtIP promotes DNA end resection.''; PubMed Europe PMC Scholia
  6. Ma Y, Pannicke U, Schwarz K, Lieber MR.; ''Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination.''; PubMed Europe PMC Scholia
  7. Eid W, Steger M, El-Shemerly M, Ferretti LP, Peña-Diaz J, König C, Valtorta E, Sartori AA, Ferrari S.; ''DNA end resection by CtIP and exonuclease 1 prevents genomic instability.''; PubMed Europe PMC Scholia
  8. Litman R, Peng M, Jin Z, Zhang F, Zhang J, Powell S, Andreassen PR, Cantor SB.; ''BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ.''; PubMed Europe PMC Scholia
  9. Baynton K, Otterlei M, Bjørås M, von Kobbe C, Bohr VA, Seeberg E.; ''WRN interacts physically and functionally with the recombination mediator protein RAD52.''; PubMed Europe PMC Scholia
  10. Fekairi S, Scaglione S, Chahwan C, Taylor ER, Tissier A, Coulon S, Dong MQ, Ruse C, Yates JR, Russell P, Fuchs RP, McGowan CH, Gaillard PHL.; ''Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases.''; PubMed Europe PMC Scholia
  11. Lee JH, Paull TT.; ''ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex.''; PubMed Europe PMC Scholia
  12. Dray E, Etchin J, Wiese C, Saro D, Williams GJ, Hammel M, Yu X, Galkin VE, Liu D, Tsai MS, Sy SM, Schild D, Egelman E, Chen J, Sung P.; ''Enhancement of RAD51 recombinase activity by the tumor suppressor PALB2.''; PubMed Europe PMC Scholia
  13. Wan L, Han J, Liu T, Dong S, Xie F, Chen H, Huang J.; ''Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair.''; PubMed Europe PMC Scholia
  14. Hanakahi LA, Bartlet-Jones M, Chappell C, Pappin D, West SC.; ''Binding of inositol phosphate to DNA-PK and stimulation of double-strand break repair.''; PubMed Europe PMC Scholia
  15. Sun J, Lee KJ, Davis AJ, Chen DJ.; ''Human Ku70/80 protein blocks exonuclease 1-mediated DNA resection in the presence of human Mre11 or Mre11/Rad50 protein complex.''; PubMed Europe PMC Scholia
  16. Pomerantz RT, Kurth I, Goodman MF, O'Donnell ME.; ''Preferential D-loop extension by a translesion DNA polymerase underlies error-prone recombination.''; PubMed Europe PMC Scholia
  17. Ciccia A, Constantinou A, West SC.; ''Identification and characterization of the human mus81-eme1 endonuclease.''; PubMed Europe PMC Scholia
  18. Ciccia A, Ling C, Coulthard R, Yan Z, Xue Y, Meetei AR, Laghmani el H, Joenje H, McDonald N, de Winter JP, Wang W, West SC.; ''Identification of FAAP24, a Fanconi anemia core complex protein that interacts with FANCM.''; PubMed Europe PMC Scholia
  19. Cotta-Ramusino C, McDonald ER, Hurov K, Sowa ME, Harper JW, Elledge SJ.; ''A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling.''; PubMed Europe PMC Scholia
  20. Thorslund T, McIlwraith MJ, Compton SA, Lekomtsev S, Petronczki M, Griffith JD, West SC.; ''The breast cancer tumor suppressor BRCA2 promotes the specific targeting of RAD51 to single-stranded DNA.''; PubMed Europe PMC Scholia
  21. Suhasini AN, Sommers JA, Mason AC, Voloshin ON, Camerini-Otero RD, Wold MS, Brosh RM.; ''FANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by replication protein A to unwind the damaged DNA substrate in a strand-specific manner.''; PubMed Europe PMC Scholia
  22. Lloyd JA, Forget AL, Knight KL.; ''Correlation of biochemical properties with the oligomeric state of human rad52 protein.''; PubMed Europe PMC Scholia
  23. Al-Minawi AZ, Saleh-Gohari N, Helleday T.; ''The ERCC1/XPF endonuclease is required for efficient single-strand annealing and gene conversion in mammalian cells.''; PubMed Europe PMC Scholia
  24. Sugiyama T, Zaitseva EM, Kowalczykowski SC.; ''A single-stranded DNA-binding protein is needed for efficient presynaptic complex formation by the Saccharomyces cerevisiae Rad51 protein.''; PubMed Europe PMC Scholia
  25. Kaidi A, Weinert BT, Choudhary C, Jackson SP.; ''Human SIRT6 promotes DNA end resection through CtIP deacetylation.''; PubMed Europe PMC Scholia
  26. Paull TT, Rogakou EP, Yamazaki V, Kirchgessner CU, Gellert M, Bonner WM.; ''A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage.''; PubMed Europe PMC Scholia
  27. Meng Z, Capalbo L, Glover DM, Dunphy WG.; ''Role for casein kinase 1 in the phosphorylation of Claspin on critical residues necessary for the activation of Chk1.''; PubMed Europe PMC Scholia
  28. Mortusewicz O, Rothbauer U, Cardoso MC, Leonhardt H.; ''Differential recruitment of DNA Ligase I and III to DNA repair sites.''; PubMed Europe PMC Scholia
  29. Jackson D, Dhar K, Wahl JK, Wold MS, Borgstahl GE.; ''Analysis of the human replication protein A:Rad52 complex: evidence for crosstalk between RPA32, RPA70, Rad52 and DNA.''; PubMed Europe PMC Scholia
  30. Liu J, Doty T, Gibson B, Heyer WD.; ''Human BRCA2 protein promotes RAD51 filament formation on RPA-covered single-stranded DNA.''; PubMed Europe PMC Scholia
  31. Lévy N, Oehlmann M, Delalande F, Nasheuer HP, Van Dorsselaer A, Schreiber V, de Murcia G, Ménissier-de Murcia J, Maiorano D, Bresson A.; ''XRCC1 interacts with the p58 subunit of DNA Pol alpha-primase and may coordinate DNA repair and replication during S phase.''; PubMed Europe PMC Scholia
  32. Luo K, Zhang H, Wang L, Yuan J, Lou Z.; ''Sumoylation of MDC1 is important for proper DNA damage response.''; PubMed Europe PMC Scholia
  33. Wang B, Matsuoka S, Ballif BA, Zhang D, Smogorzewska A, Gygi SP, Elledge SJ.; ''Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response.''; PubMed Europe PMC Scholia
  34. Ramírez-Lugo JS, Yoo HY, Yoon SJ, Dunphy WG.; ''CtIP interacts with TopBP1 and Nbs1 in the response to double-stranded DNA breaks (DSBs) in Xenopus egg extracts.''; PubMed Europe PMC Scholia
  35. Callen E, Di Virgilio M, Kruhlak MJ, Nieto-Soler M, Wong N, Chen HT, Faryabi RB, Polato F, Santos M, Starnes LM, Wesemann DR, Lee JE, Tubbs A, Sleckman BP, Daniel JA, Ge K, Alt FW, Fernandez-Capetillo O, Nussenzweig MC, Nussenzweig A.; ''53BP1 mediates productive and mutagenic DNA repair through distinct phosphoprotein interactions.''; PubMed Europe PMC Scholia
  36. Sørensen CS, Syljuåsen RG, Lukas J, Bartek J.; ''ATR, Claspin and the Rad9-Rad1-Hus1 complex regulate Chk1 and Cdc25A in the absence of DNA damage.''; PubMed Europe PMC Scholia
  37. Sørensen CS, Hansen LT, Dziegielewski J, Syljuåsen RG, Lundin C, Bartek J, Helleday T.; ''The cell-cycle checkpoint kinase Chk1 is required for mammalian homologous recombination repair.''; PubMed Europe PMC Scholia
  38. Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R.; ''RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination.''; PubMed Europe PMC Scholia
  39. Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET.; ''Characterization of a second member of the sentrin family of ubiquitin-like proteins.''; PubMed Europe PMC Scholia
  40. Thompson LH, Schild D.; ''Homologous recombinational repair of DNA ensures mammalian chromosome stability.''; PubMed Europe PMC Scholia
  41. Venkitaraman AR.; ''Cancer susceptibility and the functions of BRCA1 and BRCA2.''; PubMed Europe PMC Scholia
  42. Trujillo KM, Yuan SS, Lee EY, Sung P.; ''Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95.''; PubMed Europe PMC Scholia
  43. Xie J, Peng M, Guillemette S, Quan S, Maniatis S, Wu Y, Venkatesh A, Shaffer SA, Brosh RM, Cantor SB.; ''FANCJ/BACH1 acetylation at lysine 1249 regulates the DNA damage response.''; PubMed Europe PMC Scholia
  44. Masutani C, Kusumoto R, Iwai S, Hanaoka F.; ''Mechanisms of accurate translesion synthesis by human DNA polymerase eta.''; PubMed Europe PMC Scholia
  45. Sancar A, Lindsey-Boltz LA, Unsal-Kaçmaz K, Linn S.; ''Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints.''; PubMed Europe PMC Scholia
  46. Gravel S, Chapman JR, Magill C, Jackson SP.; ''DNA helicases Sgs1 and BLM promote DNA double-strand break resection.''; PubMed Europe PMC Scholia
  47. Nick McElhinny SA, Snowden CM, McCarville J, Ramsden DA.; ''Ku recruits the XRCC4-ligase IV complex to DNA ends.''; PubMed Europe PMC Scholia
  48. Kagawa W, Kurumizaka H, Ishitani R, Fukai S, Nureki O, Shibata T, Yokoyama S.; ''Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form.''; PubMed Europe PMC Scholia
  49. Parameswaran B, Chiang HC, Lu Y, Coates J, Deng CX, Baer R, Lin HK, Li R, Paull TT, Hu Y.; ''Damage-induced BRCA1 phosphorylation by Chk2 contributes to the timing of end resection.''; PubMed Europe PMC Scholia
  50. Unsal-Kaçmaz K, Sancar A.; ''Quaternary structure of ATR and effects of ATRIP and replication protein A on its DNA binding and kinase activities.''; PubMed Europe PMC Scholia
  51. Buisson R, Niraj J, Pauty J, Maity R, Zhao W, Coulombe Y, Sung P, Masson JY.; ''Breast cancer proteins PALB2 and BRCA2 stimulate polymerase η in recombination-associated DNA synthesis at blocked replication forks.''; PubMed Europe PMC Scholia
  52. Ciccia A, Elledge SJ.; ''The DNA damage response: making it safe to play with knives.''; PubMed Europe PMC Scholia
  53. Honda M, Okuno Y, Yoo J, Ha T, Spies M.; ''Tyrosine phosphorylation enhances RAD52-mediated annealing by modulating its DNA binding.''; PubMed Europe PMC Scholia
  54. Wiese C, Dray E, Groesser T, San Filippo J, Shi I, Collins DW, Tsai MS, Williams GJ, Rydberg B, Sung P, Schild D.; ''Promotion of homologous recombination and genomic stability by RAD51AP1 via RAD51 recombinase enhancement.''; PubMed Europe PMC Scholia
  55. Escribano-Díaz C, Orthwein A, Fradet-Turcotte A, Xing M, Young JT, Tkáč J, Cook MA, Rosebrock AP, Munro M, Canny MD, Xu D, Durocher D.; ''A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and BRCA1-CtIP controls DNA repair pathway choice.''; PubMed Europe PMC Scholia
  56. Liu Q, Guntuku S, Cui XS, Matsuoka S, Cortez D, Tamai K, Luo G, Carattini-Rivera S, DeMayo F, Bradley A, Donehower LA, Elledge SJ.; ''Chk1 is an essential kinase that is regulated by Atr and required for the G(2)/M DNA damage checkpoint.''; PubMed Europe PMC Scholia
  57. Masson JY, Tarsounas MC, Stasiak AZ, Stasiak A, Shah R, McIlwraith MJ, Benson FE, West SC.; ''Identification and purification of two distinct complexes containing the five RAD51 paralogs.''; PubMed Europe PMC Scholia
  58. Yun MH, Hiom K.; ''CtIP-BRCA1 modulates the choice of DNA double-strand-break repair pathway throughout the cell cycle.''; PubMed Europe PMC Scholia
  59. Van Dyck E, Hajibagheri NM, Stasiak A, West SC.; ''Visualisation of human rad52 protein and its complexes with hRad51 and DNA.''; PubMed Europe PMC Scholia
  60. Gottlieb TM, Jackson SP.; ''The DNA-dependent protein kinase: requirement for DNA ends and association with Ku antigen.''; PubMed Europe PMC Scholia
  61. Buis J, Stoneham T, Spehalski E, Ferguson DO.; ''Mre11 regulates CtIP-dependent double-strand break repair by interaction with CDK2.''; PubMed Europe PMC Scholia
  62. Riballo E, Kühne M, Rief N, Doherty A, Smith GC, Recio MJ, Reis C, Dahm K, Fricke A, Krempler A, Parker AR, Jackson SP, Gennery A, Jeggo PA, Löbrich M.; ''A pathway of double-strand break rejoining dependent upon ATM, Artemis, and proteins locating to gamma-H2AX foci.''; PubMed Europe PMC Scholia
  63. Puebla-Osorio N, Lacey DB, Alt FW, Zhu C.; ''Early embryonic lethality due to targeted inactivation of DNA ligase III.''; PubMed Europe PMC Scholia
  64. Bermudez VP, Lindsey-Boltz LA, Cesare AJ, Maniwa Y, Griffith JD, Hurwitz J, Sancar A.; ''Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hRad17-replication factor C complex in vitro.''; PubMed Europe PMC Scholia
  65. Zhu Z, Chung WH, Shim EY, Lee SE, Ira G.; ''Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break ends.''; PubMed Europe PMC Scholia
  66. Yoo S, Dynan WS.; ''Geometry of a complex formed by double strand break repair proteins at a single DNA end: recruitment of DNA-PKcs induces inward translocation of Ku protein.''; PubMed Europe PMC Scholia
  67. Oğrünç M, Sancar A.; ''Identification and characterization of human MUS81-MMS4 structure-specific endonuclease.''; PubMed Europe PMC Scholia
  68. Zhang F, Ma J, Wu J, Ye L, Cai H, Xia B, Yu X.; ''PALB2 links BRCA1 and BRCA2 in the DNA-damage response.''; PubMed Europe PMC Scholia
  69. Mansour WY, Schumacher S, Rosskopf R, Rhein T, Schmidt-Petersen F, Gatzemeier F, Haag F, Borgmann K, Willers H, Dahm-Daphi J.; ''Hierarchy of nonhomologous end-joining, single-strand annealing and gene conversion at site-directed DNA double-strand breaks.''; PubMed Europe PMC Scholia
  70. Kumagai A, Dunphy WG.; ''Repeated phosphopeptide motifs in Claspin mediate the regulated binding of Chk1.''; PubMed Europe PMC Scholia
  71. Barber LJ, Youds JL, Ward JD, McIlwraith MJ, O'Neil NJ, Petalcorin MI, Martin JS, Collis SJ, Cantor SB, Auclair M, Tissenbaum H, West SC, Rose AM, Boulton SJ.; ''RTEL1 maintains genomic stability by suppressing homologous recombination.''; PubMed Europe PMC Scholia
  72. Baumann P, West SC.; ''Heteroduplex formation by human Rad51 protein: effects of DNA end-structure, hRP-A and hRad52.''; PubMed Europe PMC Scholia
  73. Amunugama R, Groden J, Fishel R.; ''The HsRAD51B-HsRAD51C stabilizes the HsRAD51 nucleoprotein filament.''; PubMed Europe PMC Scholia
  74. Sung P, Krejci L, Van Komen S, Sehorn MG.; ''Rad51 recombinase and recombination mediators.''; PubMed Europe PMC Scholia
  75. Ahmad A, Robinson AR, Duensing A, van Drunen E, Beverloo HB, Weisberg DB, Hasty P, Hoeijmakers JH, Niedernhofer LJ.; ''ERCC1-XPF endonuclease facilitates DNA double-strand break repair.''; PubMed Europe PMC Scholia
  76. Kemp MG, Akan Z, Yilmaz S, Grillo M, Smith-Roe SL, Kang TH, Cordeiro-Stone M, Kaufmann WK, Abraham RT, Sancar A, Unsal-Kaçmaz K.; ''Tipin-replication protein A interaction mediates Chk1 phosphorylation by ATR in response to genotoxic stress.''; PubMed Europe PMC Scholia
  77. Stark JM, Pierce AJ, Oh J, Pastink A, Jasin M.; ''Genetic steps of mammalian homologous repair with distinct mutagenic consequences.''; PubMed Europe PMC Scholia
  78. Wyatt HD, Sarbajna S, Matos J, West SC.; ''Coordinated actions of SLX1-SLX4 and MUS81-EME1 for Holliday junction resolution in human cells.''; PubMed Europe PMC Scholia
  79. Uringa EJ, Lisaingo K, Pickett HA, Brind'Amour J, Rohde JH, Zelensky A, Essers J, Lansdorp PM.; ''RTEL1 contributes to DNA replication and repair and telomere maintenance.''; PubMed Europe PMC Scholia
  80. Yu X, Chini CC, He M, Mer G, Chen J.; ''The BRCT domain is a phospho-protein binding domain.''; PubMed Europe PMC Scholia
  81. Smits VA, Reaper PM, Jackson SP.; ''Rapid PIKK-dependent release of Chk1 from chromatin promotes the DNA-damage checkpoint response.''; PubMed Europe PMC Scholia
  82. Osman F, Dixon J, Doe CL, Whitby MC.; ''Generating crossovers by resolution of nicked Holliday junctions: a role for Mus81-Eme1 in meiosis.''; PubMed Europe PMC Scholia
  83. Vannier JB, Sandhu S, Petalcorin MI, Wu X, Nabi Z, Ding H, Boulton SJ.; ''RTEL1 is a replisome-associated helicase that promotes telomere and genome-wide replication.''; PubMed Europe PMC Scholia
  84. Suhasini AN, Rawtani NA, Wu Y, Sommers JA, Sharma S, Mosedale G, North PS, Cantor SB, Hickson ID, Brosh RM.; ''Interaction between the helicases genetically linked to Fanconi anemia group J and Bloom's syndrome.''; PubMed Europe PMC Scholia
  85. Inamdar KV, Pouliot JJ, Zhou T, Lees-Miller SP, Rasouli-Nia A, Povirk LF.; ''Conversion of phosphoglycolate to phosphate termini on 3' overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1.''; PubMed Europe PMC Scholia
  86. Compton SA, Ozgür S, Griffith JD.; ''Ring-shaped Rad51 paralog protein complexes bind Holliday junctions and replication forks as visualized by electron microscopy.''; PubMed Europe PMC Scholia
  87. Niewolik D, Pannicke U, Lu H, Ma Y, Wang LC, Kulesza P, Zandi E, Lieber MR, Schwarz K.; ''DNA-PKcs dependence of Artemis endonucleolytic activity, differences between hairpins and 5' or 3' overhangs.''; PubMed Europe PMC Scholia
  88. Suhasini AN, Brosh RM.; ''Fanconi anemia and Bloom's syndrome crosstalk through FANCJ-BLM helicase interaction.''; PubMed Europe PMC Scholia
  89. Chou DM, Elledge SJ.; ''Tipin and Timeless form a mutually protective complex required for genotoxic stress resistance and checkpoint function.''; PubMed Europe PMC Scholia
  90. Gómez-Herreros F, Romero-Granados R, Zeng Z, Alvarez-Quilón A, Quintero C, Ju L, Umans L, Vermeire L, Huylebroeck D, Caldecott KW, Cortés-Ledesma F.; ''TDP2-dependent non-homologous end-joining protects against topoisomerase II-induced DNA breaks and genome instability in cells and in vivo.''; PubMed Europe PMC Scholia
  91. Anantha RW, Vassin VM, Borowiec JA.; ''Sequential and synergistic modification of human RPA stimulates chromosomal DNA repair.''; PubMed Europe PMC Scholia
  92. Nimonkar AV, Genschel J, Kinoshita E, Polaczek P, Campbell JL, Wyman C, Modrich P, Kowalczykowski SC.; ''BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair.''; PubMed Europe PMC Scholia
  93. Pepe A, West SC.; ''Substrate specificity of the MUS81-EME2 structure selective endonuclease.''; PubMed Europe PMC Scholia
  94. Sebesta M, Burkovics P, Juhasz S, Zhang S, Szabo JE, Lee MY, Haracska L, Krejci L.; ''Role of PCNA and TLS polymerases in D-loop extension during homologous recombination in humans.''; PubMed Europe PMC Scholia
  95. Park MS, Ludwig DL, Stigger E, Lee SH.; ''Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells.''; PubMed Europe PMC Scholia
  96. Malu S, De Ioannes P, Kozlov M, Greene M, Francis D, Hanna M, Pena J, Escalante CR, Kurosawa A, Erdjument-Bromage H, Tempst P, Adachi N, Vezzoni P, Villa A, Aggarwal AK, Cortes P.; ''Artemis C-terminal region facilitates V(D)J recombination through its interactions with DNA Ligase IV and DNA-PKcs.''; PubMed Europe PMC Scholia
  97. Nimonkar AV, Ozsoy AZ, Genschel J, Modrich P, Kowalczykowski SC.; ''Human exonuclease 1 and BLM helicase interact to resect DNA and initiate DNA repair.''; PubMed Europe PMC Scholia
  98. Zimmermann M, Lottersberger F, Buonomo SB, Sfeir A, de Lange T.; ''53BP1 regulates DSB repair using Rif1 to control 5' end resection.''; PubMed Europe PMC Scholia
  99. Lee DH, Pan Y, Kanner S, Sung P, Borowiec JA, Chowdhury D.; ''A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination.''; PubMed Europe PMC Scholia
  100. Coleman KA, Greenberg RA.; ''The BRCA1-RAP80 complex regulates DNA repair mechanism utilization by restricting end resection.''; PubMed Europe PMC Scholia
  101. Liu S, Shiotani B, Lahiri M, Maréchal A, Tse A, Leung CC, Glover JN, Yang XH, Zou L.; ''ATR autophosphorylation as a molecular switch for checkpoint activation.''; PubMed Europe PMC Scholia
  102. Tsai CJ, Kim SA, Chu G.; ''Cernunnos/XLF promotes the ligation of mismatched and noncohesive DNA ends.''; PubMed Europe PMC Scholia
  103. Sturzenegger A, Burdova K, Kanagaraj R, Levikova M, Pinto C, Cejka P, Janscak P.; ''DNA2 cooperates with the WRN and BLM RecQ helicases to mediate long-range DNA end resection in human cells.''; PubMed Europe PMC Scholia
  104. Fan J, Otterlei M, Wong HK, Tomkinson AE, Wilson DM.; ''XRCC1 co-localizes and physically interacts with PCNA.''; PubMed Europe PMC Scholia
  105. Mahajan KN, Nick McElhinny SA, Mitchell BS, Ramsden DA.; ''Association of DNA polymerase mu (pol mu) with Ku and ligase IV: role for pol mu in end-joining double-strand break repair.''; PubMed Europe PMC Scholia
  106. Zhao H, Piwnica-Worms H.; ''ATR-mediated checkpoint pathways regulate phosphorylation and activation of human Chk1.''; PubMed Europe PMC Scholia
  107. Sy SM, Huen MS, Chen J.; ''PALB2 is an integral component of the BRCA complex required for homologous recombination repair.''; PubMed Europe PMC Scholia
  108. Masson JY, Stasiak AZ, Stasiak A, Benson FE, West SC.; ''Complex formation by the human RAD51C and XRCC3 recombination repair proteins.''; PubMed Europe PMC Scholia
  109. Van Dyck E, Stasiak AZ, Stasiak A, West SC.; ''Visualization of recombination intermediates produced by RAD52-mediated single-strand annealing.''; PubMed Europe PMC Scholia
  110. Motycka TA, Bessho T, Post SM, Sung P, Tomkinson AE.; ''Physical and functional interaction between the XPF/ERCC1 endonuclease and hRad52.''; PubMed Europe PMC Scholia
  111. Li X, Stith CM, Burgers PM, Heyer WD.; ''PCNA is required for initiation of recombination-associated DNA synthesis by DNA polymerase delta.''; PubMed Europe PMC Scholia
  112. Pei H, Zhang L, Luo K, Qin Y, Chesi M, Fei F, Bergsagel PL, Wang L, You Z, Lou Z.; ''MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites.''; PubMed Europe PMC Scholia
  113. Kumagai A, Lee J, Yoo HY, Dunphy WG.; ''TopBP1 activates the ATR-ATRIP complex.''; PubMed Europe PMC Scholia
  114. Jazayeri A, Falck J, Lukas C, Bartek J, Smith GC, Lukas J, Jackson SP.; ''ATM- and cell cycle-dependent regulation of ATR in response to DNA double-strand breaks.''; PubMed Europe PMC Scholia
  115. Liu S, Ho CK, Ouyang J, Zou L.; ''Nek1 kinase associates with ATR-ATRIP and primes ATR for efficient DNA damage signaling.''; PubMed Europe PMC Scholia
  116. Hopfner KP, Craig L, Moncalian G, Zinkel RA, Usui T, Owen BA, Karcher A, Henderson B, Bodmer JL, McMurray CT, Carney JP, Petrini JH, Tainer JA.; ''The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair.''; PubMed Europe PMC Scholia
  117. Yang H, Li Q, Fan J, Holloman WK, Pavletich NP.; ''The BRCA2 homologue Brh2 nucleates RAD51 filament formation at a dsDNA-ssDNA junction.''; PubMed Europe PMC Scholia
  118. Clarke CA, Clarke PR.; ''DNA-dependent phosphorylation of Chk1 and Claspin in a human cell-free system.''; PubMed Europe PMC Scholia
  119. Delacroix S, Wagner JM, Kobayashi M, Yamamoto K, Karnitz LM.; ''The Rad9-Hus1-Rad1 (9-1-1) clamp activates checkpoint signaling via TopBP1.''; PubMed Europe PMC Scholia
  120. Sarbajna S, Davies D, West SC.; ''Roles of SLX1-SLX4, MUS81-EME1, and GEN1 in avoiding genome instability and mitotic catastrophe.''; PubMed Europe PMC Scholia
  121. Cramer K, Nieborowska-Skorska M, Koptyra M, Slupianek A, Penserga ET, Eaves CJ, Aulitzky W, Skorski T.; ''BCR/ABL and other kinases from chronic myeloproliferative disorders stimulate single-strand annealing, an unfaithful DNA double-strand break repair.''; PubMed Europe PMC Scholia
  122. Ma Y, Pannicke U, Lu H, Niewolik D, Schwarz K, Lieber MR.; ''The DNA-dependent protein kinase catalytic subunit phosphorylation sites in human Artemis.''; PubMed Europe PMC Scholia
  123. Buisson R, Dion-Côté AM, Coulombe Y, Launay H, Cai H, Stasiak AZ, Stasiak A, Xia B, Masson JY.; ''Cooperation of breast cancer proteins PALB2 and piccolo BRCA2 in stimulating homologous recombination.''; PubMed Europe PMC Scholia
  124. Zou L, Elledge SJ.; ''Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes.''; PubMed Europe PMC Scholia
  125. Park JY, Singh TR, Nassar N, Zhang F, Freund M, Hanenberg H, Meetei AR, Andreassen PR.; ''Breast cancer-associated missense mutants of the PALB2 WD40 domain, which directly binds RAD51C, RAD51 and BRCA2, disrupt DNA repair.''; PubMed Europe PMC Scholia
  126. Ball HL, Cortez D.; ''ATRIP oligomerization is required for ATR-dependent checkpoint signaling.''; PubMed Europe PMC Scholia
  127. Schwartz EK, Wright WD, Ehmsen KT, Evans JE, Stahlberg H, Heyer WD.; ''Mus81-Mms4 functions as a single heterodimer to cleave nicked intermediates in recombinational DNA repair.''; PubMed Europe PMC Scholia
  128. Parsons CA, Baumann P, Van Dyck E, West SC.; ''Precise binding of single-stranded DNA termini by human RAD52 protein.''; PubMed Europe PMC Scholia
  129. Chen G, Yuan SS, Liu W, Xu Y, Trujillo K, Song B, Cong F, Goff SP, Wu Y, Arlinghaus R, Baltimore D, Gasser PJ, Park MS, Sung P, Lee EY.; ''Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl.''; PubMed Europe PMC Scholia
  130. Liu Y, Tarsounas M, O'regan P, West SC.; ''Role of RAD51C and XRCC3 in genetic recombination and DNA repair.''; PubMed Europe PMC Scholia
  131. Bahassi EM, Ovesen JL, Riesenberg AL, Bernstein WZ, Hasty PE, Stambrook PJ.; ''The checkpoint kinases Chk1 and Chk2 regulate the functional associations between hBRCA2 and Rad51 in response to DNA damage.''; PubMed Europe PMC Scholia
  132. Walker JR, Corpina RA, Goldberg J.; ''Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair.''; PubMed Europe PMC Scholia
  133. Kitao H, Yuan ZM.; ''Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation.''; PubMed Europe PMC Scholia
  134. Fan W, Wu X.; ''DNA polymerase lambda can elongate on DNA substrates mimicking non-homologous end joining and interact with XRCC4-ligase IV complex.''; PubMed Europe PMC Scholia
  135. Galanty Y, Belotserkovskaya R, Coates J, Jackson SP.; ''RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair.''; PubMed Europe PMC Scholia
  136. Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, Wahrer DC, Sgroi DC, Lane WS, Haber DA, Livingston DM.; ''BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function.''; PubMed Europe PMC Scholia
  137. Yin Y, Seifert A, Chua JS, Maure JF, Golebiowski F, Hay RT.; ''SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage.''; PubMed Europe PMC Scholia
  138. Chun J, Buechelmaier ES, Powell SN.; ''Rad51 paralog complexes BCDX2 and CX3 act at different stages in the BRCA1-BRCA2-dependent homologous recombination pathway.''; PubMed Europe PMC Scholia
  139. Liu S, Opiyo SO, Manthey K, Glanzer JG, Ashley AK, Amerin C, Troksa K, Shrivastav M, Nickoloff JA, Oakley GG.; ''Distinct roles for DNA-PK, ATM and ATR in RPA phosphorylation and checkpoint activation in response to replication stress.''; PubMed Europe PMC Scholia
  140. Jensen RB, Carreira A, Kowalczykowski SC.; ''Purified human BRCA2 stimulates RAD51-mediated recombination.''; PubMed Europe PMC Scholia
  141. Mallette FA, Mattiroli F, Cui G, Young LC, Hendzel MJ, Mer G, Sixma TK, Richard S.; ''RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites.''; PubMed Europe PMC Scholia
  142. McIlwraith MJ, Van Dyck E, Masson JY, Stasiak AZ, Stasiak A, West SC.; ''Reconstitution of the strand invasion step of double-strand break repair using human Rad51 Rad52 and RPA proteins.''; PubMed Europe PMC Scholia
  143. Lee J, Gold DA, Shevchenko A, Shevchenko A, Dunphy WG.; ''Roles of replication fork-interacting and Chk1-activating domains from Claspin in a DNA replication checkpoint response.''; PubMed Europe PMC Scholia
  144. Kolpashchikov DM, Khodyreva SN, Khlimankov DY, Wold MS, Favre A, Lavrik OI.; ''Polarity of human replication protein A binding to DNA.''; PubMed Europe PMC Scholia
  145. Wang H, Shi LZ, Wong CC, Han X, Hwang PY, Truong LN, Zhu Q, Shao Z, Chen DJ, Berns MW, Yates JR, Chen L, Wu X.; ''The interaction of CtIP and Nbs1 connects CDK and ATM to regulate HR-mediated double-strand break repair.''; PubMed Europe PMC Scholia
  146. Wilson KA, Stern DF.; ''NFBD1/MDC1, 53BP1 and BRCA1 have both redundant and unique roles in the ATM pathway.''; PubMed Europe PMC Scholia
  147. Murphy AK, Fitzgerald M, Ro T, Kim JH, Rabinowitsch AI, Chowdhury D, Schildkraut CL, Borowiec JA.; ''Phosphorylated RPA recruits PALB2 to stalled DNA replication forks to facilitate fork recovery.''; PubMed Europe PMC Scholia
  148. Friedberg EC, Lehmann AR, Fuchs RP.; ''Trading places: how do DNA polymerases switch during translesion DNA synthesis?''; PubMed Europe PMC Scholia
  149. McIlwraith MJ, Vaisman A, Liu Y, Fanning E, Woodgate R, West SC.; ''Human DNA polymerase eta promotes DNA synthesis from strand invasion intermediates of homologous recombination.''; PubMed Europe PMC Scholia
  150. Gatei M, Young D, Cerosaletti KM, Desai-Mehta A, Spring K, Kozlov S, Lavin MF, Gatti RA, Concannon P, Khanna K.; ''ATM-dependent phosphorylation of nibrin in response to radiation exposure.''; PubMed Europe PMC Scholia
  151. Danielsen JR, Povlsen LK, Villumsen BH, Streicher W, Nilsson J, Wikström M, Bekker-Jensen S, Mailand N.; ''DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger.''; PubMed Europe PMC Scholia
  152. Matsuda T, Bebenek K, Masutani C, Hanaoka F, Kunkel TA.; ''Low fidelity DNA synthesis by human DNA polymerase-eta.''; PubMed Europe PMC Scholia
  153. Davies OR, Forment JV, Sun M, Belotserkovskaya R, Coates J, Galanty Y, Demir M, Morton CR, Rzechorzek NJ, Jackson SP, Pellegrini L.; ''CtIP tetramer assembly is required for DNA-end resection and repair.''; PubMed Europe PMC Scholia
  154. Bocquet N, Bizard AH, Abdulrahman W, Larsen NB, Faty M, Cavadini S, Bunker RD, Kowalczykowski SC, Cejka P, Hickson ID, Thomä NH.; ''Structural and mechanistic insight into Holliday-junction dissolution by topoisomerase IIIα and RMI1.''; PubMed Europe PMC Scholia
  155. Stasiak AZ, Larquet E, Stasiak A, Müller S, Engel A, Van Dyck E, West SC, Egelman EH.; ''The human Rad52 protein exists as a heptameric ring.''; PubMed Europe PMC Scholia
  156. Jackson MD, Denu JM.; ''Structural identification of 2'- and 3'-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylases.''; PubMed Europe PMC Scholia
  157. Ahnesorg P, Smith P, Jackson SP.; ''XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining.''; PubMed Europe PMC Scholia
  158. Li X, Heyer WD.; ''RAD54 controls access to the invading 3'-OH end after RAD51-mediated DNA strand invasion in homologous recombination in Saccharomyces cerevisiae.''; PubMed Europe PMC Scholia
  159. Wang J, Aroumougame A, Lobrich M, Li Y, Chen D, Chen J, Gong Z.; ''PTIP associates with Artemis to dictate DNA repair pathway choice.''; PubMed Europe PMC Scholia
  160. Ohashi E, Bebenek K, Matsuda T, Feaver WJ, Gerlach VL, Friedberg EC, Ohmori H, Kunkel TA.; ''Fidelity and processivity of DNA synthesis by DNA polymerase kappa, the product of the human DINB1 gene.''; PubMed Europe PMC Scholia
  161. Wang B, Matsuoka S, Carpenter PB, Elledge SJ.; ''53BP1, a mediator of the DNA damage checkpoint.''; PubMed Europe PMC Scholia
  162. Mortusewicz O, Leonhardt H.; ''XRCC1 and PCNA are loading platforms with distinct kinetic properties and different capacities to respond to multiple DNA lesions.''; PubMed Europe PMC Scholia
  163. Stucki M, Clapperton JA, Mohammad D, Yaffe MB, Smerdon SJ, Jackson SP.; ''MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks.''; PubMed Europe PMC Scholia
  164. Stewart GS, Wang B, Bignell CR, Taylor AM, Elledge SJ.; ''MDC1 is a mediator of the mammalian DNA damage checkpoint.''; PubMed Europe PMC Scholia
  165. Liu Y, Masson JY, Shah R, O'Regan P, West SC.; ''RAD51C is required for Holliday junction processing in mammalian cells.''; PubMed Europe PMC Scholia
  166. Su HL, Li SS.; ''Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.''; PubMed Europe PMC Scholia
  167. Griffith JD, Lindsey-Boltz LA, Sancar A.; ''Structures of the human Rad17-replication factor C and checkpoint Rad 9-1-1 complexes visualized by glycerol spray/low voltage microscopy.''; PubMed Europe PMC Scholia
  168. Wang X, Zou L, Lu T, Bao S, Hurov KE, Hittelman WN, Elledge SJ, Li L.; ''Rad17 phosphorylation is required for claspin recruitment and Chk1 activation in response to replication stress.''; PubMed Europe PMC Scholia
  169. Chen L, Nievera CJ, Lee AY, Wu X.; ''Cell cycle-dependent complex formation of BRCA1.CtIP.MRN is important for DNA double-strand break repair.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
123633view09:43, 7 August 2022EgonwModified title
117752view12:49, 22 May 2021EweitzOntology Term : 'PW:0000099' removed !
117751view12:49, 22 May 2021EweitzOntology Term : 'homologous recombination pathway of double-strand break repair' added !
114770view16:26, 25 January 2021ReactomeTeamReactome version 75
113214view11:28, 2 November 2020ReactomeTeamReactome version 74
112438view15:38, 9 October 2020ReactomeTeamReactome version 73
101343view11:23, 1 November 2018ReactomeTeamreactome version 66
100881view20:57, 31 October 2018ReactomeTeamreactome version 65
100422view19:31, 31 October 2018ReactomeTeamreactome version 64
99972view16:15, 31 October 2018ReactomeTeamreactome version 63
99526view14:50, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99166view12:42, 31 October 2018ReactomeTeamreactome version 62
93754view13:34, 16 August 2017ReactomeTeamreactome version 61
93274view11:19, 9 August 2017ReactomeTeamreactome version 61
87461view14:09, 22 July 2016MkutmonOntology Term : 'DNA repair pathway' added !
86353view09:15, 11 July 2016ReactomeTeamreactome version 56
83457view12:27, 18 November 2015ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
2'-O-acetyl-ADP-riboseMetaboliteCHEBI:76279 (ChEBI)
3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-T309-RAD51:p-T3387-BRCA2:BCDX2 complex		ComplexR-HSA-5685343 (Reactome)
3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-T309-RAD51:p-T3387-BRCA2		ComplexR-HSA-5685317 (Reactome)
3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		ComplexR-HSA-5684128 (Reactome)
3'

short overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		ComplexR-HSA-5685989 (Reactome)
3'

short overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex		ComplexR-HSA-5685983 (Reactome)
3' overhanging DNA at resected DSB ends R-ALL-75156 (Reactome)
3' short overhanging ssDNA-DSBs R-ALL-5685984 (Reactome)
ADPMetaboliteCHEBI:456216 (ChEBI)
ATPMetaboliteCHEBI:30616 (ChEBI)
ATR ProteinQ13535 (Uniprot-TrEMBL)
ATR:ATRIP:RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1		ComplexR-HSA-5685039 (Reactome)
ATR:ATRIP:RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		ComplexR-HSA-5684874 (Reactome)
ATR:ATRIP:p-RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1:TIMELESS:TIPIN:p-T916,S945-CLSPN:CHEK1		ComplexR-HSA-5684883 (Reactome)
ATR:ATRIP:p-RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1		ComplexR-HSA-5685162 (Reactome)
ATR:ATRIPComplexR-HSA-176269 (Reactome) The ATR (ATM- and rad3-related) kinase is an essential checkpoint factor in human cells. In response to replication stress (i.e., stresses that cause replication fork stalling) or ultraviolet radiation, ATR becomes active and phosphorylates numerous factors involved in the checkpoint response including the checkpoint kinase Chk1. ATR is invariably associated with ATRIP (ATR-interacting protein) in human cells. Depletion of ATRIP by siRNA causes a loss of ATR without affecting ATR mRNA levels indicating that complex formation stabilizes ATR. ATRIP is also a substrate for the ATR kinase, but this modification does not play a significant role in the recruitment of ATR-ATRIP to sites of damage, the activation of Chk1, or the modification of p53.
ATRIP ProteinQ8WXE1 (Uniprot-TrEMBL)
Ac-K432,K526,K604-RBBP8 ProteinQ99708 (Uniprot-TrEMBL)
Ac-K432,K526,K604-RBBP8 homotetramerComplexR-HSA-5685960 (Reactome)
BABAM1 ProteinQ9NWV8 (Uniprot-TrEMBL)
BABAM1ProteinQ9NWV8 (Uniprot-TrEMBL)
BCDX2 complexComplexR-HSA-5685316 (Reactome)
BLM ProteinP54132 (Uniprot-TrEMBL)
BLM:TOP3A:RMI1:RMI2:SPIDRComplexR-HSA-5686409 (Reactome)
BLM:TOP3A:RMI1:RMI2ComplexR-HSA-5685972 (Reactome)
BRCA2ProteinP51587 (Uniprot-TrEMBL)
BRCC3 ProteinP46736 (Uniprot-TrEMBL)
BRCC3ProteinP46736 (Uniprot-TrEMBL)
BRE ProteinQ9NXR7 (Uniprot-TrEMBL)
BREProteinQ9NXR7 (Uniprot-TrEMBL)
CCNA1 ProteinP78396 (Uniprot-TrEMBL)
CCNA2 ProteinP20248 (Uniprot-TrEMBL)
CCNA:p-T160-CDK2ComplexR-HSA-187952 (Reactome)
CHEK1 ProteinO14757 (Uniprot-TrEMBL)
CHEK1ProteinO14757 (Uniprot-TrEMBL)
CX3 complexComplexR-HSA-5685311 (Reactome)
Cleaved D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexComplexR-HSA-5686432 (Reactome)
Cleaved

Holliday

Junction:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complex		ComplexR-HSA-5686493 (Reactome)
Cleaved D-loop R-ALL-5686442 (Reactome)
D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexComplexR-HSA-5685826 (Reactome)
D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1ComplexR-HSA-5685658 (Reactome)
DNA

DNA

DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:K63PolyUb-K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-Nucleosome:SUMO2:K1840,p-5T-MDC1:p-S102-WHSC1:RNF8:Zn2+:SUMO1:p-T4827-HERC2:UBE2N:UBE2V2:RNF168:PIAS4:p-S25,S1778-TP53BP1:p-5S,2T-BRCA1-A complex		ComplexR-HSA-5684053 (Reactome)
DNA

DNA

DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:K63PolyUb-K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-Nucleosome:p-5T-MDC1:p-S102-WHSC1:RNF8:Zn2+:SUMO1:p-T4827-HERC2:UBE2N:UBE2V2:RNF168:PIAS4:p-S25,S1778-TP53BP1:p-5S,2T-BRCA1-A complex		ComplexR-HSA-5683808 (Reactome)
DNA DSB:p-MRN:p-S1981,Ac-K3016-ATM:KAT5ComplexR-HSA-5682162 (Reactome)
DNA DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:CCNA:p-T160-CDK2:RBBP8ComplexR-HSA-5684094 (Reactome)
DNA DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:p-BRCA1-C complexComplexR-HSA-5684107 (Reactome)
DNA DSBs:p-MRN:p-S327,T847,T859-RBBP8:p-S1981,Ac-K3016-ATM:KAT5ComplexR-HSA-5684135 (Reactome)
DNA DSBs:p-MRN:p-S327,T847-RBBP8:p-S1981,Ac-K3016-ATM:KAT5ComplexR-HSA-5684095 (Reactome)
DNA DSB with annealed 3' overhanging ssDNA and flaps R-ALL-5686618 (Reactome)
DNA Double Strand Break ResponsePathwayR-HSA-5693606 (Reactome) DNA double strand break (DSB) response involves sensing of DNA DSBs by the MRN complex which triggers ATM activation. ATM phosphorylates a number of proteins involved in DNA damage checkpoint signaling, as well as proteins directly involved in the repair of DNA DSBs. For a recent review, please refer to Ciccia and Elledge, 2010.
DNA double-strand break ends R-ALL-75165 (Reactome)
DNA2 ProteinP51530 (Uniprot-TrEMBL)
EME1 ProteinQ96AY2 (Uniprot-TrEMBL)
EME1,EME2ComplexR-HSA-5686454 (Reactome)
EME2 ProteinA4GXA9 (Uniprot-TrEMBL)
ERCC1 ProteinP07992 (Uniprot-TrEMBL)
ERCC1:ERCC4ComplexR-HSA-109943 (Reactome)
ERCC4 ProteinQ92889 (Uniprot-TrEMBL)
EXO1 ProteinQ9UQ84 (Uniprot-TrEMBL)
EXO1,DNA2:BLM,WRNComplexR-HSA-5685980 (Reactome)
Extended D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexComplexR-HSA-5686104 (Reactome)
Extended D-loop R-ALL-5686092 (Reactome)
FlapR-ALL-68454 (Reactome)
GEN1 ProteinQ17RS7 (Uniprot-TrEMBL)
H2BFS ProteinP57053 (Uniprot-TrEMBL)
H2OMetaboliteCHEBI:15377 (ChEBI)
HERC2-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
HIST1H2BA ProteinQ96A08 (Uniprot-TrEMBL)
HIST1H2BB ProteinP33778 (Uniprot-TrEMBL)
HIST1H2BC ProteinP62807 (Uniprot-TrEMBL)
HIST1H2BD ProteinP58876 (Uniprot-TrEMBL)
HIST1H2BH ProteinQ93079 (Uniprot-TrEMBL)
HIST1H2BJ ProteinP06899 (Uniprot-TrEMBL)
HIST1H2BK ProteinO60814 (Uniprot-TrEMBL)
HIST1H2BL ProteinQ99880 (Uniprot-TrEMBL)
HIST1H2BM ProteinQ99879 (Uniprot-TrEMBL)
HIST1H2BN ProteinQ99877 (Uniprot-TrEMBL)
HIST1H2BO ProteinP23527 (Uniprot-TrEMBL)
HIST2H2BE ProteinQ16778 (Uniprot-TrEMBL)
HIST3H2BB ProteinQ8N257 (Uniprot-TrEMBL)
HIST3H3 ProteinQ16695 (Uniprot-TrEMBL)
HUS1 ProteinO60921 (Uniprot-TrEMBL)
Heteroduplex DNA with D-loop structure with extended pairing between invading strand and complementary heteroduplex strand R-ALL-83893 (Reactome)
Holliday Junction:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexComplexR-HSA-5686228 (Reactome)
Holliday structure R-ALL-75220 (Reactome)
K48PolyUb,SUMO2-K1840,p-5T-MDC1 ProteinQ14676 (Uniprot-TrEMBL)
K48PolyUb:SUMO2:K1840,p-5T-MDC1 dimerComplexR-HSA-5684077 (Reactome)
K63PolyUb-K14,K16,p-S140-H2AFX ProteinP16104 (Uniprot-TrEMBL)
K63PolyUb:K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-NucleosomeComplexR-HSA-5682998 (Reactome)
K6PolyUb,p-S988,S1387,S1423,S1524,S1547-BRCA1 ProteinP38398 (Uniprot-TrEMBL)
K6PolyUb,p-T714,T734-BARD1 ProteinQ99728 (Uniprot-TrEMBL)
KAT5 ProteinQ92993 (Uniprot-TrEMBL)
KAT5ProteinQ92993 (Uniprot-TrEMBL)
MDC1-SUMO2 ProteinP61956 (Uniprot-TrEMBL)
MRE11A ProteinP49959 (Uniprot-TrEMBL)
MUS81 ProteinQ96NY9 (Uniprot-TrEMBL)
MUS81:EME1, (MUS81:EME2)ComplexR-HSA-8933487 (Reactome)
MUS81ProteinQ96NY9 (Uniprot-TrEMBL)
Me2K21-HIST1H4 ProteinP62805 (Uniprot-TrEMBL)
MonoUb-K164-PCNA ProteinP12004 (Uniprot-TrEMBL)
NAD+MetaboliteCHEBI:57540 (ChEBI)
NAMMetaboliteCHEBI:17154 (ChEBI)
Nonhomologous End-Joining (NHEJ)PathwayR-HSA-5693571 (Reactome) The nonhomologous end joining (NHEJ) pathway is initiated in response to the formation of DNA double-strand breaks (DSBs) induced by DNA-damaging agents, such as ionizing radiation. DNA DSBs are recognized by the MRN complex (MRE11A:RAD50:NBN), leading to ATM activation and ATM-dependent recruitment of a number of DNA damage checkpoint and repair proteins to DNA DSB sites (Lee and Paull 2005). The ATM phosphorylated MRN complex, MDC1 and H2AFX-containing nucleosomes (gamma-H2AX) serve as scaffolds for the formation of nuclear foci known as ionizing radiation induced foci (IRIF) (Gatei et al. 2000, Paull et al. 2000, Stewart et al. 2003, Stucki et al. 2005). Ultimately, both BRCA1:BARD1 heterodimers and TP53BP1 (53BP1) are recruited to IRIF (Wang et al. 2007, Pei et al. 2011, Mallette et al. 2012), which is necessary for ATM-mediated CHEK2 activation (Wang et al. 2002, Wilson et al. 2008). In G1 cells, TP53BP1 promotes NHEJ by recruiting RIF1 and PAX1IP, which displaces BRCA1:BARD1 and associated proteins from the DNA DSB site and prevents resection of DNA DSBs needed for homologous recombination repair (HRR) (Escribano-Diaz et al. 2013, Zimmermann et al. 2013, Callen et al. 2013). TP53BP1 also plays an important role in ATM-mediated phosphorylation of DCLRE1C (ARTEMIS) (Riballo et al. 2004, Wang et al. 2014). Ku70:Ku80 heterodimer (also known as the Ku complex or XRCC5:XRCC6) binds DNA DSB ends, competing away the MRN complex and preventing MRN-mediated resection of DNA DSB ends (Walker et al. 2001, Sun et al. 2012). The catalytic subunit of the DNA-dependent protein kinase (DNA-PKcs, PRKDC) is then recruited to DNA-bound Ku to form the DNA-PK holoenzyme. Two DNA-PK complexes, one at each side of the break, bring DNA DSB ends together, joining them in a synaptic complex (Gottlieb 1993, Yoo and Dynan 2000). DNA-PK complex recruits DCLRE1C (ARTEMIS) to DNA DSB ends (Ma et al. 2002). PRKDC-mediated phosphorylation of DCLRE1C, as well as PRKDC autophosphorylation, enables DCLRE1C to trim 3'- and 5'-overhangs at DNA DSBs, preparing them for ligation (Ma et al. 2002, Ma et al. 2005, Niewolik et al. 2006). The binding of inositol phosphate may additionally stimulate the catalytic activity of PRKDC (Hanakahi et al. 2000). Other factors, such as polynucleotide kinase (PNK), TDP1 or TDP2 may remove unligatable damaged nucleotides from 5'- and 3'-ends of the DSB, converting them to ligatable substrates (Inamdar et al. 2002, Gomez-Herreros et al. 2013). DNA ligase 4 (LIG4) in complex with XRCC4 (XRCC4:LIG4) is recruited to ligatable DNA DSB ends together with the XLF (NHEJ1) homodimer and DNA polymerases mu (POLM) and/or lambda (POLL) (McElhinny et al. 2000, Hsu et al. 2002, Malu et al. 2002, Ahnesorg et al. 2006, Mahajan et al. 2002, Lee et al. 2004, Fan and Wu 2004). After POLL and/or POLM fill 1- or 2-nucleotide long single strand gaps at aligned DNA DSB ends, XRCC4:LIG4 performs the ligation of broken DNA strands, thus completing NHEJ. The presence of NHEJ1 homodimer facilitates the ligation step, especially at mismatched DSB ends (Tsai et al. 2007). Depending on other types of DNA damage present at DNA DSBs, NHEJ can result in error-free products, produce dsDNA with microdeletions and/or mismatched bases, or result in translocations (reviewed by Povrik et al. 2012).
PALB2 ProteinQ86YC2 (Uniprot-TrEMBL)
PALB2ProteinQ86YC2 (Uniprot-TrEMBL)
PCNA ProteinP12004 (Uniprot-TrEMBL)
PCNA:POLD,POLE,POLH,POLK:RPA:RFCComplexR-HSA-5686084 (Reactome)
PIAS4 ProteinQ8N2W9 (Uniprot-TrEMBL)
PIAS4ProteinQ8N2W9 (Uniprot-TrEMBL)
POLD1 ProteinP28340 (Uniprot-TrEMBL)
POLD2 ProteinP49005 (Uniprot-TrEMBL)
POLD3 ProteinQ15054 (Uniprot-TrEMBL)
POLD4 ProteinQ9HCU8 (Uniprot-TrEMBL)
POLE ProteinQ07864 (Uniprot-TrEMBL)
POLE2 ProteinP56282 (Uniprot-TrEMBL)
POLE3 ProteinQ9NRF9 (Uniprot-TrEMBL)
POLE4 ProteinQ9NR33 (Uniprot-TrEMBL)
POLH ProteinQ9Y253 (Uniprot-TrEMBL)
POLK ProteinQ9UBT6 (Uniprot-TrEMBL)
PPP4C ProteinP60510 (Uniprot-TrEMBL)
PPP4C:PPP4R2ComplexR-HSA-5687751 (Reactome)
PPP4R2 ProteinQ9NY27 (Uniprot-TrEMBL)
PPiMetaboliteCHEBI:29888 (ChEBI)
PiMetaboliteCHEBI:43474 (ChEBI)
RAD1 ProteinO60671 (Uniprot-TrEMBL)
RAD17 ProteinO75943 (Uniprot-TrEMBL)
RAD17:RFCComplexR-HSA-176353 (Reactome) The Rad17-RFC complex is a heteropentamer structurally similar to RFC. The Rad17-RFC complex contains the four smaller RFC subunits (Rfc2 [p37], Rfc3 [p36], Rfc4 [p40], and Rfc5 [p38]) and the 75 kDa Rad17 subunit in place of the Rfc1 [p140] subunit. The Rad17 complex contains a weak ATPase that is poorly stimulated by primed DNA. Along with binding the 9-1-1 complex and RPA, the Rad17-RFC complex interacts with human MCM7 protein. Each of these interactions is critical for Chk1 activation.

The Rad17 subunit is conserved evolutionarily with the protein showing 49% identity at the amino acid level with the S. pombe rad17 protein. Targeted deletion of the N-terminal region of mouse Rad17 leads to embryonic lethality, strongly suggesting that human Rad17 is also essential for long-term viability.

RAD50 ProteinQ92878 (Uniprot-TrEMBL)
RAD51 ProteinQ06609 (Uniprot-TrEMBL)
RAD51:p-Y104-RAD52:p-RPA:ATR:ATRIP:3' overhanging ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1ComplexR-HSA-5693590 (Reactome)
RAD51:p-Y104-RAD52:p-RPA:ATR:ATRIP:DNA DSBs with annealed 3' ssDNA overhangs and displaced flaps:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1ComplexR-HSA-5686613 (Reactome)
RAD51AP1 ProteinQ96B01 (Uniprot-TrEMBL)
RAD51AP1ProteinQ96B01 (Uniprot-TrEMBL)
RAD51B ProteinO15315 (Uniprot-TrEMBL)
RAD51BProteinO15315 (Uniprot-TrEMBL)
RAD51C ProteinO43502 (Uniprot-TrEMBL)
RAD51CProteinO43502 (Uniprot-TrEMBL)
RAD51D ProteinO75771 (Uniprot-TrEMBL)
RAD51DProteinO75771 (Uniprot-TrEMBL)
RAD51ProteinQ06609 (Uniprot-TrEMBL)
RAD52 ProteinP43351 (Uniprot-TrEMBL)
RAD52 heptamerComplexR-HSA-83899 (Reactome)
RAD52ProteinP43351 (Uniprot-TrEMBL)
RAD9:HUS1:RAD1ComplexR-HSA-176312 (Reactome) The Rad9-Hus1-Rad1 (9-1-1) complex is a ring-shaped heterotrimeric complex. Under genotoxic stress conditions, it can be loaded onto DNA at sites of damage or stalled forks by the Rad17 complex.
RAD9A ProteinQ99638 (Uniprot-TrEMBL)
RAD9B ProteinQ6WBX8 (Uniprot-TrEMBL)
RBBP8 ProteinQ99708 (Uniprot-TrEMBL)
RBBP8 homotetramerComplexR-HSA-5684097 (Reactome)
RFC1 ProteinP35251 (Uniprot-TrEMBL)
RFC2 ProteinP35250 (Uniprot-TrEMBL)
RFC3 ProteinP40938 (Uniprot-TrEMBL)
RFC4 ProteinP35249 (Uniprot-TrEMBL)
RFC5 ProteinP40937 (Uniprot-TrEMBL)
RHNO1 ProteinQ9BSD3 (Uniprot-TrEMBL)
RHNO1ProteinQ9BSD3 (Uniprot-TrEMBL)
RMI1 ProteinQ9H9A7 (Uniprot-TrEMBL)
RMI2 ProteinQ96E14 (Uniprot-TrEMBL)
RNF168 ProteinQ8IYW5 (Uniprot-TrEMBL)
RNF168ProteinQ8IYW5 (Uniprot-TrEMBL)
RNF4 ProteinP78317 (Uniprot-TrEMBL)
RNF4 homodimerComplexR-HSA-5684073 (Reactome)
RNF8 ProteinO76064 (Uniprot-TrEMBL)
RNF8:Zn2+ComplexR-HSA-5682540 (Reactome)
RPA heterotrimerComplexR-HSA-68462 (Reactome)
RPA1 ProteinP27694 (Uniprot-TrEMBL)
RPA2 ProteinP15927 (Uniprot-TrEMBL)
RPA3 ProteinP35244 (Uniprot-TrEMBL)
RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		ComplexR-HSA-5693552 (Reactome)
RPS27A(1-76) ProteinP62979 (Uniprot-TrEMBL)
RTEL1ProteinQ9NZ71 (Uniprot-TrEMBL)
SIRT6ProteinQ8N6T7 (Uniprot-TrEMBL)
SLX1A ProteinQ9BQ83 (Uniprot-TrEMBL)
SLX1A:SLX4:MUS81:EME1,(MUS81:EME2),GEN1ComplexR-HSA-5686489 (Reactome)
SLX1A:SLX4:MUS81:EME1,(MUS81:EME2)ComplexR-HSA-5686474 (Reactome)
SLX1A:SLX4ComplexR-HSA-5686480 (Reactome)
SLX4 ProteinQ8IY92 (Uniprot-TrEMBL)
SPIDR ProteinQ14159 (Uniprot-TrEMBL)
SPIDRProteinQ14159 (Uniprot-TrEMBL)
SSB-dsDNA with inter-SSA deletionR-ALL-5686662 (Reactome)
SUMO1:p-T4827-HERC2ComplexR-HSA-5682612 (Reactome)
SUMO2-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO2-K1840,p-5T-MDC1 ProteinQ14676 (Uniprot-TrEMBL)
SUMO2:UBE2IComplexR-HSA-2993778 (Reactome)
Sister Chromatid Arm with CrossoverR-ALL-5686464 (Reactome)
Sister Chromosomal ArmR-ALL-1638790 (Reactome)
TIMELESS ProteinQ9UNS1 (Uniprot-TrEMBL)
TIMELESS:TIPINComplexR-HSA-5684985 (Reactome)
TIPIN ProteinQ9BVW5 (Uniprot-TrEMBL)
TOP3A ProteinQ13472 (Uniprot-TrEMBL)
TOPBP1 ProteinQ92547 (Uniprot-TrEMBL)
TOPBP1ProteinQ92547 (Uniprot-TrEMBL)
UBA52(1-76) ProteinP62987 (Uniprot-TrEMBL)
UBB(1-76) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(153-228) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(77-152) ProteinP0CG47 (Uniprot-TrEMBL)
UBC(1-76) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(153-228) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(229-304) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(305-380) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(381-456) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(457-532) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(533-608) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(609-684) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(77-152) ProteinP0CG48 (Uniprot-TrEMBL)
UBE2I-G93-SUMO2 ProteinP61956 (Uniprot-TrEMBL)
UBE2IProteinP63279 (Uniprot-TrEMBL)
UBE2N ProteinP61088 (Uniprot-TrEMBL)
UBE2N:UBE2V2ComplexR-HSA-5682542 (Reactome)
UBE2V2 ProteinQ15819 (Uniprot-TrEMBL)
UIMC1 ProteinQ96RL1 (Uniprot-TrEMBL)
UIMC1ProteinQ96RL1 (Uniprot-TrEMBL)
UbComplexR-HSA-68524 (Reactome)
WRN ProteinQ14191 (Uniprot-TrEMBL)
XRCC2 ProteinO43543 (Uniprot-TrEMBL)
XRCC2ProteinO43543 (Uniprot-TrEMBL)
XRCC3 ProteinO43542 (Uniprot-TrEMBL)
XRCC3ProteinO43542 (Uniprot-TrEMBL)
Zn2+ MetaboliteCHEBI:29105 (ChEBI)
cleaved Holliday structure R-ALL-83636 (Reactome)
dNTPMetaboliteCHEBI:16516 (ChEBI)
dsDNA with crossoverR-ALL-5686458 (Reactome)
dsDNA with inter-SSA deletionR-ALL-5686649 (Reactome)
dsDNAR-HSA-5649637 (Reactome)
p-5S-BRCA1:p-2T-BARD1ComplexR-HSA-9707299 (Reactome)
p-5T-MDC1 ProteinQ14676 (Uniprot-TrEMBL)
p-MRNComplexR-HSA-5682166 (Reactome)
p-RPA heterotrimerComplexR-HSA-5685169 (Reactome)
p-S102-WHSC1 ProteinO96028 (Uniprot-TrEMBL)
p-S102-WHSC1ProteinO96028 (Uniprot-TrEMBL)
p-S1981,Ac-K3016-ATM ProteinQ13315 (Uniprot-TrEMBL)
p-S1981,Ac-K3016-ATMProteinQ13315 (Uniprot-TrEMBL)
p-S25,S1778-TP53BP1 ProteinQ12888 (Uniprot-TrEMBL)
p-S25,S1778-TP53BP1ProteinQ12888 (Uniprot-TrEMBL)
p-S317,S345-CHEK1ProteinO14757 (Uniprot-TrEMBL)
p-S327,T847,T859-RBBP8 ProteinQ99708 (Uniprot-TrEMBL)
p-S327,T847,T859-RBBP8 homotetramerComplexR-HSA-5684137 (Reactome)
p-S327,T847-RBBP8 ProteinQ99708 (Uniprot-TrEMBL)
p-S33-RPA2 ProteinP15927 (Uniprot-TrEMBL)
p-S343-NBN ProteinO60934 (Uniprot-TrEMBL)
p-S406-FAM175A ProteinQ6UWZ7 (Uniprot-TrEMBL)
p-S406-FAM175AProteinQ6UWZ7 (Uniprot-TrEMBL)
p-S456-ABL1ProteinP00519 (Uniprot-TrEMBL)
p-S988,S1387,S1423,S1524,S1547-BRCA1 ProteinP38398 (Uniprot-TrEMBL)
p-S990,Ac-K1249-BRIP1 ProteinQ9BX63 (Uniprot-TrEMBL)
p-S990,Ac-K1249-BRIP1ProteinQ9BX63 (Uniprot-TrEMBL)
p-T160-CDK2 ProteinP24941 (Uniprot-TrEMBL)
p-T309-RAD51 ProteinQ06609 (Uniprot-TrEMBL)
p-T309-RAD51ProteinQ06609 (Uniprot-TrEMBL)
p-T3387-BRCA2 ProteinP51587 (Uniprot-TrEMBL)
p-T3387-BRCA2:p-T309-RAD51 complexComplexR-HSA-5693545 (Reactome)
p-T3387-BRCA2ProteinP51587 (Uniprot-TrEMBL)
p-T4827,SUMO1-HERC2 ProteinO95714 (Uniprot-TrEMBL)
p-T714,T734-BARD1 ProteinQ99728 (Uniprot-TrEMBL)
p-T916,S945-CLSPN ProteinQ9HAW4 (Uniprot-TrEMBL)
p-T916,S945-CLSPNProteinQ9HAW4 (Uniprot-TrEMBL)
p-Y104-RAD52 heptamerComplexR-HSA-5686589 (Reactome)
p-Y104-RAD52 ProteinP43351 (Uniprot-TrEMBL)
p-Y104-RAD52:p-RPA:ATR:ATRIP:3' overhanging ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1ComplexR-HSA-5693547 (Reactome)
ss-gap-reannealed DNAR-ALL-84009 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
2'-O-acetyl-ADP-riboseArrowR-HSA-5685953 (Reactome)
3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-T309-RAD51:p-T3387-BRCA2:BCDX2 complex		ArrowR-HSA-5685341 (Reactome)
3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-T309-RAD51:p-T3387-BRCA2:BCDX2 complex		R-HSA-5693620 (Reactome)
3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-T309-RAD51:p-T3387-BRCA2		ArrowR-HSA-5693561 (Reactome)
3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-T309-RAD51:p-T3387-BRCA2		R-HSA-5685341 (Reactome)
3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		ArrowR-HSA-5685994 (Reactome)
3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		R-HSA-5693542 (Reactome)
3'

short overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		ArrowR-HSA-5685985 (Reactome)
3'

short overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		R-HSA-5685994 (Reactome)
3'

short overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		mim-catalysisR-HSA-5685994 (Reactome)
3'

short overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex		ArrowR-HSA-5693608 (Reactome)
3'

short overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex		R-HSA-5685985 (Reactome)
ADPArrowR-HSA-5684096 (Reactome)
ADPArrowR-HSA-5684140 (Reactome)
ADPArrowR-HSA-5684887 (Reactome)
ADPArrowR-HSA-5685156 (Reactome)
ADPArrowR-HSA-5685230 (Reactome)
ADPArrowR-HSA-5685242 (Reactome)
ADPArrowR-HSA-5686410 (Reactome)
ADPArrowR-HSA-5686587 (Reactome)
ADPArrowR-HSA-5693589 (Reactome)
ATPR-HSA-5684096 (Reactome)
ATPR-HSA-5684140 (Reactome)
ATPR-HSA-5684887 (Reactome)
ATPR-HSA-5685156 (Reactome)
ATPR-HSA-5685230 (Reactome)
ATPR-HSA-5685242 (Reactome)
ATPR-HSA-5686410 (Reactome)
ATPR-HSA-5686587 (Reactome)
ATPR-HSA-5693589 (Reactome)
ATR:ATRIP:RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1		ArrowR-HSA-5685011 (Reactome)
ATR:ATRIP:RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1		R-HSA-5685156 (Reactome)
ATR:ATRIP:RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1		mim-catalysisR-HSA-5685156 (Reactome)
ATR:ATRIP:RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		ArrowR-HSA-5684875 (Reactome)
ATR:ATRIP:RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		R-HSA-5685011 (Reactome)
ATR:ATRIP:p-RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1:TIMELESS:TIPIN:p-T916,S945-CLSPN:CHEK1		ArrowR-HSA-5684882 (Reactome)
ATR:ATRIP:p-RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1:TIMELESS:TIPIN:p-T916,S945-CLSPN:CHEK1		R-HSA-5684887 (Reactome)
ATR:ATRIP:p-RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1:TIMELESS:TIPIN:p-T916,S945-CLSPN:CHEK1		mim-catalysisR-HSA-5684887 (Reactome)
ATR:ATRIP:p-RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1		ArrowR-HSA-5684887 (Reactome)
ATR:ATRIP:p-RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1		ArrowR-HSA-5685156 (Reactome)
ATR:ATRIP:p-RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1		R-HSA-5684882 (Reactome)
ATR:ATRIP:p-RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1		R-HSA-5693561 (Reactome)
ATR:ATRIP:p-RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1		R-HSA-5693580 (Reactome)
ATR:ATRIPArrowR-HSA-5686657 (Reactome)
ATR:ATRIPArrowR-HSA-5693561 (Reactome)
ATR:ATRIPR-HSA-5684875 (Reactome)
Ac-K432,K526,K604-RBBP8 homotetramerR-HSA-5685953 (Reactome)
BABAM1ArrowR-HSA-5684071 (Reactome)
BCDX2 complexArrowR-HSA-5685318 (Reactome)
BCDX2 complexArrowR-HSA-5686410 (Reactome)
BCDX2 complexArrowR-HSA-5686469 (Reactome)
BCDX2 complexArrowR-HSA-5686483 (Reactome)
BCDX2 complexArrowR-HSA-5693589 (Reactome)
BCDX2 complexR-HSA-5685341 (Reactome)
BLM:TOP3A:RMI1:RMI2:SPIDRArrowR-HSA-5686398 (Reactome)
BLM:TOP3A:RMI1:RMI2:SPIDRmim-catalysisR-HSA-5686410 (Reactome)
BLM:TOP3A:RMI1:RMI2R-HSA-5686398 (Reactome)
BRCA2R-HSA-5685242 (Reactome)
BRCC3ArrowR-HSA-5684071 (Reactome)
BREArrowR-HSA-5684071 (Reactome)
CCNA:p-T160-CDK2ArrowR-HSA-5684096 (Reactome)
CCNA:p-T160-CDK2R-HSA-5684081 (Reactome)
CHEK1R-HSA-5684882 (Reactome)
CX3 complexArrowR-HSA-5685319 (Reactome)
CX3 complexArrowR-HSA-5686410 (Reactome)
CX3 complexArrowR-HSA-5686469 (Reactome)
CX3 complexArrowR-HSA-5686483 (Reactome)
CX3 complexArrowR-HSA-5693589 (Reactome)
CX3 complexR-HSA-5685838 (Reactome)
Cleaved D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexArrowR-HSA-5686440 (Reactome)
Cleaved D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexR-HSA-5686469 (Reactome)
Cleaved

Holliday

Junction:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complex		ArrowR-HSA-5693584 (Reactome)
Cleaved

Holliday

Junction:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complex		R-HSA-5686483 (Reactome)
D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexArrowR-HSA-5685838 (Reactome)
D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexR-HSA-5693593 (Reactome)
D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1ArrowR-HSA-5693620 (Reactome)
D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1R-HSA-5685838 (Reactome)
DNA

DNA

DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:K63PolyUb-K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-Nucleosome:SUMO2:K1840,p-5T-MDC1:p-S102-WHSC1:RNF8:Zn2+:SUMO1:p-T4827-HERC2:UBE2N:UBE2V2:RNF168:PIAS4:p-S25,S1778-TP53BP1:p-5S,2T-BRCA1-A complex		ArrowR-HSA-5684052 (Reactome)
DNA

DNA

DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:K63PolyUb-K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-Nucleosome:SUMO2:K1840,p-5T-MDC1:p-S102-WHSC1:RNF8:Zn2+:SUMO1:p-T4827-HERC2:UBE2N:UBE2V2:RNF168:PIAS4:p-S25,S1778-TP53BP1:p-5S,2T-BRCA1-A complex		R-HSA-5684071 (Reactome)
DNA

DNA

DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:K63PolyUb-K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-Nucleosome:p-5T-MDC1:p-S102-WHSC1:RNF8:Zn2+:SUMO1:p-T4827-HERC2:UBE2N:UBE2V2:RNF168:PIAS4:p-S25,S1778-TP53BP1:p-5S,2T-BRCA1-A complex		R-HSA-5684052 (Reactome)
DNA

DNA

DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:K63PolyUb-K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-Nucleosome:p-5T-MDC1:p-S102-WHSC1:RNF8:Zn2+:SUMO1:p-T4827-HERC2:UBE2N:UBE2V2:RNF168:PIAS4:p-S25,S1778-TP53BP1:p-5S,2T-BRCA1-A complex		mim-catalysisR-HSA-5684052 (Reactome)
DNA DSB:p-MRN:p-S1981,Ac-K3016-ATM:KAT5ArrowR-HSA-5684071 (Reactome)
DNA DSB:p-MRN:p-S1981,Ac-K3016-ATM:KAT5R-HSA-5684081 (Reactome)
DNA DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:CCNA:p-T160-CDK2:RBBP8ArrowR-HSA-5684081 (Reactome)
DNA DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:CCNA:p-T160-CDK2:RBBP8R-HSA-5684096 (Reactome)
DNA DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:CCNA:p-T160-CDK2:RBBP8mim-catalysisR-HSA-5684096 (Reactome)
DNA DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:p-BRCA1-C complexArrowR-HSA-5684108 (Reactome)
DNA DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:p-BRCA1-C complexR-HSA-5693608 (Reactome)
DNA DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:p-BRCA1-C complexmim-catalysisR-HSA-5693608 (Reactome)
DNA DSBs:p-MRN:p-S327,T847,T859-RBBP8:p-S1981,Ac-K3016-ATM:KAT5ArrowR-HSA-5684140 (Reactome)
DNA DSBs:p-MRN:p-S327,T847,T859-RBBP8:p-S1981,Ac-K3016-ATM:KAT5R-HSA-5684108 (Reactome)
DNA DSBs:p-MRN:p-S327,T847-RBBP8:p-S1981,Ac-K3016-ATM:KAT5ArrowR-HSA-5684096 (Reactome)
DNA DSBs:p-MRN:p-S327,T847-RBBP8:p-S1981,Ac-K3016-ATM:KAT5R-HSA-5684140 (Reactome)
DNA DSBs:p-MRN:p-S327,T847-RBBP8:p-S1981,Ac-K3016-ATM:KAT5mim-catalysisR-HSA-5684140 (Reactome)
EME1,EME2R-HSA-5686430 (Reactome)
ERCC1:ERCC4mim-catalysisR-HSA-5686657 (Reactome)
EXO1,DNA2:BLM,WRNArrowR-HSA-5686410 (Reactome)
EXO1,DNA2:BLM,WRNArrowR-HSA-5686469 (Reactome)
EXO1,DNA2:BLM,WRNArrowR-HSA-5686483 (Reactome)
EXO1,DNA2:BLM,WRNArrowR-HSA-5686657 (Reactome)
EXO1,DNA2:BLM,WRNArrowR-HSA-5693589 (Reactome)
EXO1,DNA2:BLM,WRNR-HSA-5685985 (Reactome)
Extended D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexArrowR-HSA-5693593 (Reactome)
Extended D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexR-HSA-5686440 (Reactome)
Extended D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexR-HSA-5693539 (Reactome)
Extended D-Loop:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexR-HSA-5693589 (Reactome)
FlapArrowR-HSA-5686657 (Reactome)
H2OR-HSA-5685994 (Reactome)
H2OR-HSA-5686410 (Reactome)
H2OR-HSA-5687758 (Reactome)
H2OR-HSA-5693589 (Reactome)
H2OR-HSA-5693608 (Reactome)
Holliday Junction:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexArrowR-HSA-5693539 (Reactome)
Holliday Junction:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexR-HSA-5686410 (Reactome)
Holliday Junction:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:p-BRCA1-C complex:PALB2:p-T3387-BRCA2:p-T309-RAD51:RAD51AP1:CX3 complexR-HSA-5693584 (Reactome)
K48PolyUb:SUMO2:K1840,p-5T-MDC1 dimerArrowR-HSA-5684071 (Reactome)
K63PolyUb:K14,K16,p-S139-H2AFX,Me2K21-HIST1H4A-NucleosomeArrowR-HSA-5684071 (Reactome)
KAT5ArrowR-HSA-5686410 (Reactome)
KAT5ArrowR-HSA-5686469 (Reactome)
KAT5ArrowR-HSA-5686483 (Reactome)
KAT5ArrowR-HSA-5686657 (Reactome)
KAT5ArrowR-HSA-5693589 (Reactome)
MUS81:EME1, (MUS81:EME2)ArrowR-HSA-5686430 (Reactome)
MUS81:EME1, (MUS81:EME2)R-HSA-5686475 (Reactome)
MUS81:EME1, (MUS81:EME2)mim-catalysisR-HSA-5686440 (Reactome)
MUS81R-HSA-5686430 (Reactome)
NAD+R-HSA-5685953 (Reactome)
NAMArrowR-HSA-5685953 (Reactome)
PALB2ArrowR-HSA-5686410 (Reactome)
PALB2ArrowR-HSA-5686469 (Reactome)
PALB2ArrowR-HSA-5686483 (Reactome)
PALB2ArrowR-HSA-5693589 (Reactome)
PALB2R-HSA-5693620 (Reactome)
PCNA:POLD,POLE,POLH,POLK:RPA:RFCmim-catalysisR-HSA-5693593 (Reactome)
PIAS4ArrowR-HSA-5684071 (Reactome)
PPP4C:PPP4R2mim-catalysisR-HSA-5687758 (Reactome)
PPiArrowR-HSA-5693593 (Reactome)
PiArrowR-HSA-5686410 (Reactome)
PiArrowR-HSA-5687758 (Reactome)
PiArrowR-HSA-5693589 (Reactome)
R-HSA-5684052 (Reactome) PIAS4 SUMOylates MDC1 at lysine residue K1840. The exact timing and regulation of this modification is not known (Luo et al. 2012, Yin et al. 2012).
R-HSA-5684071 (Reactome) SUMOylation of MDC1 by PIAS4 creates a docking site for RNF4, an E3 ubiquitin ligase. RNF4 binds to MDC1 specifically when SUMO2 is attached to lysine K1840 of MDC1. RNF4 polyubiquitinates MDC1 through ubiquitin lysine residue K48 cross-linking. RNF4-mediated ubiquitination targets MDC1 for degradation and causes dissociation of MDC1-bound proteins from DNA double strand breaks (DSBs). While additional regulation steps may be involved, the activity of RNF4 is necessary for the initiation of resection of DNA ends at DSBs and progression of homologous recombination (Luo et al. 2012, Yin et al. 2012, Galanty et al. 2012).
R-HSA-5684081 (Reactome) In the S/G2 phase of the cell cycle, CDK2:CCNA (CDK2:cyclin A) complex and CtIP (RBBP8) are recruited to DNA double strand breaks (DSBs) by the MRN complex. RBBP8 interacts with NBN (NBS1) and RAD50 subunits, while CDK2:CCNA interacts with the MRE11A subunit of the complex (Buis et al. 2012). RBBP8 functions as a homotetramer (Davies et al. 2015).
R-HSA-5684096 (Reactome) CDK2, in complex with cyclin A (CCNA), phosphorylates RBBP8 (CtIP) on serine residue S327 and threonine residue T847. Residue T847 is conserved in the yeast ortholog of CtIP, Sae2, and phosphorylation of T847 increases CtIP activity in DNA end resection. Serine S327 phosphorylation enables CtIP to bind BRCA1 (Buis et al. 2012).
R-HSA-5684108 (Reactome) BRCA1:BARD1 complex binds RBBP8 (CtIP) phosphorylated by CDK2 at DNA double strand breaks (DSBs), thus forming the so-called BRCA1-C complex. As active CDK2 in complex with CCNA (cyclin A) exists only in the S and G2 phases of the cell cycle, this limits the formation of BRCA1 complex with RBBP8 and the consequent initiation of homologous recombination to S and G2 phases, when the genome is duplicated and sister chromatids are available (Chen et al. 2008, Yun and Hiom 2009). Dissociation of the BRCA1-A complex is necessary for BRCA1 to be able to bind RBBP8 (Coleman and Greenberg 2011). Phosphorylation of BRCA1 by CHEK2 also contributes to the initiation of homologous recombination, with this phosphorylation similarly serving as a molecular clock (Parameswaran et al. 2015).
R-HSA-5684140 (Reactome) CDK2-mediated phosphorylation of RBBP8 (CtIP) triggers ATM-mediated phosphorylation of RBBP8 on several ATM consensus SQ/TQ sites. The ATM phosphorylation site at threonine residue T859 of RBBP8 is evolutionarily conserved and seems to be particularly important for the RBBP8-promoted resection of DNA double strand break (DSB) ends (Wang et al. 2013).
R-HSA-5684875 (Reactome) ATR (ATM- and rad3-related) kinase is an essential checkpoint factor in human cells constitutively associated with ATRIP (ATR-interacting protein). The ATR:ATRIP complex binds RPA complex (RPA1:RPA2:RPA3) associated with ssDNA at resected DNA double strand breaks (DSBs). Complex formation is primarily mediated by physical interaction between ATRIP and RPA1 (Zou and Elledge 2003, Jazayeri et al. 2006).
R-HSA-5684882 (Reactome) The recruitment of CHEK1 (CHK1) to resected DNA double strand breaks (DSBs) and activation by ATR-mediated phosphorylation requires the presence of CLSPN (claspin) and TIMELESS:TIPIN protein complex. TIPIN simultaneously interacts with the RPA2 subunit of the RPA complex and CLSPN, allowing CLSPN to stably associate with resected DNA DSBs (Kemp et al. 2010). Phosphorylation of CLSPN at threonine T916 and serine S945 is needed for CHEK1 binding (Kumagai et al. 2003, Clarke and Clarke 2005). CLSPN phosphorylation at these sites is independent of CHEK1 (Bennett et al. 2008). Casein kinase 1 (CK1) was proposed as a kinase responsible for CLSPN phosphorylation (Meng et al. 2011) but the exact mechanism of this modification has not been established.

ATR-mediated phosphorylation of RAD17 on serine residues S635 and S645 is implicated in CLSPN recruitment to resected DNA DSBs and CLSPN phosphorylation (Wang et al. 2006). Also, phosphorylation of the RPA2 subunit of the RPA complex positively contributes to CHEK1 activation (Liu et al. 2012).

R-HSA-5684887 (Reactome) CHEK1 (Chk1) is a checkpoint kinase activated during genotoxic stress. CHEK1 activation at resected DNA double strand breaks (DSBs) involves ATR-mediated phosphorylation of CHEK1 serine residues S317 and S345 in the presence of claspin (CLSPN), TOPBP1, RAD17:RFC complex, RAD9:HUS1:RAD1 complex, TIMELESS:TIPIN complex, RPA complex and RHNO1 (Liu et al. 2000, Zhao and Piwnica-Worms 2001, Kumagai and Dunphy 2003, Sorensen et al. 2004, Wang et al. 2006, Kemp et al. 2010, Cotta-Ramusino et al. 2011, Liu et al. 2012). Following phosphorylation, CHEK1 dissociates from chromatin and phosphorylates target proteins involved in S/G2 checkpoint activation and/or homologous recombination repair (Smits et al. 2006). CLSPN needs to interact with chromatin only transiently in order to facilitate CHEK1 activation (Lee et al. 2005).
R-HSA-5685011 (Reactome) ATR:ATRIP complex is recruited to resected DNA double strand breaks (DSBs) via interaction with the RPA complex that coats single strand DNA (ssDNA) 3'-overhangs, but this is not sufficient for ATR to become catalytically active. ATR kinase activity requires the presence of the RAD17:RFC complex, RAD9:HUS1:RAD1 (9-1-1) complex and TOPBP1. RAD17:RFC loads RAD9:HUS1:RAD1 onto junctions of single strand and double strand DNA (ssDNA-dsDNA junctions), present at resected DNA DSBs (Bermudez et al. 2003, reviewed by Sancar et al. 2004). TOPBP1 binds the C-terminal tail of RAD9, and is thus brought in the proximity of ATR, where it can activate it (Kumagai et al. 2006, Delacroix et al. 2007). The interaction of TOPBP1 and RBBP8 (CtIP) also contributes to TOPBP1 loading (Ramirez-Lugo et al. 2011). Phosphorylation of ATR at threonine residue T1989 may create a binding site for the BRCT domains of TOPBP1 (Liu et al. 2011). It is not clear whether T1989 of ATR is phosphorylated through autophosphorylation (Liu et al. 2011), as it does not conform to the SQ/TQ consensus, or by another kinase (Liu et al. 2013). RHNO1 (RHINO) protein simultaneously binds RAD9:HUS1:RAD1 complex and TOPBP1 and is required for the full catalytic activation of ATR (Cotta-Ramusino et al. 2011).
R-HSA-5685156 (Reactome) Activated ATR phosphorylates the RPA2 subunit of the RPA complex on serine residue S33. Phosphorylation of RPA2 at S33 likely stimulates additional RPA2 phosphorylation on CDK sites (S23 and S29) and DNA-PKcs (PRKDC) sites (S4, S8 and S21). DNA damage-regulated phosphorylation of RPA2 plays an important role in the progression of homologous recombination-directed repair of DNA double strand breaks (DSBs) (Anantha et al. 2007, Liu et al. 2012, Murphy et al. 2014)
R-HSA-5685230 (Reactome) Activated CHEK1 phosphorylates RAD51 on threonine residue T309, which is necessary for RAD51 association with chromatin (Sorensen et al. 2005).
R-HSA-5685242 (Reactome) CHEK1 phosphorylates BRCA2 on threonine residue T3887, in the C-terminal region of BRCA2. CHEK1-mediated BRCA2 phosphorylation, as well as CHEK1 mediated RAD51 phosphorylation, promotes the association of BRCA2 with RAD51 (Bahassi et al. 2008).
R-HSA-5685318 (Reactome) RAD51 paralogs RAD51B, RAD51C, RAD51D and XRCC2 form a complex named BCDX2 with 1:1:1:1 stoichiometry. In this complex, RAD51B directly interacts with RAD51C, which interacts with RAD51D, which interacts with XRCC2 (Masson et al. 2001, Chun et al. 2013).
R-HSA-5685319 (Reactome) RAD51 paralogs RAD51C and XRCC3 form the CX3 complex with 1:1 stoichiometry (Masson et al. 2001, Chun et al. 2013).
R-HSA-5685341 (Reactome) The BCDX2 complex, composed of RAD51 paralogs RAD51B, RAD51C, RAD51D and XRCC2, preferentially binds at the ends of 3' overhanging ssDNA created by resection of DNA double strand breaks (DSBs). The BCDX2 complex stabilizes nucleoprotein filaments formed by BRCA2-mediated RAD51 loading onto ssDNA (Masson et al. 2001, Chun et al. 2013). The BCDX2 complex may act by inhibiting displacement of RAD51 by BLM helicase (Amunugama et al. 2013).
R-HSA-5685838 (Reactome) The CX3 complex, composed of RAD51 paralogs RAD51C and XRCC3 (Masson, Tarsounas et al. 2001), binds homologous recombination repair sites at a later time point than the BCDX2 complex (Chun et al. 2013). Both RAD51C and XRCC3 can directly interact with PALB2 (Park et al. 2014). CX3 complexes, as well as BCDX2 complexes, multimerize into ring like structures with a central cavity (Masson, Stasiak et al. 2001, Compton et al. 2010). The CX3 complex may be involved in the resolution of Holliday junctions (Liu et al. 2004, Liu et al. 2007).
R-HSA-5685953 (Reactome) RBBP8 (CtIP) is constitutively acetylated in the absence of DNA damage on lysine residues K432, K526 and K604, and perhaps other lysines. DNA damage, through an unknown mechanism, triggers deacetylation of RBBP8 by SIRT6 protein lysine deacetylase. SIRT6-mediated deacetylation of RBBP8 is necessary for RBBP8-promoted resection of DNA double strand breaks (DSBs) (Kaidi et al. 2010).
R-HSA-5685985 (Reactome) After the initial resection of DNA double strand breaks (DSBs) by MRE11A and RBBP8 (CtIP), which creates short 3' ssDNA overhangs, a DNA exonuclease EXO1 or a DNA endonuclease DNA2 is recruited to perform long-range resection of DNA DSBs. The redundant function of EXO1 and DNA2 in resection of DNA DSBs is conserved in yeast (Zhu et al. 2008). BLM, the Bloom syndrome helicase, acts as an activator of DNA2 catalytic activity (Nimonkar et al. 2011) and increases affinity of EXO1 for DNA ends (Nimonkar et al. 2008). BLM directly interacts with the MRN complex, which can assist recruitment of either DNA2 or EXO1 to DNA DSBs (Nimonkar et al. 2011). EXO1 can also be recruited to DNA DSBs through its interaction with RBBP8 (CtIP) (Eid et al. 2010, Nimonkar et al. 2011). Another DNA helicase, WRN (Werner syndrome helicase) can function redundantly with BLM to facilitate/activate EXO1- or DNA2-mediated long range resection of DNA DSBs (Sturzenegger et al. 2014).

A DNA helicase BRIP1 (also known as BACH1 or FANCJ) is recruited to DNA DSBs through its interaction with BRCA1 (Cantor et al. 2001) and BLM (Suhasini et al. 2011, Suhasini and Brosh 2012). BRIP1 promotes DNA end processing events that stimulate recruitment of the RPA complex and RAD51 (Xie et al. 2012). The interaction with BRCA1 requires BRIP1 to be phosphorylated on serine residue S990 in a cell cycle-dependent manner (Yu et al. 2003). BRIP1 also has to be acetylated on lysine residue K1249 to be functional (Xie et al. 2012).

R-HSA-5685994 (Reactome) DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double strand breaks (DSBs). Both DNA nucleases act after short 3' ssDNA overhangs are created by the initial resection of DNA DSBs mediated by MRE11A and RBBP8 (CtIP). The roles of BLM (Bloom syndrome helicase) and WRN (Werner syndrome helicase) in facilitation of EXO1- or DNA2-mediated resection of DNA DSBs are also redundant.

EXO1 possesses an intrinsic 5'->3' exonuclease activity. The ATPase activity of BLM DNA helicase is not required for EXO1 catalytic activity, but BLM increases the affinity of EXO1 for DNA ends (Nimonkar et al. 2008). WRN can also positively affect EXO1 exonuclease activity, although the mechanism is not clear (Sturzenegger et al. 2014).

The DNA endonuclease DNA2 has to form a complex with either BLM (Nimonkar et al. 2011) or WRN (Sturzenegger et al. 2014) in order to perform a 5'->3' directed resection of DNA DSBs. BLM forms an evolutionarily conserved complex with TOP3A, RMI1 and RMI2, known as the STR complex in yeast (Zhu et al. 2008) and the BTB or BTRR complex in humans. The entire BTRR complex participates in the activation of DNA2-mediated resection of DNA DSBs (Sturzenegger et al. 2014).

While ATR signaling may be detectable in the absence of long-range resection of DNA DSBs by EXO1 or DNA2 (Eid et al. 2010), EXO1 or DNA2 activity may be necessary to achieve biologically meaningful level of ATR activation (Gravel et al. 2008).

BRIP1 (BACH1, FANCJ) is a DNA helicase recruited to DNA DSBs by interaction with BRCA1 (Cantor et al. 2001) and BLM (Suhasini et al. 2011). BRIP1 is necessary for BRCA1-mediated homology-directed repair of DNA DSBs, and BRIP1 loss-of-function mutations are found in familial breast cancer (Cantor et al. 2001, Litman et al. 2005). The exact role of BRIP1 in DNA repair is not completely clear. BRIP1 is needed for the successful formation of RPA foci and, subsequently, RAD51 foci (Xie et al. 2012). The available evidence suggest that it cooperates with BLM in unwinding of DNA DSBs during resection (Suhasini et al. 2011, Sarkies et al. 2012), and may be especially important for unwinding of DNA that contains oxidative damage (Suhasini et al. 2009).

R-HSA-5686398 (Reactome) SPIDR binds the BTRR complex (BLM:TOP3A:RMI1:RMI2) through a direct interaction with BLM. SPIDR also interacts with RAD51, thereby connecting the BTRR complex with Holliday Junctions (Wan et al. 2013).
R-HSA-5686410 (Reactome) The BTRR complex, composed of BLM, TOP3A, RMI1 and RMI2, dissolves double Holliday junctions by disentangling hemicatenane intermediates (Bocquet et al. 2014). This results in non-crossover products, where no exchange of genetic material happens between the sister chromatid that served as a template for the DNA repair synthesis and the repaired DNA duplex. SPIDR serves as a scaffold that connects the BTRR complex with the double Holliday junction through its simultaneous interaction with RAD51-coated DNA strands of the Holliday junction and BLM. SPIDR is needed for BTRR-mediated prevention of cross-over between sister chromatids (Wan et al. 2013).
R-HSA-5686430 (Reactome) MUS81 binds EME1 (MMS4) to form an evolutionarily conserved endonuclease complex involved in processing of aberrant replication intermediates and the cleavage of homologous recombination intermediates (Ciccia et al. 2003, Ogrunc and Sancar 2003). MUS81 can also form an endonuclease complex with EME2. EME2 is 40% identical to EME1 at the amino acid level and the MUS81:EME2 complex likely functions in a similar way to the MUS81:EME1 complex (Ciccia et al. 2007).
R-HSA-5686440 (Reactome) The complex of MUS81 and EME1 or EME2 acts as an endonuclease and processes D-loops by cleaving the sister chromatid strand complementary to the invading strand at the junction point. MUS81:EME2 complex has a higher catalytic activity than MUS81:EME1 complex and, in vitro, cleaves D-loops at several other sites in addition to the junction point (Osman et al. 2003, Pepe and West 2014). The yeast Mus81:Eme1 (Mus81:Mms4) complex also acts on D-loops (Schwartz et al. 2012).
R-HSA-5686469 (Reactome) Based on studies in yeast, D-loop cleavage by MUS81 in complex with EME1 or EME2 always produces crossovers between sister chromatids (Osman et al. 2003). The identity of the DNA polymerase(s) and ligase(s) that complete DNA repair synthesis and ligation after MUS81:EME1 or MUS81:EME2 cleavage of D-loops has not been determined.
R-HSA-5686475 (Reactome) SLX1A (SLX1) and SLX4 constitutively form a heterodimeric endonucleolytic complex that possesses a robust Holliday junction resolvase activity (Fekairi et al. 2009). SLX1A:SLX4 can form a complex with the MUS81:EME1 (and likely MUS81:EME2) complex, named SLX-MUS, through direct interaction of SLX4 with MUS81 (Fekairi et al. 2009, Wyatt et al. 2013). SLX-MUS is a more efficient and coordinated resolvase of Holliday junctions than SLX1A:SLX4 or MUS81:EME1 (or MUS81:EME2) (Wyatt et al. 2013).
R-HSA-5686483 (Reactome) The identity of DNA ligases that ligate DNA strands generated during cleavage of Holliday junctions by GEN1 or the SLX-MUS complex (composed of SLX1A:SLX4 heterodimer and MUS81:EME1 or possibly MUS81:EME2 heterodimer) is not known. The resolvase activity of GEN1 or SLX-MUS predominantly results in the generation of crossover products, with exchange of genetic material between sister chromatids (Wyatt et al. 2013).
R-HSA-5686587 (Reactome) ABL1 (c-ABL), activated by ATM-mediated phosphorylation in response to DNA double strand breaks (DSBs), phosphorylates RAD52 on tyrosine residue Y104, thus increasing the affinity of RAD52 heptamer for ssDNA and enhancing the efficiency of RAD52-mediated single strand annealing (SSA) (Honda et al. 2011).
R-HSA-5686642 (Reactome) RAD52 promotes annealing of 3' ssDNA overhangs at resected DNA double strand breaks (DSBs) through complementary regions. The complementarity between the two 3' ssDNA overhangs at resected DNA DSBs exists if 3' ssDNA overhangs contain direct repeats. While single strand annealing (SSA) requires significant homology between the annealed sequences it is nonetheless mutagenic. The parts of two 3' overhanging DNA single strands at resected DSBs that lie 3' to the annealed regions become displaced as flaps and subsequently excised. This results in the deletion (loss) of the DNA sequence lying between the two regions of homology used for SSA, as well as the deletion of one of the repeats used for annealing (Parsons et al. 2000, Van Dyck et al. 2001, Singleton et al. 2002, Stark et al. 2004, Mansour et al. 2008).
R-HSA-5686657 (Reactome) The endonuclease complex ERCC1:XPF (ERCC1:ERCC4) is recruited to single strand annealing (SSA) sites of DNA double strand break (DSB) repair through direct interaction between XPF (ERCC4) and RAD52 (Motycka et al. 2004). ERCC1:XPF cleaves the ssDNA flaps generated by displacement of non-complementary 3' parts of 3' ssDNA overhangs during RAD52-mediated annealing. The enzymatic activity of ERCC1:XPF is necessary for the completion of SSA (Motycka et al. 2004, Al-Minawi et al. 2008, Ahmad et al. 2008).
R-HSA-5686663 (Reactome) An unknown DNA ligase ligates single strand breaks (SSBs) remaining after RAD52-mediated single strand annealing (SSA) of resected DNA double strand breaks (DSBs) and cleavage of displaced flaps by ERCC1:XPF (ERCC1:ERCC4). The product of SSA is a double-strand DNA with a deletion of one complementary region (repeat) and the sequence lying between the two complementary regions used for SSA (inter-SSA deletion) (reviewed by Ciccia and Elledge 2010).
R-HSA-5687758 (Reactome) The protein serine/threonine phosphatase complex composed of a catalytic subunit PPP4C (PP4C) and a regulatory subunit PPP4R2 (PP4R2) dephosphorylates serine S33 of the RPA2 subunit of the RPA heterotrimer. By regulating the availability of unphosphorylated RPA2, PPP4C:PPP4R2 phosphatase regulates the progression of the homologous recombination repair of DNA double strand breaks and the duration of ATR checkpoint signaling (Lee et al. 2010).
R-HSA-5693539 (Reactome) Ligation of the crossed-strand intermediate results in the formation of double Holliday junctions with two crossovers. In humans, the identity of the ligase activity involved in this process is not known (reviewed by Ciccia and Elledge 2010).
R-HSA-5693542 (Reactome) Human replication protein A (RPA) is a single-stranded DNA (ssDNA) binding protein complex required for DNA replication, recombination, and repair. RPA is a stable heterotrimer consisting of subunits with molecular masses of 14, 32 and 70 kDa (p14, p32 and p70, respectively). Association of RPA with ssDNA is thought to contribute to both the protection and removal of secondary structure from single-stranded DNA (ssDNA) (McIlwraith et al. 2000). The RPA complexes coat 3'-ssDNA overhangs generated by RBBP8 (CtIP)-initiated long-range resection of DNA double strand breaks (DSBs) (Sartori et al. 2007, Chen et al. 2008).
R-HSA-5693558 (Reactome) After synthesis-dependent strand annealing (SDSA), the reannealed DNA molecule contains a single strand nick (SSB) in the newly synthesized strand, between the 3' end of the newly added stretch of nucleotides and the resected 5' end of the strand. In addition, the complementary strand contains a gap created by resection that was not filled during DNA repair synthesis. Additional DNA synthesis occurs to fill in this remaining single-strand gap present in the reannealed DNA duplex. SSBs between newly added stretches of nucleotides and resected 5' ends need to be closed by DNA ligases. The identity of DNA polymerase(s) and DNA ligase(s) involved in the completion of DNA double strand break repair through SDSA is not known. RTEL1 DNA helicase, which resolves D-loops in SDSA, binds PCNA and may promote DNA synthesis after reannealing (Vannier et al. 2013). DNA polymerase alpha is implicated in late steps of DNA repair synthesis (Levy et al. 2009), but other PCNA-bound DNA polymerases may also be involved. LIG1, as well as LIG3 in complex with XRCC1, may act to ligate SSBs (Fan et al. 2004, Mortusewicz et al. 2006, Mortusewicz et al. 2007, Puebla-Osorio et al. 2006).
R-HSA-5693561 (Reactome) BRCA2 and RAD51 interact directly through the highly conserved BRCT repeats in BRCA2 (Venkitaraman 2002). CHEK1-mediated phosphorylation of BRCA2 (at threonine residue T3387) and RAD51 (at threonine residue T309) facilitates their binding (Sorensen et al. 2005, Bahassi et al. 2008). One BRCA2 can bind up to six RAD51 molecules, thus playing an important role in RAD51 nucleation at the dsDNA-ssDNA junction created by resection of DNA double strand breaks (DSBs) (Liu et al. 2010, Thorslund et al. 2010, Jensen et al. 2010). After the nucleation step, additional RAD51 molecules bind the ssDNA and multimerize, forming RAD51 nucleoprotein filaments (Yang et al. 2005). BRCA2-mediated RAD51 loading displaces the RPA complex from 3' overhanging ssDNA at DSBs (Sugiyama et al. 1997, Jensen et al. 2010), presumably with other RPA-bound proteins, such as ATR:ATRIP and complexes involved in ATR catalytic activation.
R-HSA-5693564 (Reactome) RAD52 can simultaneously interact with RAD51 and RPA. The interaction with RAD51 may inhibit the formation of the invading RAD51 filament by sequestering RAD51 from RPA, thus promoting single strand annealing (SSA) instead of homologous recombination (Chen et al. 1999, Stark et al. 2004, Singleton et al. 2002, Mansour et al. 2008). The interaction of RAD51 and RAD52 is promoted by ABL1-mediated phosphorylation of both RAD51 and RAD52 (Chen et al. 1999, Van Dyck et al. 1999), which also increases RAD52 affinity for DNA (Honda et al. 2011).
R-HSA-5693580 (Reactome) RAD52 heptamers bind 3' overhanging ssDNA at resected DNA double strand breaks (DSBs) by simultaneously interacting with the DNA and the RPA complex. The conformation of the RAD52-ssDNA complex is thought to place the ssDNA on an exposed surface of the ring, in a configuration that may promote the DNA-DNA annealing of complementary DNA strands (Parsons et al. 2000). The interaction with RPA is necessary for RAD52-mediated homology driven repair (Park et al. 1996, Jackson et al. 2002). Phosphorylation of RAD52 at tyrosine residue Y104 by ABL1 in response to ATM signaling increases the affinity of RAD52 for DNA (Kitao et al. 2002, Cramer et al. 2008, Honda et al. 2011). Long range resection, which results in the activation of ATR/CHEK1 signaling, is needed for RAD52-mediated single strand annealing (SSA). RAD52 function may be promoted by a direct interaction with WRN helicase which participates in long-range resection of DNA DSBs (Baynton et al. 2003).
R-HSA-5693584 (Reactome) Holliday junctions are efficiently cleaved either by GEN1 endonuclease or the SLX-MUS complex, composed of the SLX1A:SLX4 heterodimer and the heterodimer of MUS81 and EME1 (or, possibly, EME2). Both SLX1A:SLX4 and MUS1:EME1,EME2 possess endonucleolytic activity and act in a coordinated fashion. SLX1A:SLX4 cleaves the double Holliday junction first, which is followed by MUS81:EME1 (or MUS81:EME2) mediated cleavage of the incised Holliday junction. Cleavage by both GEN1 and SLX-MUS predominantly leads to exchange of genetic material between sister chromatids, creating crossover products (Wyatt et al. 2013, Sarbajna et al. 2014).
R-HSA-5693589 (Reactome) Following repair synthesis, the extended D-loop strands may disassociate from their sister chromatid complements and reanneal with their original complementary strands. A DNA helicase RTEL1 disrupts preformed D-loops and promotes synthesis-dependent strand annealing, yielding non-crossover products and preventing excessive recombination between mitotic sister chromatids (Barber et al. 2008, Uringa et al. 2012).
R-HSA-5693593 (Reactome) Following branch migration, the invading 3' resected ssDNA end of the double-strand break (DSB) acts as a primer for repair DNA synthesis using the complementary strand of the invaded duplex as a template. The replicative DNA polymerases delta (POLD) and likely epsilon (POLE), as well as translesion synthesis (TLS) DNA polymerases eta (POLH) and kappa (POLK) in complex with PCNA, RFC and RPA are implicated in DNA repair synthesis and D-loop extension. While TLS polymerases increase the efficiency of homologous recombination-related DNA synthesis and can directly interact with D-loop proteins RAD51, PALB2 and BRCA2, it is likely that replicative DNA polymerases POLD and POLE, with their high processivity and fidelity, perform the major role in D-loop extension (McIlwraith et al. 2005, Sebesta et al. 2013, Pomerantz et al. 2013, Buisson et al. 2014). In addition, the presence of RAD51-translocases, homologous to yeast Rad54, that remove RAD51 from the 3' invading strand, may be necessary for the catalytic activity of POLD or POLE (Li et al. 2009, Li and Heyer 2009).
R-HSA-5693608 (Reactome) In order for repair of the DNA double-strand breaks to occur through homologous recombination or single strand annealing, the 5' ends of the break must first be resected to produce 3' overhanging single stranded DNA (ssDNA) that can subsequently invade homologous duplex DNA (e.g. in the sister chromatid) (Thompson et al. 2001, Kolpashchikov et al. 2001). The MRE11A component of the MRN complex possesses endonuclease activity (Trujillo et al. 1998, Hopfner et al. 2002) that is activated by binding of RBBP8 (CtIP) and BRCA1, in the presence of Mn2+ or Mg2+ ions (Sartori et al. 2007, Yun and Hiom 2009).
R-HSA-5693620 (Reactome) A D-loop structure is formed when complementary duplex DNA (sister chromatid arm) is progressively invaded by the RAD51 nucleoprotein filament, with base pairing of the invading ssDNA and the complementary sister chromatid DNA strand (Sung et al. 2003). PALB2 and RAD51AP1 synergistically stimulate RAD51 recombinase activity, thus enhancing RAD51-mediated strand exchange (branch migration) and promoting the formation of D-loop structures (synaptic complex assembly). PALB2 simultaneously interacts with RAD51, BRCA2 and RAD51AP1 (Modesti et al. 2007, Wiese et al. 2007, Buisson et al. 2010, Dray et al. 2010). The direct BRCA1 interaction with PALB2 helps to fine-tune the localization of BRCA2 and RAD51 at DNA double strand breaks (DSBs) (Zhang et al. 2009, Sy et al. 2009).
R-HSA-75998 (Reactome) RAD52 forms heptameric ring structure complexes (Stasiak et al. 2000, Kagawa et al. 2002, Lloyd et al. 2002, Singleton et al. 2002).
RAD17:RFCArrowR-HSA-5686657 (Reactome)
RAD17:RFCArrowR-HSA-5693561 (Reactome)
RAD17:RFCR-HSA-5685011 (Reactome)
RAD51:p-Y104-RAD52:p-RPA:ATR:ATRIP:3' overhanging ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1ArrowR-HSA-5693564 (Reactome)
RAD51:p-Y104-RAD52:p-RPA:ATR:ATRIP:3' overhanging ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1R-HSA-5686642 (Reactome)
RAD51:p-Y104-RAD52:p-RPA:ATR:ATRIP:3' overhanging ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1mim-catalysisR-HSA-5686642 (Reactome)
RAD51:p-Y104-RAD52:p-RPA:ATR:ATRIP:DNA DSBs with annealed 3' ssDNA overhangs and displaced flaps:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1ArrowR-HSA-5686642 (Reactome)
RAD51:p-Y104-RAD52:p-RPA:ATR:ATRIP:DNA DSBs with annealed 3' ssDNA overhangs and displaced flaps:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1R-HSA-5686657 (Reactome)
RAD51AP1ArrowR-HSA-5686410 (Reactome)
RAD51AP1ArrowR-HSA-5686469 (Reactome)
RAD51AP1ArrowR-HSA-5686483 (Reactome)
RAD51AP1ArrowR-HSA-5693589 (Reactome)
RAD51AP1R-HSA-5693620 (Reactome)
RAD51ArrowR-HSA-5686657 (Reactome)
RAD51BR-HSA-5685318 (Reactome)
RAD51CR-HSA-5685318 (Reactome)
RAD51CR-HSA-5685319 (Reactome)
RAD51DR-HSA-5685318 (Reactome)
RAD51R-HSA-5685230 (Reactome)
RAD51R-HSA-5693564 (Reactome)
RAD52 heptamerArrowR-HSA-75998 (Reactome)
RAD52 heptamerR-HSA-5686587 (Reactome)
RAD52R-HSA-75998 (Reactome)
RAD9:HUS1:RAD1ArrowR-HSA-5686657 (Reactome)
RAD9:HUS1:RAD1ArrowR-HSA-5693561 (Reactome)
RAD9:HUS1:RAD1R-HSA-5685011 (Reactome)
RBBP8 homotetramerArrowR-HSA-5685953 (Reactome)
RBBP8 homotetramerR-HSA-5684081 (Reactome)
RHNO1ArrowR-HSA-5686657 (Reactome)
RHNO1ArrowR-HSA-5693561 (Reactome)
RHNO1R-HSA-5685011 (Reactome)
RNF168ArrowR-HSA-5684071 (Reactome)
RNF4 homodimermim-catalysisR-HSA-5684071 (Reactome)
RNF8:Zn2+ArrowR-HSA-5684071 (Reactome)
RPA heterotrimerArrowR-HSA-5687758 (Reactome)
RPA heterotrimerR-HSA-5693542 (Reactome)
RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		ArrowR-HSA-5693542 (Reactome)
RPA:3'

overhanging

ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1		R-HSA-5684875 (Reactome)
RTEL1mim-catalysisR-HSA-5693589 (Reactome)
SIRT6mim-catalysisR-HSA-5685953 (Reactome)
SLX1A:SLX4:MUS81:EME1,(MUS81:EME2),GEN1mim-catalysisR-HSA-5693584 (Reactome)
SLX1A:SLX4:MUS81:EME1,(MUS81:EME2)ArrowR-HSA-5686475 (Reactome)
SLX1A:SLX4R-HSA-5686475 (Reactome)
SPIDRR-HSA-5686398 (Reactome)
SSB-dsDNA with inter-SSA deletionArrowR-HSA-5686657 (Reactome)
SSB-dsDNA with inter-SSA deletionR-HSA-5686663 (Reactome)
SUMO1:p-T4827-HERC2ArrowR-HSA-5684071 (Reactome)
SUMO2:UBE2IR-HSA-5684052 (Reactome)
Sister Chromatid Arm with CrossoverArrowR-HSA-5686469 (Reactome)
Sister Chromatid Arm with CrossoverArrowR-HSA-5686483 (Reactome)
Sister Chromosomal ArmArrowR-HSA-5686410 (Reactome)
Sister Chromosomal ArmArrowR-HSA-5693589 (Reactome)
Sister Chromosomal ArmR-HSA-5693620 (Reactome)
TIMELESS:TIPINArrowR-HSA-5684887 (Reactome)
TIMELESS:TIPINR-HSA-5684882 (Reactome)
TOPBP1ArrowR-HSA-5686657 (Reactome)
TOPBP1ArrowR-HSA-5693561 (Reactome)
TOPBP1R-HSA-5685011 (Reactome)
UBE2IArrowR-HSA-5684052 (Reactome)
UBE2N:UBE2V2ArrowR-HSA-5684071 (Reactome)
UIMC1ArrowR-HSA-5684071 (Reactome)
UbR-HSA-5684071 (Reactome)
XRCC2R-HSA-5685318 (Reactome)
XRCC3R-HSA-5685319 (Reactome)
dNTPArrowR-HSA-5685994 (Reactome)
dNTPArrowR-HSA-5693608 (Reactome)
dNTPR-HSA-5693593 (Reactome)
dsDNA with crossoverArrowR-HSA-5686469 (Reactome)
dsDNA with crossoverArrowR-HSA-5686483 (Reactome)
dsDNA with inter-SSA deletionArrowR-HSA-5686663 (Reactome)
dsDNAArrowR-HSA-5686410 (Reactome)
dsDNAArrowR-HSA-5693558 (Reactome)
p-5S-BRCA1:p-2T-BARD1ArrowR-HSA-5684071 (Reactome)
p-5S-BRCA1:p-2T-BARD1ArrowR-HSA-5686410 (Reactome)
p-5S-BRCA1:p-2T-BARD1ArrowR-HSA-5686469 (Reactome)
p-5S-BRCA1:p-2T-BARD1ArrowR-HSA-5686483 (Reactome)
p-5S-BRCA1:p-2T-BARD1ArrowR-HSA-5686657 (Reactome)
p-5S-BRCA1:p-2T-BARD1ArrowR-HSA-5693589 (Reactome)
p-5S-BRCA1:p-2T-BARD1R-HSA-5684108 (Reactome)
p-MRNArrowR-HSA-5686410 (Reactome)
p-MRNArrowR-HSA-5686469 (Reactome)
p-MRNArrowR-HSA-5686483 (Reactome)
p-MRNArrowR-HSA-5686657 (Reactome)
p-MRNArrowR-HSA-5693589 (Reactome)
p-RPA heterotrimerArrowR-HSA-5686657 (Reactome)
p-RPA heterotrimerArrowR-HSA-5693561 (Reactome)
p-RPA heterotrimerR-HSA-5687758 (Reactome)
p-S102-WHSC1ArrowR-HSA-5684071 (Reactome)
p-S1981,Ac-K3016-ATMArrowR-HSA-5686410 (Reactome)
p-S1981,Ac-K3016-ATMArrowR-HSA-5686469 (Reactome)
p-S1981,Ac-K3016-ATMArrowR-HSA-5686483 (Reactome)
p-S1981,Ac-K3016-ATMArrowR-HSA-5686657 (Reactome)
p-S1981,Ac-K3016-ATMArrowR-HSA-5693589 (Reactome)
p-S25,S1778-TP53BP1ArrowR-HSA-5684071 (Reactome)
p-S317,S345-CHEK1ArrowR-HSA-5684887 (Reactome)
p-S317,S345-CHEK1mim-catalysisR-HSA-5685230 (Reactome)
p-S317,S345-CHEK1mim-catalysisR-HSA-5685242 (Reactome)
p-S327,T847,T859-RBBP8 homotetramerArrowR-HSA-5686410 (Reactome)
p-S327,T847,T859-RBBP8 homotetramerArrowR-HSA-5686469 (Reactome)
p-S327,T847,T859-RBBP8 homotetramerArrowR-HSA-5686483 (Reactome)
p-S327,T847,T859-RBBP8 homotetramerArrowR-HSA-5686657 (Reactome)
p-S327,T847,T859-RBBP8 homotetramerArrowR-HSA-5693589 (Reactome)
p-S406-FAM175AArrowR-HSA-5684071 (Reactome)
p-S456-ABL1mim-catalysisR-HSA-5686587 (Reactome)
p-S990,Ac-K1249-BRIP1ArrowR-HSA-5686410 (Reactome)
p-S990,Ac-K1249-BRIP1ArrowR-HSA-5686483 (Reactome)
p-S990,Ac-K1249-BRIP1ArrowR-HSA-5686657 (Reactome)
p-S990,Ac-K1249-BRIP1ArrowR-HSA-5693589 (Reactome)
p-S990,Ac-K1249-BRIP1R-HSA-5685985 (Reactome)
p-T309-RAD51ArrowR-HSA-5685230 (Reactome)
p-T309-RAD51R-HSA-5693561 (Reactome)
p-T3387-BRCA2:p-T309-RAD51 complexArrowR-HSA-5686410 (Reactome)
p-T3387-BRCA2:p-T309-RAD51 complexArrowR-HSA-5686469 (Reactome)
p-T3387-BRCA2:p-T309-RAD51 complexArrowR-HSA-5686483 (Reactome)
p-T3387-BRCA2:p-T309-RAD51 complexArrowR-HSA-5693589 (Reactome)
p-T3387-BRCA2ArrowR-HSA-5685242 (Reactome)
p-T3387-BRCA2R-HSA-5693561 (Reactome)
p-T916,S945-CLSPNArrowR-HSA-5684887 (Reactome)
p-T916,S945-CLSPNR-HSA-5684882 (Reactome)
p-Y104-RAD52 heptamerArrowR-HSA-5686587 (Reactome)
p-Y104-RAD52 heptamerArrowR-HSA-5686657 (Reactome)
p-Y104-RAD52 heptamerR-HSA-5693580 (Reactome)
p-Y104-RAD52:p-RPA:ATR:ATRIP:3' overhanging ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1ArrowR-HSA-5693580 (Reactome)
p-Y104-RAD52:p-RPA:ATR:ATRIP:3' overhanging ssDNA-DSBs:p-MRN:p-S1981,Ac-K3016-ATM:KAT5:BRCA1-C complex:EXO1,DNA2:BLM,WRN:p-S990,Ac-K1249-BRIP1:RAD17:RFC:RAD9:HUS1:RAD1:RHNO1:TOPBP1R-HSA-5693564 (Reactome)
ss-gap-reannealed DNAArrowR-HSA-5693589 (Reactome)
ss-gap-reannealed DNAR-HSA-5693558 (Reactome)

Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP3567"
Personal tools