Cell cycle checkpoint protein RAD1 (hRAD1) (EC 3.1.11.2) (DNA repair exonuclease rad1 homolog) (Rad1-like DNA damage checkpoint protein)
1_MPLLT 6_ QQIQD 11_ EDDQY 16_ SLVAS 21_ LDNVR 26_ NLSTI 31_ LKAIH 36_ FREHA 41_ TCFAT 46_ KNGIK 51_ VTVEN 56_ AKCVQ 61_ ANAFI 66_ QAGIF 71_ QEFKV 76_ QEESV 81_ TFRIN 86_ LTVLL 91_ DCLSI 96_ FGSSP 101_ MPGTL 106_ TALRM 111_ CYQGY 116_ GYPLM 121_ LFLEE 126_ GGVVT 131_ VCKIN 136_ TQEPE 141_ ETLDF 146_ DFCST 151_ NVINK 156_ IILQS 161_ EGLRE 166_ AFSEL 171_ DMTSE 176_ VLQIT 181_ MSPDK 186_ PYFRL 191_ STFGN 196_ AGSSH 201_ LDYPK 206_ DSDLM 211_ EAFHC 216_ NQTQV 221_ NRYKI 226_ SLLKP 231_ STKAL 236_ VLSCK 241_ VSIRT 246_ DNRGF 251_ LSLQY 256_ MIRNE 261_ DGQIC 266_ FVEYY 271_ CCPDE 276_EVPES
1: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:10846170, PubMed:10884395). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:12578958). Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER) (PubMed:15871698). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates (PubMed:15314187, PubMed:15556996, PubMed:15871698). The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (PubMed:21659603)