Checkpoint protein HUS1 (hHUS1)
1_MKFRA 6_ KIVDG 11_ ACLNH 16_ FTRIS 21_ NMIAK 26_ LAKTC 31_ TLRIS 36_ PDKLN 41_ FILCD 46_ KLANG 51_ GVSMW 56_ CELEQ 61_ ENFFN 66_ EFQME 71_ GVSAE 76_ NNEIY 81_ LELTS 86_ ENLSR 91_ ALKTA 96_ QNARA 101_ LKIKL 106_ TNKHF 111_ PCLTV 116_ SVELL 121_ SMSSS 126_ SRIVT 131_ HDIPI 136_ KVIPR 141_ KLWKD 146_ LQEPV 151_ VPDPD 156_ VSIYL 161_ PVLKT 166_ MKSVV 171_ EKMKN 176_ ISNHL 181_ VIEAN 186_ LDGEL 191_ NLKIE 196_ TELVC 201_ VTTHF 206_ KDLGN 211_ PPLAS 216_ ESTHE 221_ DRNVE 226_ HMAEV 231_ HIDIR 236_ KLLQF 241_ LAGQQ 246_ VNPTK 251_ ALCNI 256_ VNNKM 261_ VHFDL 266_ LHEDV 271_SLQYF
1: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:21659603). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:21659603). Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER) (PubMed:21659603). 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:21659603). 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)