RAD1

Gene Symbol RAD1
Entrez Gene 5810
Alt Symbol HRAD1, REC1
Species Human
Gene Type protein-coding
Description RAD1 checkpoint DNA exonuclease
Other Description DNA repair exonuclease REC1|DNA repair exonuclease rad1 homolog|RAD1 homolog|cell cycle checkpoint protein Hrad1|cell cycle checkpoint protein RAD1|checkpoint control protein HRAD1|exonuclease homolog RAD1|rad1-like DNA damage checkpoint protein
Swissprots Q1W161 Q5KSM0 O95304 O60671 Q9UEP1 Q5KSM1 O75572
Accessions ABD96829 BAD86789 BAD86790 EAW55903 EAW55904 EAW55906 EAW55907 EAW55908 O60671 AF011905 AAC27243 AF030933 AAC95427 AF058392 AAC14138 AF058393 AF073524 AAC95466 AF074717 AAC98093 AF076841 AAC95523 AF084512 AAC35549 AF084513 AAC35550 AF090170 AAC95603 AJ004974 CAA06248 AJ004975 CAA06249 AK002112 BAG51017 AK096960 BC006837 AAH06837 BC009804 AAH09804 BC035771 BC037857 AAH37857 BT006908 AAP35554 DQ891144 ABM82070 DQ894324 ABM85250 NM_002853 NP_002844 NR_026591 NM_001033673 NM_133282 NM_133377
Function Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). 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. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity. {ECO:0000269|PubMed:21659603, ECO:0000269|PubMed:9660799}.
Subcellular Location Nucleus {ECO:0000269|PubMed:9716408}.
Tissue Specificity Expressed in testis, uterus, bladder, spleen, ovaries, lung, brain and muscle (at protein level). {ECO:0000269|PubMed:9716408}.

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