RAD1 Checkpoint DNA Exonuclease Peptide 1

CPTC-RAD1-1

RAD1 Checkpoint DNA Exonuclease Peptide 1

IgG

Rabbit Monoclonal Antibody

07/19/2024

Peptide

00426

RAD1 Checkpoint DNA Exonuclease Peptide 1

CPTC-RAD1 Peptide 1

RAD1 Checkpoint DNA Exonuclease; HRAD1; REC1; Rad1-Like DNA Damage Checkpoint Protein; Cell Cycle Checkpoint Protein Hrad1; DNA Repair Exonuclease Rad1 Homolog; Cell Cycle Checkpoint Protein RAD1; Checkpoint Control Protein HRAD1; RAD1 Checkpoint Clamp Component; DNA Repair Exonuclease REC1; Exonuclease Homolog RAD1; Rad1-Like DNA Damage Checkpoint; RAD1 (S. Pombe) Homolog; RAD1 Homolog (S. Pombe); RAD1 Homolog; EC 3.1.11.2; RAD1

This gene encodes a component of a heterotrimeric cell cycle checkpoint complex, known as the 9-1-1 complex, that is activated to stop cell cycle progression in response to DNA damage or incomplete DNA replication. The 9-1-1 complex is recruited by RAD17 to affected sites where it may attract specialized DNA polymerases and other DNA repair effectors. Alternatively spliced transcript variants of this gene have been described.RAD1 (RAD1 Checkpoint DNA Exonuclease) is a Protein Coding gene. Diseases associated with RAD1 include Alpha-Thalassemia/Mental Retardation Syndrome, X-Linked and Restless Legs Syndrome. Among its related pathways are Homologous DNA Pairing and Strand Exchange and E2F mediated regulation of DNA replication. Gene Ontology (GO) annotations related to this gene include damaged DNA binding and exodeoxyribonuclease III activity.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). Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity (PubMed:9660799).

5p13.2

NP_002844.1

O60671

N/A

Synthetic Peptide

N/A

990

09/20/2020