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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Cell cycle checkpoint protein RAD1

UniprotKB/SwissProt ID: O60671 (O60671)

Gene Name: RAD1

Organism: Homo sapiens (Human)

Function: 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)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR003011 Cell_cycle_checkpoint_Rad1
IPR046938 DNA_clamp_sf
IPR003021 Rad1_Rec1_Rad17

The S-nitrosylation sites of O60671

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 148 EPEETLDFDF C STNVINKIIL   
2 215 KDSDLMEAFH C NQTQVNRYKI   
3 42 KAIHFREHAT C FATKNGIKVT