Protein Name:
ATPase family AAA domain-containing protein 5
|
UniprotKB/SwissProt ID: Q96QE3 (Q96QE3)
Gene Name:
ATAD5
Organism: Homo sapiens (Human)
Function: Has an important role in DNA replication and in maintaining genome integrity during replication stress (PubMed:15983387, PubMed:19755857). Involved in a RAD9A-related damage checkpoint, a pathway that is important in determining whether DNA damage is compatible with cell survival or whether it requires cell elimination by apoptosis (PubMed:15983387). Modulates the RAD9A interaction with BCL2 and thereby induces DNA damage-induced apoptosis (PubMed:15983387). Promotes PCNA deubiquitination by recruiting the ubiquitin-specific protease 1 (USP1) and WDR48 thereby down-regulating the error-prone damage bypass pathway (PubMed:20147293). As component of the ATAD5 RFC-like complex, regulates the function of the DNA polymerase processivity factor PCNA by unloading the ring-shaped PCNA homotrimer from DNA after replication during the S phase of the cell cycle (PubMed:23277426, PubMed:23937667). This seems to be dependent on its ATPase activity (PubMed:23277426). Plays important roles in restarting stalled replication forks under replication stress, by unloading the PCNA homotrimer from DNA and recruiting RAD51 possibly through an ATR-dependent manner (PubMed:31844045). Ultimately this enables replication fork regression, breakage, and eventual fork restart (PubMed:31844045). Both the PCNA unloading activity and the interaction with WDR48 are required to efficiently recruit RAD51 to stalled replication forks (PubMed:31844045). Promotes the generation of MUS81-mediated single-stranded DNA-associated breaks in response to replication stress, which is an alternative pathway to restart stalled/regressed replication forks (PubMed:31844045)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Nucleus
|
|
|
Graphical Visualization of S-nitrosylation Sites:
|
|
The S-nitrosylation sites of Q96QE3
|
| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
290 |
EEIPDSTMSI C VPSETVDEIV |
|
|
|
| 2 |
433 |
SDKQKDLNEK C LYEVGRDDNS |
|
|
|
| 3 |
831 |
SEKSQDCDVQ C KAKRDFLMSG |
|
|
|
|
