Search Results
Overview
| Uniprot ID | Q9HAW4 |
|---|---|
| Protein Name | Claspin |
| Gene Name | CLSPN |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 105 | TKIKRIYKTVADSDE |
| 1265 | QPKAVLQKLAALSDH |
| 319 | KTIHDFFKRKPRPTC |
| 537 | ALKQRFWKHANPAAK |
| 824 | SLVSSASKSSGKLSE |
Function
Required for checkpoint mediated cell cycle arrest in response to inhibition of DNA replication or to DNA damage induced by both ionizing and UV irradiation (PubMed:12766152, PubMed:15190204, PubMed:15707391, PubMed:16123041). Adapter protein which binds to BRCA1 and the checkpoint kinase CHEK1 and facilitates the ATR-dependent phosphorylation of both proteins (PubMed:12766152, PubMed:15096610, PubMed:15707391, PubMed:16123041). Also required to maintain normal rates of replication fork progression during unperturbed DNA replication. Binds directly to DNA, with particular affinity for branched or forked molecules and interacts with multiple protein components of the replisome such as the MCM2-7 complex and TIMELESS (PubMed:15226314, PubMed:34694004, PubMed:35585232). Important for initiation of DNA replication, recruits kinase CDC7 to phosphorylate MCM2-7 components (PubMed:27401717)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005794 | Golgi apparatus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0010997 | anaphase-promoting complex binding |
| Molecular Function | GO:0000217 | DNA secondary structure binding |
| Biological Process | GO:0000077 | DNA damage checkpoint signaling |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0000076 | DNA replication checkpoint signaling |
| Biological Process | GO:0033314 | mitotic DNA replication checkpoint signaling |
| Biological Process | GO:0007095 | mitotic G2 DNA damage checkpoint signaling |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.