Recombinant Human Claspin (CLSPN), partial

1. The functions of claspin are discussed and how its deregulation may contribute to cancer initiation and progression. [REVIEW] PMID: 28942358
2. Results unveil a new aspect of PERK function and previously unknown roles for Claspin and Chk1 as negative regulators of DNA replication in the absence of genotoxic stress. PMID: 27375025
3. found that USP9X regulated the expression and stability of CLASPIN in an S-phase-specific manner. USP9X depletion profoundly impairs the progression of DNA replication forks, causing unscheduled termination events with a frequency similar to CLASPIN depletion, resulting in excessive endogenous DNA damage PMID: 26921344
4. Functional analyses indicat that the expression TopBP1 and Claspin positively affects the survival of brain cancer cells after exposure to radiation. PMID: 25216549
5. And-1 coordinates with Claspin for efficient Chk1 activation in response to replication stress. PMID: 26082189
6. Rad9, Rad17, TopBP1 and claspin play essential roles in heat-induced activation of ATR kinase and heat tolerance. PMID: 23383325
7. findings identify claspin as an in vivo substrate for the BRCA1 E3 ligase and suggest that its modification selectively triggers CHK1 activation for the homology-directed repair of a subset of genotoxic lesions PMID: 22863316
8. analysis of claspin expression could be clinically relevant in the diagnosis of HPV-related cervical lesions, in particular when applied to cervico-vaginal cytology PMID: 22731782
9. The conserved C terminus of Claspin interacts with Rad9 and ensures timely activation of the ATR-Chk1 pathway. PMID: 22732499
10. the functions of Claspin and the functional relationship between Claspin and Rad17 were studied. PMID: 21945441
11. In the presence of BRCA1, endogenous HERC2 interacts with Claspin, a protein essential for G(2)-M checkpoint activation and replication fork stability. PMID: 21775519
12. The multiple protein-DNA and protein-protein interactions is important for Claspin function during DNA replication and DNA replication checkpoint signaling. PMID: 21478680
13. Tethering DNA damage checkpoint mediator proteins topoisomerase IIbeta-binding protein 1 (TopBP1) and Claspin to DNA activates ataxia-telangiectasia mutated and RAD3-related (ATR) phosphorylation of checkpoint kinase 1 (Chk1). PMID: 21502314
14. Here, the authors demonstrate that both the NF-kappaB family of transcription factors and their upstream kinase IKK can regulate Claspin levels by controlling its mRNA expression. PMID: 20657549
15. Rad9A-mediated Claspin localization is a vital step during checkpoint activation. PMID: 20081369
16. Data show that the ATR-dependent phosphorylation of Chk1, but not p53, is strongly stimulated by Claspin. PMID: 19828454
17. Resequenced CLSPN from the germline of selected cancer families; eight nonsynonymous variants, including a recurrent mutation, were id'd from the germline of two cancer-prone individuals and 5 cancer cell lines of breast, ovarian, & hematopoietic origin. PMID: 19737971
18. Claspin has a potentially critical role in replication checkpoint control in mammalian cells PMID: 12766152
19. determination of properties of both a tumor suppressor and an oncogene PMID: 15096610
20. has a ring-like structure and binds with high affinity to branched DNA molecules. PMID: 15226314
21. Claspin has roles in the Chk1 pathway and functions in checkpoint control [review] PMID: 15279790
22. cleavage of Claspin by caspase-7 inactivates the Chk1 signaling pathway PMID: 16123041
23. Claspin and Chk1 proteins regulate each other and thus ensure the proper cell cycle progression and replication checkpoint control. PMID: 16501606
24. the Chk1 pathway is regulated through both phosphorylation of Claspin and its controlled degradation. PMID: 16828751
25. These results suggest that while TopBP1 is a general regulator of ATR, Claspin operates downstream of TopBP1 to selectively regulate the Chk1-controlled branch of the genotoxic stress response. PMID: 16880517
26. Data suggest that degradation of Claspin by SCFbetaTrCP restrains Chk1 activation. PMID: 16885021
27. The SCFbetaTrCP-dependent degradation of claspin is necessary for the efficient and timely termination of the DNA replication checkpoint. PMID: 16885022
28. The degradation of Claspin at the onset of mitosis is an essential step for the recovery of a cell from a DNA-damage-induced cell-cycle arrest. PMID: 16934469
29. Chk1 can be activated in a claspin-dependent manner leading to cyclin B1 down-regulation and providing the cells of an additional mechanism to inhibit mitosis entry in Hela cells. PMID: 16951182
30. phosphorylation of Claspin repeats in human Claspin is important for Claspin function and the regulation of Claspin-Checkpoint kinase 1 interaction in human cells PMID: 16963448
31. human Claspin is found in complex with PCNA, an essential component of the DNA replication machinery, and is released upon DNA replication arrest. dissociation of Claspin-PCNA could be part of the signal leading to Chk1 activation. PMID: 17274954
32. downregulation of Claspin protein levels by short interfering RNA resulted in an increase in apoptotic induction both in the presence and absence of DNA damage PMID: 17431426
33. Altogether seven different sequence changes were observed, but none of them appeared to associate with breast cancer susceptibility. PMID: 18077083
34. These results demonstrate that phosphorylation of Claspin within the Chk1-binding domain is catalysed by an ATR-dependent kinase distinct from Chk1. PMID: 18331829
35. Depletion of Chk1 and Claspin together doubled the percentage of very slow forks, compared with depletion of either protein alone. PMID: 18353973
36. Data show that Chk1 and the Claspin-Timeless module of replication forks not only participate in ATR signaling, but also protect stressed forks independently of ATR. PMID: 18451105
37. Claspin plays a role regulating replication fork stability that is independent of its function in mediating Chk1 phosphorylation. PMID: 19270516
38. Cdh1 reciprocally regulates the Rb pathway through competing with E2F1 to bind the hypophosphorylated form of Rb. PMID: 19477924

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HGNC: 19715

OMIM: 605434

KEGG: hsa:63967

STRING: 9606.ENSP00000312995

UniGene: Hs.175613