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Gene Review

CLSPN  -  claspin

Homo sapiens

Synonyms: Claspin, hClaspin
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Disease relevance of CLSPN

  • To this end, a monoclonal antibody was generated and the expression of claspin was investigated in normal fibroblasts and various cancer cell lines, as well as in tumour and normal tissues from patients with primary epithelial carcinomas [1].

High impact information on CLSPN


Biological context of CLSPN


Anatomical context of CLSPN


Associations of CLSPN with chemical compounds


Physical interactions of CLSPN

  • Significantly, expression of a stable Claspin mutant unable to bind betaTrCP prolongs the activation of Chk1, thereby attenuating the recovery from the DNA replication stress response and significantly delaying entry into mitosis [3].

Enzymatic interactions of CLSPN

  • Repeated phosphopeptide motifs in human claspin are phosphorylated by chk1 and mediate claspin function [7].

Regulatory relationships of CLSPN


Other interactions of CLSPN

  • Claspin localizes in the nuclei, but it only associates with Chk1 following replication stress or other types of DNA damage [8].
  • Claspin is an essential protein for the ATR-dependent activation of the DNA replication checkpoint response in Xenopus and human cells [9].
  • Moreover, Chk1 and Claspin promoter activities were also reduced after incubation with 1,25(OH)(2)D(3), and this reduction was mediated through the E2F recognition motifs within their promoters because mutation of these motifs almost completely abolished the repressive effect of 1,25(OH)(2)D(3) [10].
  • We found that during recovery from the DNA replication checkpoint response, Claspin is degraded in a betaTrCP-dependent manner [3].


  1. Evaluation of claspin as a proliferation marker in human cancer and normal tissues. Tsimaratou, K., Kletsas, D., Kastrinakis, N., Tsantoulis, P., Evangelou, K., Sideridou, M., Liontos, M., Poulias, I., Venere, M., Salmas, M., Kittas, C., Halazonetis, T., Gorgoulis, V. J. Pathol. (2007) [Pubmed]
  2. Rad17 phosphorylation is required for claspin recruitment and Chk1 activation in response to replication stress. Wang, X., Zou, L., Lu, T., Bao, S., Hurov, K.E., Hittelman, W.N., Elledge, S.J., Li, L. Mol. Cell (2006) [Pubmed]
  3. SCFbetaTrCP-mediated degradation of Claspin regulates recovery from the DNA replication checkpoint response. Peschiaroli, A., Dorrello, N.V., Guardavaccaro, D., Venere, M., Halazonetis, T., Sherman, N.E., Pagano, M. Mol. Cell (2006) [Pubmed]
  4. Human Claspin works with BRCA1 to both positively and negatively regulate cell proliferation. Lin, S.Y., Li, K., Stewart, G.S., Elledge, S.J. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  5. DNA-dependent phosphorylation of Chk1 and Claspin in a human cell-free system. Clarke, C.A., Clarke, P.R. Biochem. J. (2005) [Pubmed]
  6. DNA-Damage Control: Claspin Destruction Turns off the Checkpoint. Gewurz, B.E., Harper, J.W. Curr. Biol. (2006) [Pubmed]
  7. Repeated phosphopeptide motifs in human claspin are phosphorylated by chk1 and mediate claspin function. Chini, C.C., Chen, J. J. Biol. Chem. (2006) [Pubmed]
  8. Human claspin is required for replication checkpoint control. Chini, C.C., Chen, J. J. Biol. Chem. (2003) [Pubmed]
  9. Human claspin is a ring-shaped DNA-binding protein with high affinity to branched DNA structures. Sar, F., Lindsey-Boltz, L.A., Subramanian, D., Croteau, D.L., Hutsell, S.Q., Griffith, J.D., Sancar, A. J. Biol. Chem. (2004) [Pubmed]
  10. 1alpha,25-Dihydroxyvitamin D(3)-induced down-regulation of the checkpoint proteins, Chk1 and Claspin, is mediated by the pocket proteins p107 and p130. Verlinden, L., Eelen, G., Van Hellemont, R., Engelen, K., Beullens, I., Van Camp, M., Marchal, K., Mathieu, C., Bouillon, R., Verstuyf, A. J. Steroid Biochem. Mol. Biol. (2007) [Pubmed]
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