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Gene Review

KIF20B  -  kinesin family member 20B

Homo sapiens

Synonyms: CT90, Cancer/testis antigen 90, KRMP1, Kinesin-like protein KIF20B, Kinesin-related motor interacting with PIN1, ...
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Disease relevance of MPHOSPH1


High impact information on MPHOSPH1


Biological context of MPHOSPH1

  • Immunofluorescence analysis showed that endogenous KRMP1 was localized predominantly to the cytoplasm during interphase and dispersed throughout the cell during mitosis [4].
  • An in vivo labeling experiment revealed that KRMP1 is phosphorylated, and we also found that the region within the tail domain containing Thr-1604 as the cdc2 kinase phosphorylation site differs from the bimC box conserved in the bimC subfamily of KRPs [4].
  • The nucleotide sequence was 99% identical to MPP1, a cell-cycle-related nuclear protein phosphorylated during mitosis [1].

Anatomical context of MPHOSPH1

  • In gliding experiments using polarity-marked microtubules, MPP1 is a slow molecular motor that moves toward the microtubule plus-end at a 0.07 microm/s speed [3].
  • Overexpression of KRMP1 caused COS-7 cells to arrest at G(2)-M, and co-expression of Pin1 reversed this effect, indicating their physiological interaction [4].

Associations of MPHOSPH1 with chemical compounds

  • Analysis of the deduced amino acid sequences revealed that KRMP have a high proportion of lysine, glycine, and tyrosine, and their predict isoelectric points are higher than any other identified shell matrix protein to our knowledge [5].
  • The deduced amino acid sequences of KRMP can be divided into three regions, including an N-terminal signal peptide, a lysine-rich basic region interacting with acidic proteins or CO(3)(2-), and a Gly/Tyr-rich region involved in the protein cross-link via quinone-tanning process [5].

Regulatory relationships of MPHOSPH1

  • Together, our results suggest that KRMP1 is a mitotic target regulated by Pin1 and vice versa [4].

Other interactions of MPHOSPH1

  • Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1 [4].
  • Partial-length cDNAs encoding two MPM2-reactive proteins termed MPM2-reactive phosphoproteins 1 and 2 (MPP1 and MPP2) were isolated [2].

Analytical, diagnostic and therapeutic context of MPHOSPH1

  • RT-PCR and in situ hybridization demonstrated that KRMP mRNA was specifically expressed in the mantle edge, involved in the prismatic layer formation [5].


  1. Autoantibodies from patients with idiopathic ataxia bind to M-phase phosphoprotein-1 (MPP1). Fritzler, M.J., Kerfoot, S.M., Feasby, T.E., Zochodne, D.W., Westendorf, J.M., Dalmau, J.O., Chan, E.K. J. Investig. Med. (2000) [Pubmed]
  2. Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2 monoclonal antibody and determination of the phosphorylated epitope. Westendorf, J.M., Rao, P.N., Gerace, L. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  3. M phase phosphoprotein 1 is a human plus-end-directed kinesin-related protein required for cytokinesis. Abaza, A., Soleilhac, J.M., Westendorf, J., Piel, M., Crevel, I., Roux, A., Pirollet, F. J. Biol. Chem. (2003) [Pubmed]
  4. Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1. Kamimoto, T., Zama, T., Aoki, R., Muro, Y., Hagiwara, M. J. Biol. Chem. (2001) [Pubmed]
  5. A novel matrix protein family participating in the prismatic layer framework formation of pearl oyster, Pinctada fucata. Zhang, C., Xie, L., Huang, J., Liu, X., Zhang, R. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
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