The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

Syntide-2     (2S)-6-amino-2-[[(2S)-6- amino-2-[2-[[(2S)...

Synonyms: AC1NX8MJ, 108334-68-5
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Syntide-2

  • Although recombinant CaMKIx expressed in Escherichia coli showed no protein kinase activity against syntide-2, a synthetic peptide substrate, it was activated when phosphorylated by mouse Ca(2+)/calmodulin-dependent protein kinase kinase alpha (CaMKKalpha) [1].

High impact information on Syntide-2

  • NR2B inhibits both the Ca(2+)/calmodulin-dependent and autonomous activities of CaMKII by a mechanism that is competitive with autocamtide-2 substrate, non-competitive with syntide-2 substrate, and uncompetitive with respect to ATP [2].
  • In contrast, addition of purified PKCepsilon to the incubation mixture induced rapid Ser(744) and Ser(748) phosphorylation, concomitant with persistent 2-3-fold increases in PKD activity, measured using reimmunoprecipitated PKD to phosphorylate an exogenous peptide, syntide-2 [3].
  • Deletion of the entire PH domain (amino acids 429-557) markedly increased the basal activity of the enzyme as assessed by autophosphorylation ( approximately 16-fold) and exogenous syntide-2 peptide substrate phosphorylation assays (approximately 12-fold) [4].
  • The kinetics of bacterially expressed human CaMKI show that the peptide syntide-2 is a relatively poor substrate, whereas the synapsin site-1 peptide is 17-fold more specific [5].
  • Our results demonstrate that bombesin rapidly induces PKD activation in Swiss 3T3 cells, as shown by autophosphorylation and syntide-2 phosphorylation assays [6].

Biological context of Syntide-2

  • CaMK-(281-309), but not CaMK-(281-289), bound calmodulin and was a potent inhibitor (IC50 = 0.88 +/- 0.7 microM using 20 microM syntide-2) of exogenous substrate (syntide-2 or glycogen synthase) phosphorylation by a completely Ca2+/calmodulin-independent form of the kinase generated by limited proteolysis with chymotrypsin [7].
  • Based on molecular mass, calcium/calmodulin-dependent autophosphorylation, substrate specificity, KN-62 inhibition, apparent Km for ATP and syntide-2, these proteins were identified as calcium/calmodulin-dependent protein kinase II (CaM kinase II) [8].
  • This kinase phosphorylates the synthetic peptides such as syntide 2, autocamtide-2, site 3 in a Ca2+/CaM-dependent manner, but not myosin light chain-peptide, gamma-peptide, and cAMP Response Element Binding Protein (CREB) peptide [9].

Anatomical context of Syntide-2

  • Ionomycin treatment of these cells resulted in increased kinase activity of cytosolic extracts toward syntide-2, a synthetic peptide substrate for calcium/calmodulin-dependent kinase II (CaM-KII), with kinetics similar to those of CD20 phosphorylation in the cell line [10].
  • The immunoprecipitates with the antibodies from K562 cells phosphorylates the synthetic peptide substrates, syntide-2 [11].
  • PKD expressed in COS cells showed syntide-2 kinase activity that was stimulated by phorbol esters in the presence of phospholipids [12].
  • The motility of demembranated spermatozoa at 30 degrees C remained high in control samples and following the addition of Kemptide, Syntide 2 and PKC substrate peptide, but decreased markedly following the addition of MLCK substrate peptide [13].
  • Biochemical analyses showed that NtCPK4 phosphorylated itself and calf thymus histones fraction III-S (histone III-S) in a calcium-dependent manner, and the K0.5 of calcium activation was 0.29 microM or 0.25 microM with histone III-S or syntide-2 as substrates, respectively [14].

Associations of Syntide-2 with other chemical compounds


Gene context of Syntide-2

  • PKD prepared by elution from immunoprecipitates with the immunizing peptide efficiently phosphorylated the synthetic peptide syntide-2 [15].
  • Activation of CaM-kinase IV resulted in a 10-fold decrease in Km for syntide-2 with little effect on Km for ATP or Vmax [19].
  • The optimum concentration of poly(Lys) for the phosphorylation of 1 microM CaM was about 10 microg/ml, but poly(Lys) strongly inhibited CaM-kinase IV activity toward syntide-2 at this concentration, suggesting that the phosphorylation of CaM is not due to simple activation of the catalytic activity [20].
  • The CaM kinase V had an apparent Km for ATP of 75 +/- 11 microM and for syntide-2 of 20 +/- 4 microM [21].
  • Kinetic analysis showed that the kinase not previously autophosphorylated had a Km for the synthetic peptide syntide-2 of 7 microM and Vmax of 9.8 mumol/min/mg when assayed in the presence of Ca2+ and CaM [22].


  1. Cloning and characterization of a novel Ca2+/calmodulin-dependent protein kinase I homologue in Xenopus laevis. Kinoshita, S., Sueyoshi, N., Shoju, H., Suetake, I., Nakamura, M., Tajima, S., Kameshita, I. J. Biochem. (2004) [Pubmed]
  2. Differential modulation of Ca2+/calmodulin-dependent protein kinase II activity by regulated interactions with N-methyl-D-aspartate receptor NR2B subunits and alpha-actinin. Robison, A.J., Bartlett, R.K., Bass, M.A., Colbran, R.J. J. Biol. Chem. (2005) [Pubmed]
  3. Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain. Waldron, R.T., Rozengurt, E. J. Biol. Chem. (2003) [Pubmed]
  4. Protein kinase D activation by mutations within its pleckstrin homology domain. Iglesias, T., Rozengurt, E. J. Biol. Chem. (1998) [Pubmed]
  5. Characterization of substrate phosphorylation and use of calmodulin mutants to address implications from the enzyme crystal structure of calmodulin-dependent protein kinase I. Chin, D., Winkler, K.E., Means, A.R. J. Biol. Chem. (1997) [Pubmed]
  6. Bombesin, vasopressin, endothelin, bradykinin, and platelet-derived growth factor rapidly activate protein kinase D through a protein kinase C-dependent signal transduction pathway. Zugaza, J.L., Waldron, R.T., Sinnett-Smith, J., Rozengurt, E. J. Biol. Chem. (1997) [Pubmed]
  7. Regulatory interactions of the calmodulin-binding, inhibitory, and autophosphorylation domains of Ca2+/calmodulin-dependent protein kinase II. Colbran, R.J., Fong, Y.L., Schworer, C.M., Soderling, T.R. J. Biol. Chem. (1988) [Pubmed]
  8. Identification, characterization, immunocytochemical localization, and developmental changes in the activity of calcium/calmodulin-dependent protein kinase II in the CNS of Bombyx mori during postembryonic development. Shanavas, A., Dutta-Gupta, A., Murthy, C.R. J. Neurochem. (1998) [Pubmed]
  9. A novel Ca2+/calmodulin-dependent protein kinase lacking autophosphorylation activity in the rabbit heart. Uemura, A., Okazaki, K., Takesue, H., Matsubara, T., Hidaka, H. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  10. Phosphorylation of CD20 in cells from a hairy cell leukemia cell line. Evidence for involvement of calcium/calmodulin-dependent protein kinase II. Genot, E.M., Meier, K.E., Licciardi, K.A., Ahn, N.G., Uittenbogaart, C.H., Wietzerbin, J., Clark, E.A., Valentine, M.A. J. Immunol. (1993) [Pubmed]
  11. The effect of KN-62, Ca2+/calmodulin dependent protein kinase II inhibitor on cell cycle. Minami, H., Inoue, S., Hidaka, H. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  12. Protein kinase D (PKD): a novel target for diacylglycerol and phorbol esters. Rozengurt, E., Sinnett-Smith, J., Van Lint, J., Valverde, A.M. Mutat. Res. (1995) [Pubmed]
  13. Dephosphorylation of a 30-kDa protein of fowl spermatozoa by the addition of myosin light chain kinase substrate peptide inhibits the flagellar motility. Ashizawa, K., Wishart, G.J., Hashimoto, K., Tsuzuki, Y. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  14. Cloning and functional characterization of NtCPK4, a new tobacco calcium-dependent protein kinase. Zhang, M., Liang, S., Lu, Y.T. Biochim. Biophys. Acta (2005) [Pubmed]
  15. Expression and characterization of PKD, a phorbol ester and diacylglycerol-stimulated serine protein kinase. Van Lint, J.V., Sinnett-Smith, J., Rozengurt, E. J. Biol. Chem. (1995) [Pubmed]
  16. Identification of in vivo phosphorylation sites required for protein kinase D activation. Iglesias, T., Waldron, R.T., Rozengurt, E. J. Biol. Chem. (1998) [Pubmed]
  17. Differential effects of suramin on protein kinase C isoenzymes. A novel tool for discriminating protein kinase C activities. Gschwendt, M., Kittstein, W., Johannes, F.J. FEBS Lett. (1998) [Pubmed]
  18. Effects of resveratrol on the autophosphorylation of phorbol ester-responsive protein kinases: inhibition of protein kinase D but not protein kinase C isozyme autophosphorylation. Stewart, J.R., Christman, K.L., O'Brian, C.A. Biochem. Pharmacol. (2000) [Pubmed]
  19. Activation mechanisms for Ca2+/calmodulin-dependent protein kinase IV. Identification of a brain CaM-kinase IV kinase. Tokumitsu, H., Brickey, D.A., Glod, J., Hidaka, H., Sikela, J., Soderling, T.R. J. Biol. Chem. (1994) [Pubmed]
  20. Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase IV. Ishida, A., Kameshita, I., Okuno, S., Kitani, T., Fujisawa, H. Arch. Biochem. Biophys. (2002) [Pubmed]
  21. Purification and characterization of Ca2+/calmodulin-dependent protein kinase V from rat cerebrum. Mochizuki, H., Ito, T., Hidaka, H. J. Biol. Chem. (1993) [Pubmed]
  22. Autophosphorylation of Ca2+/calmodulin-dependent protein kinase II. Effects on total and Ca2+-independent activities and kinetic parameters. Hashimoto, Y., Schworer, C.M., Colbran, R.J., Soderling, T.R. J. Biol. Chem. (1987) [Pubmed]
WikiGenes - Universities