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Volumn 16, Issue 11, 1996, Pages 6486-6493

A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1

Author keywords

[No Author keywords available]

Indexed keywords

CALCINEURIN; CASEIN KINASE I; CASEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; PHOSPHORYLASE KINASE; PROTEIN SERINE THREONINE KINASE;

EID: 0343177223     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.11.6486     Document Type: Article
Times cited : (499)

References (27)
  • 1
    • 0027460805 scopus 로고
    • Identification of mitogen-activated protein kinase phosphorylation sequences in mammalian h-caldesmon
    • Adam, L. P., and D. R. Hathaway. 1993. Identification of mitogen-activated protein kinase phosphorylation sequences in mammalian h-caldesmon. FEBS Lett. 322:56-60.
    • (1993) FEBS Lett. , vol.322 , pp. 56-60
    • Adam, L.P.1    Hathaway, D.R.2
  • 2
    • 0028273487 scopus 로고
    • Cell-cycle-regulated phosphorylation of oncoprotein 18 on Ser16, Ser25 and Ser38
    • Brattsand, G., U. Marklund, K. Nylander, G. Roos, and M. Gullberg. 1994. Cell-cycle-regulated phosphorylation of oncoprotein 18 on Ser16, Ser25 and Ser38. Eur. J. Biochem. 220:359-368.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 359-368
    • Brattsand, G.1    Marklund, U.2    Nylander, K.3    Roos, G.4    Gullberg, M.5
  • 3
    • 0027475972 scopus 로고
    • Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulated protein kinase ERK1
    • Cheng, J. T., M. H. Cobb, and R. Baer. 1993. Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulated protein kinase ERK1. Mol. Cell. Biol. 13:801-808.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 801-808
    • Cheng, J.T.1    Cobb, M.H.2    Baer, R.3
  • 6
    • 0025888298 scopus 로고
    • Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases
    • Gonzalez, F. A., D. L. Raden, and R. L. Davis. 1991. Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases. J. Biol. Chem. 266:22159-22163.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22159-22163
    • Gonzalez, F.A.1    Raden, D.L.2    Davis, R.L.3
  • 7
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Uses in identification of conserved features of primary structure and classification of novel family members
    • Hanks, S. K., and A. M. Quinn. 1991. Protein kinase catalytic domain sequence database: uses in identification of conserved features of primary structure and classification of novel family members. Methods Enzymol. 200:38-62.
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 8
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks, S. K., A. M. Quinn, and T. Hunter. 1988. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241:42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 9
    • 0026568161 scopus 로고
    • ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ
    • Haycock, J. W., N. G. Ahn, M. H. Cobb, and E. G. Krebs. 1992. ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ. Proc. Natl. Acad. Sci. USA 89:2365-2369.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2365-2369
    • Haycock, J.W.1    Ahn, N.G.2    Cobb, M.H.3    Krebs, E.G.4
  • 10
    • 0028287635 scopus 로고
    • Insights into autoregulation from the crystal structure of twitchin kinase
    • Hu, S. H., M. W. Parker, J. Y. Lei, M. C. Wilce, G. M. Benian, and B. E. Kemp. 1994. Insights into autoregulation from the crystal structure of twitchin kinase. Nature (London) 369:581-584.
    • (1994) Nature (London) , vol.369 , pp. 581-584
    • Hu, S.H.1    Parker, M.W.2    Lei, J.Y.3    Wilce, M.C.4    Benian, G.M.5    Kemp, B.E.6
  • 11
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard, S. R., L. Wei, L. Ellis, and W. A. Hendrickson. 1994. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature (London) 372:746-754.
    • (1994) Nature (London) , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 13
    • 85035174597 scopus 로고    scopus 로고
    • Unpublished data
    • 12a. Johnson, L. Unpublished data.
    • Johnson, L.1
  • 14
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D. R., J. H. Zheng, L. F. Ten Eyck, N. H. Xuong, S. S. Taylor, and J. M. Sowadski. 1991. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253:414-420.
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Xuong, N.H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 15
    • 0023645087 scopus 로고
    • Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides
    • Kuenzel, E. A., J. A. Mulligan, J. Sommercorn, and E. G. Krebs. 1987. Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides. J. Biol. Chem. 262:9136-9140.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9136-9140
    • Kuenzel, E.A.1    Mulligan, J.A.2    Sommercorn, J.3    Krebs, E.G.4
  • 16
    • 0028318168 scopus 로고
    • Identification of substrate specificity determinants for the cell cycle-regulated NIMA protein kinase
    • Lu, K. P., B. E. Kemp, and A. R. Means. 1994. Identification of substrate specificity determinants for the cell cycle-regulated NIMA protein kinase. J. Biol. Chem. 269:6603-6607.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6603-6607
    • Lu, K.P.1    Kemp, B.E.2    Means, A.R.3
  • 17
    • 0026048594 scopus 로고
    • Parallel activation of the NIMA and p34cdc2 cell cycle-regulated protein kinases is required to initiate mitosis in A. nidulans
    • Osmani, A. H., S. L. McGuire, and S. A. Osmani. 1991. Parallel activation of the NIMA and p34cdc2 cell cycle-regulated protein kinases is required to initiate mitosis in A. nidulans. Cell 67:283-291.
    • (1991) Cell , vol.67 , pp. 283-291
    • Osmani, A.H.1    McGuire, S.L.2    Osmani, S.A.3
  • 18
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Pearson, R. B., and B. E. Kemp. 1991. Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. Methods Enzymol. 200:62-81.
    • (1991) Methods Enzymol. , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 20
    • 0027165323 scopus 로고
    • cdc2-like kinase from rat spinal cord specifically phosphorylates KSPXK motifs in neurofilament proteins: Isolation and characterization
    • Shetty, K. T., W. T. Link, and H. C. Pant. 1993. cdc2-like kinase from rat spinal cord specifically phosphorylates KSPXK motifs in neurofilament proteins: isolation and characterization. Proc. Natl. Acad. Sci. USA 90:6844-6848.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6844-6848
    • Shetty, K.T.1    Link, W.T.2    Pant, H.C.3
  • 21
    • 0027185999 scopus 로고
    • CAK, the p34cdc2 activating kinase, contains a protein identical or closely related to p40MO15
    • Solomon, M. J., J. W. Harper, and J. Shuttleworth. 1993. CAK, the p34cdc2 activating kinase, contains a protein identical or closely related to p40MO15. EMBO J. 12:3133-3142.
    • (1993) EMBO J. , vol.12 , pp. 3133-3142
    • Solomon, M.J.1    Harper, J.W.2    Shuttleworth, J.3
  • 24
    • 0027317396 scopus 로고
    • Identification of a human epidermal growth factor receptor-associated protein kinase as a new member of the mitogen-activated protein kinase/extracellular signal-regulated protein kinase family
    • Williams, R., J. Sanghera, F. Wu, D. Carbonaro-Hall, D. L. Campbell, D. Warburton, S. Pelech, and F. Hall. 1993. Identification of a human epidermal growth factor receptor-associated protein kinase as a new member of the mitogen-activated protein kinase/extracellular signal-regulated protein kinase family. J. Biol. Chem. 268:18213-18217.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18213-18217
    • Williams, R.1    Sanghera, J.2    Wu, F.3    Carbonaro-Hall, D.4    Campbell, D.L.5    Warburton, D.6    Pelech, S.7    Hall, F.8
  • 25
    • 0028913538 scopus 로고
    • Crystal structure of casein kinase-1, a phosphate-directed protein kinase
    • Xu, R. M., G. Carmel, R. M. Sweet, J. Kuret, and X. Cheng. 1995. Crystal structure of casein kinase-1, a phosphate-directed protein kinase. EMBO J. 14:1015-1023.
    • (1995) EMBO J. , vol.14 , pp. 1015-1023
    • Xu, R.M.1    Carmel, G.2    Sweet, R.M.3    Kuret, J.4    Cheng, X.5
  • 26
    • 0027250459 scopus 로고
    • Phosphorylase kinase, a metal ion-dependent dual specificity kinase
    • Yuan, C. J., C. Y. Huang, and D. J. Graves. 1993. Phosphorylase kinase, a metal ion-dependent dual specificity kinase. J. Biol. Chem. 268:17683-17686.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17683-17686
    • Yuan, C.J.1    Huang, C.Y.2    Graves, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.