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Gene Review

SRC  -  v-src sarcoma viral oncogene

Gallus gallus

Synonyms: PP60C-SCR, SDR
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Disease relevance of SRC

  • The Rous sarcoma virus oncogene product, pp60v-src, transforms cultured fibroblasts but its corresponding proto-oncogene product, pp60c-src, does not [1].
  • Expression of pp60c-src persisted in mature neuronal cells that were postmitotic, fully differentiated, and functional. pp60c-src immunoreactivity was localized within processes and cell bodies of ganglion neurons, processes of rods and cones, and in some but not all neurons of the inner nuclear layer [2].
  • Activation of cSrc and expression of the HO-1 gene product are each induced under conditions of hypoxia [3].
  • A difference of 25 g was observed between the mean body weights of SDR males and females and between the SDS males and females after one generation of selection [4].
  • The SDR males and females had an average of 17% increase in weight gain at 21 days of age when fed the -Se diet compared with the control line males and females fed the same diet for the three generations of selection [4].

High impact information on SRC


Chemical compound and disease context of SRC

  • The transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src) appear to be protein kinases that phosphorylate tyrosine in a variety of protein substrates [7].

Biological context of SRC


Anatomical context of SRC

  • While the c-src locus is expressed as a 4.0-kilobase (kb) mRNA coding for pp60c-src in various chicken tissues, including embryonic muscle, it is expressed as a novel 3.0-kb mRNA in adult skeletal muscle [11].
  • Thus the use of a highly specific antibody reveals that enzymatically active pp60v-src and pp60c-src molecules are present in other intracellular structures, probably juxtareticular nuclear membranes, in addition to the plasma membrane in normal, uninfected, and wild-type RSV-infected cells [12].
  • Initial studies of pp60c-src in chick lens tissues during development indicate that higher kinase activity is found in the epithelial cells relative to mature lens fibres [13].
  • A monoclonal antibody to a 60-kDa substrate of the insulin receptor tyrosine kinase is utilized in the present studies to examine this molecule in 3T3 cells expressing either the transforming chicken c-Src (mutant Phe-527), the wild type molecule, or the parental cells [14].
  • In this study, we have used this antibody as an in vitro activator and purified a c-Src-related protein-tyrosine kinase from the particulate fraction of Xenopus laevis oocytes [15].

Associations of SRC with chemical compounds

  • In this study, it was observed that the tyrosine phosphorylated in pp60c-src is Tyr527, six residues from the COOH-terminus of the protein [1].
  • Activation of YRP kinase by protein kinase C was found to be potentiated by vanadate treatment or overexpression of c-Src [16].
  • We have identified two phosphotyrosine-containing cellular proteins with relative molecular masses of 130,000 (pp130) and 110,000 (pp110) daltons in chicken embryo cells that coimmunoprecipitated with pp60v-src and activated forms of chicken pp60c-src (pp60(527)F) [17].
  • Nongenomic action of 1 alpha,25(OH)(2)-vitamin D3. Activation of muscle cell PLC gamma through the tyrosine kinase c-Src and PtdIns 3-kinase [18].
  • 1 alpha,25(OH)(2)D(3)-induced membrane translocation of PLC gamma was prevented to a great extent by c-Src and PtdIns3K inhibitors, PP1 and LY294002 [18].

Enzymatic interactions of SRC


Other interactions of SRC


Analytical, diagnostic and therapeutic context of SRC


  1. Tyr527 is phosphorylated in pp60c-src: implications for regulation. Cooper, J.A., Gould, K.L., Cartwright, C.A., Hunter, T. Science (1986) [Pubmed]
  2. pp60c-src is developmentally regulated in the neural retina. Sorge, L.K., Levy, B.T., Maness, P.F. Cell (1984) [Pubmed]
  3. Chimeric constructs containing the SH4/Unique domains of cYes can restrict the ability of Src(527F) to upregulate heme oxygenase-1 expression efficiently. Hoey, J.G., Summy, J., Flynn, D.C. Cell. Signal. (2000) [Pubmed]
  4. Response to divergent selection for early growth of chickens fed a diet deficient in selenium. Cunningham, D.L., Combs, G.F., Saroka, J.A., LaVorgna, M.W. Poult. Sci. (1987) [Pubmed]
  5. Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Young, M.A., Gonfloni, S., Superti-Furga, G., Roux, B., Kuriyan, J. Cell (2001) [Pubmed]
  6. Purified maturation promoting factor phosphorylates pp60c-src at the sites phosphorylated during fibroblast mitosis. Shenoy, S., Choi, J.K., Bagrodia, S., Copeland, T.D., Maller, J.L., Shalloway, D. Cell (1989) [Pubmed]
  7. Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src). Smart, J.E., Oppermann, H., Czernilofsky, A.P., Purchio, A.F., Erikson, R.L., Bishop, J.M. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  8. Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus. Takeya, T., Hanafusa, H. Cell (1983) [Pubmed]
  9. Analysis of cDNAs of the proto-oncogene c-src: heterogeneity in 5' exons and possible mechanism for the genesis of the 3' end of v-src. Dorai, T., Levy, J.B., Kang, L., Brugge, J.S., Wang, L.H. Mol. Cell. Biol. (1991) [Pubmed]
  10. Cell transformation by pp60c-src mutated in the carboxy-terminal regulatory domain. Cartwright, C.A., Eckhart, W., Simon, S., Kaplan, P.L. Cell (1987) [Pubmed]
  11. An alternative non-tyrosine protein kinase product of the c-src gene in chicken skeletal muscle. Dorai, T., Wang, L.H. Mol. Cell. Biol. (1990) [Pubmed]
  12. Highly specific antibody to Rous sarcoma virus src gene product recognizes a novel population of pp60v-src and pp60c-src molecules. Resh, M.D., Erikson, R.L. J. Cell Biol. (1985) [Pubmed]
  13. pp60c-src expression in transdifferentiating cultures of embryonic chick neural retina cells. Ellis, D.K., Carr, A., de Pomerai, D.I. Development (1987) [Pubmed]
  14. Evidence for two distinct 60-kilodalton substrates of the SRC tyrosine kinase. Ogawa, W., Hosomi, Y., Shii, K., Roth, R.A. J. Biol. Chem. (1994) [Pubmed]
  15. Purification and characterization of a Src-related p57 protein-tyrosine kinase from Xenopus oocytes. Isolation of an inactive form of the enzyme and its activation and translocation upon fertilization. Sato, K., Aoto, M., Mori, K., Akasofu, S., Tokmakov, A.A., Sahara, S., Fukami, Y. J. Biol. Chem. (1996) [Pubmed]
  16. Activation of YRP kinase by v-Src and protein kinase C-mediated signal transduction pathways. Scholz, G., Felder, M.P., Hanafusa, H. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  17. Stable association of activated pp60src with two tyrosine-phosphorylated cellular proteins. Reynolds, A.B., Kanner, S.B., Wang, H.C., Parsons, J.T. Mol. Cell. Biol. (1989) [Pubmed]
  18. Nongenomic action of 1 alpha,25(OH)(2)-vitamin D3. Activation of muscle cell PLC gamma through the tyrosine kinase c-Src and PtdIns 3-kinase. Buitrago, C., González Pardo, V., de Boland, A.R. Eur. J. Biochem. (2002) [Pubmed]
  19. Myristylation is required for Tyr-527 dephosphorylation and activation of pp60c-src in mitosis. Bagrodia, S., Taylor, S.J., Shalloway, D. Mol. Cell. Biol. (1993) [Pubmed]
  20. A protein tyrosine kinase involved in regulation of pp60c-src function. Okada, M., Nakagawa, H. J. Biol. Chem. (1989) [Pubmed]
  21. Regulatory role for SRC and phosphatidylinositol 3-kinase in initiation of fibronectin matrix assembly. Wierzbicka-Patynowski, I., Schwarzbauer, J.E. J. Biol. Chem. (2002) [Pubmed]
  22. Molecular cloning and expression of chicken C-terminal Src kinase: lack of stable association with c-Src protein. Sabe, H., Knudsen, B., Okada, M., Nada, S., Nakagawa, H., Hanafusa, H. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  23. c-Src is required for stimulation of gelsolin-associated phosphatidylinositol 3-kinase. Chellaiah, M., Fitzgerald, C., Alvarez, U., Hruska, K. J. Biol. Chem. (1998) [Pubmed]
  24. Intestinal crypt cells contain higher levels of cytoskeletal-associated pp60c-src protein tyrosine kinase activity than do differentiated enterocytes. Cartwright, C.A., Mamajiwalla, S., Skolnick, S.A., Eckhart, W., Burgess, D.R. Oncogene (1993) [Pubmed]
  25. Highly specific antibody to Rous sarcoma virus src gene product recognizes nuclear and nucleolar antigens in human cells. David-Pfeuty, T., Nouvian-Dooghe, Y. J. Virol. (1995) [Pubmed]
  26. Altered expression of pp60c-src induced by peripheral nerve injury. Ignelzi, M.A., Padilla, S.S., Warder, D.E., Maness, P.F. J. Comp. Neurol. (1992) [Pubmed]
  27. Band 3 tyrosine kinase in avian erythrocyte plasma membrane is immunologically related to pp60c-src. Hillsgrove, D., Shores, C.G., Parker, J.C., Maness, P.F. Am. J. Physiol. (1987) [Pubmed]
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