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Gene Review

SEC62  -  Sec62p

Saccharomyces cerevisiae S288c

Synonyms: LPG14C, Sec62/63 complex 30 kDa subunit, Translocation protein SEC62, YPL094C
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High impact information on SEC62


Biological context of SEC62


Anatomical context of SEC62


Associations of SEC62 with chemical compounds

  • Exchanging either threonine 652 or threonine 654 against the nonphosphorylatable alanines in Sec63p impairs the binding to Sec62p and interferes with the efficient translocation of proteins across the membrane of the endoplasmic reticulum [9].
  • Sec62p is predicted to display significant NH2- and COOH-terminal hydrophilic domains on the cytoplasmic surface of the ER membrane [4].

Enzymatic interactions of SEC62

  • We show that Sec63p is phosphorylated at its C-terminal domain by the protein kinase CK2 and that this phosphorylation strengthens the interaction between the cytosolic domains of Sec63p and Sec62p [9].

Other interactions of SEC62

  • Mutations in SEC62 and SEC63 decrease the ability of Sec61p to be cross-linked to the secretory polypeptide trapped in translocation [12].
  • The yeast homologue of the heavy chain-binding protein, BiP (encoded by the KAR2 gene), and the product of the SEC62 gene were present in two fractions having equilibrium densities of 1.146 and 1.192 g/ml, respectively [13].
  • Cub fusions that bore the signal sequence of invertase resulted in a much lower Ub reconstitution with Nub-Sec62p than otherwise identical test proteins bearing the signal sequence of prepro-alpha-factor [14].

Analytical, diagnostic and therapeutic context of SEC62


  1. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Plath, K., Mothes, W., Wilkinson, B.M., Stirling, C.J., Rapoport, T.A. Cell (1998) [Pubmed]
  2. Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Lyman, S.K., Schekman, R. Cell (1997) [Pubmed]
  3. Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex. Deshaies, R.J., Sanders, S.L., Feldheim, D.A., Schekman, R. Nature (1991) [Pubmed]
  4. SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum. Deshaies, R.J., Schekman, R. J. Cell Biol. (1989) [Pubmed]
  5. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. Rothblatt, J.A., Deshaies, R.J., Sanders, S.L., Daum, G., Schekman, R. J. Cell Biol. (1989) [Pubmed]
  6. Structural and functional dissection of Sec62p, a membrane-bound component of the yeast endoplasmic reticulum protein import machinery. Deshaies, R.J., Schekman, R. Mol. Cell. Biol. (1990) [Pubmed]
  7. Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complex. Wittke, S., Dünnwald, M., Johnsson, N. Mol. Biol. Cell (2000) [Pubmed]
  8. Cloning the Yarrowia lipolytica homologue of the Saccharomyces cerevisiae SEC62 gene. Swennen, D., Joyet, P., Gaillardin, C. Curr. Genet. (1997) [Pubmed]
  9. Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus. Wang, X., Johnsson, N. J. Cell. Sci. (2005) [Pubmed]
  10. Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Hanein, D., Matlack, K.E., Jungnickel, B., Plath, K., Kalies, K.U., Miller, K.R., Rapoport, T.A., Akey, C.W. Cell (1996) [Pubmed]
  11. A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. Finke, K., Plath, K., Panzner, S., Prehn, S., Rapoport, T.A., Hartmann, E., Sommer, T. EMBO J. (1996) [Pubmed]
  12. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Sanders, S.L., Whitfield, K.M., Vogel, J.P., Rose, M.D., Schekman, R.W. Cell (1992) [Pubmed]
  13. Purification and functional characterization of membranes derived from the rough endoplasmic reticulum of Saccharomyces cerevisiae. Sanderson, C.M., Meyer, D.I. J. Biol. Chem. (1991) [Pubmed]
  14. Detection of transient in vivo interactions between substrate and transporter during protein translocation into the endoplasmic reticulum. Dünnwald, M., Varshavsky, A., Johnsson, N. Mol. Biol. Cell (1999) [Pubmed]
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