FOG12971
EOG8K6DQW
sce:OST4
Genes: 5
SGD DescriptionSubunit of the oligosaccharyltransferase complex of the ER lumen; complex catalyzes protein asparagine-linked glycosylation; type I membrane protein required for incorporation of Ost3p or Ost6p into the OST complex
PomBase Descriptionoligosaccharyltransferase subunit Ost4 (predicted)
References
Kelleher DJ, et al. (1994 Apr 29). The Saccharomyces cerevisiae oligosaccharyltransferase is a protein complex composed of Wbp1p, Swp1p, and four additional polypeptides.
Chi JH, et al. (1996 Feb 9). The OST4 gene of Saccharomyces cerevisiae encodes an unusually small protein required for normal levels of oligosaccharyltransferase activity.
Karaoglu D, et al. (1997 Dec 19). The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p.
Knauer R, et al. (1999 Jan 6). The oligosaccharyltransferase complex from yeast.
Kim H, et al. (2000 Feb 15). Studies on the role of the hydrophobic domain of Ost4p in interactions with other subunits of yeast oligosaccharyl transferase.
Kim H, et al. (2003 Jun 24). Determination of the membrane topology of Ost4p and its subunit interactions in the oligosaccharyltransferase complex in Saccharomyces cerevisiae.
Zubkov S, et al. (2004 Mar 16). Structural basis for the function of a minimembrane protein subunit of yeast oligosaccharyltransferase.
Spirig U, et al. (2005 Dec). The 3.4-kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast.
Yan A, et al. (2005 Dec). Two oligosaccharyl transferase complexes exist in yeast and associate with two different translocons.
Schwarz M, et al. (2005 Dec 5). Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit.
Chavan M, et al. (2005 Jun 17). Subunits of the translocon interact with components of the oligosaccharyl transferase complex.
Yan A, et al. (2005 May 17). Studies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: topological features and in vivo interactions.