PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8768330-8 1996 For sites able for formation of alpha-helices and neighbouring sites there was shown high homology of primary structure observed by us both at the comparison of ALG1 and ALG2 with each other and at the comparison with other enzymes of dolichol cycle. Dolichols 235-243 GDP-Man:Man(1)GlcNAc(2)-PP-dolichol alpha-1,3-mannosyltransferase Saccharomyces cerevisiae S288C 170-174 9795208-4 1998 Five introns intervened the R. pusillus alg2 encoding a 455-amino-acid (aa) protein that showed end-to-end similarity in aa sequence to yeast Alg2 and contained a dolichol-binding consensus sequence (Val/Ile-x-Phe-x-x-Ile, where x is any aa) very near its C-terminus. Dolichols 163-171 GDP-Man:Man(1)GlcNAc(2)-PP-dolichol alpha-1,3-mannosyltransferase Saccharomyces cerevisiae S288C 40-44 8400550-16 1993 The putative translation product of ALG2 contained a potential dolichol recognition domain similar to that found in all three glycosyltransferases of the lipid-linked pathway that have been sequenced. Dolichols 63-71 GDP-Man:Man(1)GlcNAc(2)-PP-dolichol alpha-1,3-mannosyltransferase Saccharomyces cerevisiae S288C 36-40 8563151-2 1995 Recently, we reported that mRNAs of genes that function at the early steps in the dolichol pathway in yeast, ALG7, ALG1 and ALG2, were co-ordinately induced following growth stimulation of G0-arrested cells in a manner similar to that of the transcripts of the early growth response genes (Kukuruzinska, M.A. Dolichols 82-90 GDP-Man:Man(1)GlcNAc(2)-PP-dolichol alpha-1,3-mannosyltransferase Saccharomyces cerevisiae S288C 124-128 7827405-1 1994 The Saccharomyces cerevisiae ALG7, ALG1 and ALG2 genes, whose products function early in the dolichol pathway of protein N-glycosylation, are essential for cell viability, and perturbation in their expression causes G1-specific cell cycle arrest. Dolichols 93-101 GDP-Man:Man(1)GlcNAc(2)-PP-dolichol alpha-1,3-mannosyltransferase Saccharomyces cerevisiae S288C 44-48