ALG14/YBR070C Summary Help

Standard Name ALG14 1, 2
Systematic Name YBR070C
Feature Type ORF, Verified
Description Component of UDP-GlcNAc transferase; required for the second step of dolichyl-linked oligosaccharide synthesis; anchors the catalytic subunit Alg13p to the ER membrane; similar to bacterial and human glycosyltransferases (1, 2, 3 and see Summary Paragraph)
Name Description Asparagine Linked Glycosylation 4
Chromosomal Location
ChrII:379934 to 379221 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All ALG14 GO evidence and references
  View Computational GO annotations for ALG14
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 15 genes
Classical genetics
reduction of function
Large-scale survey
reduction of function
33 total interaction(s) for 21 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 1
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 10
  • Co-fractionation: 4
  • Co-purification: 1
  • PCA: 1

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 8
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 2

Expression Summary
Length (a.a.) 237
Molecular Weight (Da) 27,035
Isoelectric Point (pI) 10.49
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrII:379934 to 379221 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..714 379934..379221 2011-02-03 1997-01-28
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000274

During N-linked glycosylation of proteins, oligosaccharide chains are assembled on the carrier molecule dolichyl pyrophosphate in the following order: 2 molecules of N-acetylglucosamine (GlcNAc), 9 molecules of mannose, and 3 molecules of glucose. These 14-residue oligosaccharide cores are then transferred to asparagine residues on nascent polypeptide chains in the endoplasmic reticulum (ER). As proteins progress through the Golgi apparatus, the oligosaccharide cores are modified by trimming and extension to generate a diverse array of glycosylated proteins (reviewed in 5, 6).

Together, Alg13p and Alg14p comprise a glycosyltransferase (EC that adds the second N-acetylglucosamine (GlcNAc) moiety to the growing lipid-linked oligosaccharide (LLO) on the cytosolic side of the endoplasmic reticulum (2). (Alg7p adds the first GlcNAc, and Alg1p adds the next residue, the first mannose.) Alg13p, the catalytic subunit, lacks a recognizable transmembrane domain; its localization to the ER membrane requires interaction with the integral ER membrane protein Alg14p. Consistent with this model, overexpression of ALG13 or attenuation of ALG14 causes Alg13p to be partitioned into the cytoplasm (2). Cells in which ALG13 or ALG14 expression has been repressed exhibit slow growth and defective protein glycosylation and accumulate LLO's with one GlcNAc residue (1). Co-expression of the human homologs of ALG13 and ALG14 can complement deletion of either gene, but neither neither individual human gene can complement deletion of its yeast homolog, probably because the yeast and human proteins fail to interact with each other (2). ALG14 and ALG13 are homologous to separate proteins in Streptococcus pneumoniae (Cps14f and Cps14g, respectively) and to the N- and C-termini of E. coli MurG (1).

Last updated: 2005-07-12 Contact SGD

References cited on this page View Complete Literature Guide for ALG14
1) Chantret I, et al.  (2005) Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem 280(10):9236-42
2) Gao XD, et al.  (2005) Alg14 Recruits Alg13 to the Cytoplasmic Face of the Endoplasmic Reticulum to Form a Novel Bipartite UDP-N-acetylglucosamine Transferase Required for the Second Step of N-Linked Glycosylation. J Biol Chem 280(43):36254-62
3) Bickel T, et al.  (2005) Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J Biol Chem 280(41):34500-6
4) Huffaker TC and Robbins PW  (1982) Temperature-sensitive yeast mutants deficient in asparagine-linked glycosylation. J Biol Chem 257(6):3203-10
5) Herscovics A and Orlean P  (1993) Glycoprotein biosynthesis in yeast. FASEB J 7(6):540-50
6) Burda P and Aebi M  (1999) The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta 1426(2):239-57