ALG13/YGL047W Summary Help

Standard Name ALG13 1, 2
Systematic Name YGL047W
Feature Type ORF, Verified
Description Catalytic component of UDP-GlcNAc transferase; required for the second step of dolichyl-linked oligosaccharide synthesis; anchored to the ER membrane via interaction with Alg14p; similar to bacterial and human glycosyltransferases; protein abundance increases in response to DNA replication stress (1, 2, 3, 4 and see Summary Paragraph)
Name Description Asparagine-Linked Glycosylation 5
Chromosomal Location
ChrVII:411552 to 412160 | ORF Map | GBrowse
Gene Ontology Annotations All ALG13 GO evidence and references
  View Computational GO annotations for ALG13
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Classical genetics
Large-scale survey
reduction of function
33 total interaction(s) for 22 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 1
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 9
  • Co-crystal Structure: 1
  • Co-fractionation: 2
  • Co-purification: 1

Genetic Interactions
  • Dosage Growth Defect: 2
  • Negative Genetic: 7
  • Positive Genetic: 3
  • Synthetic Growth Defect: 4
  • Synthetic Lethality: 2

Expression Summary
Length (a.a.) 202
Molecular Weight (Da) 22,661
Isoelectric Point (pI) 5.72
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:411552 to 412160 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..609 411552..412160 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003015

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 6, 7).

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 ALG13
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) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
5) Huffaker TC and Robbins PW  (1982) Temperature-sensitive yeast mutants deficient in asparagine-linked glycosylation. J Biol Chem 257(6):3203-10
6) Herscovics A and Orlean P  (1993) Glycoprotein biosynthesis in yeast. FASEB J 7(6):540-50
7) Burda P and Aebi M  (1999) The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta 1426(2):239-57