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UDP-N-acetylglucosamine transferase subunit ALG14 homolog is a protein that in humans is encoded by the ALG14 gene.[5][6]

ALG14
Identifiers
AliasesALG14, CMS15, UDP-N-acetylglucosaminyltransferase subunit, ALG14 UDP-N-acetylglucosaminyltransferase subunit, IDDEBF, MEPCA
External IDsOMIM: 612866; MGI: 1914039; HomoloGene: 49751; GeneCards: ALG14; OMA:ALG14 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001305242
NM_144988

NM_024178

RefSeq (protein)

NP_001292171
NP_659425

NP_077140

Location (UCSC)Chr 1: 94.97 – 95.07 MbChr 3: 121.09 – 121.16 Mb
PubMed search[3][4]
Wikidata
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Asparagine (N)-glycosylation is an essential modification that regulates protein folding and stability. ALG13 and ALG14 (this protein) constitute the UDP-GlcNAc transferase, which catalyzes a key step in endoplasmic reticulum N-linked glycosylation.[7]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172339Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039887Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: asparagine-linked glycosylation 14 homolog (S. cerevisiae)".
  6. ^ Chantret I, Dancourt J, Barbat A, Moore SE (March 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. doi:10.1074/jbc.M413941200. PMID 15615718.
  7. ^ Averbeck N, Keppler-Ross S, Dean N (October 2007). "Membrane topology of the Alg14 endoplasmic reticulum UDP-GlcNAc transferase subunit". J. Biol. Chem. 282 (40): 29081–8. doi:10.1074/jbc.M704410200. PMID 17686769.
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Further reading

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