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ALG14
Identifiers
Aliases	ALG14, CMS15, UDP-N-acetylglucosaminyltransferase subunit, ALG14 UDP-N-acetylglucosaminyltransferase subunit, IDDEBF, MEPCA
External IDs	OMIM: 612866; MGI: 1914039; HomoloGene: 49751; GeneCards: ALG14; OMA:ALG14 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p21.3 Start 94,974,405 bp End 95,072,951 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 G1 Start 121,085,422 bp End 121,156,743 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in corpus epididymis jejunal mucosa mucosa of colon mucosa of sigmoid colon right adrenal gland oral cavity left adrenal gland caput epididymis Achilles tendon palpebral conjunctiva Top expressed in sciatic nerve retinal pigment epithelium vestibular membrane of cochlear duct calvaria otic placode lumbar spinal ganglion morula genital tubercle carotid body right kidney More reference expression data BioGPS n/a
Gene ontology Molecular function N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity Cellular component integral component of membrane nuclear membrane endoplasmic reticulum membrane endoplasmic reticulum membrane nucleus UDP-N-acetylglucosamine transferase complex Biological process dolichol-linked oligosaccharide biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 199857 66789 Ensembl ENSG00000172339 ENSMUSG00000039887 UniProt Q96F25 Q9D081 RefSeq (mRNA) NM_001305242 NM_144988 NM_024178 RefSeq (protein) NP_001292171 NP_659425 NP_077140 Location (UCSC) Chr 1: 94.97 – 95.07 Mb Chr 3: 121.09 – 121.16 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

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.

See also

• Congenital disorder of glycosylation

References

1. ^ GRCh38: Ensembl release 89: ENSG00000172339 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000039887 – Ensembl, 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.

External links

• Human ALG14 genome location and ALG14 gene details page in the UCSC Genome Browser.

Further reading

• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gao XD, Tachikawa H, Sato T, 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. doi:10.1074/jbc.M507569200. PMID 16100110.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

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