ALG14 (original) (raw)
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Protein-coding gene in the species Homo sapiens
ALG14 | |
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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)[1]Band1p21.3Start94,974,405 bp[1]End95,072,951 bp[1] | |
Gene location (Mouse)Chr.Chromosome 3 (mouse)[2]Band3|3 G1Start121,085,422 bp[2]End121,156,743 bp[2] | |
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed incorpus epididymisjejunal mucosamucosa of colonmucosa of sigmoid colonright adrenal glandoral cavityleft adrenal glandcaput epididymisAchilles tendonpalpebral conjunctivaTop expressed insciatic nerveretinal pigment epitheliumvestibular membrane of cochlear ductcalvariaotic placodelumbar spinal ganglionmorulagenital tuberclecarotid bodyright kidneyMore reference expression dataBioGPSn/a | |
Gene ontologyMolecular 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 | |
OrthologsSpeciesHuman MouseEntrez19985766789EnsemblENSG00000172339ENSMUSG00000039887UniProtQ96F25Q9D081RefSeq (mRNA)NM_001305242NM_144988NM_024178RefSeq (protein)NP_001292171NP_659425NP_077140Location (UCSC)Chr 1: 94.97 – 95.07 MbChr 3: 121.09 – 121.16 MbPubMed search[3][4] | |
Wikidata | |
View/Edit HumanView/Edit Mouse |
UDP-N-acetylglucosamine transferase subunit ALG14 homolog is a protein that in humans is encoded by the ALG14 gene.[5][6]
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]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000172339 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039887 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Entrez Gene: asparagine-linked glycosylation 14 homolog (S. cerevisiae)".
- ^ 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.
- ^ 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.
Human ALG14 genome location and ALG14 gene details page in the UCSC Genome Browser.
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.