ALG14

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

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)[1] Band 1p21.3 Start 94,974,405 bp[1] End 95,072,951 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 G1 Start 121,085,422 bp[2] End 121,156,743 bp[2]
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 [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

• Congenital disorder of glycosylation