ALG2
Alpha-1,3/1,6-mannosyltransferase ALG2 is an enzyme that is encoded by the ALG2 gene.[5] Mutations in the human gene are associated with congenital defects in glycosylation [6][7] The protein encoded by the ALG2 gene belongs to two classes of enzymes: (EC 2.4.1.132) and GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase (EC 2.4.1.257).
Function[]
This gene encodes a member of the glycosyltransferase 1 family. The encoded protein acts as an alpha 1,3 mannosyltransferase, mannosylating Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. Defects in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ii).[7]
Interactions[]
ALG2 has been shown to interact with ANXA7[8] and ANXA11.[8]
References[]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000119523 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039740 - 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.
- ^ Jackson BJ, Kukuruzinska MA, Robbins P (August 1993). "Biosynthesis of asparagine-linked oligosaccharides in Saccharomyces cerevisiae: the alg2 mutation". Glycobiology. 3 (4): 357–64. doi:10.1093/glycob/3.4.357. PMID 8400550.
- ^ Thiel C, Schwarz M, Peng J, Grzmil M, Hasilik M, Braulke T, Kohlschütter A, von Figura K, Lehle L, Körner C (June 2003). "A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis". The Journal of Biological Chemistry. 278 (25): 22498–505. doi:10.1074/jbc.M302850200. PMID 12684507.
- ^ a b "Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)".
- ^ a b Satoh H, Nakano Y, Shibata H, Maki M (November 2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1600 (1–2): 61–7. doi:10.1016/S1570-9639(02)00445-4. PMID 12445460.
Further reading[]
- Jaeken J (2005). "Congenital disorders of glycosylation (CDG): update and new developments". Journal of Inherited Metabolic Disease. 27 (3): 423–6. doi:10.1023/B:BOLI.0000031221.44647.9e. PMID 15272470. S2CID 7608163.
- Jaeken J, Carchon H (August 2004). "Congenital disorders of glycosylation: a booming chapter of pediatrics". Current Opinion in Pediatrics. 16 (4): 434–9. doi:10.1097/01.mop.0000133636.56790.4a. PMID 15273506.
- Satoh H, Shibata H, Nakano Y, Kitaura Y, Maki M (March 2002). "ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner". Biochemical and Biophysical Research Communications. 291 (5): 1166–72. doi:10.1006/bbrc.2002.6600. PMID 11883939. NB ALG-2 is NOT the protein product of the ALG2 gene.
- Satoh H, Nakano Y, Shibata H, Maki M (November 2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1600 (1–2): 61–7. doi:10.1016/S1570-9639(02)00445-4. PMID 12445460. NB ALG-2 is NOT the protein product of the ALG2 gene.
- Hansen C, Tarabykina S, la Cour JM, Lollike K, Berchtold MW (June 2003). "The PEF family proteins sorcin and grancalcin interact in vivo and in vitro". FEBS Letters. 545 (2–3): 151–4. doi:10.1016/S0014-5793(03)00518-0. PMID 12804766. S2CID 42572647.
- Shibata H, Yamada K, Mizuno T, Yorikawa C, Takahashi H, Satoh H, Kitaura Y, Maki M (January 2004). "The penta-EF-hand protein ALG-2 interacts with a region containing PxY repeats in Alix/AIP1, which is required for the subcellular punctate distribution of the amino-terminal truncation form of Alix/AIP1". Journal of Biochemistry. 135 (1): 117–28. doi:10.1093/jb/mvh014. PMID 14999017. NB ALG-2 is NOT the protein product of the ALG2 gene.
- Katoh K, Suzuki H, Terasawa Y, Mizuno T, Yasuda J, Shibata H, Maki M (November 2005). "The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B". The Biochemical Journal. 391 (Pt 3): 677–85. doi:10.1042/BJ20050398. PMC 1276969. PMID 16004603. NB ALG-2 is NOT the protein product of the ALG2 gene.
- Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Research. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
- Draeby I, Woods YL, la Cour JM, Mollerup J, Bourdon JC, Berchtold MW (November 2007). "The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane". Archives of Biochemistry and Biophysics. 467 (1): 87–94. doi:10.1016/j.abb.2007.07.028. PMC 2691584. PMID 17889823. NB ALG-2 is NOT the protein product of the ALG2 gene.
External links[]
- GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview
- Human ALG2 genome location and ALG2 gene details page in the UCSC Genome Browser.
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