ALG2

From Wikipedia, the free encyclopedia

Asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)

Identifiers

ALG2; CDGIi; FLJ14511; hALPG2

External IDs

OMIM: 607905 MGI: 1914731 HomoloGene: 5930

Gene ontology
Molecular Function:	• transferase activity, transferring glycosyl groups
Cellular Component:	• membrane • integral to membrane
Biological Process:	• biosynthetic process

Orthologs

Human

Mouse

Refseq

NM_033087 (mRNA)
NP_149078 (protein)

NM_019998 (mRNA)
NP_064382 (protein)

Location

Chr 9: 101.02 - 101.02 Mb

Chr 4: 47.49 - 47.5 Mb

Pubmed search

[1]

[2]

Asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase), also known as ALG2, is a human gene.^[1]

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).^[1]

[edit] References

^ ^a ^b Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase).

[edit] Further reading

Jaeken J (2005). "Congenital disorders of glycosylation (CDG): update and new developments.". J. Inherit. Metab. Dis. 27 (3): 423-6. PMID 15272470.
Jaeken J, Carchon H (2004). "Congenital disorders of glycosylation: a booming chapter of pediatrics.". Curr. Opin. Pediatr. 16 (4): 434-9. PMID 15273506.
Satoh H, Shibata H, Nakano Y, et al. (2002). "ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner.". Biochem. Biophys. Res. Commun. 291 (5): 1166-72. doi:10.1006/bbrc.2002.6600. PMID 11883939.
Satoh H, Nakano Y, Shibata H, Maki M (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.". Biochim. Biophys. Acta 1600 (1-2): 61-7. PMID 12445460.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. doi:10.1073/pnas.242603899. PMID 12477932.
Thiel C, Schwarz M, Peng J, et al. (2003). "A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis.". J. Biol. Chem. 278 (25): 22498-505. doi:10.1074/jbc.M302850200. PMID 12684507.
Hansen C, Tarabykina S, la Cour JM, et al. (2003). "The PEF family proteins sorcin and grancalcin interact in vivo and in vitro.". FEBS Lett. 545 (2-3): 151-4. PMID 12804766.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265-70. doi:10.1101/gr.1293003. PMID 12975309.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.
Shibata H, Yamada K, Mizuno T, et al. (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.". J. Biochem. 135 (1): 117-28. PMID 14999017.
Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9.". Nature 429 (6990): 369-74. doi:10.1038/nature02465. PMID 15164053.
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. PMID 15489334.
Katoh K, Suzuki H, Terasawa Y, et al. (2006). "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.". Biochem. J. 391 (Pt 3): 677-85. doi:10.1042/BJ20050398. PMID 16004603.
Otsuki T, Ota T, Nishikawa T, et al. (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 Res. 12 (2): 117-26. doi:10.1093/dnares/12.2.117. PMID 16303743.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55-65. doi:10.1101/gr.4039406. PMID 16344560.
Draeby I, Woods YL, la Cour JM, et al. (2007). "The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane.". Arch. Biochem. Biophys. 467 (1): 87-94. doi:10.1016/j.abb.2007.07.028. PMID 17889823.