ALG2

ALG2
Identifiers
Aliases	ALG2, CDGIi, NET38, hALPG2, CMS14, CMSTA3, alpha-1,3/1,6-mannosyltransferase, CDG1I, ALG2 alpha-1,3/1,6-mannosyltransferase
External IDs	OMIM: 607905; MGI: 1914731; HomoloGene: 5930; GeneCards: ALG2; OMA:ALG2 - orthologs
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	47,474,333 bp
RNA expression pattern
	Top expressed in
	pancreatic epithelial cell; ; corpus epididymis; ; caput epididymis; ; secondary oocyte; ; germinal epithelium; ; tibia; ; islet of Langerhans; ; body of pancreas; ; visceral pleura; ; parietal pleura;
	Top expressed in
	median eminence; ; dorsomedial hypothalamic nucleus; ; paraventricular nucleus of hypothalamus; ; supraoptic nucleus; ; arcuate nucleus; ; dorsal tegmental nucleus; ; ventral tegmental area; ; suprachiasmatic nucleus; ; habenula; ; lateral hypothalamus;
	More reference expression data
	n/a
Gene ontology
Molecular function	GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; transferase activity; protein N-terminus binding; protein heterodimerization activity; glycosyltransferase activity; protein binding; calcium-dependent protein binding; alpha-1,3-mannosyltransferase activity; GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase activity;
Cellular component	cytoplasm; integral component of membrane; nucleus; membrane; perinuclear region of cytoplasm; endoplasmic reticulum membrane; cytosol; actin cytoskeleton;
Biological process	response to calcium ion; protein glycosylation; dolichol-linked oligosaccharide biosynthetic process; mannosylation; oligosaccharide-lipid intermediate biosynthetic process;
	Sources:Amigo / QuickGO
Orthologs
	85365
	56737
	n/a
	ENSMUSG00000039740
	Q9H553
	Q9DBE8
	NM_033087; NM_197973
	NM_019998; NM_001355496
	NP_149078
	NP_064382; NP_001342425
	Wikidata
View/Edit Human	View/Edit Mouse

Alpha-1,3-mannosyltransferase ALG2 is an enzyme that is encoded by the ALG2 gene.^[4] Mutations in the human gene are associated with congenital defects in glycosylation ^[5]^[6]

Template:PBB Summary

Interactions

ALG2 has been shown to interact with ANXA7^[7] and ANXA11.^[7]

References

^ ^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 (Jun 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.; Kohlschutter, A.; von Figura, K.; Lehle, L.; Korner, C. (2003). "A New Type of Congenital Disorders of Glycosylation (CDG-Ii) Provides New Insights into the Early Steps of Dolichol-linked Oligosaccharide Biosynthesis". Journal of Biological Chemistry. 278 (25): 22498–22505. doi:10.1074/jbc.M302850200. ISSN 0021-9258. PMID 12684507.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ "Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)".
^ ^a ^b Satoh, Hirokazu; Nakano Yoshimi; Shibata Hideki; Maki Masatoshi (Nov 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). Netherlands: 61–7. doi:10.1016/S1570-9639(02)00445-4. ISSN 0006-3002. PMID 12445460. {{cite journal}}: Cite has empty unknown parameters: |laysummary=, |laydate=, and |laysource= (help)

External links

GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview

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This article on a gene on human chromosome 9 is a stub. You can help Wikipedia by expanding it.

[refGRCm38Ensembl-1] GRCm38: Ensembl release 89: ENSMUSG00000039740 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid18400550-4] Jackson BJ, Kukuruzinska MA, Robbins P (Jun 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.

[ThielSchwarz2003-5] Thiel, C.; Schwarz, M.; Peng, J.; Grzmil, M.; Hasilik, M.; Braulke, T.; Kohlschutter, A.; von Figura, K.; Lehle, L.; Korner, C. (2003). "A New Type of Congenital Disorders of Glycosylation (CDG-Ii) Provides New Insights into the Early Steps of Dolichol-linked Oligosaccharide Biosynthesis". Journal of Biological Chemistry. 278 (25): 22498–22505. doi:10.1074/jbc.M302850200. ISSN 0021-9258. PMID 12684507.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[entrez-6] "Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)".

[pmid12445460-7] Satoh, Hirokazu; Nakano Yoshimi; Shibata Hideki; Maki Masatoshi (Nov 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). Netherlands: 61–7. doi:10.1016/S1570-9639(02)00445-4. ISSN 0006-3002. PMID 12445460. {{cite journal}}: Cite has empty unknown parameters: |laysummary=, |laydate=, and |laysource= (help)

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Interactions

References

Further reading

External links