# ALG2

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Protein-coding gene in the species Homo sapiens

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)[1] Band 4|4 B1 Start 47,465,067 bp[1] End 47,474,333 bp[1] RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 85365 56737 Ensembl n/a ENSMUSG00000039740 UniProt Q9H553 Q9DBE8 RefSeq (mRNA) NM_033087 NM_197973 NM_019998 NM_001355496 RefSeq (protein) NP_149078 NP_064382 NP_001342425 Location (UCSC) n/a Chr 4: 47.47 – 47.47 Mb PubMed search [2] [3] Wikidata View/Edit Human View/Edit Mouse

**Alpha-1,3/1,6-mannosyltransferase ALG2** is an [enzyme](/source/Enzyme) that is encoded by the *ALG2* [gene](/source/Gene).[4] Mutations in the human gene are associated with congenital defects in glycosylation [5][6] The protein encoded by the ALG2 gene belongs to two classes of enzymes: [GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase](https://en.wikipedia.org/w/index.php?title=GDP-Man:Man1GlcNAc2-PP-dolichol_alpha-1,3-mannosyltransferase&action=edit&redlink=1) ([EC](/source/Enzyme_Commission_number) [2.4.1.132](https://enzyme.expasy.org/EC/2.4.1.132)) and [GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase](/source/GDP-Man%3AMan2GlcNAc2-PP-dolichol_alpha-1%2C6-mannosyltransferase) ([EC](/source/Enzyme_Commission_number) [2.4.1.257](https://enzyme.expasy.org/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).[6]

## Interactions

ALG2 has been shown to [interact](/source/Protein-protein_interaction) with [ANXA7](/source/ANXA7)[7] and [ANXA11](/source/ANXA11).[7]

## References

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_1-0) [***b***](#cite_ref-refGRCm38Ensembl_1-1) [***c***](#cite_ref-refGRCm38Ensembl_1-2) [GRCm38: Ensembl release 89: ENSMUSG00000039740](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000039740) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-2)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=85365). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-3)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=56737). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid18400550_4-0)** 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](/source/Doi_(identifier)):[10.1093/glycob/3.4.357](https://doi.org/10.1093%2Fglycob%2F3.4.357). [PMID](/source/PMID_(identifier)) [8400550](https://pubmed.ncbi.nlm.nih.gov/8400550).

1. **[^](#cite_ref-ThielSchwarz2003_5-0)** 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"](https://doi.org/10.1074%2Fjbc.M302850200). *The Journal of Biological Chemistry*. **278** (25): 22498–505. [doi](/source/Doi_(identifier)):[10.1074/jbc.M302850200](https://doi.org/10.1074%2Fjbc.M302850200). [PMID](/source/PMID_(identifier)) [12684507](https://pubmed.ncbi.nlm.nih.gov/12684507).

1. ^ [***a***](#cite_ref-entrez_6-0) [***b***](#cite_ref-entrez_6-1) ["Entrez Gene: ALG2 asparagine-linked glycosylation 2 homolog (S. cerevisiae, alpha-1,3-mannosyltransferase)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=85365).

1. ^ [***a***](#cite_ref-pmid12445460_7-0) [***b***](#cite_ref-pmid12445460_7-1) 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](/source/Doi_(identifier)):[10.1016/S1570-9639(02)00445-4](https://doi.org/10.1016%2FS1570-9639%2802%2900445-4). [PMID](/source/PMID_(identifier)) [12445460](https://pubmed.ncbi.nlm.nih.gov/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](/source/Doi_(identifier)):[10.1023/B:BOLI.0000031221.44647.9e](https://doi.org/10.1023%2FB%3ABOLI.0000031221.44647.9e). [PMID](/source/PMID_(identifier)) [15272470](https://pubmed.ncbi.nlm.nih.gov/15272470). [S2CID](/source/S2CID_(identifier)) [7608163](https://api.semanticscholar.org/CorpusID: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](/source/Doi_(identifier)):[10.1097/01.mop.0000133636.56790.4a](https://doi.org/10.1097%2F01.mop.0000133636.56790.4a). [PMID](/source/PMID_(identifier)) [15273506](https://pubmed.ncbi.nlm.nih.gov/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](/source/Doi_(identifier)):[10.1006/bbrc.2002.6600](https://doi.org/10.1006%2Fbbrc.2002.6600). [PMID](/source/PMID_(identifier)) [11883939](https://pubmed.ncbi.nlm.nih.gov/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](/source/Doi_(identifier)):[10.1016/S1570-9639(02)00445-4](https://doi.org/10.1016%2FS1570-9639%2802%2900445-4). [PMID](/source/PMID_(identifier)) [12445460](https://pubmed.ncbi.nlm.nih.gov/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. [Bibcode](/source/Bibcode_(identifier)):[2003FEBSL.545..151H](https://ui.adsabs.harvard.edu/abs/2003FEBSL.545..151H). [doi](/source/Doi_(identifier)):[10.1016/S0014-5793(03)00518-0](https://doi.org/10.1016%2FS0014-5793%2803%2900518-0). [PMID](/source/PMID_(identifier)) [12804766](https://pubmed.ncbi.nlm.nih.gov/12804766). [S2CID](/source/S2CID_(identifier)) [42572647](https://api.semanticscholar.org/CorpusID: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"](https://doi.org/10.1093%2Fjb%2Fmvh014). *Journal of Biochemistry*. **135** (1): 117–28. [doi](/source/Doi_(identifier)):[10.1093/jb/mvh014](https://doi.org/10.1093%2Fjb%2Fmvh014). [PMID](/source/PMID_(identifier)) [14999017](https://pubmed.ncbi.nlm.nih.gov/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"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1276969). *The Biochemical Journal*. **391** (Pt 3): 677–85. [doi](/source/Doi_(identifier)):[10.1042/BJ20050398](https://doi.org/10.1042%2FBJ20050398). [PMC](/source/PMC_(identifier)) [1276969](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1276969). [PMID](/source/PMID_(identifier)) [16004603](https://pubmed.ncbi.nlm.nih.gov/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"](https://doi.org/10.1093%2Fdnares%2F12.2.117). *DNA Research*. **12** (2): 117–26. [doi](/source/Doi_(identifier)):[10.1093/dnares/12.2.117](https://doi.org/10.1093%2Fdnares%2F12.2.117). [PMID](/source/PMID_(identifier)) [16303743](https://pubmed.ncbi.nlm.nih.gov/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"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2691584). *Archives of Biochemistry and Biophysics*. **467** (1): 87–94. [doi](/source/Doi_(identifier)):[10.1016/j.abb.2007.07.028](https://doi.org/10.1016%2Fj.abb.2007.07.028). [PMC](/source/PMC_(identifier)) [2691584](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2691584). [PMID](/source/PMID_(identifier)) [17889823](https://pubmed.ncbi.nlm.nih.gov/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](https://www.ncbi.nlm.nih.gov/books/NBK1332/)

- Human [*ALG2*](https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=ALG2) genome location and [*ALG2*](https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=ALG2) gene details page in the [UCSC Genome Browser](/source/UCSC_Genome_Browser).

v t e Transferases: glycosyltransferases (EC 2.4) 2.4.1: Hexosyl- transferases Glucosyl- Phosphorylase Starch Glycogen Cellobiose Myo- Glycogen synthase Debranching enzyme Branching enzyme 1,3-Beta-glucan synthase Ceramide glucosyltransferase N-glycosyltransferase Galactosyl- Lactose synthase B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (C1GALT1) Glucuronosyl- B3GAT1 B3GAT2 B3GAT3 UGT1A1 UGT1A3 UGT1A4 UGT1A5 UGT1A6 UGT1A7 UGT1A8 UGT1A9 UGT1A10 UGT2A1 UGT2A2 UGT2A3 UGT2B4 UGT2B7 UGT2B10 UGT2B11 UGT2B15 UGT2B17 UGT2B28 Hyaluronan synthase: HAS1 HAS2 HAS3 Fucosyl- POFUT1 POFUT2 FUT1 FUT2 FUT3 FUT4 FUT5 FUT6 FUT7 FUT8 FUT9 FUT10 FUT11 Mannosyl- Dolichyl-phosphate-mannose-protein mannosyltransferase POMT1 POMT2 DPM1 DPM3 ALG1 ALG2 ALG3 ALG6 ALG8 ALG9 ALG12 2.4.2: Pentosyl- transferases Ribose ADP-ribosyltransferase NAD+:diphthamide ADP-ribosyltransferase Diphtheria toxin Pseudomonas exotoxin NAD(P)+:arginine ADP-ribosyltransferase Pertussis toxin Cholera toxin Poly ADP ribose polymerase Sirtuin Phosphoribosyltransferase Adenine phosphoribosyltransferase Hypoxanthine-guanine phosphoribosyltransferase Uracil phosphoribosyltransferase Amidophosphoribosyltransferase Other Purine nucleoside phosphorylase: Thymidine phosphorylase TYMP Other Xylosyltransferase XYLT1 XYLT2 Arabinosyltransferase Indolylacetylinositol arabinosyltransferase 2.4.99: Sialyl transferases Beta-galactoside alpha-2,6-sialyltransferase Monosialoganglioside sialyltransferase ST8SIA4

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Adapted from the Wikipedia article [ALG2](https://en.wikipedia.org/wiki/ALG2) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/ALG2?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.