# GANAB

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Protein-coding gene in the species Homo sapiens

GANAB Identifiers Aliases GANAB, G2AN, GLUII, GIIA, glucosidase II alpha subunit, PKD3 External IDs OMIM: 104160; MGI: 1097667; HomoloGene: 5426; GeneCards: GANAB; OMA:GANAB - orthologs Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q12.3 Start 62,624,826 bp[1] End 62,646,726 bp[1] Gene location (Mouse) Chr. Chromosome 19 (mouse)[2] Band 19|19 A Start 8,875,435 bp[2] End 8,894,036 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium islet of Langerhans ventricular zone right ovary left ovary right lobe of thyroid gland body of pancreas canal of the cervix smooth muscle tissue body of uterus Top expressed in cumulus cell ventricular zone yolk sac neural layer of retina gastrula epiblast lip tail of embryo dentate gyrus of hippocampal formation granule cell right kidney More reference expression data BioGPS More reference expression data Gene ontology Molecular function hydrolase activity, hydrolyzing O-glycosyl compounds catalytic activity hydrolase activity carbohydrate binding hydrolase activity, acting on glycosyl bonds glucan 1,3-alpha-glucosidase activity RNA binding protein binding alpha-glucosidase activity Cellular component melanosome Golgi apparatus endoplasmic reticulum lumen glucosidase II complex membrane extracellular exosome endoplasmic reticulum extracellular matrix intracellular membrane-bounded organelle Biological process metabolism protein folding carbohydrate metabolic process N-glycan processing Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 23193 14376 Ensembl ENSG00000089597 ENSMUSG00000071650 UniProt Q14697 Q8BHN3 RefSeq (mRNA) NM_198335 NM_001278192 NM_001278193 NM_001278194 NM_014610 NM_198334 NM_001329222 NM_001329223 NM_001329224 NM_001329225 NM_001293621 NM_008060 RefSeq (protein) NP_001265121 NP_001265122 NP_001265123 NP_001316151 NP_001316152 NP_001316153 NP_001316154 NP_938148 NP_938149 NP_001280550 NP_032086 Location (UCSC) Chr 11: 62.62 – 62.65 Mb Chr 19: 8.88 – 8.89 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Neutral alpha-glucosidase AB** is an [enzyme](/source/Enzyme) that in humans is encoded by the *GANAB* [gene](/source/Gene).[5][6][7]

## Interactions

GANAB has been shown to [interact](/source/Protein-protein_interaction) with [PTPRC](/source/PTPRC).[8][9][10]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000089597](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000089597) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000071650](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000071650) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=23193). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=14376). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid10764838_5-0)** Treml K, Meimaroglou D, Hentges A, Bause E (May 2000). ["The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver"](https://doi.org/10.1093%2Fglycob%2F10.5.493). *Glycobiology*. **10** (5): 493–502. [doi](/source/Doi_(identifier)):[10.1093/glycob/10.5.493](https://doi.org/10.1093%2Fglycob%2F10.5.493). [PMID](/source/PMID_(identifier)) [10764838](https://pubmed.ncbi.nlm.nih.gov/10764838).

1. **[^](#cite_ref-pmid6342981_6-0)** Martiniuk F, Smith M, Ellenbogen A, Desnick RJ, Astrin K, Mitra J, Hirschhorn R (July 1983). ["Assignment of the gene for neutral alpha-glucosidase AB to chromosome 11"](http://www.escholarship.org/uc/item/0hd6221m). *Cytogenet Cell Genet*. **35** (2): 110–6. [doi](/source/Doi_(identifier)):[10.1159/000131851](https://doi.org/10.1159%2F000131851). [PMID](/source/PMID_(identifier)) [6342981](https://pubmed.ncbi.nlm.nih.gov/6342981). [S2CID](/source/S2CID_(identifier)) [46749795](https://api.semanticscholar.org/CorpusID:46749795).

1. **[^](#cite_ref-entrez_7-0)** ["Entrez Gene: GANAB glucosidase, alpha; neutral AB"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=23193).

1. **[^](#cite_ref-pmid9148925_8-0)** Arendt CW, Ostergaard HL (May 1997). ["Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II"](https://doi.org/10.1074%2Fjbc.272.20.13117). *J. Biol. Chem*. **272** (20): 13117–25. [doi](/source/Doi_(identifier)):[10.1074/jbc.272.20.13117](https://doi.org/10.1074%2Fjbc.272.20.13117). [PMID](/source/PMID_(identifier)) [9148925](https://pubmed.ncbi.nlm.nih.gov/9148925).

1. **[^](#cite_ref-pmid10921916_9-0)** Baldwin TA, Gogela-Spehar M, Ostergaard HL (October 2000). ["Specific isoforms of the resident endoplasmic reticulum protein glucosidase II associate with the CD45 protein-tyrosine phosphatase via a lectin-like interaction"](https://doi.org/10.1074%2Fjbc.M003088200). *J. Biol. Chem*. **275** (41): 32071–6. [doi](/source/Doi_(identifier)):[10.1074/jbc.M003088200](https://doi.org/10.1074%2Fjbc.M003088200). [PMID](/source/PMID_(identifier)) [10921916](https://pubmed.ncbi.nlm.nih.gov/10921916).

1. **[^](#cite_ref-pmid11564800_10-0)** Baldwin TA, Ostergaard HL (October 2001). ["Developmentally regulated changes in glucosidase II association with, and carbohydrate content of, the protein tyrosine phosphatase CD45"](https://doi.org/10.4049%2Fjimmunol.167.7.3829). *J. Immunol*. **167** (7): 3829–35. [doi](/source/Doi_(identifier)):[10.4049/jimmunol.167.7.3829](https://doi.org/10.4049%2Fjimmunol.167.7.3829). [PMID](/source/PMID_(identifier)) [11564800](https://pubmed.ncbi.nlm.nih.gov/11564800).

## Further reading

- Feizi T, Larkin M (1992). "AIDS and glycosylation". *Glycobiology*. **1** (1): 17–23. [doi](/source/Doi_(identifier)):[10.1093/glycob/1.1.17](https://doi.org/10.1093%2Fglycob%2F1.1.17). [PMID](/source/PMID_(identifier)) [2136376](https://pubmed.ncbi.nlm.nih.gov/2136376).

- Land A, Braakman I (2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". *Biochimie*. **83** (8): 783–90. [doi](/source/Doi_(identifier)):[10.1016/S0300-9084(01)01314-1](https://doi.org/10.1016%2FS0300-9084%2801%2901314-1). [hdl](/source/Hdl_(identifier)):[1874/5091](https://hdl.handle.net/1874%2F5091). [PMID](/source/PMID_(identifier)) [11530211](https://pubmed.ncbi.nlm.nih.gov/11530211). [S2CID](/source/S2CID_(identifier)) [13576808](https://api.semanticscholar.org/CorpusID:13576808).

- Fenouillet E, Gluckman JC (1991). ["Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein"](https://doi.org/10.1099%2F0022-1317-72-8-1919). *J. Gen. Virol*. **72** (8): 1919–26. [doi](/source/Doi_(identifier)):[10.1099/0022-1317-72-8-1919](https://doi.org/10.1099%2F0022-1317-72-8-1919). [PMID](/source/PMID_(identifier)) [1678778](https://pubmed.ncbi.nlm.nih.gov/1678778).

- Ratner L, vander Heyden N, Dedera D (1991). "Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity". *Virology*. **181** (1): 180–92. [doi](/source/Doi_(identifier)):[10.1016/0042-6822(91)90483-R](https://doi.org/10.1016%2F0042-6822%2891%2990483-R). [PMID](/source/PMID_(identifier)) [1704656](https://pubmed.ncbi.nlm.nih.gov/1704656).

- Dedera DA, Gu RL, Ratner L (1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function". *Virology*. **187** (1): 377–82. [doi](/source/Doi_(identifier)):[10.1016/0042-6822(92)90331-I](https://doi.org/10.1016%2F0042-6822%2892%2990331-I). [PMID](/source/PMID_(identifier)) [1736542](https://pubmed.ncbi.nlm.nih.gov/1736542).

- Murphy CI, Lennick M, Lehar SM, Beltz GA, Young E (1991). "Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding". *Genet. Anal. Tech. Appl*. **7** (6): 160–71. [doi](/source/Doi_(identifier)):[10.1016/0735-0651(90)90030-J](https://doi.org/10.1016%2F0735-0651%2890%2990030-J). [PMID](/source/PMID_(identifier)) [2076345](https://pubmed.ncbi.nlm.nih.gov/2076345).

- Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG (1990). ["Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1"](https://zenodo.org/record/1235229). *AIDS Res. Hum. Retroviruses*. **6** (3): 371–80. [doi](/source/Doi_(identifier)):[10.1089/aid.1990.6.371](https://doi.org/10.1089%2Faid.1990.6.371). [PMID](/source/PMID_(identifier)) [2187500](https://pubmed.ncbi.nlm.nih.gov/2187500).

- Shimizu H, Tsuchie H, Honma H, Yoshida K, Tsuruoka T, Ushijima H, Kitamura T (1991). ["Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins"](https://doi.org/10.7883%2Fyoken1952.43.75). *Jpn. J. Med. Sci. Biol*. **43** (3): 75–87. [doi](/source/Doi_(identifier)):[10.7883/yoken1952.43.75](https://doi.org/10.7883%2Fyoken1952.43.75). [PMID](/source/PMID_(identifier)) [2283726](https://pubmed.ncbi.nlm.nih.gov/2283726).

- Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ (1990). ["Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells"](https://doi.org/10.1016%2FS0021-9258%2818%2986956-3). *J. Biol. Chem*. **265** (18): 10373–82. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(18)86956-3](https://doi.org/10.1016%2FS0021-9258%2818%2986956-3). [PMID](/source/PMID_(identifier)) [2355006](https://pubmed.ncbi.nlm.nih.gov/2355006).

- Pal R, Hoke GM, Sarngadharan MG (1989). ["Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC287137). *Proc. Natl. Acad. Sci. U.S.A*. **86** (9): 3384–8. [Bibcode](/source/Bibcode_(identifier)):[1989PNAS...86.3384P](https://ui.adsabs.harvard.edu/abs/1989PNAS...86.3384P). [doi](/source/Doi_(identifier)):[10.1073/pnas.86.9.3384](https://doi.org/10.1073%2Fpnas.86.9.3384). [PMC](/source/PMC_(identifier)) [287137](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC287137). [PMID](/source/PMID_(identifier)) [2541446](https://pubmed.ncbi.nlm.nih.gov/2541446).

- Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (1989). ["Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC250699). *J. Virol*. **63** (6): 2452–6. [doi](/source/Doi_(identifier)):[10.1128/jvi.63.6.2452-2456.1989](https://doi.org/10.1128%2Fjvi.63.6.2452-2456.1989). [PMC](/source/PMC_(identifier)) [250699](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC250699). [PMID](/source/PMID_(identifier)) [2542563](https://pubmed.ncbi.nlm.nih.gov/2542563).

- Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". *J. Acquir. Immune Defic. Syndr*. **2** (2): 163–9. [PMID](/source/PMID_(identifier)) [2649653](https://pubmed.ncbi.nlm.nih.gov/2649653).

- Walker BD, Kowalski M, Goh WC, Kozarsky K, Krieger M, Rosen C, Rohrschneider L, Haseltine WA, Sodroski J (1987). ["Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC299490). *Proc. Natl. Acad. Sci. U.S.A*. **84** (22): 8120–4. [Bibcode](/source/Bibcode_(identifier)):[1987PNAS...84.8120W](https://ui.adsabs.harvard.edu/abs/1987PNAS...84.8120W). [doi](/source/Doi_(identifier)):[10.1073/pnas.84.22.8120](https://doi.org/10.1073%2Fpnas.84.22.8120). [PMC](/source/PMC_(identifier)) [299490](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC299490). [PMID](/source/PMID_(identifier)) [2825177](https://pubmed.ncbi.nlm.nih.gov/2825177).

- Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". *AIDS Res. Hum. Retroviruses*. **3** (3): 265–82. [doi](/source/Doi_(identifier)):[10.1089/aid.1987.3.265](https://doi.org/10.1089%2Faid.1987.3.265). [PMID](/source/PMID_(identifier)) [2829950](https://pubmed.ncbi.nlm.nih.gov/2829950).

- Gruters RA, Neefjes JJ, Tersmette M, de Goede RE, Tulp A, Huisman HG, Miedema F, Ploegh HL (1987). "Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase". *Nature*. **330** (6143): 74–7. [Bibcode](/source/Bibcode_(identifier)):[1987Natur.330...74G](https://ui.adsabs.harvard.edu/abs/1987Natur.330...74G). [doi](/source/Doi_(identifier)):[10.1038/330074a0](https://doi.org/10.1038%2F330074a0). [PMID](/source/PMID_(identifier)) [2959866](https://pubmed.ncbi.nlm.nih.gov/2959866). [S2CID](/source/S2CID_(identifier)) [4270139](https://api.semanticscholar.org/CorpusID:4270139).

- Blough HA, Pauwels R, De Clercq E, Cogniaux J, Sprecher-Goldberger S, Thiry L (1987). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". *Biochem. Biophys. Res. Commun*. **141** (1): 33–8. [doi](/source/Doi_(identifier)):[10.1016/S0006-291X(86)80330-8](https://doi.org/10.1016%2FS0006-291X%2886%2980330-8). [PMID](/source/PMID_(identifier)) [3099781](https://pubmed.ncbi.nlm.nih.gov/3099781).

- Montefiori DC, Robinson WE, Mitchell WM (1988). ["Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC282716). *Proc. Natl. Acad. Sci. U.S.A*. **85** (23): 9248–52. [Bibcode](/source/Bibcode_(identifier)):[1988PNAS...85.9248M](https://ui.adsabs.harvard.edu/abs/1988PNAS...85.9248M). [doi](/source/Doi_(identifier)):[10.1073/pnas.85.23.9248](https://doi.org/10.1073%2Fpnas.85.23.9248). [PMC](/source/PMC_(identifier)) [282716](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC282716). [PMID](/source/PMID_(identifier)) [3264072](https://pubmed.ncbi.nlm.nih.gov/3264072).

- Martiniuk F, Ellenbogen A, Hirschhorn R (1985). ["Identity of neutral alpha-glucosidase AB and the glycoprotein processing enzyme glucosidase II. Biochemical and genetic studies"](https://doi.org/10.1016%2FS0021-9258%2820%2971234-2). *J. Biol. Chem*. **260** (2): 1238–42. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(20)71234-2](https://doi.org/10.1016%2FS0021-9258%2820%2971234-2). [PMID](/source/PMID_(identifier)) [3881423](https://pubmed.ncbi.nlm.nih.gov/3881423).

v t e Hydrolase: sugar hydrolases (EC 3.2) 3.2.1: Glycoside hydrolases Disaccharidase Sucrase/Sucrase-isomaltase/Invertase Maltase Trehalase Lactase Glucosidases Cellulase Alpha-glucosidase Acid Neutral AB Neutral C β-Glucosidase cytosolic Debranching enzyme Other Amylase α β Chitinase Lysozyme Neuraminidase NEU1 NEU2 NEU3 NEU4 Bacterial neuraminidase Viral neuraminidase Galactosidases α β α-Mannosidase Glucuronidase Klotho Hyaluronidase Pullulanase Glucosylceramidase lysosomal non-lysosomal Galactosylceramidase α-N-acetylgalactosaminidase NAGA α-N-Acetylglucosaminidase Fucosidase Hexosaminidase HEXA HEXB Iduronidase Maltase-glucoamylase Heparanase HPSE2 3.2.2: Hydrolysing N-Glycosyl compounds DNA glycosylases: Oxoguanine glycosylase

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