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{{Infobox_gene}}
{{PBB_Controls
'''Neutral alpha-glucosidase AB''' is an [[enzyme]] that in humans is encoded by the ''GANAB'' [[gene]].<ref name="pmid10764838">{{cite journal | vauthors = Treml K, Meimaroglou D, Hentges A, Bause E | title = The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver | journal = Glycobiology | volume = 10 | issue = 5 | pages = 493–502 | date = May 2000 | pmid = 10764838 | pmc =  | doi = 10.1093/glycob/10.5.493 }}</ref><ref name="pmid6342981">{{cite journal | vauthors = Martiniuk F, Smith M, Ellenbogen A, Desnick RJ, Astrin K, Mitra J, Hirschhorn R | title = Assignment of the gene for neutral alpha-glucosidase AB to chromosome 11 | journal = Cytogenet Cell Genet | volume = 35 | issue = 2 | pages = 110–6 | date = July 1983 | pmid = 6342981 | pmc =  | doi = 10.1159/000131851 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GANAB glucosidase, alpha; neutral AB| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23193| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Glucosidase, alpha; neutral AB
| HGNCid = 4138
| Symbol = GANAB
| AltSymbols =; G2AN; GluII; KIAA0088
| OMIM = 104160
| ECnumber = 
| Homologene = 5426
| MGIid = 1097667
| GeneAtlas_image1 = PBB_GE_GANAB_211934_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_GANAB_214626_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004553 |text = hydrolase activity, hydrolyzing O-glycosyl compounds}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 23193
    | Hs_Ensembl = ENSG00000089597
    | Hs_RefseqProtein = NP_938148
    | Hs_RefseqmRNA = NM_198334
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 62148882
    | Hs_GenLoc_end = 62170680
    | Hs_Uniprot = Q14697
    | Mm_EntrezGene = 14376
    | Mm_Ensembl = ENSMUSG00000071650
    | Mm_RefseqmRNA = NM_008060
    | Mm_RefseqProtein = NP_032086
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 8965141
    | Mm_GenLoc_end = 8983778
    | Mm_Uniprot = Q149A6
  }}
}}
'''Glucosidase, alpha; neutral AB''', also known as '''GANAB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GANAB glucosidase, alpha; neutral AB| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23193| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
GANAB has been shown to [[Protein-protein interaction|interact]] with [[PTPRC]].<ref name=pmid9148925>{{cite journal | vauthors = Arendt CW, Ostergaard HL | title = Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II | journal = J. Biol. Chem. | volume = 272 | issue = 20 | pages = 13117–25 | date = May 1997 | pmid = 9148925 | doi = 10.1074/jbc.272.20.13117 }}</ref><ref name=pmid10921916>{{cite journal | vauthors = Baldwin TA, Gogela-Spehar M, Ostergaard HL | title = Specific isoforms of the resident endoplasmic reticulum protein glucosidase II associate with the CD45 protein-tyrosine phosphatase via a lectin-like interaction | journal = J. Biol. Chem. | volume = 275 | issue = 41 | pages = 32071–6 | date = October 2000 | pmid = 10921916 | doi = 10.1074/jbc.M003088200 }}</ref><ref name=pmid11564800>{{cite journal | vauthors = Baldwin TA, Ostergaard HL | title = Developmentally regulated changes in glucosidase II association with, and carbohydrate content of, the protein tyrosine phosphatase CD45 | journal = J. Immunol. | volume = 167 | issue = 7 | pages = 3829–35 | date = October 2001 | pmid = 11564800 | doi = 10.4049/jimmunol.167.7.3829 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text =  
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Feizi T, Larkin M | title = AIDS and glycosylation. | journal = Glycobiology | volume = 1 | issue = 1 | pages = 17–23 | year = 1992 | pmid = 2136376 | doi = 10.1093/glycob/1.1.17 }}
| citations =
* {{cite journal | vauthors = Land A, Braakman I | title = Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum. | journal = Biochimie | volume = 83 | issue = 8 | pages = 783–90 | year = 2001 | pmid = 11530211 | doi = 10.1016/S0300-9084(01)01314-1 }}
*{{cite journal | author=Feizi T, Larkin M |title=AIDS and glycosylation. |journal=Glycobiology |volume=1 |issue= 1 |pages= 17-23 |year= 1992 |pmid= 2136376 |doi= }}
* {{cite journal | vauthors = Fenouillet E, Gluckman JC | title = Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein. | journal = J. Gen. Virol. | volume = 72 ( Pt 8) | issue = 8 | pages = 1919–26 | year = 1991 | pmid = 1678778 | doi = 10.1099/0022-1317-72-8-1919 }}
*{{cite journal | author=Land A, Braakman I |title=Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum. |journal=Biochimie |volume=83 |issue= 8 |pages= 783-90 |year= 2001 |pmid= 11530211 |doi= }}
* {{cite journal | vauthors = Ratner L, vander Heyden N, Dedera D | title = Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity. | journal = Virology | volume = 181 | issue = 1 | pages = 180–92 | year = 1991 | pmid = 1704656 | doi = 10.1016/0042-6822(91)90483-R }}
*{{cite journal | author=Fenouillet E, Gluckman JC |title=Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein. |journal=J. Gen. Virol. |volume=72 ( Pt 8) |issue= |pages= 1919-26 |year= 1991 |pmid= 1678778 |doi= }}
* {{cite journal | vauthors = Dedera DA, Gu RL, Ratner L | title = Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function. | journal = Virology | volume = 187 | issue = 1 | pages = 377–82 | year = 1992 | pmid = 1736542 | doi = 10.1016/0042-6822(92)90331-I }}
*{{cite journal | author=Ratner L, vander Heyden N, Dedera D |title=Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity. |journal=Virology |volume=181 |issue= 1 |pages= 180-92 |year= 1991 |pmid= 1704656 |doi= }}
* {{cite journal | vauthors = Murphy CI, Lennick M, Lehar SM, Beltz GA, Young E | title = Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding. | journal = Genet. Anal. Tech. Appl. | volume = 7 | issue = 6 | pages = 160–71 | year = 1991 | pmid = 2076345 | doi = 10.1016/0735-0651(90)90030-J }}
*{{cite journal | author=Dedera DA, Gu RL, Ratner L |title=Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function. |journal=Virology |volume=187 |issue= 1 |pages= 377-82 |year= 1992 |pmid= 1736542 |doi= }}
* {{cite journal | vauthors = Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG | title = Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1. | journal = AIDS Res. Hum. Retroviruses | volume = 6 | issue = 3 | pages = 371–80 | year = 1990 | pmid = 2187500 | doi = 10.1089/aid.1990.6.371 }}
*{{cite journal | author=Murphy CI, Lennick M, Lehar SM, ''et al.'' |title=Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding. |journal=Genet. Anal. Tech. Appl. |volume=7 |issue= 6 |pages= 160-71 |year= 1991 |pmid= 2076345 |doi= }}
* {{cite journal | vauthors = Shimizu H, Tsuchie H, Honma H, Yoshida K, Tsuruoka T, Ushijima H, Kitamura T | title = Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins. | journal = Jpn. J. Med. Sci. Biol. | volume = 43 | issue = 3 | pages = 75–87 | year = 1991 | pmid = 2283726 | doi = 10.7883/yoken1952.43.75 }}
*{{cite journal | author=Kalyanaraman VS, Rodriguez V, Veronese F, ''et al.'' |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371-80 |year= 1990 |pmid= 2187500 |doi= }}
* {{cite journal | vauthors = Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ | title = 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. | journal = J. Biol. Chem. | volume = 265 | issue = 18 | pages = 10373–82 | year = 1990 | pmid = 2355006 | doi =  }}
*{{cite journal | author=Shimizu H, Tsuchie H, Honma H, ''et al.'' |title=Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins. |journal=Jpn. J. Med. Sci. Biol. |volume=43 |issue= 3 |pages= 75-87 |year= 1991 |pmid= 2283726 |doi= }}
* {{cite journal | vauthors = Pal R, Hoke GM, Sarngadharan MG | title = Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 86 | issue = 9 | pages = 3384–8 | year = 1989 | pmid = 2541446 | pmc = 287137 | doi = 10.1073/pnas.86.9.3384 }}
*{{cite journal | author=Leonard CK, Spellman MW, Riddle L, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=265 |issue= 18 |pages= 10373-82 |year= 1990 |pmid= 2355006 |doi=  }}
* {{cite journal | vauthors = Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP | title = Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport. | journal = J. Virol. | volume = 63 | issue = 6 | pages = 2452–6 | year = 1989 | pmid = 2542563 | pmc = 250699 | doi =  }}
*{{cite journal | author=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384-8 |year= 1989 |pmid= 2541446 |doi= }}
* {{cite journal | vauthors = Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M | title = Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. | journal = J. Acquir. Immune Defic. Syndr. | volume = 2 | issue = 2 | pages = 163–9 | year = 1989 | pmid = 2649653 | doi =  }}
*{{cite journal | author=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport. |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452-6 |year= 1989 |pmid= 2542563 |doi=  }}
* {{cite journal | vauthors = Walker BD, Kowalski M, Goh WC, Kozarsky K, Krieger M, Rosen C, Rohrschneider L, Haseltine WA, Sodroski J | title = Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 84 | issue = 22 | pages = 8120–4 | year = 1987 | pmid = 2825177 | pmc = 299490 | doi = 10.1073/pnas.84.22.8120 }}
*{{cite journal | author=Kozarsky K, Penman M, Basiripour L, ''et al.'' |title=Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. |journal=J. Acquir. Immune Defic. Syndr. |volume=2 |issue= 2 |pages= 163-9 |year= 1989 |pmid= 2649653 |doi=  }}
* {{cite journal | vauthors = Robinson WE, Montefiori DC, Mitchell WM | title = Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis. | journal = AIDS Res. Hum. Retroviruses | volume = 3 | issue = 3 | pages = 265–82 | year = 1988 | pmid = 2829950 | doi = 10.1089/aid.1987.3.265 }}
*{{cite journal | author=Walker BD, Kowalski M, Goh WC, ''et al.'' |title=Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 22 |pages= 8120-4 |year= 1987 |pmid= 2825177 |doi= }}
* {{cite journal | vauthors = Gruters RA, Neefjes JJ, Tersmette M, de Goede RE, Tulp A, Huisman HG, Miedema F, Ploegh HL | title = Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase. | journal = Nature | volume = 330 | issue = 6143 | pages = 74–7 | year = 1987 | pmid = 2959866 | doi = 10.1038/330074a0 }}
*{{cite journal | author=Robinson WE, Montefiori DC, Mitchell WM |title=Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis. |journal=AIDS Res. Hum. Retroviruses |volume=3 |issue= 3 |pages= 265-82 |year= 1988 |pmid= 2829950 |doi= }}
* {{cite journal | vauthors = Blough HA, Pauwels R, De Clercq E, Cogniaux J, Sprecher-Goldberger S, Thiry L | title = Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins. | journal = Biochem. Biophys. Res. Commun. | volume = 141 | issue = 1 | pages = 33–8 | year = 1987 | pmid = 3099781 | doi = 10.1016/S0006-291X(86)80330-8 }}
*{{cite journal | author=Gruters RA, Neefjes JJ, Tersmette M, ''et al.'' |title=Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase. |journal=Nature |volume=330 |issue= 6143 |pages= 74-7 |year= 1987 |pmid= 2959866 |doi= 10.1038/330074a0 }}
* {{cite journal | vauthors = Montefiori DC, Robinson WE, Mitchell WM | title = Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 85 | issue = 23 | pages = 9248–52 | year = 1988 | pmid = 3264072 | pmc = 282716 | doi = 10.1073/pnas.85.23.9248 }}
*{{cite journal | author=Blough HA, Pauwels R, De Clercq E, ''et al.'' |title=Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins. |journal=Biochem. Biophys. Res. Commun. |volume=141 |issue= 1 |pages= 33-8 |year= 1987 |pmid= 3099781 |doi= }}
* {{cite journal | vauthors = Martiniuk F, Ellenbogen A, Hirschhorn R | title = Identity of neutral alpha-glucosidase AB and the glycoprotein processing enzyme glucosidase II. Biochemical and genetic studies. | journal = J. Biol. Chem. | volume = 260 | issue = 2 | pages = 1238–42 | year = 1985 | pmid = 3881423 | doi =  }}
*{{cite journal | author=Montefiori DC, Robinson WE, Mitchell WM |title=Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 23 |pages= 9248-52 |year= 1988 |pmid= 3264072 |doi= }}
*{{cite journal | author=Martiniuk F, Ellenbogen A, Hirschhorn R |title=Identity of neutral alpha-glucosidase AB and the glycoprotein processing enzyme glucosidase II. Biochemical and genetic studies. |journal=J. Biol. Chem. |volume=260 |issue= 2 |pages= 1238-42 |year= 1985 |pmid= 3881423 |doi=  }}
*{{cite journal  | author=Martiniuk F, Smith M, Ellenbogen A, ''et al.'' |title=Assignment of the gene for neutral alpha-glucosidase AB to chromosome 11. |journal=Cytogenet. Cell Genet. |volume=35 |issue= 2 |pages= 110-6 |year= 1983 |pmid= 6342981 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Sugar hydrolases}}
{{WikiDoc Sources}}
 
 
{{gene-11-stub}}

Latest revision as of 02:18, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Neutral alpha-glucosidase AB is an enzyme that in humans is encoded by the GANAB gene.[1][2][3]

Interactions

GANAB has been shown to interact with PTPRC.[4][5][6]

References

  1. ↑ 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". Glycobiology. 10 (5): 493–502. doi:10.1093/glycob/10.5.493. PMID 10764838.
  2. ↑ 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". Cytogenet Cell Genet. 35 (2): 110–6. doi:10.1159/000131851. PMID 6342981.
  3. ↑ "Entrez Gene: GANAB glucosidase, alpha; neutral AB".
  4. ↑ 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". J. Biol. Chem. 272 (20): 13117–25. doi:10.1074/jbc.272.20.13117. PMID 9148925.
  5. ↑ 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". J. Biol. Chem. 275 (41): 32071–6. doi:10.1074/jbc.M003088200. PMID 10921916.
  6. ↑ Baldwin TA, Ostergaard HL (October 2001). "Developmentally regulated changes in glucosidase II association with, and carbohydrate content of, the protein tyrosine phosphatase CD45". J. Immunol. 167 (7): 3829–35. doi:10.4049/jimmunol.167.7.3829. PMID 11564800.

Further reading


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