Endo-beta-n-acetylglucosaminidase

Endo-beta-N-acetylglucosaminidase is a protein that in humans is encoded by the ENGASE gene.

ENGASE
Identifiers
Aliases	ENGASE, endo-beta-N-acetylglucosaminidase
External IDs	OMIM: 611898; MGI: 2443788; HomoloGene: 13666; GeneCards: ENGASE; OMA:ENGASE - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17q25.3 Start 79,074,824 bp End 79,088,599 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 E2 Start 118,476,829 bp End 118,489,209 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon spleen granulocyte pancreatic ductal cell tendon of biceps brachii sural nerve right lobe of thyroid gland left ovary right ovary body of stomach Top expressed in ankle lip yolk sac neural layer of retina thymus duodenum muscle of thigh Paneth cell stomach bone marrow More reference expression data BioGPS n/a
Gene ontology Molecular function hydrolase activity hydrolase activity, acting on glycosyl bonds mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Cellular component cytoplasm lysosome cytosol Biological process metabolism protein folding protein deglycosylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 64772 217364 Ensembl ENSG00000167280 ENSMUSG00000033857 UniProt Q8NFI3 Q8BX80 RefSeq (mRNA) NM_001042573 NM_022759 NM_001396052 NM_001396053 NM_001396054 NM_001396055 NM_172573 NM_001359368 RefSeq (protein) NP_001036038 NP_766161 NP_001346297 NP_001390767 NP_001390768 NP_001390769 NP_001390770 Location (UCSC) Chr 17: 79.07 – 79.09 Mb Chr 11: 118.48 – 118.49 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a cytosolic enzyme which catalyzes the hydrolysis of peptides and proteins with mannose modifications to produce free oligosaccharides. [provided by RefSeq, Feb 2012].

Further reading

• Suzuki T, Yano K, Sugimoto S, Kitajima K, Lennarz WJ, Inoue S, Inoue Y, Emori Y (July 2002). "Endo-beta-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol". Proc. Natl. Acad. Sci. U.S.A. 99 (15): 9691–6. Bibcode:2002PNAS...99.9691S. doi:10.1073/pnas.152333599. PMC 124980. PMID 12114544.
• Ortutay Z, Polgár A, Gömör B, Géher P, Lakatos T, Glant TT, Gay RE, Gay S, Pállinger E, Farkas C, Farkas E, Tóthfalusi L, Kocsis K, Falus A, Buzás EI (August 2003). "Synovial fluid exoglycosidases are predictors of rheumatoid arthritis and are effective in cartilage glycosaminoglycan depletion". Arthritis Rheum. 48 (8): 2163–72. doi:10.1002/art.11093. PMID 12905469.
• Butkinaree C, Cheung WD, Park S, Park K, Barber M, Hart GW (August 2008). "Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3 during apoptosis". J. Biol. Chem. 283 (35): 23557–66. doi:10.1074/jbc.M804116200. PMC 2527095. PMID 18586680.
• Dorfmueller HC, van Aalten DM (February 2010). "Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds". FEBS Lett. 584 (4): 694–700. doi:10.1016/j.febslet.2009.12.020. PMC 2828546. PMID 20026047.
• Park K, Saudek CD, Hart GW (July 2010). "Increased expression of beta-N-acetylglucosaminidase in erythrocytes from individuals with pre-diabetes and diabetes". Diabetes. 59 (7): 1845–50. doi:10.2337/db09-1086. PMC 2889787. PMID 20413512.
• Chantret I, Fasseu M, Zaoui K, Le Bizec C, Sadou Yayé H, Dupré T, Moore SE (July 2010). "Identification of roles for peptide: N-glycanase and endo-beta-N-acetylglucosaminidase (Engase1p) during protein N-glycosylation in human HepG2 cells". PLOS ONE. 5 (7): e11734. Bibcode:2010PLoSO...511734C. doi:10.1371/journal.pone.0011734. PMC 2909182. PMID 20668520.
• Xiao F, Zheng X, Cui M, Shi G, Chen X, Li R, Song Z, Rudolph KL, Chen B, Ju Z (October 2011). "Telomere dysfunction-related serological markers are associated with type 2 diabetes". Diabetes Care. 34 (10): 2273–8. doi:10.2337/dc10-2431. PMC 3177723. PMID 21873561.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.