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Identification
HMDB Protein ID HMDBP00895
Secondary Accession Numbers
  • 6177
Name N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
Synonyms
  1. Aspartylglucosaminidase
  2. Glycosylasparaginase
  3. Glycosylasparaginase alpha chain
  4. Glycosylasparaginase beta chain
  5. N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
Gene Name AGA
Protein Type Enzyme
Biological Properties
General Function Involved in hydrolase activity
Specific Function Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.
Pathways
  • Lysosome
  • Other glycan degradation
Reactions
N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + Water → N-Acetyl-b-glucosaminylamine + L-Aspartic acid details
GO Classification
Biological Process
protein deglycosylation
protein maturation
proteolysis
Cellular Component
endoplasmic reticulum
lysosome
Function
catalytic activity
hydrolase activity
Molecular Function
N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
peptidase activity
Cellular Location
  1. Lysosome
Gene Properties
Chromosome Location 4
Locus 4q34.3
SNPs AGA
Gene Sequence
>1041 bp
ATGGCGCGGAAGTCGAACTTGCCTGTGCTTCTCGTGCCGTTTCTGCTCTGCCAGGCCCTA
GTGCGCTGCTCCAGCCCTCTGCCCCTGGTCGTCAACACTTGGCCCTTTAAGAATGCAACC
GAAGCAGCGTGGAGGGCATTAGCATCTGGAGGCTCTGCCCTGGATGCAGTGGAGAGCGGC
TGTGCCATGTGTGAGAGAGAGCAGTGTGACGGCTCTGTAGGCTTTGGAGGAAGTCCTGAT
GAACTTGGAGAAACCACACTAGATGCCATGATCATGGATGGCACTACTATGGATGTAGGA
GCAGTAGGAGATCTCAGACGAATTAAAAATGCTATTGGTGTGGCACGGAAAGTACTGGAA
CATACAACACACACACTTTTAGTAGGAGAGTCAGCCACCACATTTGCTCAAAGTATGGGG
TTTATCAATGAAGACTTATCTACCAGTGCTTCTCAAGCTCTTCATTCAGATTGGCTTGCT
CGGAATTGCCAGCCAAATTATTGGAGGAATGTTATACCAGATCCCTCAAAATACTGCGGA
CCCTACAAACCACCTGGTATCTTAAAGCAGGATATTCCTATCCATAAAGAAACAGAAGAT
GATCGTGGTCATGACACTATTGGCATGGTTGTAATCCATAAGACAGGACATATTGCTGCT
GGTACATCTACAAATGGTATAAAATTCAAAATACATGGCCGTGTAGGAGACTCACCAATA
CCTGGAGCTGGAGCCTATGCTGACGATACTGCAGGGGCAGCCGCAGCCACTGGGAATGGT
GATATATTGATGCGCTTCCTGCCAAGCTACCAAGCTGTAGAATACATGAGAAGAGGAGAA
GATCCAACCATAGCTTGCCAAAAAGTGATTTCAAGAATCCAGAAGCATTTTCCAGAATTC
TTTGGGGCTGTTATATGTGCCAATGTGACTGGAAGTTACGGTGCTGCTTGCAATAAACTT
TCAACATTTACTCAGTTTAGTTTCATGGTTTATAATTCCGAAAAAAATCAGCCAACTGAG
GAAAAAGTGGACTGCATCTAA
Protein Properties
Number of Residues 346
Molecular Weight 37207.955
Theoretical pI 6.281
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
MARKSNLPVLLVPFLLCQALVRCSSPLPLVVNTWPFKNATEAAWRALASGGSALDAVESG
CAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVARKVLE
HTTHTLLVGESATTFAQSMGFINEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCG
PYKPPGILKQDIPIHKETEDDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPI
PGAGAYADDTAGAAAATGNGDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFPEF
FGAVICANVTGSYGAACNKLSTFTQFSFMVYNSEKNQPTEEKVDCI
GenBank ID Protein 34760
UniProtKB/Swiss-Prot ID P20933
UniProtKB/Swiss-Prot Entry Name ASPG_HUMAN
PDB IDs
GenBank Gene ID X55762
GeneCard ID AGA
GenAtlas ID AGA
HGNC ID HGNC:318
References
General References
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  8. Fisher KJ, Aronson NN Jr: Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits. J Biol Chem. 1991 Jun 25;266(18):12105-13. [PubMed:1904874 ]
  9. Mononen I, Heisterkamp N, Kaartinen V, Williams JC, Yates JR 3rd, Griffin PR, Hood LE, Groffen J: Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2941-5. [PubMed:2011603 ]
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  13. Peltola M, Tikkanen R, Peltonen L, Jalanko A: Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation. Hum Mol Genet. 1996 Jun;5(6):737-43. [PubMed:8776587 ]
  14. Laitinen A, Hietala M, Haworth JC, Schroeder ML, Seargeant LE, Greenberg CR, Aula P: Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation. Clin Genet. 1997 Mar;51(3):174-8. [PubMed:9137882 ]
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