Variant position: 163 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 346 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human NEDLSTTASQALHSDWLARN CQPNYWRNVIPDPSKYCGPYK
Mouse NEDLSTKTSRDLHSDWLSRN CQPNYWRNVIPDPSKYCGPYK
Rat SEDLSTNTSRALHSDWLSRN CQPNYWRNVIPDPSKYCGPYK
Caenorhabditis elegans EEDLSTEETKSWISKWKTEK CQPNFWKNVSPDPSSSCGPYK
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
24 – 205 Glycosylasparaginase alpha chain
163 – 179
Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.
Ikonen E.; Baumann M.; Groen K.; Syvaenen A.-C.; Enomaa N.; Halila R.; Aula P.; Peltonen L.;
EMBO J. 10:51-58(1991)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; PROTEIN SEQUENCE OF 206-235; ACTIVATION BY CLEAVAGE; CATALYTIC ACTIVITY; VARIANTS SER-149; AGU GLN-161 AND SER-163; CHARACTERIZATION OF VARIANT AGU SER-163; FUNCTION;
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.
Fisher K.J.; Aronson N.N. Jr.;
J. Biol. Chem. 266:12105-12113(1991)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; AUTOCATALYTIC CLEAVAGE; CATALYTIC ACTIVITY; VARIANTS SER-149; AGU GLN-161 AND SER-163; FUNCTION;
Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.
Mononen I.; Heisterkamp N.; Kaartinen V.; Williams J.C.; Yates J.R. III; Griffin P.R.; Hood L.E.; Groffen J.;
Proc. Natl. Acad. Sci. U.S.A. 88:2941-2945(1991)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; PROTEIN SEQUENCE OF 24-45; 47-60; 67-84; 98-120; 123-190; 206-314 AND 320-343; VARIANTS AGU GLN-161 AND SER-163;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.