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UniProtKB/Swiss-Prot P20933: Variant p.Arg161Gln

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
Gene: AGA
Variant information

Variant position:  161
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Arginine (R) to Glutamine (Q) at position 161 (R161Q, p.Arg161Gln).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from large size and basic (R) to medium size and polar (Q)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  In AGU.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  161
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:   FINEDLSTTASQALHSDWLA  R NCQPNYWRNVIPDPSKYCGP
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                         FINEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCGP

Mouse                         FTNEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCGP

Rat                           FTSEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCGP

Caenorhabditis elegans        FKEEDLSTEETKSWISKWKTEKCQPNFWKNVSPDPSSSCGP

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.

TypePositionsDescription
Chain 24 – 205 Glycosylasparaginase alpha chain


Literature citations

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;

Disclaimer: 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.