UniProtKB/SwissProt variant VAR

Variant information

Variant position:

163

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 Cysteine (C) to Serine (S) at position 163 (C163S, p.Cys163Ser).

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 medium size and polar (C) to small size and polar (S)

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; most frequent mutation; abolishes autocatalytic cleavage and enzyme activity.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs121964904 [ dbSNP | Ensembl ]

Sequence information

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:

NEDLSTTASQALHSDWLARN C QPNYWRNVIPDPSKYCGPYK

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                         NEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYK

Mouse                         NEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCGPYK

Rat                           SEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCGPYK

Caenorhabditis elegans        EEDLSTEETKSWISKWKTEKCQPNFWKNVSPDPSSSCGPYK

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
Chain	24 – 205	Glycosylasparaginase alpha chain
Disulfide bond	163 – 179

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;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P20933: Variant p.Cys163Ser