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UniProtKB/Swiss-Prot P00966: Variant p.Glu191Gln

Argininosuccinate synthase
Gene: ASS1
Variant information

Variant position:  191
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 Glutamate (E) to Glutamine (Q) at position 191 (E191Q, p.Glu191Gln).
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 acidic (E) to medium size and polar (Q)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  2
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 CTLN1; loss of argininosuccinate synthase activity.
Any additional useful information about the variant.



Sequence information

Variant position:  191
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  412
The length of the canonical sequence.

Location on the sequence:   IPVTPKNPWSMDENLMHISY  E AGILENPKNQAPPGLYTKTQ
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                         IPVTPKNPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQ

Mouse                         IPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQ

Rat                           IPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQ

Bovine                        VPVTPKNPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQ

Chicken                       VPVTPKAPWSMDENLMHISYEAGILENPKNRAPLDLYTKTC

Xenopus laevis                VPVTPKSPWSMDENLMHISYEGGILENPKNHAPPGLYLKTK

Xenopus tropicalis            VPVTPKDPWSMDENIMHISYEGGILENPKNHAPPGLYLKTK

Zebrafish                     VPVTPKAPWSMDANLMHISYESGILENPKNHAPSDLYQMTK

Drosophila                    VSAKPATPWSTDANILHISYESGILEDPNTVAPENLYEMTV

Baker's yeast                 VAQTKAKPWSTDENQAHISYEAGILEDPDTTPPKDMWKLIV

Fission yeast                 VTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTV

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 1 – 412 Argininosuccinate synthase
Binding site 180 – 180 Citrulline
Binding site 189 – 189 Citrulline
Modified residue 176 – 176 N6-acetyllysine; by CLOCK
Modified residue 180 – 180 Phosphoserine
Mutagenesis 176 – 176 K -> QR. Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-165 or R-165.


Literature citations

Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene.
Engel K.; Hoehne W.; Haeberle J.;
Hum. Mutat. 30:300-307(2009)
Cited for: VARIANTS CTLN1 PRO-79; HIS-96; GLN-127; TRP-127; PRO-160; GLN-191; PRO-206; CYS-265; THR-277; ILE-284; SER-291; GLY-296; VAL-324; PHE-341; ARG-347 AND ASP-359;

Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation.
Diez-Fernandez C.; Wellauer O.; Gemperle C.; Ruefenacht V.; Fingerhut R.; Haeberle J.;
J. Med. Genet. 53:710-719(2016)
Cited for: VARIANTS CTLN1 PRO-91; LEU-96; SER-117; THR-118; ILE-119; ASN-124; CYS-157; HIS-157; CYS-272; HIS-272 AND LEU-272; CHARACTERIZATION OF VARIANTS CTLN1 PRO-91; SER-95; HIS-96; LEU-96; SER-96; SER-117; THR-118; ILE-119; ASN-124; GLN-127; TRP-127; CYS-157; HIS-157; ASN-180; ILE-180; GLN-191; GLN-270; CYS-272; HIS-272 AND LEU-272; CHARACTERIZATION OF VARIANT LEU-127; CATALYTIC ACTIVITY; PATHWAY; FUNCTION; SUBCELLULAR LOCATION;

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.