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UniProtKB/Swiss-Prot P00966: Variant p.Ala164Pro

Argininosuccinate synthase
Gene: ASS1
Variant information

Variant position:  164
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 Alanine (A) to Proline (P) at position 164 (A164P, p.Ala164Pro).
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 small size and hydrophobic (A) to medium size and hydrophobic (P)
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 CTLN1.
Any additional useful information about the variant.



Sequence information

Variant position:  164
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:   PWRMPEFYNRFKGRNDLMEY  A KQHGIPIPVTPKNPWSMDEN
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                         PWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWSMDEN

Mouse                         PWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKSPWSMDEN

Rat                           PWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKSPWSMDEN

Bovine                        PWRMPEFYNRFQGRNDLMEYAKQHGIPVPVTPKNPWSMDEN

Chicken                       PWRMPEFYQRFPGRRELMEYAQKHGIPVPVTPKAPWSMDEN

Xenopus laevis                PWRMPEFYNRFRGRSDLMEYAKKHNISVPVTPKSPWSMDEN

Xenopus tropicalis            PWRMPEFYNRFRGRSDLMEYAKKHNIPVPVTPKDPWSMDEN

Zebrafish                     PWRIPEFYNRFRGRKDLMEYAEKHNIPVPVTPKAPWSMDAN

Drosophila                    PWRDVEFCCQFQGRQDLIAYAQQHGIEVSAKPATPWSTDAN

Baker's yeast                 PWRMPEFFERFAGRKDLLDYAAQKGIPVAQTKAKPWSTDEN

Fission yeast                 PWRLPVFFERFAGRKDLLEYAAAKGIPVTQTTKKPWSMDEN

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
Modified residue 165 – 165 N6-acetyllysine; by CLOCK
Modified residue 176 – 176 N6-acetyllysine; by CLOCK
Modified residue 180 – 180 Phosphoserine
Mutagenesis 165 – 165 K -> QR. Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-176 or R-176.
Mutagenesis 176 – 176 K -> QR. Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-165 or R-165.
Helix 158 – 166


Literature citations

Mutations in the human argininosuccinate synthetase (ASS1) gene, impact on patients, common changes, and structural considerations.
Diez-Fernandez C.; Ruefenacht V.; Haeberle J.;
Hum. Mutat. 38:471-484(2017)
Cited for: VARIANTS CTLN1 27-GLN--LYS-412 DEL; ILE-64; PRO-79; 97-CYS--LYS-412 DEL; CYS-100; HIS-100; ASP-111; CYS-117; 138-GLN--LYS-412 DEL; SER-157; PRO-160; 163-TYR--LYS-412 DEL; PRO-164; LYS-184; ASP-190; PRO-206; ARG-230; ILE-237; PRO-258; VAL-258; CYS-265; 275-GLY--LYS-412 DEL; THR-277; 279-ARG--LYS-412 DEL; ILE-284; PRO-290; SER-291; GLY-296; ASP-299; VAL-302; GLY-306; CYS-307; 311-GLN--LYS-412 DEL; MET-321; SER-324; VAL-324; HIS-335; PHE-341; 344-ARG--LYS-412 DEL; ARG-347; VAL-356; 357-GLN--LYS-412 DEL; ASP-359; 380-GLN--LYS-412 DEL AND PRO-389;

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.