Variant position: 160 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:
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 KVIAPWRMPEFYNRFKGRND LMEYAKQHGIPIPVTPKNPWS
Mouse KVIAPWRMPEFYNRFKGRND LMEYAKQHGIPIPVTPKSPWS
Rat KVIAPWRMPEFYNRFKGRND LMEYAKQHGIPIPVTPKSPWS
Bovine KVIAPWRMPEFYNRFQGRND LMEYAKQHGIPVPVTPKNPWS
Chicken KVIAPWRMPEFYQRFPGRRE LMEYAQKHGIPVPVTPKAPWS
Xenopus laevis KIIAPWRMPEFYNRFRGRSD LMEYAKKHNISVPVTPKSPWS
Xenopus tropicalis KIIAPWRMPEFYNRFRGRSD LMEYAKKHNIPVPVTPKDPWS
Zebrafish QVIAPWRIPEFYNRFRGRKD LMEYAEKHNIPVPVTPKAPWS
Drosophila KIIAPWRDVEFCCQFQGRQD LIAYAQQHGIEVSAKPATPWS
Baker's yeast KCITPWRMPEFFERFAGRKD LLDYAAQKGIPVAQTKAKPWS
Fission yeast QVIAPWRLPVFFERFAGRKD LLEYAAAKGIPVTQTTKKPWS
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
1 – 412 Argininosuccinate synthase
180 – 180 Citrulline
165 – 165 N6-acetyllysine; by CLOCK
176 – 176 N6-acetyllysine; by CLOCK
180 – 180 Phosphoserine
165 – 165 K -> QR. Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-176 or R-176.
176 – 176 K -> QR. Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-165 or R-165.
158 – 166
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;
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;
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.