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:
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 IPVTPKNPWSMDENLMHISY EAGILENPKNQAPPGLYTKTQ
Mouse IPVTPKSPWSMDENLMHISY EAGILENPKNQAPPGLYTKTQ
Rat IPVTPKSPWSMDENLMHISY EAGILENPKNQAPPGLYTKTQ
Bovine VPVTPKNPWSMDENLMHISY EAGILENPKNQAPPGLYTKTQ
Chicken VPVTPKAPWSMDENLMHISY EAGILENPKNRAPLDLYTKTC
Xenopus laevis VPVTPKSPWSMDENLMHISY EGGILENPKNHAPPGLYLKTK
Xenopus tropicalis VPVTPKDPWSMDENIMHISY EGGILENPKNHAPPGLYLKTK
Zebrafish VPVTPKAPWSMDANLMHISY ESGILENPKNHAPSDLYQMTK
Drosophila VSAKPATPWSTDANILHISY ESGILEDPNTVAPENLYEMTV
Baker's yeast VAQTKAKPWSTDENQAHISY EAGILEDPDTTPPKDMWKLIV
Fission yeast VTQTTKKPWSMDENIVHCSY EAGILEDPSMTPPKDMWKLTV
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
189 – 189 Citrulline
176 – 176 N6-acetyllysine; by CLOCK
180 – 180 Phosphoserine
176 – 176 K -> QR. Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-165 or R-165.
Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients.
Gao H.-Z.; Kobayashi K.; Tabata A.; Tsuge H.; Iijima M.; Yasuda T.; Kalkanoglu H.S.; Dursun A.; Tokatli A.; Coskun T.; Trefz F.K.; Skladal D.; Mandel H.; Seidel J.; Kodama S.; Shirane S.; Ichida T.; Makino S.; Yoshino M.; Kang J.-H.; Mizuguchi M.; Barshop B.A.; Fuchinoue S.; Seneca S.; Zeesman S.; Knerr I.; Rodes M.; Wasant P.; Yoshida I.; De Meirleir L.; Abdul-Jalil M.; Begum L.; Horiuchi M.; Katunuma N.; Nakagawa S.; Saheki T.;
Hum. Mutat. 22:24-34(2003)
Cited for: VARIANTS CTLN1 ARG-19; HIS-86; SER-95; SER-96; ASP-117; SER-117; CYS-157; ARG-179; LYS-191; HIS-265; MET-269; CYS-272; LYS-283; TRP-304; GLN-310; SER-324; VAL-362; GLN-363; TRP-363; ILE-389 AND ARG-390;
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.