Variant position: 157 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 PQIKVIAPWRMPEFYNRFKG RNDLMEYAKQHGIPIPVTPKN
Mouse PQIKVIAPWRMPEFYNRFKG RNDLMEYAKQHGIPIPVTPKS
Rat PQIKVIAPWRMPEFYNRFKG RNDLMEYAKQHGIPIPVTPKS
Bovine PQIKVIAPWRMPEFYNRFQG RNDLMEYAKQHGIPVPVTPKN
Chicken PSIKVIAPWRMPEFYQRFPG RRELMEYAQKHGIPVPVTPKA
Xenopus laevis PEVKIIAPWRMPEFYNRFRG RSDLMEYAKKHNISVPVTPKS
Xenopus tropicalis PEVKIIAPWRMPEFYNRFRG RSDLMEYAKKHNIPVPVTPKD
Zebrafish PQVQVIAPWRIPEFYNRFRG RKDLMEYAEKHNIPVPVTPKA
Drosophila PDLKIIAPWRDVEFCCQFQG RQDLIAYAQQHGIEVSAKPAT
Baker's yeast PDVKCITPWRMPEFFERFAG RKDLLDYAAQKGIPVAQTKAK
Fission yeast PDVQVIAPWRLPVFFERFAG RKDLLEYAAAKGIPVTQTTKK
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
165 – 165 N6-acetyllysine; by CLOCK
176 – 176 N6-acetyllysine; by CLOCK
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.
Heterogeneity of mutations in argininosuccinate synthetase causing human citrullinemia.
Kobayashi K.; Jackson M.J.; Tick D.B.; O'Brien W.E.; Beaudet A.L.;
J. Biol. Chem. 265:11361-11367(1990)
Cited for: INVOLVEMENT IN CTLN1; VARIANTS CTLN1 SER-14; HIS-157; ASN-180; TRP-304; SER-324; TRP-363 AND ARG-390;
Prenatal diagnosis of citrullinemia and argininosuccinic aciduria: evidence for a transmission ratio distortion in citrullinemia.
Kleijer W.J.; Garritsen V.H.; van der Sterre M.L.; Berning C.; Haeberle J.; Huijmans J.G.M.;
Prenat. Diagn. 26:242-247(2006)
Cited for: VARIANTS CTLN1 ASN-124; HIS-157; GLN-270; GLN-279; LYS-283; SER-324; GLY-363 AND ARG-390;
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;
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.