Variant position: 234 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 423 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 PKPTMADELYNQDYPIHSVE DRHKLAAQGKFVTTEFEPCFD
Mouse PKPTMADELYDQNYPIHSVE DRHKLAAQGKFVTTEFEPCFD
Rat PKPTMADELYDQDYPIHSVE DRHKLAAQGKFVTTEFEPCFD
Pig PKPTMADELYDQDYPIYSVE DRHKLAAQGKFVTTEFEPCFD
Bovine PKPTMADELYDQDYPIHSVE DRHKLAAQGKFVTTEFEPCFD
Chicken PKPTMADELYDQDYPIRSVE DRHKLAAQGKFVTTEFEPCFD
Xenopus laevis PKPTMADELYDQDYPIRTVE DRHKLAAMGKFVTTEFEPCFD
Xenopus tropicalis PKPTMADELYDQDYPIRTVE DRHKLAAMGKFVTTEFEPCFD
Zebrafish PKPTMADQLYDQDYPIRTVE DRHKLAAQGKFVTTEFEPCFD
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
38 – 423 Glycine amidinotransferase, mitochondrial
254 – 254
233 – 233 E -> K. Complete loss of activity; when associated with S-407.
254 – 254 D -> N. Significantly reduced activity.
232 – 240
Arginine-Glycine Amidinotransferase Deficiency and Functional Characterization of Missense Variants in GATM.
DesRoches C.L.; Bruun T.; Wang P.; Marshall C.R.; Mercimek-Mahmutoglu S.;
Hum. Mutat. 37:926-932(2016)
Cited for: VARIANTS CCDS3 GLN-23; VAL-93; ASN-102; LEU-105; LYS-181; PRO-185; CYS-189; SER-203; THR-208; HIS-282; VAL-329; LEU-346; TRP-413; GLN-413 AND GLN-415; CHARACTERIZATION OF VARIANTS CCDS3 GLN-23; VAL-93; ASN-102; LEU-105; LYS-181; PRO-185; CYS-189; SER-203; THR-208; HIS-282; VAL-329; LEU-346; TRP-413; GLN-413 AND GLN-415; VARIANTS CYS-231 AND GLY-234; CHARACTERIZATION OF VARIANTS CYS-231 AND GLY-234; CATALYTIC ACTIVITY;
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.