Variant position: 50 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 236 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 ADTHLRILGKPVMERWETPY MHALAAAASSKGGRVLEVGFG
Mouse SDTHLQILGKPVMERWETPY MHALAAAAASRGGRVLEVGFG
Rat SDTHLQILGKPVMERWETPY MHSLAAAAASRGGRVLEVGFG
Bovine SDTHLQILGKPVMERWETPY MHALAAAAASRGGRVLEVGFG
Xenopus tropicalis TDTHLEILGKPVMERWETPY MHSLASVAASKGGRVLEIGFG
Zebrafish ADTHLEIMGKPVMERWETPY MHSLATVAASKGGRVLEIGFG
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
2 – 236 Guanidinoacetate N-methyltransferase
13 – 236 RMT2
42 – 42 Guanidinoacetate
46 – 46 Guanidinoacetate
50 – 50 S-adenosyl-L-methionine
47 – 57
High frequency of creatine deficiency syndromes in patients with unexplained mental retardation.
Lion-Francois L.; Cheillan D.; Pitelet G.; Acquaviva-Bourdain C.; Bussy G.; Cotton F.; Guibaud L.; Gerard D.; Rivier C.; Vianey-Saban C.; Jakobs C.; Salomons G.S.; des Portes V.;
Cited for: VARIANT CCDS2 LEU-50;
Thirteen new patients with guanidinoacetate methyltransferase deficiency and functional characterization of nineteen novel missense variants in the GAMT gene.
Mercimek-Mahmutoglu S.; Ndika J.; Kanhai W.; de Villemeur T.B.; Cheillan D.; Christensen E.; Dorison N.; Hannig V.; Hendriks Y.; Hofstede F.C.; Lion-Francois L.; Lund A.M.; Mundy H.; Pitelet G.; Raspall-Chaure M.; Scott-Schwoerer J.A.; Szakszon K.; Valayannopoulos V.; Williams M.; Salomons G.S.;
Hum. Mutat. 35:462-469(2014)
Cited for: VARIANTS CCDS2 CYS-68; VAL-75; PHE-110; TYR-147; PRO-159 AND PRO-208; VARIANTS THR-8 AND HIS-27; CHARACTERIZATION OF VARIANTS CCDS2 ARG-45; LEU-50; PRO-51; PRO-54; CYS-68; VAL-75; PHE-110; TYR-147; PRO-159; PRO-166; TYR-169; PRO-197 AND PRO-208; CHARACTERIZATION OF VARIANTS THR-8 AND HIS-27; FUNCTION;
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.