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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q14353: Variant p.Met50Leu

Guanidinoacetate N-methyltransferase
Gene: GAMT
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Variant information Variant position: help 50 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Methionine (M) to Leucine (L) at position 50 (M50L, p.Met50Leu). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 2 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In CCDS2; retains no significant activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 50 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 236 The length of the canonical sequence.
Location on the sequence: help ADTHLRILGKPVMERWETPY M HALAAAASSKGGRVLEVGFG 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         ADTHLRILGKPVMERWETPYMHALAAAASSKGGRVLEVGFG

Mouse                         SDTHLQILGKPVMERWETPYMHALAAAAASRGGRVLEVGFG

Rat                           SDTHLQILGKPVMERWETPYMHSLAAAAASRGGRVLEVGFG

Bovine                        SDTHLQILGKPVMERWETPYMHALAAAAASRGGRVLEVGFG

Xenopus tropicalis            TDTHLEILGKPVMERWETPYMHSLASVAASKGGRVLEIGFG

Zebrafish                     ADTHLEIMGKPVMERWETPYMHSLATVAASKGGRVLEIGFG
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 2 – 236 Guanidinoacetate N-methyltransferase
Domain 13 – 236 RMT2
Binding site 42 – 42
Binding site 46 – 46
Binding site 50 – 50
Helix 47 – 57



Literature citations
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.;
Neurology 67:1713-1714(2006)
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;
Disclaimer: 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.