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UniProtKB/Swiss-Prot P46597: Variant p.Val171Met

Acetylserotonin O-methyltransferase
Gene: ASMT
Variant information

Variant position:  171
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LB/B
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:  From Valine (V) to Methionine (M) at position 171 (V171M, p.Val171Met).
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:  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:  1
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:  Nearly abolishes enzyme activity.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  171
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  345
The length of the canonical sequence.

Location on the sequence:   GERLQFMQALQEVWSVNGRS  V LTAFDLSVFPLMCDLGGGAG
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                         GERLQFMQALQEVWSVNGRSVLTAFDLSVFPLMCDLGGGAG

Rhesus macaque                GERLQFMQALQEVWSVNGRSVLTAFDLSGFPLMCDLGGGPG

Mouse                         AERLLFMRGLQETWSLCGGRVLTAFDLSPFRVICDLGGGSG

Rat                           PERLLFMRGLQETWSLCGGRVLTAFDLSRFRVICDLGGGSG

Bovine                        DERLQFMQGLQDVWRLEGATVLAAFDLSPFPLICDLGGGSG

Chicken                       EEMLKFLAGQNSIWSICGRDVLTAFDLSPFTQIYDLGGGGG

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.

TypePositionsDescription
Chain 1 – 345 Acetylserotonin O-methyltransferase
Binding site 164 – 164 S-adenosyl-L-methionine
Alternative sequence 188 – 188 G -> GTWIKLETIILSKLSQGQKTKHRVFSLIG. In isoform 3.
Helix 164 – 173


Literature citations

Crystal structure and functional mapping of human ASMT, the last enzyme of the melatonin synthesis pathway.
Botros H.G.; Legrand P.; Pagan C.; Bondet V.; Weber P.; Ben-Abdallah M.; Lemiere N.; Huguet G.; Bellalou J.; Maronde E.; Beguin P.; Haouz A.; Shepard W.; Bourgeron T.;
J. Pineal Res. 54:46-57(2013)
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH S-ADENOSYL-L-METHIONINE; N-ACETYL SEROTONIN AND ZINC IONS; CATALYTIC ACTIVITY; FUNCTION; ACTIVE SITE; CHARACTERIZATION OF ISOFORMS 1; 2 AND 3; SUBUNIT; TISSUE SPECIFICITY; CHARACTERIZATION OF VARIANTS HIS-13; LYS-17; GLN-61; GLU-81; MET-171; GLY-210; ARG-219; LEU-243; MET-269; SER-273; ALA-278; ASP-288; GLN-291; PHE-298 AND MET-305; MUTAGENESIS OF LEU-11; ARG-111; TYR-248; THR-296 AND HIS-318;

Mutation screening of ASMT, the last enzyme of the melatonin pathway, in a large sample of patients with intellectual disability.
Pagan C.; Botros H.G.; Poirier K.; Dumaine A.; Jamain S.; Moreno S.; de Brouwer A.; Van Esch H.; Delorme R.; Launay J.M.; Tzschach A.; Kalscheuer V.; Lacombe D.; Briault S.; Laumonnier F.; Raynaud M.; van Bon B.W.; Willemsen M.H.; Leboyer M.; Chelly J.; Bourgeron T.;
BMC Med. Genet. 12:17-17(2011)
Cited for: VARIANTS HIS-13; LYS-17; GLN-61; MET-171; GLY-210; ARG-219; LEU-243; SER-273; ASP-288; GLN-291 AND PHE-298;

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.