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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q14749: Variant p.His177Asn

Glycine N-methyltransferase
Gene: GNMT
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Variant information Variant position: help 177 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 Histidine (H) to Asparagine (N) at position 177 (H177N, p.His177Asn). 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 polar. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In GNMT deficiency; 75% wild-type glycine N-methyltransferase activity, decreases stability of the tetramer. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 177 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 295 The length of the canonical sequence.
Location on the sequence: help RLALKNIASMVRAGGLLVID H RNYDHILSTGCAPPGKNIYY 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                         RLALKNIASMVRAGGLLVIDHRNYDHILSTGCAPPGKNIYY

Mouse                         RLALKNIASMVRPGGLLVIDHRNYDYILSTGCAPPGKNIYY

Rat                           RLALKNIASMVRPGGLLVIDHRNYDYILSTGCAPPGKNIYY

Pig                           RLALKNITSMVRSGGLLVIDHRNYDHILSTGCAPPGKNIYY

Rabbit                        RQALKNIASMVRTGGLLVIDHRNYDHILSTGCAPPGKNIYY
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 – 295 Glycine N-methyltransferase
Binding site 178 – 178
Modified residue 193 – 193 N6-succinyllysine
Beta strand 167 – 178



Literature citations
Destabilization of human glycine N-methyltransferase by H176N mutation.
Luka Z.; Pakhomova S.; Luka Y.; Newcomer M.E.; Wagner C.;
Protein Sci. 16:1957-1964(2007)
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-294; SUBUNIT; FUNCTION; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANT GNMT DEFICIENCY ASN-177; Mutations in human glycine N-methyltransferase give insights into its role in methionine metabolism.
Luka Z.; Cerone R.; Phillips J.A. III; Mudd S.H.; Wagner C.;
Hum. Genet. 110:68-74(2002)
Cited for: VARIANTS GNMT DEFICIENCY PRO-50 AND ASN-177; Effect of naturally occurring mutations in human glycine N-methyltransferase on activity and conformation.
Luka Z.; Wagner C.;
Biochem. Biophys. Res. Commun. 312:1067-1072(2003)
Cited for: CHARACTERIZATION OF VARIANTS GNMT DEFICIENCY PRO-50; SER-141 AND ASN-177; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES;
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.