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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P48728: Variant p.Arg320His

Aminomethyltransferase, mitochondrial
Gene: AMT
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Variant information Variant position: help 320 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 Arginine (R) to Histidine (H) at position 320 (R320H, p.Arg320His). 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 Change from large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 GCE2; loss of aminomethyltransferase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 320 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 403 The length of the canonical sequence.
Location on the sequence: help MDFPGAKVIVPQLKGRVQRR R VGLMCEGAPMRAHSPILNME 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                         MD----FPGAKVIVPQLKGRV-QRRRVGLM--CEGAPMRAHSPILNME

                              MD----FPGASVIIAQLKGKV-QRRRVGLT--CEGAPVRAH

Mouse                         MD----FPGAKIIVPQLKGEV-QRRRVGLI--CEGAPVRAH

Bovine                        MD----FPGASVIVPQLKSKA-QRRRVGLM--CDGAPVRAQ

Chicken                       MD----FPGAAIIMEQVKEKP-KRKRVGLT--SVGPPLRPP

Slime mold                    GG----FPGASIIQKQLQKDGCPQKRVGVI--INGAPAREG

Baker's yeast                 VDQKYWFNGYAKIMDQLNNKTYSKVRVGFKYLKKGPAARNG

Fission yeast                 GG----FVGSSRILKELKDGP-SRRRVGFIV-EK-VPARHG
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 29 – 403 Aminomethyltransferase, mitochondrial
Beta strand 319 – 328



Literature citations
Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia.
Okamura-Ikeda K.; Hosaka H.; Yoshimura M.; Yamashita E.; Toma S.; Nakagawa A.; Fujiwara K.; Motokawa Y.; Taniguchi H.;
J. Mol. Biol. 351:1146-1159(2005)
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-403 ALONE AND IN COMPLEX WITH 5-METHYLTETRAHYDROFOLATE; SUBSTRATE-BINDING SITES; CATALYTIC ACTIVITY; FUNCTION; SUBUNIT; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS GCE2 ILE-145; ASP-269 AND HIS-320; MUTAGENESIS OF ASP-129; Identification of the mutations in the T-protein gene causing typical and atypical nonketotic hyperglycinemia.
Nanao K.; Okamura-Ikeda K.; Motokawa Y.; Danks D.M.; Baumgartner E.R.; Takada G.; Hayasaka K.;
Hum. Genet. 93:655-658(1994)
Cited for: VARIANTS GCE2 ARG-47; ASP-269 AND HIS-320; INVOLVEMENT IN GCE2; Biochemical and molecular investigations of patients with nonketotic hyperglycinemia.
Toone J.R.; Applegarth D.A.; Coulter-Mackie M.B.; James E.R.;
Mol. Genet. Metab. 70:116-121(2000)
Cited for: VARIANTS GCE2 LYS-211 AND HIS-320; Recurrent mutations in P- and T-proteins of the glycine cleavage complex and a novel T-protein mutation (N145I): a strategy for the molecular investigation of patients with nonketotic hyperglycinemia (NKH).
Toone J.R.; Applegarth D.A.; Coulter-Mackie M.B.; James E.R.;
Mol. Genet. Metab. 72:322-325(2001)
Cited for: VARIANTS GCE2 ILE-145 AND HIS-320;
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.