Variant position: 145 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 403 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 GILDDLIVTNT-SEGHLYVVS NAGCWEKDLALMQDKVRELQ--N
Mouse GILDDLIVSNT-SEGHLYVVS NAGCRDKDLALMQDKVKEFQ
Bovine GILDDLIVTSA-SEGHLYVVS NAGCREKDLTLMQDKVRELQ
Chicken DIVDDLIVTNT-AEDHLYVVS NAGCADKDRAVMEGRAAELR
Slime mold GIIDDTMITN--AGDSLYVVV NAGCADKDISHINEKIKEFK
Baker's yeast GVVDDTIITKENDDNEFYIVT NAGCAERDTEFFHDELQNGS
Fission yeast GIIDDTIISKQ-DENTYYIVT NAACSEKDEANLKKHIENWK
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
29 – 403 Aminomethyltransferase, mitochondrial
113 – 156 Missing. In isoform 3.
129 – 129 D -> AN. Loss of aminomethyltransferase activity.
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 NKH ILE-145; ASP-269 AND HIS-320; MUTAGENESIS OF ASP-129;
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 NKH ILE-145 AND HIS-320;
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