Variant position: 259 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 296 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 NNTLFETDERYRHLGFSVDD LGCCKVIRHSLWGTHVVVGSI
Mouse NNTLFETDERYRHLGFSVDD LGCCKVIRHSLWGTHVVVGSI
Rat NNTLFETDERYRHLGFSVDD LGCCKVIRHGLWGTHVVVGSI
Chicken NNTLFETDERYRHFGFSVDD LGCCKVIRHNIWGTHVVVGSI
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
39 – 296 Methylmalonic aciduria and homocystinuria type D protein, mitochondrial
266 – 266 R -> A. Mildly decreases methylcobalamin levels and strongly increases adenosylcobalamin levels.
270 – 270 W -> A. Decreases methylcobalamin levels.
278 – 278 S -> A. Marginally decreases methylcobalamin levels and strongly increases adenosylcobalamin levels.
Gene identification for the cblD defect of vitamin B12 metabolism.
Coelho D.; Suormala T.; Stucki M.; Lerner-Ellis J.P.; Rosenblatt D.S.; Newbold R.F.; Baumgartner M.R.; Fowler B.;
N. Engl. J. Med. 358:1454-1464(2008)
Cited for: FUNCTION; TISSUE SPECIFICITY; VARIANTS MAHCD LEU-ALA-GLU-PRO-LEU-SER-108 INS; ASN-182; 204-PHE--ALA-232 DEL; CYS-249 AND PRO-259;
Characterization of functional domains of the cblD (MMADHC) gene product.
Jusufi J.; Suormala T.; Burda P.; Fowler B.; Froese D.S.; Baumgartner M.R.;
J. Inherit. Metab. Dis. 37:841-849(2014)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANT MAHCD PRO-259; MUTAGENESIS OF PHE-165; MET-186; TRP-189; ARG-197; PHE-204; CYS-212; ASP-226; TYR-237; ARG-266; TRP-270; SER-278 AND PHE-280;
Structural insights into the MMACHC-MMADHC protein complex involved in vitamin B12 trafficking.
Froese D.S.; Kopec J.; Fitzpatrick F.; Schuller M.; McCorvie T.J.; Chalk R.; Plessl T.; Fettelschoss V.; Fowler B.; Baumgartner M.R.; Yue W.W.;
J. Biol. Chem. 290:29167-29177(2015)
Cited for: INTERACTION WITH MMACHC; CHARACTERIZATION OF VARIANTS MAHCD ASN-182 AND PRO-259; MUTAGENESIS OF TRP-189 AND ASP-226;
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