Variant position: 145 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 418 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 KVLLYHREQEQSNKGKPLAF RVGLSGPPGAGKSTFIEYFGK
Mouse RVLALQREQELRNQGKPLTF RVGLSGPPGAGKSTFIECFGK
Rabbit KVLLFQREQEQPNKGNPLAF RLGLSGPPGAGKSTFIEYSGK
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
66 – 418 Methylmalonic aciduria type A protein, mitochondrial
144 – 149
Mutations in the MMAA gene in patients with the cblA disorder of vitamin B(12) metabolism.
Lerner-Ellis J.P.; Dobson C.M.; Wai T.; Watkins D.; Tirone J.C.; Leclerc D.; Dore C.; Lepage P.; Gravel R.A.; Rosenblatt D.S.;
Hum. Mutat. 24:509-516(2004)
Cited for: VARIANTS MMAA 22-ARG--ASP-418 DEL; 54-TRP--ASP-418 DEL; PRO-89; 129-TYR--ASP-418 DEL; 145-ARG--ASP-418 DEL; GLN-145; GLU-147; CYS-207; GLU-218; 248-GLN--ASP-418 DEL; 320-TRP--ASP-418 DEL; 330-ARG--ASP-418 DEL AND GLN-359; VARIANT HIS-363;
Protein destabilization and loss of protein-protein interaction are fundamental mechanisms in cblA-type methylmalonic aciduria.
Plessl T.; Buerer C.; Lutz S.; Yue W.W.; Baumgartner M.R.; Froese D.S.;
Hum. Mutat. 38:988-1001(2017)
Cited for: VARIANTS MMAA 24-TYR--ASP-418 DEL; 68-GLN--ASP-418 DEL; PRO-89; 95-GLN--ASP-418 DEL; GLY-98; 100-CYS--ALA-104 DEL; 145-ARG--ASP-418 DEL; GLN-145; GLU-147; ARG-188; ASP-192; 196-ARG--ASP-418 DEL; GLN-196; CYS-207; SER-209; GLU-218; MET-220; PHE-241; ASN-243; 248-GLN--ASP-418 DEL; LYS-250; ASN-258; SER-274; GLU-276; ASP-287; VAL-292; 330-ARG--ASP-418 DEL; 359-ARG--ASP-418 DEL; GLN-359; GLY-359 AND VAL-399; CHARACTERIZATION OF VARIANTS MMAA PRO-89; GLY-98; GLN-145; GLU-147; ARG-188; ASP-192; GLN-196; CYS-207; SER-209; GLU-218; MET-220; PHE-241; ASN-243; LYS-250; SER-274; GLU-276; ASP-287; VAL-292; GLN-359; GLY-359 AND VAL-399; FUNCTION; GTP-BINDING; MUTAGENESIS OF LYS-290 AND ASP-292; BIOPHYSICOCHEMICAL PROPERTIES; ACTIVITY REGULATION; CATALYTIC ACTIVITY; PATHWAY;
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