Sequence information
Variant position: 359 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:
WDKMKDFQDLMLASGELTAK
R RKQQKVWMWNLIQESVLEHF
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 WDKMKDFQDLMLASGELTAKR RKQQKVWMWNLIQES--VLEHF
Mouse WDTMREFQHQMLASGELAAKR QTQHKVWMWNLIQEN--VLE
Rabbit WNVGYDARILGPNTCQRGAAC QTTKATESLDVEPHSGKRVR
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
Chain
66 – 418
Methylmalonic aciduria type A protein, mitochondrial
Helix
354 – 381
Literature citations
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;
High resolution melting analysis of the MMAA gene in patients with cblA and in those with undiagnosed methylmalonic aciduria.
Dempsey-Nunez L.; Illson M.L.; Kent J.; Huang Q.; Brebner A.; Watkins D.; Gilfix B.M.; Wittwer C.T.; Rosenblatt D.S.;
Mol. Genet. Metab. 107:363-367(2012)
Cited for: VARIANTS MMAA SER-209; LYS-250; ASP-274; SER-274; GLU-276 AND GLN-359;
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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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.