Sequence information
Variant position: 188 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:
TERGHKLSVLAVDPSSCTSG
G SLLGDKTRMTELSRDMNAYI
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 TERGHKLSVLAVDPSSCTSGG SLLGDKTRMTELSRDMNAYI
Mouse TEQGHRLSVLAVDPSSCTSGG SLLGDKTRMIELSRDMNAYI
Rabbit TERGHKLSVLAVGPSSCNSGG SLLGDKTRMTEFSRDMNAYI
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
Literature citations
Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation.
Froese D.S.; Kochan G.; Muniz J.R.; Wu X.; Gileadi C.; Ugochukwu E.; Krysztofinska E.; Gravel R.A.; Oppermann U.; Yue W.W.;
J. Biol. Chem. 285:38204-38213(2010)
Cited for: X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 72-418 IN COMPLEX WITH GDP; SUBUNIT; BIOPHYSICOCHEMICAL PROPERTIES; INTERACTION WITH MMUT; FUNCTION; CHARACTERIZATION OF VARIANT MMAA ARG-188; ACTIVITY REGULATION; CATALYTIC ACTIVITY; PATHWAY; GTP-BINDING;
Methylmalonic acidaemia: examination of genotype and biochemical data in 32 patients belonging to mut, cblA or cblB complementation group.
Merinero B.; Perez B.; Perez-Cerda C.; Rincon A.; Desviat L.R.; Martinez M.A.; Sala P.R.; Garcia M.J.; Aldamiz-Echevarria L.; Campos J.; Cornejo V.; Del Toro M.; Mahfoud A.; Martinez-Pardo M.; Parini R.; Pedron C.; Pena-Quintana L.; Perez M.; Pourfarzam M.; Ugarte M.;
J. Inherit. Metab. Dis. 31:55-66(2008)
Cited for: VARIANTS MMAA 22-ARG--ASP-418 DEL; 120-GLN--ASP-418 DEL; 133-GLN--ASP-418 DEL; 145-ARG--ASP-418 DEL AND ARG-188;
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;
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.