Variant position: 387 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 750 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 IVRTAIEAMAAVFGGTQSLH TNSFDEALGLPTVKSARIARN
Mouse IVRTAIEAMAAVFGGTQSLH TNSFDEALGLPTVKSARIARN
Pig IIRTTVEAMAAVFGGTQSLH TNSFDEALGLPTVKSARIARN
Bovine IIRTTIEAMAAVFGGTQSLH TNSFDEALGLPTVKSARIARN
Caenorhabditis elegans IIRTTIEAMASVFGGTQSLH TNSFDEALGLPTKFSARIARN
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
33 – 750 Methylmalonyl-CoA mutase, mitochondrial
Microarray based mutational analysis of patients with methylmalonic acidemia: identification of 10 no vel mutations.
Duendar H.; Oezguel R.K.; Guezel-Ozantuerk A.; Dursun A.; Sivri S.; Aliefendioglu D.; Coskun T.; Tokatli A.;
Mol. Genet. Metab. 106:419-423(2012)
Cited for: VARIANTS MMAM GLY-137; TYR-219; SER-305; PHE-328; ILE-387; GLU-454; GLU-514; LEU-615; THR-615; VAL-625 AND PHE-674; VARIANTS THR-499; HIS-532 AND VAL-671;
Functional characterization and categorization of missense mutations that cause methylmalonyl-CoA mutase (MUT) deficiency.
Forny P.; Froese D.S.; Suormala T.; Yue W.W.; Baumgartner M.R.;
Hum. Mutat. 35:1449-1458(2014)
Cited for: CHARACTERIZATION OF VARIANTS MMAM LEU-86; CYS-100; GLU-191; HIS-218; TYR-219; ASN-231; CYS-316; PHE-328; PHE-344; SER-366; HIS-369; ILE-387; ARG-426; SER-573; LEU-615; THR-615; GLY-633; ASP-648; LEU-694; TRP-694; LYS-700; VAL-717 AND PHE-736; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES;
Spectrum of mutations in 60 Saudi patients with Mut methylmalonic acidemia.
Imtiaz F.; Al-Mubarak B.M.; Al-Mostafa A.; Al-Hamed M.; Allam R.; Al-Hassnan Z.; Al-Owain M.; Al-Zaidan H.; Rahbeeni Z.; Qari A.; Faqeih E.A.; Alasmari A.; Al-Mutairi F.; Alfadhel M.; Eyaid W.M.; Rashed M.S.; Al-Sayed M.;
JIMD Rep. 29:39-46(2016)
Cited for: VARIANTS MMAM HIS-93; CYS-108; CYS-110; SER-174; SER-215; SER-364; ILE-387; PRO-692 AND TRP-694;
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