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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P22033: Variant p.Thr387Ile

Methylmalonyl-CoA mutase, mitochondrial
Gene: MMUT
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Variant information Variant position: help 387 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Threonine (T) to Isoleucine (I) at position 387 (T387I, p.Thr387Ile). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and polar (T) to medium size and hydrophobic (I) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. Any additional useful information about the variant.


Sequence information Variant position: help 387 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 750 The length of the canonical sequence.
Location on the sequence: help IVRTAIEAMAAVFGGTQSLH T NSFDEALGLPTVKSARIARN 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         IVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARN

Mouse                         IVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARN

Pig                           IIRTTVEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARN

Bovine                        IIRTTIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARN

Caenorhabditis elegans        IIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARN
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 33 – 750 Methylmalonyl-CoA mutase, mitochondrial



Literature citations
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;
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.