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UniProtKB/Swiss-Prot P22033: Variant p.Gly215Ser

Methylmalonyl-CoA mutase, mitochondrial
Gene: MMUT
Variant information

Variant position:  215
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Glycine (G) to Serine (S) at position 215 (G215S, p.Gly215Ser).
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:  Change from glycine (G) to small size and polar (S)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  0
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:  In MMAM; mut0.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  215
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:   VLANFIVTGEEQGVPKEKLT  G TIQNDILKEFMVRNTYIFPP
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                         VLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPP

Mouse                         VLATFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPP

Pig                           VLATFIVSGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPP

Bovine                        VLATFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPP

Caenorhabditis elegans        VLAMYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPP

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.

TypePositionsDescription
Chain 33 – 750 Methylmalonyl-CoA mutase, mitochondrial
Binding site 228 – 228 malonyl-CoA
Modified residue 212 – 212 N6-acetyllysine
Beta strand 214 – 217


Literature citations

Molecular basis of methylmalonyl-CoA mutase apoenzyme defect in 40 European patients affected by mut(o) and mut- forms of methylmalonic acidemia: identification of 29 novel mutations in the MUT gene.
Acquaviva C.; Benoist J.-F.; Pereira S.; Callebaut I.; Koskas T.; Porquet D.; Elion J.;
Hum. Mutat. 25:167-176(2005)
Cited for: VARIANTS MMAM HIS-108; LEU-148; ASN-156; VAL-158; GLU-191; ARG-203; SER-215; TYR-219; ASN-262; PRO-293; PHE-328; CYS-587; THR-615; ASN-621; ARG-623; ARG-624; ARG-627; GLU-637; ILE-638; TYR-640; ARG-642; TRP-694 AND LYS-700;

Spectrum of mutations in mut methylmalonic acidemia and identification of a common Hispanic mutation and haplotype.
Worgan L.C.; Niles K.; Tirone J.C.; Hofmann A.; Verner A.; Sammak A.; Kucic T.; Lepage P.; Rosenblatt D.S.;
Hum. Mutat. 27:31-43(2006)
Cited for: VARIANTS MMAM LEU-86; GLU-87; HIS-93; ARG-94; VAL-94; ARG-95; ARG-105; CYS-108; GLY-108; HIS-108; SER-145; SER-174; VAL-186; LYS-189; GLU-191; GLU-197; ARG-203; CYS-215; SER-215; HIS-218; TYR-219; GLN-228; ILE-230; ASN-231; ASN-262; TYR-265; SER-281; GLU-291; SER-305; PHE-306; VAL-312; CYS-316; THR-324; LEU-346 DEL; ARG-347; TYR-350; CYS-369; HIS-369; PRO-370; GLU-377; HIS-383; PRO-383; ARG-386; ASN-386; HIS-388; SER-389 DEL; ILE-412 DEL; ARG-426; ASP-427; PRO-518; TYR-560; ARG-566; SER-573; ARG-615; CYS-616; ARG-623; GLU-630; GLY-633; ARG-637; ARG-642; ARG-678; ARG-685; TRP-694; LYS-700; ARG-703 AND VAL-717; VARIANTS VAL-69; THR-499; HIS-532 AND VAL-671;

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.