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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9HCC0: Variant p.Ala218Val

Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
Gene: MCCC2
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Variant information Variant position: help 218 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 Alanine (A) to Valine (V) at position 218 (A218V, p.Ala218Val). 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 small size and hydrophobic (A) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In MCC2D. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 218 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 563 The length of the canonical sequence.
Location on the sequence: help QAIMSSKNIAQIAVVMGSCT A GGAYVPAMADENIIVRKQGT 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                         QAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGT

Mouse                         QAIMSSKNITQIAVVMGSCTAGGAYVPAMADENIIVQKQGT

Rat                           QAIMSSKNITQIAVVMGSCTAGGAYVPAMADENIIVQRQGT

Caenorhabditis elegans        QATMSSEGIPQLAVVMGSCTAGGAYVPAMSDQAIIVKGTGT

Drosophila                    QANMSAQGIPQIAVVMGSCTAGGAYVPAMADESIIVKKQGT

Slime mold                    QANMSAKRIPQIAVVMGSCTAGGAYVPAMADESVIVKGTGT
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 23 – 563 Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
Domain 49 – 306 CoA carboxyltransferase N-terminal
Region 49 – 555 Carboxyltransferase
Alternative sequence 209 – 246 Missing. In isoform 2.



Literature citations
Novel mutations in five Japanese patients with 3-methylcrotonyl-CoA carboxylase deficiency.
Uematsu M.; Sakamoto O.; Sugawara N.; Kumagai N.; Morimoto T.; Yamaguchi S.; Hasegawa Y.; Kobayashi H.; Ihara K.; Yoshino M.; Watanabe Y.; Inokuchi T.; Yokoyama T.; Kiwaki K.; Nakamura K.; Endo F.; Tsuchiya S.; Ohura T.;
J. Hum. Genet. 52:1040-1043(2007)
Cited for: VARIANTS MCC2D ARG-190; VAL-218 AND TYR-280; A single mutation in MCCC1 or MCCC2 as a potential cause of positive screening for 3-methylcrotonyl-CoA carboxylase deficiency.
Morscher R.J.; Grunert S.C.; Burer C.; Burda P.; Suormala T.; Fowler B.; Baumgartner M.R.;
Mol. Genet. Metab. 105:602-606(2012)
Cited for: VARIANTS MCC2D VAL-218; MET-339 AND GLY-523; 3-methylcrotonyl-CoA carboxylase deficiency: clinical, biochemical, enzymatic and molecular studies in 88 individuals.
Gruenert S.C.; Stucki M.; Morscher R.J.; Suormala T.; Buerer C.; Burda P.; Christensen E.; Ficicioglu C.; Herwig J.; Koelker S.; Moeslinger D.; Pasquini E.; Santer R.; Schwab K.O.; Wilcken B.; Fowler B.; Yue W.W.; Baumgartner M.R.;
Orphanet J. Rare Dis. 7:31-54(2012)
Cited for: VARIANTS MCC2D PHE-39; GLN-99; PHE-101; GLY-118 DEL; PHE-131; ASN-146; THR-152; TRP-155; ARG-167; ASP-169; LEU-173; ARG-190; TYR-190; CYS-193; HIS-193; ASN-200; THR-218; VAL-218; GLU-220; LEU-224; ASP-237; LEU-266; TYR-280; ARG-282; ARG-310; MET-339; VAL-340; ARG-352; PHE-355; PHE-375; THR-403; LEU-434; VAL-456; ARG-475; ARG-477; ARG-517; SER-520; GLY-523 AND GLU-555; CHARACTERIZATION OF VARIANTS MCC2D PHE-39; GLY-118 DEL; ASN-146; ARG-282; LEU-434; VAL-456; ARG-475 AND GLY-523;
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.