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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y4W6: Variant p.Arg468Cys

AFG3-like protein 2
Gene: AFG3L2
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Variant information Variant position: help 468 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 Arginine (R) to Cysteine (C) at position 468 (R468C, p.Arg468Cys). 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 large size and basic (R) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 OPA12; decreased proteolytic function resulting in impaired autocatalytic processing and impaired proteolytic maturation of SPG7; does not affect the interaction with SPG7. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 468 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 797 The length of the canonical sequence.
Location on the sequence: help VILAGTNRPDILDPALLRPG R FDRQIFIGPPDIKGRASIFK 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                         VILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFK

Mouse                         VILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFK

Bovine                        VILAGTNRPDILDPALMRPGRFDRQIFIGPPDIKGRASIFK
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 67 – 797 AFG3-like protein 2



Literature citations
A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability.
Charif M.; Roubertie A.; Salime S.; Mamouni S.; Goizet C.; Hamel C.P.; Lenaers G.;
Front. Genet. 6:311-311(2015)
Cited for: VARIANT OPA12 CYS-468; INVOLVEMENT IN OPA12; Non-syndromic isolated dominant optic atrophy caused by the p.R468C mutation in the AFG3 like matrix AAA peptidase subunit 2 gene.
Colavito D.; Maritan V.; Suppiej A.; Del Giudice E.; Mazzarolo M.; Miotto S.; Farina S.; Dalle Carbonare M.; Piermarocchi S.; Leon A.;
Biomed. Rep. 7:451-454(2017)
Cited for: VARIANT OPA12 CYS-468; INVOLVEMENT IN OPA12; Concurrent AFG3L2 and SPG7 mutations associated with syndromic parkinsonism and optic atrophy with aberrant OPA1 processing and mitochondrial network fragmentation.
Magri S.; Fracasso V.; Plumari M.; Alfei E.; Ghezzi D.; Gellera C.; Rusmini P.; Poletti A.; Di Bella D.; Elia A.E.; Pantaleoni C.; Taroni F.;
Hum. Mutat. 39:2060-2071(2018)
Cited for: VARIANT OPA12 CYS-468; CHARACTERIZATION OF VARIANT OPA12 CYS-468; CHARACTERIZATION OF VARIANT SCA28 LYS-691; MUTAGENESIS OF GLU-575; FUNCTION; INTERACTION WITH SPG7;
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.