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UniProtKB/Swiss-Prot Q9BXM7: Variant p.Gly386Ala

Serine/threonine-protein kinase PINK1, mitochondrial
Gene: PINK1
Variant information

Variant position:  386
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 Alanine (A) at position 386 (G386A, p.Gly386Ala).
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 hydrophobic (A)
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 PARK6; abolishes kinase activity.
Any additional useful information about the variant.

Sequence information

Variant position:  386
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  581
The length of the canonical 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.






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.

Chain 78 – 581 Serine/threonine-protein kinase PINK1, mitochondrial
Topological domain 111 – 581 Cytoplasmic
Domain 156 – 511 Protein kinase
Modified residue 402 – 402 Phosphoserine; by autocatalysis
Mutagenesis 384 – 384 D -> A. Abolishes MFN2 phosphorylation and interaction with PRKN; when associated with A-219 and A-362. Loss of enzyme activity and impaired localization of PRKN to mitochondria; when associated with M-219 and A-362.
Mutagenesis 384 – 384 D -> N. Loss of activity. Abolishes Drp1 phosphorylation. No effect on localization to mitochondria.

Literature citations

Ubiquitin is phosphorylated by PINK1 to activate parkin.
Koyano F.; Okatsu K.; Kosako H.; Tamura Y.; Go E.; Kimura M.; Kimura Y.; Tsuchiya H.; Yoshihara H.; Hirokawa T.; Endo T.; Fon E.A.; Trempe J.F.; Saeki Y.; Tanaka K.; Matsuda N.;
Nature 510:162-166(2014)

Mutational analysis of the PINK1 gene in early-onset parkinsonism in Europe and North Africa.
Ibanez P.; Lesage S.; Lohmann E.; Thobois S.; De Michele G.; Borg M.; Agid Y.; Durr A.; Brice A.;
Brain 129:686-694(2006)
Cited for: VARIANTS PARK6 GLY-125; LYS-240; PRO-369; ALA-386 AND VAL-409;

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.