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UniProtKB/Swiss-Prot Q9BXM7: Variant p.Thr313Met

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

Variant position:  313
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 Threonine (T) to Methionine (M) at position 313 (T313M, p.Thr313Met).
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 medium size and polar (T) to medium size and hydrophobic (M)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In PARK6; decreases PRKN and SNCAIP ubiquitination and degradation; slightly decreases Drp1 phosphorylation.
Any additional useful information about the variant.

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



Sequence information

Variant position:  313
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  581
The length of the canonical sequence.

Location on the sequence:   VDYPDVLPSRLHPEGLGHGR  T LFLVMKNYPCTLRQYLCVNT
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                         VDYPDVL-PSRLHPEGLGHGRTLFLVMKNYPCTLRQYLCVNT

Mouse                         ADYPDML-PPHYYPEGLGHGRTLFLVMKNYPCTLRQYLEEQ

Rat                           ADYPDML-PPHYYPEGLGHGRTLFLVMKNYPCTLRQYLEEQ

Caenorhabditis elegans        ERYPDALHTARWYESIASEPKTMYVVMRRYRQTLHEYVWTR

Drosophila                    LLYPVAQ-PQRINPQGYGRNMSLYLLMKRYDHSLRGLLDSQ

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 78 – 581 Serine/threonine-protein kinase PINK1, mitochondrial
Topological domain 111 – 581 Cytoplasmic
Domain 156 – 511 Protein kinase
Alternative sequence 308 – 320 LGHGRTLFLVMKN -> MCGSQRPSPLSTS. In isoform 2.


Literature citations

Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation.
Xiong H.; Wang D.; Chen L.; Choo Y.S.; Ma H.; Tang C.; Xia K.; Jiang W.; Ronai Z.; Zhuang X.; Zhang Z.;
J. Clin. Invest. 119:650-660(2009)
Cited for: FUNCTION; COMPONENT OF A COMPLEX COMPOSED OF PRKN; PARK7 AND PINK1; SUBCELLULAR LOCATION; PROTEOLYTIC CLEAVAGE; CHARACTERIZATION OF VARIANTS PARK6 ASP-309 AND MET-313; CHARACTERIZATION OF VARIANT LEU-399;

PINK1 phosphorylates Drp1S616 to regulate mitophagy-independent mitochondrial dynamics.
Han H.; Tan J.; Wang R.; Wan H.; He Y.; Yan X.; Guo J.; Gao Q.; Li J.; Shang S.; Chen F.; Tian R.; Liu W.; Liao L.; Tang B.; Zhang Z.;
EMBO Rep. 21:48686-48686(2020)
Cited for: FUNCTION; CATALYTIC ACTIVITY; MUTAGENESIS OF GLY-309 AND ASP-384; CHARACTERIZATION OF VARIANTS ASP-309; MET-313 AND 492-ARG--LYS-581 DEL;

T313M PINK1 mutation in an extended highly consanguineous Saudi family with early-onset Parkinson disease.
Chishti M.A.; Bohlega S.; Ahmed M.; Loualich A.; Carroll P.; Sato C.; St George-Hyslop P.; Westaway D.; Rogaeva E.;
Arch. Neurol. 63:1483-1485(2006)
Cited for: VARIANT PARK6 MET-313;

Mutation analysis of Parkin, PINK1, DJ-1 and ATP13A2 genes in Chinese patients with autosomal recessive early-onset Parkinsonism.
Guo J.F.; Xiao B.; Liao B.; Zhang X.W.; Nie L.L.; Zhang Y.H.; Shen L.; Jiang H.; Xia K.; Pan Q.; Yan X.X.; Tang B.S.;
Mov. Disord. 23:2074-2079(2008)
Cited for: VARIANTS PARK6 MET-313 AND 492-ARG--LYS-581 DEL;

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.