Variant position: 383 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:
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 LKSDNILVELD-PDGCPWLVI ADFGCCLADESIGLQLPFSSW
Mouse LKSDNILVEWD-SDGCPWLVI SDFGCCLADQHVGLRLPFNS
Rat LKSDNILVEWD-SDGCPWLVI SDFGCCLADERVGLQLPFNS
Caenorhabditis elegans MKSDNILLEYDFDDEIPQLVV ADFGCALA--CDNWQVDYES
Drosophila LKSDNVLIELQ-DDAAPVLVL SDFGCCLADKVHGLRLPYVS
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.
Type Positions Description
78 – 581 Serine/threonine-protein kinase PINK1, mitochondrial
111 – 581 Cytoplasmic
156 – 511 Protein kinase
402 – 402 Phosphoserine; by autocatalysis
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.
384 – 384 D -> N. Loss of activity. Abolishes Drp1 phosphorylation. No effect on localization to mitochondria.
A heterozygous effect for PINK1 mutations in Parkinson's disease?
Abou-Sleiman P.M.; Muqit M.M.K.; McDonald N.Q.; Yang Y.X.; Gandhi S.; Healy D.G.; Harvey K.; Harvey R.J.; Deas E.; Bhatia K.; Quinn N.; Lees A.; Latchman D.S.; Wood N.W.;
Ann. Neurol. 60:414-419(2006)
Cited for: VARIANTS ILE-317; THR-339; THR-383; SER-411; HIS-431; SER-451; SER-461; LYS-476; PRO-501 AND ARG-575; CHARACTERIZATION OF VARIANTS HIS-431; SER-451; LYS-476; PRO-501 AND ARG-575;
PINK1 heterozygous rare variants: prevalence, significance and phenotypic spectrum.
Marongiu R.; Ferraris A.; Ialongo T.; Michiorri S.; Soleti F.; Ferrari F.; Elia A.E.; Ghezzi D.; Albanese A.; Altavista M.C.; Antonini A.; Barone P.; Brusa L.; Cortelli P.; Martinelli P.; Pellecchia M.T.; Pezzoli G.; Scaglione C.; Stanzione P.; Tinazzi M.; Zecchinelli A.; Zeviani M.; Cassetta E.; Garavaglia B.; Dallapiccola B.; Bentivoglio A.R.; Valente E.M.;
Hum. Mutat. 29:565-565(2008)
Cited for: VARIANTS PHE-67; PRO-68; TRP-98; SER-111; VAL-124; MET-145; ASN-186; ILE-257 VAL-268; GLN-276; LEU-296; ILE-317; LEU-322; THR-339; THR-383; VAL-395; THR-442; LYS-476; ASN-525 AND THR-537;
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.