Variant position: 82 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 465 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 DQQSIVHIVQRPWRKGQEMN ATGGDDPRNAAGGCEREPQSL
Mouse EQQSIVHIVQRPRRRSHETN ASGGDEPQSTSEGSIWESRSL
Rat EQQSIVHIVQRPQRKSHETN ASGGDKPQSTPEGSIWEPRSL
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
1 – 465 E3 ubiquitin-protein ligase parkin
77 – 237 Necessary for PINK1-dependent localization to mitochondria
65 – 65 Phosphoserine; by PINK1
1 – 191 Missing. In isoform 4.
58 – 206 Missing. In isoform 6.
65 – 65 S -> A. Loss of phosphorylation. Undergoes autoubiquitination in the presence of phosphorylated ubiquitin.
65 – 65 S -> E. Phosphomimetic mutant; still requires PINK1 for activation. PRKN is activated in presence of phosphorylated ubiquitin.
The importance of gene dosage studies: mutational analysis of the parkin gene in early-onset parkinsonism.
Hedrich K.; Kann M.; Lanthaler A.J.; Dalski A.; Eskelson C.; Landt O.; Schwinger E.; Vieregge P.; Lang A.E.; Breakefield X.O.; Ozelius L.J.; Pramstaller P.P.; Klein C.;
Hum. Mol. Genet. 10:1649-1656(2001)
Cited for: VARIANT PARK2 GLU-82;
Complex relationship between parkin mutations and Parkinson disease.
West A.; Periquet M.; Lincoln S.; Luecking C.B.; Nicholl D.; Bonifati V.; Rawal N.; Gasser T.; Lohmann E.; Deleuze J.-F.; Maraganore D.; Levey A.; Wood N.W.; Duerr A.; Hardy J.; Brice A.; Farrer M.;
Am. J. Med. Genet. 114:584-591(2002)
Cited for: VARIANTS PARK2 GLU-82; CYS-256; TRP-275; GLU-328 AND ARG-441;
Parkin mutations and susceptibility alleles in late-onset Parkinson's disease.
Oliveira S.A.; Scott W.K.; Martin E.R.; Nance M.A.; Watts R.L.; Hubble J.P.; Koller W.C.; Pahwa R.; Stern M.B.; Hiner B.C.; Ondo W.G.; Allen F.H. Jr.; Scott B.L.; Goetz C.G.; Small G.W.; Mastaglia F.; Stajich J.M.; Zhang F.; Booze M.W.; Winn M.P.; Middleton L.T.; Haines J.L.; Pericak-Vance M.A.; Vance J.M.;
Ann. Neurol. 53:624-629(2003)
Cited for: VARIANTS PARK2 GLN-33; GLU-82; ASP-430 AND LEU-437; VARIANTS PARK TYR-253; CYS-256; TRP-275 AND ASN-280; VARIANTS LEU-380 AND ASN-394;
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.