Variant position: 64 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 189 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 VQCSRDVVICPDASLEDA-KK EGPYDVVVLPGG--NLGAQNLSE
Mouse VQCSRDVMICPDTSLEDA-KT QGPYDVVVLPGG--NLGAQN
Rat VQCSRDVVICPDTSLEEA-KT QGPYDVVVLPGG--NLGAQN
Bovine VQCSRDVVICPDASLEDA-KK EGPYDVVVLPGG--NLGAQN
Chicken VQCSRDVLICPDASLEDA-RK EGPYDVIVLPGG--NLGAQN
Zebrafish VQCSREVMICPDSSLEDA-HK QGPYDVVLLPGG--LLGAQN
Slime mold VTSTFGVKVQVDVLLGEVVKS LDEFDALAIPGGFENYSFYE
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
67 – 67 Phosphotyrosine
46 – 46 S-palmitoyl cysteine
53 – 53 S-palmitoyl cysteine
46 – 46 C -> A. Reduced localization in lipid rafts; when associated with A-106.
46 – 46 C -> A. Reduces protein stability. No effect on oxidation.
46 – 46 C -> S. No effect on mitochondrial translocation neither on deglycase activity.
51 – 51 V -> A. Disrupts dimer formation and strongly reduces ability to eliminate hydrogen peroxide.
53 – 53 C -> A. Strongly reduces chaperone activity and ability to eliminate hydrogen peroxide.
53 – 53 C -> S. No effect on mitochondrial translocation neither on deglycase activity.
Novel homozygous p.E64D mutation in DJ1 in early onset Parkinson disease (PARK7).
Hering R.; Strauss K.M.; Tao X.; Bauer A.; Woitalla D.; Mietz E.M.; Petrovic S.; Bauer P.; Schaible W.; Mueller T.; Schoels L.; Klein C.; Berg D.; Meyer P.T.; Schulz J.B.; Wollnik B.; Tong L.; Krueger R.; Riess O.;
Hum. Mutat. 24:321-329(2004)
Cited for: VARIANT PARK7 ASP-64; X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS);
Differential effects of Parkinson's disease-associated mutations on stability and folding of DJ-1.
Goerner K.; Holtorf E.; Odoy S.; Nuscher B.; Yamamoto A.; Regula J.T.; Beyer K.; Haass C.; Kahle P.J.;
J. Biol. Chem. 279:6943-6951(2004)
Cited for: CHARACTERIZATION OF VARIANTS PARK7 ASP-64 AND PRO-166;
Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1.
Krebiehl G.; Ruckerbauer S.; Burbulla L.F.; Kieper N.; Maurer B.; Waak J.; Wolburg H.; Gizatullina Z.; Gellerich F.N.; Woitalla D.; Riess O.; Kahle P.J.; Proikas-Cezanne T.; Kruger R.;
PLoS ONE 5:E9367-E9367(2010)
Cited for: VARIANT ASP-64; FUNCTION;
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