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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60260: Variant p.Ala82Glu

E3 ubiquitin-protein ligase parkin
Gene: PRKN
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Variant information Variant position: help 82 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Alanine (A) to Glutamate (E) at position 82 (A82E, p.Ala82Glu). 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: help Change from small size and hydrophobic (A) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In PARK2. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 82 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 465 The length of the canonical sequence.
Location on the sequence: help DQQSIVHIVQRPWRKGQEMN A TGGDDPRNAAGGCEREPQSL 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         DQQSIVHIVQ-RPWRKGQEMNATGGDDPRNAAGGCEREPQSL

Mouse                         EQQSIVHIVQ-RPRRRSHETNASGGDEPQSTSEGSIWESRS

Rat                           EQQSIVHIVQ-RPQRKSHETNASGGDKPQSTPEGSIWEPRS

Drosophila                    GQQSVLHAIRLRPPVQRQKIQSATLEEEEPSLSDEASKPLN
Sequence annotation in neighborhood: help 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 1 – 465 E3 ubiquitin-protein ligase parkin
Region 77 – 237 Necessary for PINK1-dependent localization to mitochondria
Region 77 – 99 Disordered
Modified residue 65 – 65 Phosphoserine; by PINK1
Alternative sequence 1 – 191 Missing. In isoform 4.
Alternative sequence 58 – 206 Missing. In isoform 6.
Mutagenesis 65 – 65 S -> A. Loss of phosphorylation. Undergoes autoubiquitination in the presence of phosphorylated ubiquitin.
Mutagenesis 65 – 65 S -> E. Phosphomimetic mutant; still requires PINK1 for activation. PRKN is activated in presence of phosphorylated ubiquitin.



Literature citations
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;
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.