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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60260: Variant p.Cys212Tyr

E3 ubiquitin-protein ligase parkin
Gene: PRKN
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Variant information Variant position: help 212 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 Cysteine (C) to Tyrosine (Y) at position 212 (C212Y, p.Cys212Tyr). 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 medium size and polar (C) to large size and aromatic (Y) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 212 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 MSGECQSPHCPGTSAEFFFK C GAHPTSDKETSVALHLIATN 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                         MSGECQSPHCPGTS--------AEFFFKCGAHPT-SDKETSVALHLIATN

Mouse                         MSGECQSPDCPGTR--------AEFFFKCGAHPT-SDKDTS

Rat                           MSGECQSPDCPGTR--------AEFFFKCGAHPT-SDKDTS

Drosophila                    IPGHCESLEVACVDNAAGDPPFAEFFFKCAEHVSGGEKDFA
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
Zinc finger 141 – 225 RING-type 0; atypical
Region 77 – 237 Necessary for PINK1-dependent localization to mitochondria
Region 204 – 238 SYT11 binding 1
Modified residue 217 – 217 Phosphothreonine
Mutagenesis 211 – 211 K -> N. Loss of activity towards MIRO1.
Mutagenesis 217 – 217 T -> A. Loss of phosphorylation. Reduced mitochondrial localization; when associated with A-175.
Mutagenesis 217 – 217 T -> E. Phosphomimetic mutant. Mostly localizes to the mitochondria; when associated with E-175.
Beta strand 205 – 212



Literature citations
A novel Cys212Tyr founder mutation in parkin and allelic heterogeneity of juvenile parkinsonism in a population from North West Colombia.
Pineda-Trujillo N.; Carvajal-Carmona L.G.; Buritica O.; Moreno S.; Uribe C.; Pineda D.; Toro M.; Garcia F.; Arias W.; Bedoya G.; Lopera F.; Ruiz-Linares A.;
Neurosci. Lett. 298:87-90(2001)
Cited for: VARIANT PARK2 TYR-212; Molecular findings in familial Parkinson disease in Spain.
Hoenicka J.; Vidal L.; Morales B.; Ampuero I.; Jimenez-Jimenez F.J.; Berciano J.; del Ser T.; Jimenez A.; Ruiz P.G.; de Yebenes J.G.;
Arch. Neurol. 59:966-970(2002)
Cited for: VARIANTS PARK2 GLU-56 AND TYR-212;
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.