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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60260: Variant p.Thr351Pro

E3 ubiquitin-protein ligase parkin
Gene: PRKN
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Variant information Variant position: help 351 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 Threonine (T) to Proline (P) at position 351 (T351P, p.Thr351Pro). 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 (T) to medium size and hydrophobic (P) 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; impairs folding of IBR domain. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 351 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 LCPRPGCGAGLLPEPDQRKV T CEGGNGLGCGFAFCRECKEA 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                         LCPRPGCGAGLLPEPDQRKVTCEGGNGLGCGFAFCRECKEA

Mouse                         LCPRPGCGAGLLPEQGQRKVTCEGGNGLGCGFVFCRDCKEA

Rat                           LCPRPGCGAGLLPEQGQKKVTCEGGNGLGCGFVFCRDCKEA

Drosophila                    LCPQPGCGMGLLVEPDCRKVTCQN----GCGYVFCRNCLQG
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 313 – 377 IBR-type
Region 234 – 465 TRIAD supradomain
Binding site 332 – 332
Binding site 337 – 337
Binding site 352 – 352
Binding site 360 – 360
Binding site 365 – 365
Binding site 368 – 368
Cross 349 – 349 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
Cross 369 – 369 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
Alternative sequence 298 – 465 Missing. In isoform 3.
Alternative sequence 312 – 361 Missing. In isoform 7 and isoform 8.
Mutagenesis 332 – 332 C -> S. Impairs folding of IBR domain.
Mutagenesis 337 – 337 C -> A. Impairs the ability to ubiquitinate SNCAIP.
Mutagenesis 365 – 365 C -> S. Impairs protein folding.
Beta strand 348 – 351



Literature citations
Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease.
Beasley S.A.; Hristova V.A.; Shaw G.S.;
Proc. Natl. Acad. Sci. U.S.A. 104:3095-3100(2007)
Cited for: STRUCTURE BY NMR OF 307-384 IN COMPLEX WITH ZINC IONS; CHARACTERIZATION OF VARIANT PARK2 PRO-351; MUTAGENESIS OF CYS-332 AND CYS-365; IDENTIFICATION BY MASS SPECTROMETRY; Role of parkin mutations in 111 community-based patients with early-onset parkinsonism.
Kann M.; Jacobs H.; Mohrmann K.; Schumacher K.; Hedrich K.; Garrels J.; Wiegers K.; Schwinger E.; Pramstaller P.P.; Breakefield X.O.; Ozelius L.J.; Vieregge P.; Klein C.;
Ann. Neurol. 51:621-625(2002)
Cited for: VARIANTS PARK2 LEU-37 AND PRO-351;
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.