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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60260: Variant p.Gly328Glu

E3 ubiquitin-protein ligase parkin
Gene: PRKN
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Variant information Variant position: help 328 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 Glycine (G) to Glutamate (E) at position 328 (G328E, p.Gly328Glu). 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 glycine (G) to medium size and acidic (E) 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; does not affect PINK-1 dependent localization to depolarized mitochondria. Any additional useful information about the variant.


Sequence information Variant position: help 328 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 GEEQYNRYQQYGAEECVLQM G GVLCPRPGCGAGLLPEPDQR 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                         GEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEPDQR

Mouse                         GEEQYTRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEQGQR

Rat                           GEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEQGQK

Drosophila                    TREEYDRYQRFATEEYVLQAGGVLCPQPGCGMGLLVEPDCR
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
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.



Literature citations
Association between early-onset Parkinson's disease and mutations in the parkin gene.
Luecking C.B.; Duerr A.; Bonifati V.; Vaughan J.R.; De Michele G.; Gasser T.; Harhangi B.S.; Meco G.; Denefle P.; Wood N.W.; Agid Y.; Brice A.;
N. Engl. J. Med. 342:1560-1567(2000)
Cited for: VARIANTS PARK2 ASN-161; ASN-211; CYS-256; TRP-275; ASN-280; GLY-289; GLU-328; ASN-415 AND ASP-430; VARIANT CYS-334; 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; PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy.
Matsuda N.; Sato S.; Shiba K.; Okatsu K.; Saisho K.; Gautier C.A.; Sou Y.S.; Saiki S.; Kawajiri S.; Sato F.; Kimura M.; Komatsu M.; Hattori N.; Tanaka K.;
J. Cell Biol. 189:211-221(2010)
Cited for: CHARACTERIZATION OF VARIANTS PARK2 ASN-161; ASN-211; ARG-240; ASN-280 AND GLU-328;
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.