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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60260: Variant p.Lys211Asn

E3 ubiquitin-protein ligase parkin
Gene: PRKN
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Variant information Variant position: help 211 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 Lysine (K) to Asparagine (N) at position 211 (K211N, p.Lys211Asn). 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 large size and basic (K) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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; severely compromises the mitochondrial localization; fails to stabilize BCL2. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 211 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 RMSGECQSPHCPGTSAEFFF K CGAHPTSDKETSVALHLIAT 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                         RMSGECQSPHCPGTS--------AEFFFKCGAHPT-SDKETSVALHLIAT

Mouse                         RMSGECQSPDCPGTR--------AEFFFKCGAHPT-SDKDT

Rat                           RMSGECQSPDCPGTR--------AEFFFKCGAHPT-SDKDT

Drosophila                    RIPGHCESLEVACVDNAAGDPPFAEFFFKCAEHVSGGEKDF
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
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; Origin of the mutations in the parkin gene in Europe: exon rearrangements are independent recurrent events, whereas point mutations may result from founder effects.
Periquet M.; Luecking C.B.; Vaughan J.R.; Bonifati V.; Duerr A.; De Michele G.; Horstink M.; Farrer M.; Illarioshkin S.N.; Pollak P.; Borg M.; Brefel-Courbon C.; Denefle P.; Meco G.; Gasser T.; Breteler M.M.; Wood N.W.; Agid Y.; Brice A.;
Am. J. Hum. Genet. 68:617-626(2001)
Cited for: VARIANTS PARK2 ASN-211; TRP-275 AND ASP-430; Linkage stratification and mutation analysis at the parkin locus identifies mutation positive Parkinson's disease families.
Nichols W.C.; Pankratz N.; Uniacke S.K.; Pauciulo M.W.; Halter C.; Rudolph A.; Conneally P.M.; Foroud T.;
J. Med. Genet. 39:489-492(2002)
Cited for: VARIANTS PARK2 ASN-211; TRP-275; ASP-430 AND LEU-437; Heterozygosity for a mutation in the parkin gene leads to later onset Parkinson disease.
Foroud T.; Uniacke S.K.; Liu L.; Pankratz N.; Rudolph A.; Halter C.; Shults C.; Marder K.; Conneally P.M.; Nichols W.C.;
Neurology 60:796-801(2003)
Cited for: VARIANTS PARK2 VAL-192; ASN-211; MET-240 AND LEU-437; VARIANT ASN-167; INVOLVEMENT IN LATE-ONSET PARK; 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.