Variant position: 431 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 465 The length of the canonical sequence.
Location on the sequence:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human IKKTTKPCPRCHVPVEKNGG CMHMKCPQPQCRLEWCWNCGC
Mouse IKKTTKPCPRCNVPIEKNGG CMHMKCPQPQCKLEWCWNCGC
Rat IKKTTKPCPRCNVPIEKNGG CMHMKCPQPQCKLEWCWNCGC
Sequence annotation in neighborhood: 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.
Type Positions Description
1 – 465 E3 ubiquitin-protein ligase parkin
418 – 449 RING-type 2; atypical
234 – 465 TRIAD supradomain
431 – 431
418 – 418 Zinc 5
421 – 421 Zinc 5
436 – 436 Zinc 5
441 – 441 Zinc 5
446 – 446 Zinc 6
449 – 449 Zinc 6
298 – 465 Missing. In isoform 3.
369 – 465 Missing. In isoform 5.
415 – 415 T -> N. Loss of activity and self-ubiquitination. Loss of monoubiquitination resulting in an increase in apoptosis. No effect on polyubiquitination or mitophagy.
421 – 421 C -> A. Impairs the ability of self-ubiquitination and to ubiquitinate SNCAIP.
429 – 429 G -> E. Reduced self-ubiquitination.
430 – 430 G -> D. Loss of self-ubiquitination.
431 – 431 C -> A. Loss of activity.
431 – 431 C -> S. Impairs the ability to ubiquitinate target proteins. No effect on translocation to mitochondria.
433 – 433 H -> NA. Impaired activity.
444 – 444 E -> QA. Impaired activity.
429 – 431
Parkin mono-ubiquitinates Bcl-2 and regulates autophagy.
Chen D.; Gao F.; Li B.; Wang H.; Xu Y.; Zhu C.; Wang G.;
J. Biol. Chem. 285:38214-38223(2010)
Cited for: FUNCTION; INTERACTION WITH BCL2; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS PARK2 ASN-161; ARG-240; PHE-431 AND LEU-437;
PARIS (ZNF746) repression of PGC-1alpha contributes to neurodegeneration in Parkinson's disease.
Shin J.H.; Ko H.S.; Kang H.; Lee Y.; Lee Y.I.; Pletinkova O.; Troconso J.C.; Dawson V.L.; Dawson T.M.;
Cited for: FUNCTION; INTERACTION WITH ZNF746; CHARACTERIZATION OF VARIANTS PARK2 TRP-275; ASP-430 AND PHE-431;
Novel mutations, pseudo-dominant inheritance, and possible familial affects in patients with autosomal recessive juvenile parkinsonism.
Maruyama M.; Ikeuchi T.; Saito M.; Ishikawa A.; Yuasa T.; Tanaka H.; Hayashi S.; Wakabayashi K.; Takahashi H.; Tsuji S.;
Ann. Neurol. 48:245-250(2000)
Cited for: VARIANT PARK2 PHE-431;
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