Variant position: 441 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 CHVPVEKNGGCMHMKCPQPQ CRLEWCWNCGCEWNRVCMGDH
Mouse CNVPIEKNGGCMHMKCPQPQ CKLEWCWNCGCEWNRACMGDH
Rat CNVPIEKNGGCMHMKCPQPQ CKLEWCWNCGCEWNRACMGDH
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
421 – 421 Zinc 5
436 – 436 Zinc 5
441 – 441 Zinc 5
446 – 446 Zinc 6
449 – 449 Zinc 6
457 – 457 Zinc 6
461 – 461 Zinc 6; via tele nitrogen
298 – 465 Missing. In isoform 3.
369 – 465 Missing. In isoform 5.
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.
439 – 441
Transcriptional repression of p53 by parkin and impairment by mutations associated with autosomal recessive juvenile Parkinson's disease.
da Costa C.A.; Sunyach C.; Giaime E.; West A.; Corti O.; Brice A.; Safe S.; Abou-Sleiman P.M.; Wood N.W.; Takahashi H.; Goldberg M.S.; Shen J.; Checler F.;
Nat. Cell Biol. 11:1370-1375(2009)
Cited for: FUNCTION IN PROTECTION OF APOPTOSIS; CHARACTERIZATION OF VARIANTS PARK2 ASN-161; CYS-256; TRP-275; ARG-418 AND ARG-441; DOMAIN;
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;
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.