SPRINT Home UMBER Home Contents Standard Search Advanced Search Relation Search

==SPRINT==> PRINTS View



  selected as


PR01475

Identifier
PARKIN  [View Relations]  [View Alignment]  
Accession
PR01475
No. of Motifs
9
Creation Date
25-MAR-2001
Title
Parkin signature
Database References
Literature References
1. KITADA, T., ASAKAWA, S., HATTORI, N., MATSUMINE, H., YAMAMURA, Y.,
MINOSHIMA, S., YOKOCHI, M., MIZUNO, Y. AND SHIMIZU, N.
Mutations in the parkin gene cause autosomal recessive juvenile
parkinsonism.
NATURE 392 605-608 (1998).
 
2. ZHANG, Y., GAO, J., CHUNG, K.K.K., HUANG, H., DAWSON, V.L. AND
DAWSON, T.M.
Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes
the degradation of the synaptic vesicle-associated protein.
PROC.NATL.ACAD.SCI.U.S.A. 97 13354-13359 (2000).

Documentation
Parkinson's disease (PD) is a common neurodegenerative disorder with complex
clinical features and a poorly understood aetiology. PD is accompanied by a
progressive loss of dopamine-containing neurons in the substantia nigra,
with patients suffering from rigidity, slowness of movement, tremour and
disturbances of balance. Autosomal recessive juvenile parkinsonism (AR-JP)
is a rare form of familial PD mapped to chromosome 6 and linked strongly to
a pair of markers. One of these markers has been cloned, yielding a sequence
that encodes a protein, 465 amino acids long [1]. The protein sequence,
named parkin, shows moderate similarity with ubiquitin at the N-terminus and
a ring-finger domain at the C-terminus.
 
In normal individuals, parkin binds to the E2 ubiquitin-conjugating human
enzyme 8 (UbcH8) through the C-terminal ring-finger domain. In the presence
of UbcH8, parkin has ubiquitin-protein ligase activity and even catalyses 
its own ubiquitination. Furthermore, parkin appears to target the synaptic
vesicle-associated protein CDCrel-1 for ubiquitination and thus promotes its
degradation. The mutated forms of parkin implicated in AR-JP appear to be
defective in terms of UbcH8 binding, E3 ubiquitin protein-ligase activity,
self-ubiquitination, and CDCrel-1 binding and ubiquitination [2].
 
PARKIN is a 9-element fingerprint that provides a signature for parkin and
parkin-like proteins. The fingerprint was derived from an initial alignment
of 6 sequences: the motifs were drawn from conserved regions spanning 
virtually the full alignment length, but largely avoiding the N- and 
C-terminal ubiquitin-like and ring-finger domains respectively. A single
iteration on SPTR39_15f was required to reach convergence, no further
sequences being identified beyond the starting set.
Summary Information
6 codes involving  9 elements
0 codes involving 8 elements
0 codes involving 7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
9666666666
8000000000
7000000000
6000000000
5000000000
4000000000
3000000000
2000000000
123456789
True Positives
O60260        Q9JK66        Q9JM64        Q9VP72        
Q9WVS6 Q9XUS3
Sequence Titles
O60260      PARKIN - Homo sapiens (Human).                
Q9JK66 PARKIN - Rattus norvegicus (Rat).
Q9JM64 PARKIN - Rattus norvegicus (Rat).
Q9VP72 CG10523 PROTEIN - Drosophila melanogaster (Fruit fly).
Q9WVS6 PARKIN - Mus musculus (Mouse).
Q9XUS3 K08E3.7 PROTEIN - Caenorhabditis elegans.
Scan History
SPTR39_15f 1  100  NSINGLE    
Initial Motifs
Motif 1  width=21
Element Seqn Id St Int Rpt
VAKRQGVPADQLRVIFAGKEL Q9JK66 30 30 -
VAKRQGVPADQLRVIFAGKEL Q9JM64 30 30 -
VAKRQGVPADQLRVIFAGKEL Q9WVS6 30 30 -
VAKRQGVPADQLRVIFAGKEL O60260 30 30 -
VAPQLGLQPDDLKIIFAGKEL Q9VP72 45 45 -
VEKLTEIPSDELEVVFCGKKL Q9XUS3 37 37 -

Motif 2 width=16
Element Seqn Id St Int Rpt
CDDVKRGKLRVYCQKC Q9XUS3 111 53 -
CHKVQPGKLRVQCGTC Q9JM64 154 103 -
CHKVQPGKLRVQCGTC Q9WVS6 153 102 -
CHKVQPGKLRVQCGTC Q9JK66 154 103 -
CQRVQPGKLRVQCSTC O60260 154 103 -
CDKLCNGKLRVRCALC Q9VP72 152 86 -

Motif 3 width=24
Element Seqn Id St Int Rpt
TLAQGPSCWDDVLIPNRMSGECQS Q9JK66 175 5 -
TLAQGPSCWDDVLIPNRMSGECQS Q9JM64 175 5 -
TLAQGPSCWDDVLIPNRMSGECQS Q9WVS6 174 5 -
TLTQGPSCWDDVLIPNRMSGECQS O60260 175 5 -
TVHRDPECWDDVLKSRRIPGHCES Q9VP72 173 5 -
LVKSEPQNWSDVLKSKRIPAVCEE Q9XUS3 132 5 -

Motif 4 width=11
Element Seqn Id St Int Rpt
RAEFFFKCGAH Q9JK66 205 6 -
RAEFFFKCGAH Q9JM64 205 6 -
RAEFFFKCGAH Q9WVS6 204 6 -
SAEFFFKCGAH O60260 205 6 -
FAEFFFKCAEH Q9VP72 211 14 -
FAEFKFKCLAC Q9XUS3 162 6 -

Motif 5 width=21
Element Seqn Id St Int Rpt
ETPVALHLIATNSRNITCITC O60260 221 5 -
DTSVALNLITNNSRSIPCIAC Q9JK66 221 5 -
DTSVALNLITNNSRSIPCIAC Q9JM64 221 5 -
DTSVALNLITSNRRSIPCIAC Q9WVS6 220 5 -
DFAAPLNLIKNNIKNVPCLAC Q9VP72 228 6 -
DPAAALTHVRGNWQMTECCVC Q9XUS3 174 1 -

Motif 6 width=17
Element Seqn Id St Int Rpt
LVFQCNHRHVICLDCFH Q9JK66 249 7 -
LVFQCNHRHVICLDCFH Q9JM64 249 7 -
LVFQCNHRHVICLDCFH Q9WVS6 248 7 -
LVFQCNSRHVICLDCFH O60260 249 7 -
LVFPCASQHVTCIDCFR Q9VP72 256 7 -
VIFDLGCNHITCQFCFR Q9XUS3 200 5 -

Motif 7 width=22
Element Seqn Id St Int Rpt
ELHHFRILGEEQYNRYQQYGAE Q9JK66 300 34 -
ELHHFRILGEEQYNRYQQYGAE Q9JM64 300 34 -
ELHHFRILGEEQYTRYQQYGAE Q9WVS6 299 34 -
ELHHFRILGEEQYNRYQQYGAE O60260 300 34 -
EIHHFKLLTREEYDRYQRFATE Q9VP72 307 34 -
DVHHFHIMGQTSYSEYQRKATE Q9XUS3 222 5 -

Motif 8 width=17
Element Seqn Id St Int Rpt
GVLCPRPGCGAGLLPEQ Q9JK66 329 7 -
GVLCPRPGCGAGLLPEQ Q9JM64 329 7 -
GVLCPRPGCGAGLLPEQ Q9WVS6 328 7 -
GVLCPRPGCGAGLLPEP O60260 329 7 -
GVLCPQPGCGMGLLVEP Q9VP72 336 7 -
GVTCPNVSCGQSFFWEP Q9XUS3 252 8 -

Motif 9 width=23
Element Seqn Id St Int Rpt
CKLEWCWNCGCEWNRACMGDHWF Q9JK66 441 95 -
CKLEWCWNCGCEWNRACMGDHWF Q9JM64 441 95 -
CKLEWCWNCGCEWNRACMGDHWF Q9WVS6 440 95 -
CRLEWCWNCGCEWNRVCMGDHWF O60260 441 95 -
CGFEWCWVCQTEWTRDCMGAHWF Q9VP72 445 92 -
CGMDWCFKCKTEWKEECQWDHWF Q9XUS3 334 65 -
Final Motifs
Motif 1  width=21
Element Seqn Id St Int Rpt
VAKRQGVPADQLRVIFAGKEL Q9JK66 30 30 -
VAKRQGVPADQLRVIFAGKEL Q9JM64 30 30 -
VAKRQGVPADQLRVIFAGKEL Q9WVS6 30 30 -
VAKRQGVPADQLRVIFAGKEL O60260 30 30 -
VAPQLGLQPDDLKIIFAGKEL Q9VP72 45 45 -
VEKLTEIPSDELEVVFCGKKL Q9XUS3 37 37 -

Motif 2 width=16
Element Seqn Id St Int Rpt
CDDVKRGKLRVYCQKC Q9XUS3 111 53 -
CHKVQPGKLRVQCGTC Q9JM64 154 103 -
CHKVQPGKLRVQCGTC Q9WVS6 153 102 -
CHKVQPGKLRVQCGTC Q9JK66 154 103 -
CQRVQPGKLRVQCSTC O60260 154 103 -
CDKLCNGKLRVRCALC Q9VP72 152 86 -

Motif 3 width=24
Element Seqn Id St Int Rpt
TLAQGPSCWDDVLIPNRMSGECQS Q9JK66 175 5 -
TLAQGPSCWDDVLIPNRMSGECQS Q9JM64 175 5 -
TLAQGPSCWDDVLIPNRMSGECQS Q9WVS6 174 5 -
TLTQGPSCWDDVLIPNRMSGECQS O60260 175 5 -
TVHRDPECWDDVLKSRRIPGHCES Q9VP72 173 5 -
LVKSEPQNWSDVLKSKRIPAVCEE Q9XUS3 132 5 -

Motif 4 width=11
Element Seqn Id St Int Rpt
RAEFFFKCGAH Q9JK66 205 6 -
RAEFFFKCGAH Q9JM64 205 6 -
RAEFFFKCGAH Q9WVS6 204 6 -
SAEFFFKCGAH O60260 205 6 -
FAEFFFKCAEH Q9VP72 211 14 -
FAEFKFKCLAC Q9XUS3 162 6 -

Motif 5 width=21
Element Seqn Id St Int Rpt
ETPVALHLIATNSRNITCITC O60260 221 5 -
DTSVALNLITNNSRSIPCIAC Q9JK66 221 5 -
DTSVALNLITNNSRSIPCIAC Q9JM64 221 5 -
DTSVALNLITSNRRSIPCIAC Q9WVS6 220 5 -
DFAAPLNLIKNNIKNVPCLAC Q9VP72 228 6 -
DPAAALTHVRGNWQMTECCVC Q9XUS3 174 1 -

Motif 6 width=17
Element Seqn Id St Int Rpt
LVFQCNHRHVICLDCFH Q9JK66 249 7 -
LVFQCNHRHVICLDCFH Q9JM64 249 7 -
LVFQCNHRHVICLDCFH Q9WVS6 248 7 -
LVFQCNSRHVICLDCFH O60260 249 7 -
LVFPCASQHVTCIDCFR Q9VP72 256 7 -
VIFDLGCNHITCQFCFR Q9XUS3 200 5 -

Motif 7 width=22
Element Seqn Id St Int Rpt
ELHHFRILGEEQYNRYQQYGAE Q9JK66 300 34 -
ELHHFRILGEEQYNRYQQYGAE Q9JM64 300 34 -
ELHHFRILGEEQYTRYQQYGAE Q9WVS6 299 34 -
ELHHFRILGEEQYNRYQQYGAE O60260 300 34 -
EIHHFKLLTREEYDRYQRFATE Q9VP72 307 34 -
DVHHFHIMGQTSYSEYQRKATE Q9XUS3 222 5 -

Motif 8 width=17
Element Seqn Id St Int Rpt
GVLCPRPGCGAGLLPEQ Q9JK66 329 7 -
GVLCPRPGCGAGLLPEQ Q9JM64 329 7 -
GVLCPRPGCGAGLLPEQ Q9WVS6 328 7 -
GVLCPRPGCGAGLLPEP O60260 329 7 -
GVLCPQPGCGMGLLVEP Q9VP72 336 7 -
GVTCPNVSCGQSFFWEP Q9XUS3 252 8 -

Motif 9 width=23
Element Seqn Id St Int Rpt
CKLEWCWNCGCEWNRACMGDHWF Q9JK66 441 95 -
CKLEWCWNCGCEWNRACMGDHWF Q9JM64 441 95 -
CKLEWCWNCGCEWNRACMGDHWF Q9WVS6 440 95 -
CRLEWCWNCGCEWNRVCMGDHWF O60260 441 95 -
CGFEWCWVCQTEWTRDCMGAHWF Q9VP72 445 92 -
CGMDWCFKCKTEWKEECQWDHWF Q9XUS3 334 65 -