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Q5S007

- LRRK2_HUMAN

UniProt

Q5S007 - LRRK2_HUMAN

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Protein

Leucine-rich repeat serine/threonine-protein kinase 2

Gene

LRRK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). Phosphorylates PRDX3. May also have GTPase activity. May play a role in the phosphorylation of proteins central to Parkinson disease.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1906 – 19061ATPPROSITE-ProRule annotation
Active sitei1994 – 19941Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1341 – 13488GTPPROSITE-ProRule annotation
Nucleotide bindingi1885 – 18939ATPPROSITE-ProRule annotation
Nucleotide bindingi2098 – 212124GTPPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi2295 – 22984GTPPROSITE-ProRule annotation

GO - Molecular functioni

  1. actin binding Source: ParkinsonsUK-UCL
  2. ATP binding Source: UniProtKB-KW
  3. clathrin binding Source: ParkinsonsUK-UCL
  4. glycoprotein binding Source: ParkinsonsUK-UCL
  5. GTPase activator activity Source: UniProtKB
  6. GTPase activity Source: BHF-UCL
  7. GTP binding Source: UniProtKB
  8. GTP-dependent protein kinase activity Source: UniProtKB
  9. identical protein binding Source: IntAct
  10. ion channel binding Source: UniProtKB
  11. kinase activity Source: UniProtKB
  12. MAP kinase kinase activity Source: BHF-UCL
  13. peroxidase inhibitor activity Source: ParkinsonsUK-UCL
  14. protein homodimerization activity Source: UniProtKB
  15. protein kinase A binding Source: ParkinsonsUK-UCL
  16. protein kinase activity Source: UniProtKB
  17. protein serine/threonine kinase activity Source: UniProtKB
  18. Rho GTPase binding Source: BHF-UCL
  19. SNARE binding Source: ParkinsonsUK-UCL
  20. syntaxin-1 binding Source: ParkinsonsUK-UCL
  21. tubulin binding Source: BHF-UCL

GO - Biological processi

  1. activation of MAPK activity Source: GOC
  2. activation of MAPKK activity Source: BHF-UCL
  3. autophagy Source: UniProtKB-KW
  4. cellular protein localization Source: ParkinsonsUK-UCL
  5. cellular response to dopamine Source: ParkinsonsUK-UCL
  6. cellular response to manganese ion Source: ParkinsonsUK-UCL
  7. cellular response to oxidative stress Source: ParkinsonsUK-UCL
  8. determination of adult lifespan Source: BHF-UCL
  9. endocytosis Source: ParkinsonsUK-UCL
  10. exploration behavior Source: BHF-UCL
  11. GTP catabolic process Source: BHF-UCL
  12. intracellular distribution of mitochondria Source: BHF-UCL
  13. intracellular signal transduction Source: ParkinsonsUK-UCL
  14. locomotory exploration behavior Source: Ensembl
  15. MAPK cascade Source: UniProtKB
  16. negative regulation of GTPase activity Source: MGI
  17. negative regulation of hydrogen peroxide-induced cell death Source: ParkinsonsUK-UCL
  18. negative regulation of late endosome to lysosome transport Source: ParkinsonsUK-UCL
  19. negative regulation of peroxidase activity Source: GOC
  20. negative regulation of protein binding Source: ParkinsonsUK-UCL
  21. negative regulation of protein phosphorylation Source: ParkinsonsUK-UCL
  22. negative regulation of protein processing Source: ParkinsonsUK-UCL
  23. negative regulation of protein processing involved in protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  24. negative regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  25. negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL
  26. neuromuscular junction development Source: BHF-UCL
  27. neuron death Source: BHF-UCL
  28. neuron projection morphogenesis Source: UniProtKB
  29. olfactory bulb development Source: BHF-UCL
  30. peptidyl-serine phosphorylation Source: BHF-UCL
  31. peptidyl-threonine phosphorylation Source: BHF-UCL
  32. positive regulation of autophagy Source: UniProtKB
  33. positive regulation of dopamine receptor signaling pathway Source: BHF-UCL
  34. positive regulation of GTPase activity Source: GOC
  35. positive regulation of MAP kinase activity Source: ParkinsonsUK-UCL
  36. positive regulation of programmed cell death Source: UniProtKB
  37. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  38. positive regulation of protein autoubiquitination Source: ParkinsonsUK-UCL
  39. positive regulation of protein binding Source: ParkinsonsUK-UCL
  40. positive regulation of protein phosphorylation Source: BHF-UCL
  41. positive regulation of protein ubiquitination Source: UniProtKB
  42. protein autophosphorylation Source: UniProtKB
  43. protein phosphorylation Source: ParkinsonsUK-UCL
  44. reactive oxygen species metabolic process Source: ParkinsonsUK-UCL
  45. regulation of branching morphogenesis of a nerve Source: BHF-UCL
  46. regulation of dendritic spine morphogenesis Source: BHF-UCL
  47. regulation of dopamine receptor signaling pathway Source: ParkinsonsUK-UCL
  48. regulation of excitatory postsynaptic membrane potential Source: ParkinsonsUK-UCL
  49. regulation of kidney size Source: BHF-UCL
  50. regulation of locomotion Source: BHF-UCL
  51. regulation of membrane potential Source: BHF-UCL
  52. regulation of mitochondrial depolarization Source: ParkinsonsUK-UCL
  53. regulation of neuroblast proliferation Source: ParkinsonsUK-UCL
  54. regulation of neuron death Source: ParkinsonsUK-UCL
  55. regulation of neuron maturation Source: BHF-UCL
  56. regulation of protein kinase A signaling Source: ParkinsonsUK-UCL
  57. regulation of synaptic transmission, glutamatergic Source: ParkinsonsUK-UCL
  58. regulation of synaptic vesicle exocytosis Source: ParkinsonsUK-UCL
  59. regulation of synaptic vesicle transport Source: ParkinsonsUK-UCL
  60. response to oxidative stress Source: BHF-UCL
  61. small GTPase mediated signal transduction Source: InterPro
  62. tangential migration from the subventricular zone to the olfactory bulb Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Autophagy, Differentiation

Keywords - Ligandi

ATP-binding, GTP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ5S007.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat serine/threonine-protein kinase 2 (EC:2.7.11.1)
Alternative name(s):
Dardarin
Gene namesi
Name:LRRK2
Synonyms:PARK8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:18618. LRRK2.

Subcellular locationi

Membrane; Peripheral membrane protein. Cytoplasm. Perikaryon. Mitochondrion. Golgi apparatus. Cell projectionaxon. Cell projectiondendrite. Endoplasmic reticulum By similarity. Cytoplasmic vesicle By similarity. Endosome By similarity. Lysosome By similarity. Mitochondrion outer membrane By similarity. Mitochondrion inner membrane By similarity. Mitochondrion matrix By similarity
Note: Predominantly associated with intracytoplasmic vesicular and membranous structures (By similarity). Localized in the cytoplasm and associated with cellular membrane structures. Predominantly associated with the mitochondrial outer membrane of the mitochondria. Colocalized with RAB29 along tubular structures emerging from Golgi apparatus. Localizes in intracytoplasmic punctate structures of neuronal perikarya and dendritic and axonal processes.By similarity

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic side of mitochondrial outer membrane Source: UniProtKB
  4. cytoplasmic vesicle Source: UniProtKB
  5. cytosol Source: ParkinsonsUK-UCL
  6. dendrite Source: UniProtKB
  7. dendrite cytoplasm Source: BHF-UCL
  8. endoplasmic reticulum Source: UniProtKB
  9. endosome Source: UniProtKB
  10. extracellular space Source: UniProt
  11. extracellular vesicular exosome Source: UniProt
  12. Golgi apparatus Source: UniProtKB
  13. inclusion body Source: ParkinsonsUK-UCL
  14. lysosome Source: UniProtKB
  15. membrane raft Source: Ensembl
  16. mitochondrial inner membrane Source: UniProtKB
  17. mitochondrial matrix Source: UniProtKB
  18. mitochondrial membrane Source: ParkinsonsUK-UCL
  19. mitochondrial outer membrane Source: UniProtKB
  20. mitochondrion Source: UniProtKB
  21. neuronal cell body Source: BHF-UCL
  22. neuron projection Source: BHF-UCL
  23. perikaryon Source: UniProtKB
  24. plasma membrane Source: Ensembl
  25. synaptic vesicle Source: Ensembl
  26. terminal bouton Source: ParkinsonsUK-UCL
  27. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Parkinson disease 8 (PARK8) [MIM:607060]: A slowly progressive neurodegenerative disorder characterized by bradykinesia, rigidity, resting tremor, postural instability, neuronal loss in the substantia nigra, and the presence of neurofibrillary MAPT (tau)-positive and Lewy bodies in some patients.28 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti712 – 7121M → V in PARK8. 1 Publication
VAR_054741
Natural varianti793 – 7931R → M in PARK8; unknown pathological significance. 3 Publications
Corresponds to variant rs35173587 [ dbSNP | Ensembl ].
VAR_024935
Natural varianti930 – 9301Q → R in PARK8; unknown pathological significance. 1 Publication
VAR_024936
Natural varianti1067 – 10671R → Q in PARK8. 1 Publication
VAR_024938
Natural varianti1096 – 10961S → C in PARK8; unknown pathological significance.
VAR_024939
Natural varianti1122 – 11221I → V in PARK8. 2 Publications
Corresponds to variant rs34805604 [ dbSNP | Ensembl ].
VAR_024940
Natural varianti1228 – 12281S → T in PARK8. 1 Publication
VAR_024941
Natural varianti1371 – 13711I → V in PARK8; unknown pathological significance. 2 Publications
Corresponds to variant rs17466213 [ dbSNP | Ensembl ].
VAR_024943
Natural varianti1441 – 14411R → G in PARK8; shows a progressive reduction in neurite length and branching. 4 Publications
Corresponds to variant rs33939927 [ dbSNP | Ensembl ].
VAR_024946
Natural varianti1441 – 14411R → H in PARK8; pathogenicity has yet to be confirmed. 2 Publications
Corresponds to variant rs34995376 [ dbSNP | Ensembl ].
VAR_024947
Natural varianti1514 – 15141R → Q in PARK8; pathogenicity has yet to be confirmed; might have an effect on protein structure. 3 Publications
Corresponds to variant rs35507033 [ dbSNP | Ensembl ].
VAR_024948
Natural varianti1542 – 15421P → S in PARK8; pathogenicity has yet to be confirmed; might have an effect on protein structure. 3 Publications
Corresponds to variant rs33958906 [ dbSNP | Ensembl ].
VAR_024949
Natural varianti1598 – 15981V → E in PARK8; pathogenicity has yet to be confirmed; might have an effect on protein structure. 1 Publication
Corresponds to variant rs721710 [ dbSNP | Ensembl ].
VAR_024950
Natural varianti1699 – 16991Y → C in PARK8; shows no progressive reduction in neurite length and branching. 4 Publications
Corresponds to variant rs35801418 [ dbSNP | Ensembl ].
VAR_024954
Natural varianti1728 – 17281R → H in PARK8. 1 Publication
VAR_054744
Natural varianti1728 – 17281R → L in PARK8. 1 Publication
VAR_054745
Natural varianti1869 – 18691M → T in PARK8; pathogenicity has yet to be confirmed. 2 Publications
Corresponds to variant rs35602796 [ dbSNP | Ensembl ].
VAR_024955
Natural varianti1941 – 19411R → H in PARK8. 1 Publication
VAR_024956
Natural varianti2012 – 20121I → T in PARK8; pathogenicity uncertain. 1 Publication
Corresponds to variant rs34015634 [ dbSNP | Ensembl ].
VAR_024957
Natural varianti2019 – 20191G → S in PARK8; shows an increase in activity in both autophosphorylation and phosphorylation of a generic substrate; results in increased PRDX3 phosphorylation promoting dysregulation of mitochondrial function and oxidative damage; does not inhibit interaction with RAB29; shows a progressive reduction in neurite length and branching; shows distinctive spheroid-like inclusions within both neuronal processes and at intracellular membranous structures; shows lysosomal swelling and reduced retrograde transport of selective cargo between lysosomes and the Golgi apparatus; shows apoptotic mechanism of cell death. 24 Publications
Corresponds to variant rs34637584 [ dbSNP | Ensembl ].
VAR_024958
Natural varianti2020 – 20201I → T in PARK8; significant increase in autophosphorylation of about 40% in comparison to wild-type protein in vitro; shows a progressive reduction in neurite length and branching. 4 Publications
Corresponds to variant rs35870237 [ dbSNP | Ensembl ].
VAR_024959
Natural varianti2141 – 21411T → M in PARK8. 1 Publication
VAR_054747
Natural varianti2143 – 21431R → H in PARK8. 1 Publication
VAR_054748
Natural varianti2356 – 23561T → I in PARK8. 1 Publication
VAR_024963
Natural varianti2466 – 24661L → H in PARK8. 1 Publication
VAR_054750

Keywords - Diseasei

Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism

Organism-specific databases

MIMi168600. phenotype.
607060. phenotype.
Orphaneti2828. Young adult-onset Parkinsonism.
PharmGKBiPA134968052.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25272527Leucine-rich repeat serine/threonine-protein kinase 2PRO_0000086238Add
BLAST

Post-translational modificationi

Autophosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5S007.
PaxDbiQ5S007.
PRIDEiQ5S007.

PTM databases

PhosphoSiteiQ5S007.

Expressioni

Tissue specificityi

Expressed in the brain. Expressed in pyramidal neurons in all cortical laminae of the visual cortex, in neurons of the substantia nigra pars compacta and caudate putamen (at protein level). Expressed throughout the adult brain, but at a lower level than in heart and liver. Also expressed in placenta, lung, skeletal muscle, kidney and pancreas. In the brain, expressed in the cerebellum, cerebral cortex, medulla, spinal cord occipital pole, frontal lobe, temporal lobe and putamen. Expression is particularly high in brain dopaminoceptive areas.4 Publications

Gene expression databases

BgeeiQ5S007.
CleanExiHS_LRRK2.
ExpressionAtlasiQ5S007. baseline and differential.
GenevestigatoriQ5S007.

Organism-specific databases

HPAiCAB037160.
HPA014293.

Interactioni

Subunit structurei

Homodimer. Interacts with PARK2, PRDX3, RAB29, TPCN2 and VPS35.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself56EBI-5323863,EBI-5323863
AGO2Q9UKV83EBI-5323863,EBI-528269
AKT1P317496EBI-5323863,EBI-296087
ARFGAP1Q8N6T3-26EBI-5323863,EBI-6288865
Arfgap1Q628487EBI-5323863,EBI-4398879From a different organism.
ARHGEF7Q141556EBI-5323863,EBI-717515
BAG2O958162EBI-5323863,EBI-355275
BAG3O958172EBI-5323863,EBI-747185
BAG5Q9UL1512EBI-5323863,EBI-356517
CDC37Q165437EBI-5323863,EBI-295634
CDC42P609533EBI-5323863,EBI-81752
CHGBP050602EBI-5323863,EBI-712619
Ckmt1P302752EBI-5323863,EBI-773103From a different organism.
DAPK1P533552EBI-5323863,EBI-358616
DNM1Q051934EBI-5323863,EBI-713135
Dnm1P390533EBI-5323863,EBI-397785From a different organism.
DNM1LO0042911EBI-5323863,EBI-724571
DNM1LO00429-32EBI-5323863,EBI-6896746
DVL1O14640-27EBI-5323863,EBI-6504027
DVL2O146413EBI-5323863,EBI-740850
DVL3Q929974EBI-5323863,EBI-739789
ECHS1P300842EBI-5323863,EBI-719602
FADDQ131584EBI-5323863,EBI-494804
GAKO1497610EBI-5323863,EBI-714707
GSK3BP498417EBI-5323863,EBI-373586
HSPA8P111425EBI-5323863,EBI-351896
LDHBP071952EBI-5323863,EBI-358748
LRP6O755813EBI-5323863,EBI-910915
LRRK1Q38SD25EBI-5323863,EBI-1050422
MAP1BP468215EBI-5323863,EBI-9517186
MAP2K3P467345EBI-5323863,EBI-602462
MAP2K6P525644EBI-5323863,EBI-448135
MAP2K7O147333EBI-5323863,EBI-492605
MAPTP10636-23EBI-5323863,EBI-7796412
MAPTP10636-89EBI-5323863,EBI-366233
MATKP426792EBI-5323863,EBI-751664
MBPP026873EBI-5323863,EBI-908215From a different organism.
Mfn1Q811U43EBI-5323863,EBI-9029118From a different organism.
MFN2O951403EBI-5323863,EBI-3324756
MSNP2603815EBI-5323863,EBI-528768
NEK1Q96PY62EBI-5323863,EBI-373615
NFATC2Q134693EBI-5323863,EBI-716258
NUP133Q8WUM02EBI-5323863,EBI-295695
OPA1O603133EBI-5323863,EBI-1054131
PAK6Q9NQU52EBI-5323863,EBI-1053685
PARK2O602603EBI-5323863,EBI-716346
phoAP006342EBI-5323863,EBI-552958From a different organism.
PPP1CAP621366EBI-5323863,EBI-357253
PRDX3P3004812EBI-5323863,EBI-748336
PRKACAP176126EBI-5323863,EBI-476586
Prkar2bP123693EBI-5323863,EBI-6096160From a different organism.
RAB29O149667EBI-5323863,EBI-372165
Rab29Q634813EBI-5323863,EBI-6513837From a different organism.
RAB5BP610204EBI-5323863,EBI-399401
Rab5bP610212EBI-5323863,EBI-8320093From a different organism.
RAC1P630005EBI-5323863,EBI-413628
RGS2P412206EBI-5323863,EBI-712388
RPL10AP629062EBI-5323863,EBI-356860
RPL13P263732EBI-5323863,EBI-356849
RPL14P509142EBI-5323863,EBI-356746
RPL23AP627502EBI-5323863,EBI-353254
RPS11P622803EBI-5323863,EBI-1047710
RPS15P628418EBI-5323863,EBI-372635
RPS16P622492EBI-5323863,EBI-352480
RPS2P158802EBI-5323863,EBI-443446
RPS20P608662EBI-5323863,EBI-353105
RPS23P622662EBI-5323863,EBI-353072
RPS27P426772EBI-5323863,EBI-356336
RPS3P233962EBI-5323863,EBI-351193
SH3GL2Q999622EBI-5323863,EBI-77938
SLC25A4P122352EBI-5323863,EBI-359074
SLC25A5P051412EBI-5323863,EBI-355133
SLC25A6P122362EBI-5323863,EBI-356254
SNAPINO952955EBI-5323863,EBI-296723
SNCAP378406EBI-5323863,EBI-985879
Spag9Q58A652EBI-5323863,EBI-6530207From a different organism.
TUBBP074374EBI-5323863,EBI-350864
TUBB4AP043504EBI-5323863,EBI-355007
YWHABP319465EBI-5323863,EBI-359815
YWHAEP622586EBI-5323863,EBI-356498
YWHAGP619814EBI-5323863,EBI-359832
YwhagP619836EBI-5323863,EBI-359821From a different organism.
YWHAHQ049173EBI-5323863,EBI-306940
YWHAQP273488EBI-5323863,EBI-359854
YWHAZP631049EBI-5323863,EBI-347088

Protein-protein interaction databases

BioGridi125700. 139 interactions.
DIPiDIP-29684N.
IntActiQ5S007. 527 interactions.
MINTiMINT-7997594.
STRINGi9606.ENSP00000298910.

Structurei

Secondary structure

1
2527
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1336 – 13416Combined sources
Helixi1347 – 13548Combined sources
Beta strandi1370 – 13778Combined sources
Beta strandi1389 – 13957Combined sources
Helixi1398 – 14025Combined sources
Helixi1406 – 14116Combined sources
Beta strandi1412 – 14209Combined sources
Helixi1421 – 14233Combined sources
Helixi1425 – 14295Combined sources
Helixi1431 – 144111Combined sources
Beta strandi1446 – 14527Combined sources
Helixi1454 – 14563Combined sources
Helixi1459 – 147214Combined sources
Turni1473 – 14753Combined sources
Beta strandi1481 – 14877Combined sources
Helixi1495 – 150915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZEJX-ray2.00A/B1333-1516[»]
3D6TX-ray2.43B1335-1505[»]
ProteinModelPortaliQ5S007.
SMRiQ5S007. Positions 1335-1512.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5S007.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati983 – 100422LRR 1Add
BLAST
Repeati1012 – 103322LRR 2Add
BLAST
Repeati1036 – 105722LRR 3Add
BLAST
Repeati1059 – 108022LRR 4Add
BLAST
Repeati1084 – 110522LRR 5Add
BLAST
Repeati1108 – 112922LRR 6Add
BLAST
Repeati1130 – 115021LRR 7Add
BLAST
Repeati1174 – 119623LRR 8Add
BLAST
Repeati1197 – 121822LRR 9Add
BLAST
Repeati1221 – 124121LRR 10Add
BLAST
Repeati1246 – 126722LRR 11Add
BLAST
Repeati1269 – 129123LRR 12Add
BLAST
Domaini1328 – 1511184RocPROSITE-ProRule annotationAdd
BLAST
Domaini1879 – 2138260Protein kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili319 – 34830Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi728 – 7314Poly-Leu

Sequence similaritiesi

Contains 12 LRR (leucine-rich) repeats.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 Roc domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00530000063477.
HOGENOMiHOG000293315.
HOVERGENiHBG081937.
InParanoidiQ5S007.
KOiK08844.
OMAiFKIRDQP.
PhylomeDBiQ5S007.
TreeFamiTF313679.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
1.25.40.20. 1 hit.
2.130.10.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR020683. Ankyrin_rpt-contain_dom.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR020859. ROC_GTPase.
IPR008271. Ser/Thr_kinase_AS.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF13855. LRR_8. 1 hit.
PF08477. Miro. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00369. LRR_TYP. 1 hit.
SM00320. WD40. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF50978. SSF50978. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56112. SSF56112. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51450. LRR. 11 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS51424. ROC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5S007-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASGSCQGCE EDEETLKKLI VRLNNVQEGK QIETLVQILE DLLVFTYSER
60 70 80 90 100
ASKLFQGKNI HVPLLIVLDS YMRVASVQQV GWSLLCKLIE VCPGTMQSLM
110 120 130 140 150
GPQDVGNDWE VLGVHQLILK MLTVHNASVN LSVIGLKTLD LLLTSGKITL
160 170 180 190 200
LILDEESDIF MLIFDAMHSF PANDEVQKLG CKALHVLFER VSEEQLTEFV
210 220 230 240 250
ENKDYMILLS ALTNFKDEEE IVLHVLHCLH SLAIPCNNVE VLMSGNVRCY
260 270 280 290 300
NIVVEAMKAF PMSERIQEVS CCLLHRLTLG NFFNILVLNE VHEFVVKAVQ
310 320 330 340 350
QYPENAALQI SALSCLALLT ETIFLNQDLE EKNENQENDD EGEEDKLFWL
360 370 380 390 400
EACYKALTWH RKNKHVQEAA CWALNNLLMY QNSLHEKIGD EDGHFPAHRE
410 420 430 440 450
VMLSMLMHSS SKEVFQASAN ALSTLLEQNV NFRKILLSKG IHLNVLELMQ
460 470 480 490 500
KHIHSPEVAE SGCKMLNHLF EGSNTSLDIM AAVVPKILTV MKRHETSLPV
510 520 530 540 550
QLEALRAILH FIVPGMPEES REDTEFHHKL NMVKKQCFKN DIHKLVLAAL
560 570 580 590 600
NRFIGNPGIQ KCGLKVISSI VHFPDALEML SLEGAMDSVL HTLQMYPDDQ
610 620 630 640 650
EIQCLGLSLI GYLITKKNVF IGTGHLLAKI LVSSLYRFKD VAEIQTKGFQ
660 670 680 690 700
TILAILKLSA SFSKLLVHHS FDLVIFHQMS SNIMEQKDQQ FLNLCCKCFA
710 720 730 740 750
KVAMDDYLKN VMLERACDQN NSIMVECLLL LGADANQAKE GSSLICQVCE
760 770 780 790 800
KESSPKLVEL LLNSGSREQD VRKALTISIG KGDSQIISLL LRRLALDVAN
810 820 830 840 850
NSICLGGFCI GKVEPSWLGP LFPDKTSNLR KQTNIASTLA RMVIRYQMKS
860 870 880 890 900
AVEEGTASGS DGNFSEDVLS KFDEWTFIPD SSMDSVFAQS DDLDSEGSEG
910 920 930 940 950
SFLVKKKSNS ISVGEFYRDA VLQRCSPNLQ RHSNSLGPIF DHEDLLKRKR
960 970 980 990 1000
KILSSDDSLR SSKLQSHMRH SDSISSLASE REYITSLDLS ANELRDIDAL
1010 1020 1030 1040 1050
SQKCCISVHL EHLEKLELHQ NALTSFPQQL CETLKSLTHL DLHSNKFTSF
1060 1070 1080 1090 1100
PSYLLKMSCI ANLDVSRNDI GPSVVLDPTV KCPTLKQFNL SYNQLSFVPE
1110 1120 1130 1140 1150
NLTDVVEKLE QLILEGNKIS GICSPLRLKE LKILNLSKNH ISSLSENFLE
1160 1170 1180 1190 1200
ACPKVESFSA RMNFLAAMPF LPPSMTILKL SQNKFSCIPE AILNLPHLRS
1210 1220 1230 1240 1250
LDMSSNDIQY LPGPAHWKSL NLRELLFSHN QISILDLSEK AYLWSRVEKL
1260 1270 1280 1290 1300
HLSHNKLKEI PPEIGCLENL TSLDVSYNLE LRSFPNEMGK LSKIWDLPLD
1310 1320 1330 1340 1350
ELHLNFDFKH IGCKAKDIIR FLQQRLKKAV PYNRMKLMIV GNTGSGKTTL
1360 1370 1380 1390 1400
LQQLMKTKKS DLGMQSATVG IDVKDWPIQI RDKRKRDLVL NVWDFAGREE
1410 1420 1430 1440 1450
FYSTHPHFMT QRALYLAVYD LSKGQAEVDA MKPWLFNIKA RASSSPVILV
1460 1470 1480 1490 1500
GTHLDVSDEK QRKACMSKIT KELLNKRGFP AIRDYHFVNA TEESDALAKL
1510 1520 1530 1540 1550
RKTIINESLN FKIRDQLVVG QLIPDCYVEL EKIILSERKN VPIEFPVIDR
1560 1570 1580 1590 1600
KRLLQLVREN QLQLDENELP HAVHFLNESG VLLHFQDPAL QLSDLYFVEP
1610 1620 1630 1640 1650
KWLCKIMAQI LTVKVEGCPK HPKGIISRRD VEKFLSKKRK FPKNYMSQYF
1660 1670 1680 1690 1700
KLLEKFQIAL PIGEEYLLVP SSLSDHRPVI ELPHCENSEI IIRLYEMPYF
1710 1720 1730 1740 1750
PMGFWSRLIN RLLEISPYML SGRERALRPN RMYWRQGIYL NWSPEAYCLV
1760 1770 1780 1790 1800
GSEVLDNHPE SFLKITVPSC RKGCILLGQV VDHIDSLMEE WFPGLLEIDI
1810 1820 1830 1840 1850
CGEGETLLKK WALYSFNDGE EHQKILLDDL MKKAEEGDLL VNPDQPRLTI
1860 1870 1880 1890 1900
PISQIAPDLI LADLPRNIML NNDELEFEQA PEFLLGDGSF GSVYRAAYEG
1910 1920 1930 1940 1950
EEVAVKIFNK HTSLRLLRQE LVVLCHLHHP SLISLLAAGI RPRMLVMELA
1960 1970 1980 1990 2000
SKGSLDRLLQ QDKASLTRTL QHRIALHVAD GLRYLHSAMI IYRDLKPHNV
2010 2020 2030 2040 2050
LLFTLYPNAA IIAKIADYGI AQYCCRMGIK TSEGTPGFRA PEVARGNVIY
2060 2070 2080 2090 2100
NQQADVYSFG LLLYDILTTG GRIVEGLKFP NEFDELEIQG KLPDPVKEYG
2110 2120 2130 2140 2150
CAPWPMVEKL IKQCLKENPQ ERPTSAQVFD ILNSAELVCL TRRILLPKNV
2160 2170 2180 2190 2200
IVECMVATHH NSRNASIWLG CGHTDRGQLS FLDLNTEGYT SEEVADSRIL
2210 2220 2230 2240 2250
CLALVHLPVE KESWIVSGTQ SGTLLVINTE DGKKRHTLEK MTDSVTCLYC
2260 2270 2280 2290 2300
NSFSKQSKQK NFLLVGTADG KLAIFEDKTV KLKGAAPLKI LNIGNVSTPL
2310 2320 2330 2340 2350
MCLSESTNST ERNVMWGGCG TKIFSFSNDF TIQKLIETRT SQLFSYAAFS
2360 2370 2380 2390 2400
DSNIITVVVD TALYIAKQNS PVVEVWDKKT EKLCGLIDCV HFLREVMVKE
2410 2420 2430 2440 2450
NKESKHKMSY SGRVKTLCLQ KNTALWIGTG GGHILLLDLS TRRLIRVIYN
2460 2470 2480 2490 2500
FCNSVRVMMT AQLGSLKNVM LVLGYNRKNT EGTQKQKEIQ SCLTVWDINL
2510 2520
PHEVQNLEKH IEVRKELAEK MRRTSVE
Length:2,527
Mass (Da):286,103
Last modified:April 20, 2010 - v2
Checksum:i26142A0CECBBC3F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121L → S in AAV63975. (PubMed:15541309)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501R → H.
Corresponds to variant rs2256408 [ dbSNP | Ensembl ].
VAR_024931
Natural varianti119 – 1191L → P.2 Publications
Corresponds to variant rs33995463 [ dbSNP | Ensembl ].
VAR_024932
Natural varianti228 – 2281C → S.1 Publication
Corresponds to variant rs56108242 [ dbSNP | Ensembl ].
VAR_054740
Natural varianti419 – 4191A → V.1 Publication
Corresponds to variant rs34594498 [ dbSNP | Ensembl ].
VAR_033903
Natural varianti551 – 5511N → K.4 Publications
Corresponds to variant rs7308720 [ dbSNP | Ensembl ].
VAR_024933
Natural varianti712 – 7121M → V in PARK8. 1 Publication
VAR_054741
Natural varianti716 – 7161A → V.1 Publication
VAR_054742
Natural varianti723 – 7231I → V.3 Publications
Corresponds to variant rs10878307 [ dbSNP | Ensembl ].
VAR_024934
Natural varianti755 – 7551P → L.
Corresponds to variant rs34410987 [ dbSNP | Ensembl ].
VAR_033904
Natural varianti793 – 7931R → M in PARK8; unknown pathological significance. 3 Publications
Corresponds to variant rs35173587 [ dbSNP | Ensembl ].
VAR_024935
Natural varianti871 – 8711K → E.1 Publication
VAR_054743
Natural varianti930 – 9301Q → R in PARK8; unknown pathological significance. 1 Publication
VAR_024936
Natural varianti944 – 9441D → Y.
Corresponds to variant rs17519916 [ dbSNP | Ensembl ].
VAR_024937
Natural varianti1067 – 10671R → Q in PARK8. 1 Publication
VAR_024938
Natural varianti1096 – 10961S → C in PARK8; unknown pathological significance.
VAR_024939
Natural varianti1122 – 11221I → V in PARK8. 2 Publications
Corresponds to variant rs34805604 [ dbSNP | Ensembl ].
VAR_024940
Natural varianti1228 – 12281S → T in PARK8. 1 Publication
VAR_024941
Natural varianti1262 – 12621P → A.1 Publication
Corresponds to variant rs4640000 [ dbSNP | Ensembl ].
VAR_024942
Natural varianti1359 – 13591K → I Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064728
Natural varianti1371 – 13711I → V in PARK8; unknown pathological significance. 2 Publications
Corresponds to variant rs17466213 [ dbSNP | Ensembl ].
VAR_024943
Natural varianti1375 – 13751D → E.
Corresponds to variant rs28365226 [ dbSNP | Ensembl ].
VAR_047022
Natural varianti1398 – 13981R → H.4 Publications
Corresponds to variant rs7133914 [ dbSNP | Ensembl ].
VAR_024944
Natural varianti1441 – 14411R → C in PARK; shows an increase in activity in both autophosphorylation and phosphorylation of a generic substrate. 5 Publications
VAR_024945
Natural varianti1441 – 14411R → G in PARK8; shows a progressive reduction in neurite length and branching. 4 Publications
Corresponds to variant rs33939927 [ dbSNP | Ensembl ].
VAR_024946
Natural varianti1441 – 14411R → H in PARK8; pathogenicity has yet to be confirmed. 2 Publications
Corresponds to variant rs34995376 [ dbSNP | Ensembl ].
VAR_024947
Natural varianti1514 – 15141R → Q in PARK8; pathogenicity has yet to be confirmed; might have an effect on protein structure. 3 Publications
Corresponds to variant rs35507033 [ dbSNP | Ensembl ].
VAR_024948
Natural varianti1542 – 15421P → S in PARK8; pathogenicity has yet to be confirmed; might have an effect on protein structure. 3 Publications
Corresponds to variant rs33958906 [ dbSNP | Ensembl ].
VAR_024949
Natural varianti1550 – 15501R → Q in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
VAR_040678
Natural varianti1598 – 15981V → E in PARK8; pathogenicity has yet to be confirmed; might have an effect on protein structure. 1 Publication
Corresponds to variant rs721710 [ dbSNP | Ensembl ].
VAR_024950
Natural varianti1628 – 16281R → P May be associated with Parkinson disease in some populations. 2 Publications
Corresponds to variant rs33949390 [ dbSNP | Ensembl ].
VAR_024951
Natural varianti1646 – 16461M → T.2 Publications
Corresponds to variant rs35303786 [ dbSNP | Ensembl ].
VAR_024952
Natural varianti1647 – 16471S → T.2 Publications
Corresponds to variant rs11564148 [ dbSNP | Ensembl ].
VAR_024953
Natural varianti1699 – 16991Y → C in PARK8; shows no progressive reduction in neurite length and branching. 4 Publications
Corresponds to variant rs35801418 [ dbSNP | Ensembl ].
VAR_024954
Natural varianti1723 – 17231R → P in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
VAR_040679
Natural varianti1728 – 17281R → H in PARK8. 1 Publication
VAR_054744
Natural varianti1728 – 17281R → L in PARK8. 1 Publication
VAR_054745
Natural varianti1869 – 18691M → T in PARK8; pathogenicity has yet to be confirmed. 2 Publications
Corresponds to variant rs35602796 [ dbSNP | Ensembl ].
VAR_024955
Natural varianti1870 – 18701L → F.1 Publication
VAR_054746
Natural varianti1906 – 19061K → M Does not inhibit interaction with RAB29; shows a progressive increase in neurite length and branching. 1 Publication
VAR_071101
Natural varianti1941 – 19411R → H in PARK8. 1 Publication
VAR_024956
Natural varianti2012 – 20121I → T in PARK8; pathogenicity uncertain. 1 Publication
Corresponds to variant rs34015634 [ dbSNP | Ensembl ].
VAR_024957
Natural varianti2019 – 20191G → S in PARK8; shows an increase in activity in both autophosphorylation and phosphorylation of a generic substrate; results in increased PRDX3 phosphorylation promoting dysregulation of mitochondrial function and oxidative damage; does not inhibit interaction with RAB29; shows a progressive reduction in neurite length and branching; shows distinctive spheroid-like inclusions within both neuronal processes and at intracellular membranous structures; shows lysosomal swelling and reduced retrograde transport of selective cargo between lysosomes and the Golgi apparatus; shows apoptotic mechanism of cell death. 24 Publications
Corresponds to variant rs34637584 [ dbSNP | Ensembl ].
VAR_024958
Natural varianti2020 – 20201I → T in PARK8; significant increase in autophosphorylation of about 40% in comparison to wild-type protein in vitro; shows a progressive reduction in neurite length and branching. 4 Publications
Corresponds to variant rs35870237 [ dbSNP | Ensembl ].
VAR_024959
Natural varianti2081 – 20811N → D.2 Publications
Corresponds to variant rs33995883 [ dbSNP | Ensembl ].
VAR_024960
Natural varianti2119 – 21191P → L.1 Publication
Corresponds to variant rs12423862 [ dbSNP | Ensembl ].
VAR_024961
Natural varianti2141 – 21411T → M in PARK8. 1 Publication
VAR_054747
Natural varianti2143 – 21431R → H in PARK8. 1 Publication
VAR_054748
Natural varianti2261 – 22611N → I.1 Publication
Corresponds to variant rs12581902 [ dbSNP | Ensembl ].
VAR_024962
Natural varianti2356 – 23561T → I in PARK8. 1 Publication
VAR_024963
Natural varianti2385 – 23851G → R Associated with Parkinson disease; under conditions of oxidative stress the variant protein is more toxic and is associated with a higher rate of apoptosis. 1 Publication
Corresponds to variant rs34778348 [ dbSNP | Ensembl ].
VAR_024964
Natural varianti2395 – 23951E → K.1 Publication
VAR_054749
Natural varianti2397 – 23971M → T.3 Publications
Corresponds to variant rs3761863 [ dbSNP | Ensembl ].
VAR_024965
Natural varianti2466 – 24661L → H in PARK8. 1 Publication
VAR_054750

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY792511 mRNA. Translation: AAV63975.1.
AC079630 Genomic DNA. No translation available.
AC084290 Genomic DNA. No translation available.
AC107023 Genomic DNA. No translation available.
AL834529 mRNA. Translation: CAD39185.1.
CCDSiCCDS31774.1.
RefSeqiNP_940980.3. NM_198578.3.
UniGeneiHs.187636.

Genome annotation databases

EnsembliENST00000298910; ENSP00000298910; ENSG00000188906.
GeneIDi120892.
KEGGihsa:120892.
UCSCiuc001rmg.4. human.

Polymorphism databases

DMDMi294862450.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY792511 mRNA. Translation: AAV63975.1 .
AC079630 Genomic DNA. No translation available.
AC084290 Genomic DNA. No translation available.
AC107023 Genomic DNA. No translation available.
AL834529 mRNA. Translation: CAD39185.1 .
CCDSi CCDS31774.1.
RefSeqi NP_940980.3. NM_198578.3.
UniGenei Hs.187636.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZEJ X-ray 2.00 A/B 1333-1516 [» ]
3D6T X-ray 2.43 B 1335-1505 [» ]
ProteinModelPortali Q5S007.
SMRi Q5S007. Positions 1335-1512.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125700. 139 interactions.
DIPi DIP-29684N.
IntActi Q5S007. 527 interactions.
MINTi MINT-7997594.
STRINGi 9606.ENSP00000298910.

Chemistry

BindingDBi Q5S007.
ChEMBLi CHEMBL1075104.
GuidetoPHARMACOLOGYi 2059.

PTM databases

PhosphoSitei Q5S007.

Polymorphism databases

DMDMi 294862450.

Proteomic databases

MaxQBi Q5S007.
PaxDbi Q5S007.
PRIDEi Q5S007.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000298910 ; ENSP00000298910 ; ENSG00000188906 .
GeneIDi 120892.
KEGGi hsa:120892.
UCSCi uc001rmg.4. human.

Organism-specific databases

CTDi 120892.
GeneCardsi GC12P040590.
GeneReviewsi LRRK2.
HGNCi HGNC:18618. LRRK2.
HPAi CAB037160.
HPA014293.
MIMi 168600. phenotype.
607060. phenotype.
609007. gene.
neXtProti NX_Q5S007.
Orphaneti 2828. Young adult-onset Parkinsonism.
PharmGKBi PA134968052.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4886.
GeneTreei ENSGT00530000063477.
HOGENOMi HOG000293315.
HOVERGENi HBG081937.
InParanoidi Q5S007.
KOi K08844.
OMAi FKIRDQP.
PhylomeDBi Q5S007.
TreeFami TF313679.

Enzyme and pathway databases

SignaLinki Q5S007.

Miscellaneous databases

ChiTaRSi LRRK2. human.
EvolutionaryTracei Q5S007.
GeneWikii LRRK2.
GenomeRNAii 120892.
NextBioi 80641.
PROi Q5S007.
SOURCEi Search...

Gene expression databases

Bgeei Q5S007.
CleanExi HS_LRRK2.
ExpressionAtlasi Q5S007. baseline and differential.
Genevestigatori Q5S007.

Family and domain databases

Gene3Di 1.25.10.10. 2 hits.
1.25.40.20. 1 hit.
2.130.10.10. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR020683. Ankyrin_rpt-contain_dom.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR020859. ROC_GTPase.
IPR008271. Ser/Thr_kinase_AS.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF13855. LRR_8. 1 hit.
PF08477. Miro. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00369. LRR_TYP. 1 hit.
SM00320. WD40. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
SSF50978. SSF50978. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56112. SSF56112. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51450. LRR. 11 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS51424. ROC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS PARK8 VAL-1122; CYS-1441; CYS-1699 AND THR-2020.
    Tissue: Brain.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2128-2527.
    Tissue: Testis.
  4. "PET in LRRK2 mutations: comparison to sporadic Parkinson's disease and evidence for presymptomatic compensation."
    Adams J.R., van Netten H., Schulzer M., Mak E., McKenzie J., Strongosky A., Sossi V., Ruth T.J., Lee C.S., Farrer M., Gasser T., Uitti R.J., Calne D.B., Wszolek Z.K., Stoessl A.J.
    Brain 128:2777-2785(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE.
  5. "The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity."
    Gloeckner C.J., Kinkl N., Schumacher A., Braun R.J., O'Neill E., Meitinger T., Kolch W., Prokisch H., Ueffing M.
    Hum. Mol. Genet. 15:223-232(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PARK8 THR-2020.
  6. Cited for: DISEASE.
  7. "Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity."
    West A.B., Moore D.J., Biskup S., Bugayenko A., Smith W.W., Ross C.A., Dawson V.L., Dawson T.M.
    Proc. Natl. Acad. Sci. U.S.A. 102:16842-16847(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS PARK8 CYS-1441 AND SER-2019.
  8. "Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin and mutant LRRK2 induces neuronal degeneration."
    Smith W.W., Pei Z., Jiang H., Moore D.J., Liang Y., West A.B., Dawson V.L., Dawson T.M., Ross C.A.
    Proc. Natl. Acad. Sci. U.S.A. 102:18676-18681(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PARK2, POSSIBLE FUNCTION.
  9. Cited for: TISSUE SPECIFICITY.
  10. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. "The familial Parkinsonism gene LRRK2 regulates neurite process morphology."
    MacLeod D., Dowman J., Hammond R., Leete T., Inoue K., Abeliovich A.
    Neuron 52:587-593(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF VARIANTS PARK8 GLY-1441; CYS-1699; SER-2019 AND THR-2020, VARIANT MET-1906.
  12. "Signal transduction protein array analysis links LRRK2 to Ste20 kinases and PKC zeta that modulate neuronal plasticity."
    Zach S., Felk S., Gillardon F.
    PLoS ONE 5:E13191-E13191(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death."
    Angeles D.C., Gan B.H., Onstead L., Zhao Y., Lim K.L., Dachsel J., Melrose H., Farrer M., Wszolek Z.K., Dickson D.W., Tan E.K.
    Hum. Mutat. 32:1390-1397(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRDX3, CHARACTERIZATION OF VARIANT PARK8 SER-2019.
  14. "Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP."
    Gomez-Suaga P., Luzon-Toro B., Churamani D., Zhang L., Bloor-Young D., Patel S., Woodman P.G., Churchill G.C., Hilfiker S.
    Hum. Mol. Genet. 21:511-525(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TPCN2.
  15. "Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimers."
    Civiero L., Vancraenenbroeck R., Belluzzi E., Beilina A., Lobbestael E., Reyniers L., Gao F., Micetic I., De Maeyer M., Bubacco L., Baekelandt V., Cookson M.R., Greggio E., Taymans J.M.
    PLoS ONE 7:E43472-E43472(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, AUTOPHOSPHORYLATION.
  16. "RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson's disease risk."
    MacLeod D.A., Rhinn H., Kuwahara T., Zolin A., Di Paolo G., McCabe B.D., MacCabe B.D., Marder K.S., Honig L.S., Clark L.N., Small S.A., Abeliovich A.
    Neuron 77:425-439(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RETROGRADE TRANSPORT, INTERACTION WITH RAB29 AND VPS35, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PARK8 SER-2019, CHARACTERIZATION OF VARIANT MET-1906.
  17. Cited for: VARIANTS PARK8 GLY-1441 AND CYS-1699, TISSUE SPECIFICITY.
  18. "Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations."
    Kachergus J.M., Mata I.F., Hulihan M., Taylor J.P., Lincoln S., Aasly J.O., Gibson J.M., Ross O.A., Lynch T., Wiley J., Payami H., Nutt J., Maraganore D.M., Czyzewski K., Styczynska M., Wszolek Z.K., Farrer M.J., Toft M.
    Am. J. Hum. Genet. 76:672-680(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK8 SER-2019.
  19. Cited for: VARIANT PARK8 SER-2019.
  20. "Clinical features of LRRK2-associated Parkinson's disease in central Norway."
    Aasly J.O., Toft M., Fernandez-Mata I., Kachergus J.M., Hulihan M., White L.R., Farrer M.J.
    Ann. Neurol. 57:762-765(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK8/PD SER-2019.
  21. Cited for: VARIANT PARK8 SER-2019.
  22. "An LRRK2 mutation as a cause for the parkinsonism in the original PARK8 family."
    Funayama M., Hasegawa K., Ohta E., Kawashima N., Komiyama M., Kowa H., Tsuji S., Obata F.
    Ann. Neurol. 57:918-921(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK8 THR-2020.
  23. "Genetic and clinical identification of Parkinson's disease patients with LRRK2 G2019S mutation."
    Deng H., Le W., Guo Y., Hunter C.B., Xie W., Jankovic J.
    Ann. Neurol. 57:933-934(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK8 SER-2019.
  24. "Type and frequency of mutations in the LRRK2 gene in familial and sporadic Parkinson's disease."
    Berg D., Schweitzer K., Leitner P., Zimprich A., Lichtner P., Belcredi P., Bruessel T., Schulte C., Maass S., Naegele T.
    Brain 128:3000-3011(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PARK8 MET-793; ARG-930; CYS-1096 THR-1228; SER-2019 AND THR-2020, VARIANT LYS-551.
  25. "Mutations in the gene LRRK2 encoding dardarin (PARK8) cause familial Parkinson's disease: clinical, pathological, olfactory and functional imaging and genetic data."
    Khan N.L., Jain S., Lynch J.M., Pavese N., Abou-Sleiman P.M., Holton J.L., Healy D.G., Gilks W.P., Sweeney M.G., Ganguly M., Gibbons V., Gandhi S., Vaughan J., Eunson L.H., Katzenschlager R., Gayton J., Lennox G., Revesz T.
    , Nicholl D., Bhatia K.P., Quinn N., Brooks D., Lees A.J., Davis M.B., Piccini P., Singleton A.B., Wood N.W.
    Brain 128:2786-2796(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PARK8 CYS-1699; HIS-1941; SER-2019 AND ILE-2356.
  26. Cited for: VARIANTS PARK8 VAL-1371; CYS-1441 AND SER-2019.
  27. Cited for: VARIANT PARK8 SER-2019.
  28. Cited for: VARIANT PARK8 SER-2019.
  29. Cited for: VARIANT PARK8 SER-2019.
  30. Cited for: VARIANT PARK8 SER-2019.
  31. Cited for: VARIANT PARK8 SER-2019.
  32. "Escaping Parkinson's disease: a neurologically healthy octogenarian with the LRRK2 G2019S mutation."
    Kay D.M., Kramer P., Higgins D.S., Zabetian C.P., Payami H.
    Mov. Disord. 20:1077-1078(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-2019.
  33. "Parkinson's disease and LRRK2: frequency of a common mutation in U.S. movement disorder clinics."
    Kay D.M., Zabetian C.P., Factor S.A., Nutt J.G., Samii A., Griffith A., Bird T.D., Kramer P., Higgins D.S., Payami H.
    Mov. Disord. 21:519-523(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK8 SER-2019.
  34. Cited for: VARIANTS PARK8 CYS-1441; GLY-1441; HIS-1441; GLN-1514; SER-1542; GLU-1598; CYS-1699; THR-1869; THR-2012; SER-2019; THR-2020 AND ARG-2385, VARIANTS PRO-119; LYS-551; VAL-723; MET-793; VAL-1122; ALA-1262; HIS-1398; PRO-1628; THR-1646; THR-1647; ASP-2081; LEU-2119; ILE-2261 AND THR-2397.
  35. Cited for: VARIANTS PARK8 VAL-1371 AND SER-2019, VARIANTS HIS-1398 AND THR-2397.
  36. Cited for: VARIANT PARK8 GLN-1067.
  37. Cited for: VARIANTS PARK8 MET-793; THR-1869 AND SER-2019.
  38. "A clinic-based study of the LRRK2 gene in Parkinson disease yields new mutations."
    Zabetian C.P., Samii A., Mosley A.D., Roberts J.W., Leis B.C., Yearout D., Raskind W.H., Griffith A.
    Neurology 65:741-744(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PARK8 CYS-1441; HIS-1441 AND SER-2019.
  39. Cited for: VARIANT PARK8 GLY-1441.
  40. "LRRK2 G2019S is a common mutation in Spanish patients with late-onset Parkinson's disease."
    Infante J., Rodriguez E., Combarros O., Mateo I., Fontalba A., Pascual J., Oterino A., Polo J.M., Leno C., Berciano J.
    Neurosci. Lett. 395:224-226(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK8 SER-2019.
  41. "Clinical traits of LRRK2-associated Parkinson's disease in Ireland: a link between familial and idiopathic PD."
    Gosal D., Ross O.A., Wiley J., Irvine G.B., Johnston J.A., Toft M., Mata I.F., Kachergus J., Hulihan M., Taylor J.P., Lincoln S.J., Farrer M.J., Lynch T., Mark Gibson J.
    Parkinsonism Relat. Disord. 11:349-352(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK8 SER-2019.
  42. "LRRK2 mutations in Spanish patients with Parkinson disease: frequency, clinical features, and incomplete penetrance."
    Gaig C., Ezquerra M., Marti M.J., Munoz E., Valldeoriola F., Tolosa E.
    Arch. Neurol. 63:377-382(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PARK8 CYS-1441; GLY-1441 AND SER-2019.
  43. "The LRRK2 Gly2385Arg variant is associated with Parkinson's disease: genetic and functional evidence."
    Tan E.K., Zhao Y., Skipper L., Tan M.G., Di Fonzo A., Sun L., Fook-Chong S., Tang S., Chua E., Yuen Y., Tan L., Pavanni R., Wong M.C., Kolatkar P., Lu C.S., Bonifati V., Liu J.J.