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Leucine-rich repeat serine/threonine-protein kinase 2 (EC 2.7.11.1) (Dardarin)

 LRRK2_HUMAN             Reviewed;        2527 AA.
Q5S007; A6NJU2; Q6ZS50; Q8NCX9;
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 2.
30-AUG-2017, entry version 147.
RecName: Full=Leucine-rich repeat serine/threonine-protein kinase 2;
EC=2.7.11.1;
AltName: Full=Dardarin;
Name=LRRK2; Synonyms=PARK8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS PARK8
VAL-1122; CYS-1441; CYS-1699 AND THR-2020.
TISSUE=Brain;
PubMed=15541309; DOI=10.1016/j.neuron.2004.11.005;
Zimprich A., Biskup S., Leitner P., Lichtner P., Farrer M.,
Lincoln S.J., Kachergus J.M., Hulihan M.M., Uitti R.J., Calne D.B.,
Stoessl A.J., Pfeiffer R.F., Patenge N., Carballo Carbajal I.,
Vieregge P., Asmus F., Mueller-Myhsok B., Dickson D.W., Meitinger T.,
Strom T.M., Wszolek Z.K., Gasser T.;
"Mutations in LRRK2 cause autosomal-dominant parkinsonism with
pleomorphic pathology.";
Neuron 44:601-607(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2128-2527.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
DISEASE.
PubMed=16081470; DOI=10.1093/brain/awh607;
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.;
"PET in LRRK2 mutations: comparison to sporadic Parkinson's disease
and evidence for presymptomatic compensation.";
Brain 128:2777-2785(2005).
[5]
SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT PARK8 THR-2020.
PubMed=16321986; DOI=10.1093/hmg/ddi439;
Gloeckner C.J., Kinkl N., Schumacher A., Braun R.J., O'Neill E.,
Meitinger T., Kolch W., Prokisch H., Ueffing M.;
"The Parkinson disease causing LRRK2 mutation I2020T is associated
with increased kinase activity.";
Hum. Mol. Genet. 15:223-232(2006).
[6]
DISEASE.
PubMed=16087219; DOI=10.1016/j.mad.2005.06.010;
Toft M., Sando S.B., Melquist S., Ross O.A., White L.R., Aasly J.O.,
Farrer M.J.;
"LRRK2 mutations are not common in Alzheimer's disease.";
Mech. Ageing Dev. 126:1201-1205(2005).
[7]
SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS PARK8 CYS-1441
AND SER-2019.
PubMed=16269541; DOI=10.1073/pnas.0507360102;
West A.B., Moore D.J., Biskup S., Bugayenko A., Smith W.W., Ross C.A.,
Dawson V.L., Dawson T.M.;
"Parkinson's disease-associated mutations in leucine-rich repeat
kinase 2 augment kinase activity.";
Proc. Natl. Acad. Sci. U.S.A. 102:16842-16847(2005).
[8]
SUBCELLULAR LOCATION, INTERACTION WITH PRKN, AND POSSIBLE FUNCTION.
PubMed=16352719; DOI=10.1073/pnas.0508052102;
Smith W.W., Pei Z., Jiang H., Moore D.J., Liang Y., West A.B.,
Dawson V.L., Dawson T.M., Ross C.A.;
"Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin and mutant
LRRK2 induces neuronal degeneration.";
Proc. Natl. Acad. Sci. U.S.A. 102:18676-18681(2005).
[9]
TISSUE SPECIFICITY.
PubMed=16532471; DOI=10.1002/ana.20808;
Galter D., Westerlund M., Carmine A., Lindqvist E., Sydow O.,
Olson L.;
"LRRK2 expression linked to dopamine-innervated areas.";
Ann. Neurol. 59:714-719(2006).
[10]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17120249; DOI=10.1002/ana.21019;
Biskup S., Moore D.J., Celsi F., Higashi S., West A.B., Andrabi S.A.,
Kurkinen K., Yu S.W., Savitt J.M., Waldvogel H.J., Faull R.L.,
Emson P.C., Torp R., Ottersen O.P., Dawson T.M., Dawson V.L.;
"Localization of LRRK2 to membranous and vesicular structures in
mammalian brain.";
Ann. Neurol. 60:557-569(2006).
[11]
FUNCTION, CHARACTERIZATION OF VARIANTS PARK8 GLY-1441; CYS-1699;
SER-2019 AND THR-2020, AND VARIANT MET-1906.
PubMed=17114044; DOI=10.1016/j.neuron.2006.10.008;
MacLeod D., Dowman J., Hammond R., Leete T., Inoue K., Abeliovich A.;
"The familial Parkinsonism gene LRRK2 regulates neurite process
morphology.";
Neuron 52:587-593(2006).
[12]
FUNCTION.
PubMed=20949042; DOI=10.1371/journal.pone.0013191;
Zach S., Felk S., Gillardon F.;
"Signal transduction protein array analysis links LRRK2 to Ste20
kinases and PKC zeta that modulate neuronal plasticity.";
PLoS ONE 5:E13191-E13191(2010).
[13]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRDX3, AND
CHARACTERIZATION OF VARIANT PARK8 SER-2019.
PubMed=21850687; DOI=10.1002/humu.21582;
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.;
"Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3
exacerbating oxidative stress-induced neuronal death.";
Hum. Mutat. 32:1390-1397(2011).
[14]
FUNCTION, AND INTERACTION WITH TPCN2.
PubMed=22012985; DOI=10.1093/hmg/ddr481;
Gomez-Suaga P., Luzon-Toro B., Churamani D., Zhang L., Bloor-Young D.,
Patel S., Woodman P.G., Churchill G.C., Hilfiker S.;
"Leucine-rich repeat kinase 2 regulates autophagy through a calcium-
dependent pathway involving NAADP.";
Hum. Mol. Genet. 21:511-525(2012).
[15]
SUBUNIT, AND AUTOPHOSPHORYLATION.
PubMed=22952686; DOI=10.1371/journal.pone.0043472;
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.;
"Biochemical characterization of highly purified leucine-rich repeat
kinases 1 and 2 demonstrates formation of homodimers.";
PLoS ONE 7:E43472-E43472(2012).
[16]
FUNCTION IN RETROGRADE TRANSPORT, INTERACTION WITH RAB29 AND VPS35,
SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PARK8 SER-2019, AND
CHARACTERIZATION OF VARIANT MET-1906.
PubMed=23395371; DOI=10.1016/j.neuron.2012.11.033;
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.;
"RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting
and Parkinson's disease risk.";
Neuron 77:425-439(2013).
[17]
WD REPEATS.
PubMed=23776530; DOI=10.1371/journal.pone.0065705;
Wang Y., Jiang F., Zhuo Z., Wu X.H., Wu Y.D.;
"A method for WD40 repeat detection and secondary structure
prediction.";
PLoS ONE 8:E65705-E65705(2013).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
FUNCTION, SUBCELLULAR LOCATION, ELECTRON MICROSCOPY, WD REPEATS, AND
CHARACTERIZATION OF VARIANT ARG-2385.
PubMed=24687852; DOI=10.1128/MCB.00914-13;
Piccoli G., Onofri F., Cirnaru M.D., Kaiser C.J., Jagtap P.,
Kastenmuller A., Pischedda F., Marte A., von Zweydorf F., Vogt A.,
Giesert F., Pan L., Antonucci F., Kiel C., Zhang M., Weinkauf S.,
Sattler M., Sala C., Matteoli M., Ueffing M., Gloeckner C.J.;
"Leucine-rich repeat kinase 2 binds to neuronal vesicles through
protein interactions mediated by its C-terminal WD40 domain.";
Mol. Cell. Biol. 34:2147-2161(2014).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1333-1516 IN COMPLEX WITH
GDP, FUNCTION, GTPASE ACTIVITY, SUBUNIT, DOMAIN ROC, AND MUTAGENESIS
OF THR-1343 AND ARG-1398.
PubMed=18230735; DOI=10.1073/pnas.0709098105;
Deng J., Lewis P.A., Greggio E., Sluch E., Beilina A., Cookson M.R.;
"Structure of the ROC domain from the Parkinson's disease-associated
leucine-rich repeat kinase 2 reveals a dimeric GTPase.";
Proc. Natl. Acad. Sci. U.S.A. 105:1499-1504(2008).
[21]
VARIANTS PARK8 GLY-1441 AND CYS-1699, AND TISSUE SPECIFICITY.
PubMed=15541308; DOI=10.1016/j.neuron.2004.10.023;
Paisan-Ruiz C., Jain S., Evans E.W., Gilks W.P., Simon J.,
van der Brug M., Lopez de Munain A., Aparicio S., Gil A.M., Khan N.L.,
Johnson J., Martinez J.R., Nicholl D., Carrera I.M., Pena A.S.,
de Silva R., Lees A.J., Marti-Masso J.F., Perez-Tur J., Wood N.W.,
Singleton A.B.;
"Cloning of the gene containing mutations that cause PARK8-linked
Parkinson's disease.";
Neuron 44:595-600(2004).
[22]
VARIANT PARK8 SER-2019.
PubMed=15726496; DOI=10.1086/429256;
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.;
"Identification of a novel LRRK2 mutation linked to autosomal dominant
parkinsonism: evidence of a common founder across European
populations.";
Am. J. Hum. Genet. 76:672-680(2005).
[23]
VARIANT PARK8 SER-2019.
PubMed=15732108; DOI=10.1002/ana.20401;
Hernandez D.G., Paisan-Ruiz C., McInerney-Leo A., Jain S.,
Meyer-Lindenberg A., Evans E.W., Berman K.F., Johnson J., Auburger G.,
Schaeffer A.A., Lopez G.J., Nussbaum R.L., Singleton A.B.;
"Clinical and positron emission tomography of Parkinson's disease
caused by LRRK2.";
Ann. Neurol. 57:453-456(2005).
[24]
VARIANT PARK8/PD SER-2019.
PubMed=15852371; DOI=10.1002/ana.20456;
Aasly J.O., Toft M., Fernandez-Mata I., Kachergus J.M., Hulihan M.,
White L.R., Farrer M.J.;
"Clinical features of LRRK2-associated Parkinson's disease in central
Norway.";
Ann. Neurol. 57:762-765(2005).
[25]
VARIANT PARK8 SER-2019.
PubMed=16240353; DOI=10.1002/ana.20636;
French Parkinson's disease genetics study group;
Lesage S., Ibanez P., Lohmann E., Pollak P., Tison F., Tazir M.,
Leutenegger A.-L., Guimaraes J., Bonnet A.-M., Agid Y., Duerr A.,
Brice A.;
"G2019S LRRK2 mutation in French and North African families with
Parkinson's disease.";
Ann. Neurol. 58:784-787(2005).
[26]
VARIANT PARK8 THR-2020.
PubMed=15880653; DOI=10.1002/ana.20484;
Funayama M., Hasegawa K., Ohta E., Kawashima N., Komiyama M., Kowa H.,
Tsuji S., Obata F.;
"An LRRK2 mutation as a cause for the parkinsonism in the original
PARK8 family.";
Ann. Neurol. 57:918-921(2005).
[27]
VARIANT PARK8 SER-2019.
PubMed=15929036; DOI=10.1002/ana.20510;
Deng H., Le W., Guo Y., Hunter C.B., Xie W., Jankovic J.;
"Genetic and clinical identification of Parkinson's disease patients
with LRRK2 G2019S mutation.";
Ann. Neurol. 57:933-934(2005).
[28]
VARIANTS PARK8 MET-793; ARG-930; CYS-1096 THR-1228; SER-2019 AND
THR-2020, AND VARIANT LYS-551.
PubMed=16251215; DOI=10.1093/brain/awh666;
Berg D., Schweitzer K., Leitner P., Zimprich A., Lichtner P.,
Belcredi P., Bruessel T., Schulte C., Maass S., Naegele T.;
"Type and frequency of mutations in the LRRK2 gene in familial and
sporadic Parkinson's disease.";
Brain 128:3000-3011(2005).
[29]
VARIANTS PARK8 CYS-1699; HIS-1941; SER-2019 AND ILE-2356.
PubMed=16272164; DOI=10.1093/brain/awh667;
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.;
"Mutations in the gene LRRK2 encoding dardarin (PARK8) cause familial
Parkinson's disease: clinical, pathological, olfactory and functional
imaging and genetic data.";
Brain 128:2786-2796(2005).
[30]
VARIANTS PARK8 VAL-1371; CYS-1441 AND SER-2019.
PubMed=16333314; DOI=10.1038/sj.ejhg.5201539;
Di Fonzo A., Tassorelli C., De Mari M., Chien H.F., Ferreira J.,
Rohe C.F., Riboldazzi G., Antonini A., Albani G., Mauro A.,
Marconi R., Abbruzzese G., Lopiano L., Fincati E., Guidi M.,
Marini P., Stocchi F., Onofrj M., Toni V., Tinazzi M., Fabbrini G.,
Lamberti P., Vanacore N., Meco G., Leitner P., Uitti R.J.,
Wszolek Z.K., Gasser T., Simons E.J., Breedveld G.J., Goldwurm S.,
Pezzoli G., Sampaio C., Barbosa E., Martignoni E., Oostra B.A.,
Bonifati V.;
"Comprehensive analysis of the LRRK2 gene in sixty families with
Parkinson's disease.";
Eur. J. Hum. Genet. 14:322-331(2006).
[31]
VARIANT PARK8 SER-2019.
PubMed=16272257; DOI=10.1136/jmg.2005.035568;
Goldwurm S., Di Fonzo A., Simons E.J., Rohe C.F., Zini M., Canesi M.,
Tesei S., Zecchinelli A., Antonini A., Mariani C., Meucci N.,
Sacilotto G., Sironi F., Salani G., Ferreira J., Chien H.F.,
Fabrizio E., Vanacore N., Dalla Libera A., Stocchi F., Diroma C.,
Lamberti P., Sampaio C., Meco G., Barbosa E., Bertoli-Avella A.M.,
Breedveld G.J., Oostra B.A., Pezzoli G., Bonifati V.;
"The G6055A (G2019S) mutation in LRRK2 is frequent in both early and
late onset Parkinson's disease and originates from a common
ancestor.";
J. Med. Genet. 42:E65-E65(2005).
[32]
VARIANT PARK8 SER-2019.
PubMed=15680455; DOI=10.1016/S0140-6736(05)70235-X;
The Parkinson study group-PROGENI investigators;
Nichols W.C., Pankratz N., Hernandez D., Paisan-Ruiz C., Jain S.,
Halter C.A., Michaels V.E., Reed T., Rudolph A., Shults C.W.,
Singleton A., Foroud T.;
"Genetic screening for a single common LRRK2 mutation in familial
Parkinson's disease.";
Lancet 365:410-412(2005).
[33]
VARIANT PARK8 SER-2019.
PubMed=15680456; DOI=10.1016/S0140-6736(05)70236-1;
The Italian Parkinson genetics network;
Di Fonzo A., Rohe C.F., Ferreira J., Chien H.F., Vacca L., Stocchi F.,
Guedes L., Fabrizio E., Manfredi M., Vanacore N., Goldwurm S.,
Breedveld G.J., Sampaio C., Meco G., Barbosa E., Oostra B.A.,
Bonifati V.;
"A frequent LRRK2 gene mutation associated with autosomal dominant
Parkinson's disease.";
Lancet 365:412-415(2005).
[34]
VARIANT PARK8 SER-2019.
PubMed=15680457; DOI=10.1016/S0140-6736(05)70237-3;
Gilks W.P., Abou-Sleiman P.M., Gandhi S., Jain S., Singleton A.,
Lees A.J., Shaw K., Bhatia K.P., Bonifati V., Quinn N.P., Lynch J.M.,
Healy D.G., Holton J.L., Revesz T., Wood N.W.;
"A common LRRK2 mutation in idiopathic Parkinson's disease.";
Lancet 365:415-416(2005).
[35]
VARIANT PARK8 SER-2019.
PubMed=15811454; DOI=10.1016/S0140-6736(05)74809-1;
Toft M., Mata I.F., Kachergus J.M., Ross O.A., Farrer M.J.;
"LRRK2 mutations and Parkinsonism.";
Lancet 365:1229-1230(2005).
[36]
VARIANT SER-2019.
PubMed=16001413; DOI=10.1002/mds.20618;
Kay D.M., Kramer P., Higgins D.S., Zabetian C.P., Payami H.;
"Escaping Parkinson's disease: a neurologically healthy octogenarian
with the LRRK2 G2019S mutation.";
Mov. Disord. 20:1077-1078(2005).
[37]
VARIANT PARK8 SER-2019.
PubMed=16250030; DOI=10.1002/mds.20751;
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.;
"Parkinson's disease and LRRK2: frequency of a common mutation in U.S.
movement disorder clinics.";
Mov. Disord. 21:519-523(2006).
[38]
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, AND 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.
PubMed=16172858; DOI=10.1007/s10048-005-0005-1;
Mata I.F., Kachergus J.M., Taylor J.P., Lincoln S., Aasly J.,
Lynch T., Hulihan M.M., Cobb S.A., Wu R.-M., Lu C.-S., Lahoz C.,
Wszolek Z.K., Farrer M.J.;
"Lrrk2 pathogenic substitutions in Parkinson's disease.";
Neurogenetics 6:171-177(2005).
[39]
VARIANTS PARK8 VAL-1371 AND SER-2019, AND VARIANTS HIS-1398 AND
THR-2397.
PubMed=16157901; DOI=10.1212/01.WNL.0000167552.79769.b3;
Paisan-Ruiz C., Lang A.E., Kawarai T., Sato C., Salehi-Rad S.,
Fisman G.K., Al-Khairallah T., St George-Hyslop P.H., Singleton A.,
Rogaeva E.;
"LRRK2 gene in Parkinson disease: mutation analysis and case control
association study.";
Neurology 65:696-700(2005).
[40]
VARIANT PARK8 GLN-1067.
PubMed=16247070; DOI=10.1212/01.wnl.0000180517.70572.37;
Skipper L., Shen H., Chua E., Bonnard C., Kolatkar P., Tan L.C.S.,
Jamora R.D., Puvan K., Puong K.Y., Zhao Y., Pavanni R., Wong M.C.,
Yuen Y., Farrer M., Liu J.J., Tan E.K.;
"Analysis of LRRK2 functional domains in nondominant Parkinson
disease.";
Neurology 65:1319-1321(2005).
[41]
VARIANTS PARK8 MET-793; THR-1869 AND SER-2019.
PubMed=16157908; DOI=10.1212/01.WNL.0000169023.51764.b0;
Farrer M., Stone J., Mata I.F., Lincoln S., Kachergus J., Hulihan M.,
Strain K.J., Maraganore D.M.;
"LRRK2 mutations in Parkinson disease.";
Neurology 65:738-740(2005).
[42]
VARIANTS PARK8 CYS-1441; HIS-1441 AND SER-2019.
PubMed=16157909; DOI=10.1212/01.WNL.0000172630.22804.73;
Zabetian C.P., Samii A., Mosley A.D., Roberts J.W., Leis B.C.,
Yearout D., Raskind W.H., Griffith A.;
"A clinic-based study of the LRRK2 gene in Parkinson disease yields
new mutations.";
Neurology 65:741-744(2005).
[43]
VARIANT PARK8 GLY-1441.
PubMed=15925109; DOI=10.1016/j.neulet.2005.03.033;
Mata I.F., Taylor J.P., Kachergus J., Hulihan M., Huerta C., Lahoz C.,
Blazquez M., Guisasola L.M., Salvador C., Ribacoba R., Martinez C.,
Farrer M., Alvarez V.;
"LRRK2 R1441G in Spanish patients with Parkinson's disease.";
Neurosci. Lett. 382:309-311(2005).
[44]
VARIANT PARK8 SER-2019.
PubMed=16298482; DOI=10.1016/j.neulet.2005.10.083;
Infante J., Rodriguez E., Combarros O., Mateo I., Fontalba A.,
Pascual J., Oterino A., Polo J.M., Leno C., Berciano J.;
"LRRK2 G2019S is a common mutation in Spanish patients with late-onset
Parkinson's disease.";
Neurosci. Lett. 395:224-226(2006).
[45]
VARIANT PARK8 SER-2019.
PubMed=16102999; DOI=10.1016/j.parkreldis.2005.05.004;
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.;
"Clinical traits of LRRK2-associated Parkinson's disease in Ireland: a
link between familial and idiopathic PD.";
Parkinsonism Relat. Disord. 11:349-352(2005).
[46]
VARIANTS PARK8 CYS-1441; GLY-1441 AND SER-2019.
PubMed=16533964; DOI=10.1001/archneur.63.3.377;
Gaig C., Ezquerra M., Marti M.J., Munoz E., Valldeoriola F.,
Tolosa E.;
"LRRK2 mutations in Spanish patients with Parkinson disease:
frequency, clinical features, and incomplete penetrance.";
Arch. Neurol. 63:377-382(2006).
[47]
CHARACTERIZATION OF VARIANT ARG-2385, AND ASSOCIATION WITH PARKINSON
DISEASE.
PubMed=17019612; DOI=10.1007/s00439-006-0268-0;
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.;
"The LRRK2 Gly2385Arg variant is associated with Parkinson's disease:
genetic and functional evidence.";
Hum. Genet. 120:857-863(2007).
[48]
VARIANTS [LARGE SCALE ANALYSIS] PRO-119; VAL-419; LYS-551; VAL-723;
HIS-1398; GLN-1514; SER-1542; GLN-1550 AND PRO-1723.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[49]
VARIANTS PARK8 VAL-712; LEU-1728; HIS-1728; SER-2019; MET-2141;
HIS-2143 AND HIS-2466, AND VARIANTS SER-228; VAL-716; GLU-871;
PHE-1870 AND LYS-2395.
PubMed=18213618; DOI=10.1002/humu.20668;
Paisan-Ruiz C., Nath P., Washecka N., Gibbs J.R., Singleton A.B.;
"Comprehensive analysis of LRRK2 in publicly available Parkinson's
disease cases and neurologically normal controls.";
Hum. Mutat. 29:485-490(2008).
[50]
VARIANT ILE-1359.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
[51]
ASSOCIATION OF VARIANTS PRO-1628 AND ARG-2385 WITH PARKINSON DISEASE.
PubMed=21641266; DOI=10.1016/j.parkreldis.2010.11.008;
Bardien S., Lesage S., Brice A., Carr J.;
"Genetic characteristics of leucine-rich repeat kinase 2 (LRRK2)
associated Parkinson's disease.";
Parkinsonism Relat. Disord. 17:501-508(2011).
[52]
VARIANTS LYS-551; VAL-723; HIS-1398; GLN-1514; SER-1542; PRO-1628;
THR-1646; THR-1647; ASP-2081 AND THR-2397.
PubMed=22415848; DOI=10.1002/humu.22075;
Rubio J.P., Topp S., Warren L., St Jean P.L., Wegmann D., Kessner D.,
Novembre J., Shen J., Fraser D., Aponte J., Nangle K., Cardon L.R.,
Ehm M.G., Chissoe S.L., Whittaker J.C., Nelson M.R., Mooser V.E.;
"Deep sequencing of the LRRK2 gene in 14,002 individuals reveals
evidence of purifying selection and independent origin of the
p.Arg1628Pro mutation in Europe.";
Hum. Mutat. 33:1087-1098(2012).
[53]
VARIANT PARK8 SER-2019.
PubMed=22956510; DOI=10.1002/mds.25132;
Kilarski L.L., Pearson J.P., Newsway V., Majounie E., Knipe M.D.,
Misbahuddin A., Chinnery P.F., Burn D.J., Clarke C.E., Marion M.H.,
Lewthwaite A.J., Nicholl D.J., Wood N.W., Morrison K.E.,
Williams-Gray C.H., Evans J.R., Sawcer S.J., Barker R.A.,
Wickremaratchi M.M., Ben-Shlomo Y., Williams N.M., Morris H.R.;
"Systematic review and UK-based study of PARK2 (parkin), PINK1, PARK7
(DJ-1) and LRRK2 in early-onset Parkinson's disease.";
Mov. Disord. 27:1522-1529(2012).
-!- FUNCTION: 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).
Plays a role in synaptic vesicle trafficking. Phosphorylates
PRDX3. Has GTPase activity. May play a role in the phosphorylation
of proteins central to Parkinson disease.
{ECO:0000269|PubMed:17114044, ECO:0000269|PubMed:18230735,
ECO:0000269|PubMed:20949042, ECO:0000269|PubMed:21850687,
ECO:0000269|PubMed:22012985, ECO:0000269|PubMed:23395371,
ECO:0000269|PubMed:24687852}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Homodimer. Interacts with PRKN, PRDX3, RAB29, TPCN2 and
VPS35. {ECO:0000269|PubMed:16352719, ECO:0000269|PubMed:18230735,
ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:22012985,
ECO:0000269|PubMed:22952686, ECO:0000269|PubMed:23395371}.
-!- INTERACTION:
Self; NbExp=66; IntAct=EBI-5323863, EBI-5323863;
Q9UKV8:AGO2; NbExp=3; IntAct=EBI-5323863, EBI-528269;
P31749:AKT1; NbExp=6; IntAct=EBI-5323863, EBI-296087;
Q8N6T3-2:ARFGAP1; NbExp=6; IntAct=EBI-5323863, EBI-6288865;
Q62848:Arfgap1 (xeno); NbExp=7; IntAct=EBI-5323863, EBI-4398879;
Q14155:ARHGEF7; NbExp=7; IntAct=EBI-5323863, EBI-717515;
O95816:BAG2; NbExp=2; IntAct=EBI-5323863, EBI-355275;
O95817:BAG3; NbExp=2; IntAct=EBI-5323863, EBI-747185;
Q9UL15:BAG5; NbExp=12; IntAct=EBI-5323863, EBI-356517;
P10415-1:BCL2; NbExp=2; IntAct=EBI-5323863, EBI-4370304;
Q16543:CDC37; NbExp=7; IntAct=EBI-5323863, EBI-295634;
P60953:CDC42; NbExp=3; IntAct=EBI-5323863, EBI-81752;
P05060:CHGB; NbExp=2; IntAct=EBI-5323863, EBI-712619;
P30275:Ckmt1 (xeno); NbExp=2; IntAct=EBI-5323863, EBI-773103;
P48729-1:CSNK1A1; NbExp=2; IntAct=EBI-5323863, EBI-10106282;
P53355:DAPK1; NbExp=2; IntAct=EBI-5323863, EBI-358616;
Q05193:DNM1; NbExp=4; IntAct=EBI-5323863, EBI-713135;
P39053:Dnm1 (xeno); NbExp=3; IntAct=EBI-5323863, EBI-397785;
O00429:DNM1L; NbExp=11; IntAct=EBI-5323863, EBI-724571;
O00429-3:DNM1L; NbExp=2; IntAct=EBI-5323863, EBI-6896746;
O14640-2:DVL1; NbExp=7; IntAct=EBI-5323863, EBI-6504027;
O14641:DVL2; NbExp=3; IntAct=EBI-5323863, EBI-740850;
Q92997:DVL3; NbExp=4; IntAct=EBI-5323863, EBI-739789;
P30084:ECHS1; NbExp=2; IntAct=EBI-5323863, EBI-719602;
Q13158:FADD; NbExp=4; IntAct=EBI-5323863, EBI-494804;
O14976:GAK; NbExp=10; IntAct=EBI-5323863, EBI-714707;
P49841:GSK3B; NbExp=7; IntAct=EBI-5323863, EBI-373586;
P11142:HSPA8; NbExp=5; IntAct=EBI-5323863, EBI-351896;
P07195:LDHB; NbExp=2; IntAct=EBI-5323863, EBI-358748;
O75581:LRP6; NbExp=4; IntAct=EBI-5323863, EBI-910915;
Q38SD2:LRRK1; NbExp=5; IntAct=EBI-5323863, EBI-1050422;
P46821:MAP1B; NbExp=5; IntAct=EBI-5323863, EBI-9517186;
P46734:MAP2K3; NbExp=5; IntAct=EBI-5323863, EBI-602462;
P52564:MAP2K6; NbExp=4; IntAct=EBI-5323863, EBI-448135;
O14733:MAP2K7; NbExp=3; IntAct=EBI-5323863, EBI-492605;
P10636-2:MAPT; NbExp=3; IntAct=EBI-5323863, EBI-7796412;
P10636-8:MAPT; NbExp=9; IntAct=EBI-5323863, EBI-366233;
P42679:MATK; NbExp=2; IntAct=EBI-5323863, EBI-751664;
P02687:MBP (xeno); NbExp=3; IntAct=EBI-5323863, EBI-908215;
Q811U4:Mfn1 (xeno); NbExp=3; IntAct=EBI-5323863, EBI-9029118;
O95140:MFN2; NbExp=3; IntAct=EBI-5323863, EBI-3324756;
P26038:MSN; NbExp=17; IntAct=EBI-5323863, EBI-528768;
Q96PY6:NEK1; NbExp=2; IntAct=EBI-5323863, EBI-373615;
Q13469:NFATC2; NbExp=3; IntAct=EBI-5323863, EBI-716258;
Q8WUM0:NUP133; NbExp=2; IntAct=EBI-5323863, EBI-295695;
O60313:OPA1; NbExp=3; IntAct=EBI-5323863, EBI-1054131;
Q9NQU5:PAK6; NbExp=2; IntAct=EBI-5323863, EBI-1053685;
P00634:phoA (xeno); NbExp=2; IntAct=EBI-5323863, EBI-552958;
P62136:PPP1CA; NbExp=6; IntAct=EBI-5323863, EBI-357253;
P30048:PRDX3; NbExp=12; IntAct=EBI-5323863, EBI-748336;
P17612:PRKACA; NbExp=6; IntAct=EBI-5323863, EBI-476586;
P12369:Prkar2b (xeno); NbExp=3; IntAct=EBI-5323863, EBI-6096160;
O60260:PRKN; NbExp=3; IntAct=EBI-5323863, EBI-716346;
P61026:RAB10; NbExp=5; IntAct=EBI-5323863, EBI-726075;
Q6IQ22:RAB12; NbExp=2; IntAct=EBI-5323863, EBI-4289591;
Q9H0U4:RAB1B; NbExp=3; IntAct=EBI-5323863, EBI-1045214;
O14966:RAB29; NbExp=7; IntAct=EBI-5323863, EBI-372165;
Q63481:Rab29 (xeno); NbExp=3; IntAct=EBI-5323863, EBI-6513837;
Q13637:RAB32; NbExp=6; IntAct=EBI-5323863, EBI-9837586;
P61020:RAB5B; NbExp=9; IntAct=EBI-5323863, EBI-399401;
P61021:Rab5b (xeno); NbExp=2; IntAct=EBI-5323863, EBI-8320093;
P61006:RAB8A; NbExp=6; IntAct=EBI-5323863, EBI-722293;
P63000:RAC1; NbExp=5; IntAct=EBI-5323863, EBI-413628;
P41220:RGS2; NbExp=6; IntAct=EBI-5323863, EBI-712388;
P62906:RPL10A; NbExp=2; IntAct=EBI-5323863, EBI-356860;
P26373:RPL13; NbExp=2; IntAct=EBI-5323863, EBI-356849;
P50914:RPL14; NbExp=2; IntAct=EBI-5323863, EBI-356746;
P62750:RPL23A; NbExp=2; IntAct=EBI-5323863, EBI-353254;
P62280:RPS11; NbExp=3; IntAct=EBI-5323863, EBI-1047710;
P62841:RPS15; NbExp=9; IntAct=EBI-5323863, EBI-372635;
P62249:RPS16; NbExp=2; IntAct=EBI-5323863, EBI-352480;
P15880:RPS2; NbExp=2; IntAct=EBI-5323863, EBI-443446;
P60866:RPS20; NbExp=2; IntAct=EBI-5323863, EBI-353105;
P62266:RPS23; NbExp=2; IntAct=EBI-5323863, EBI-353072;
P42677:RPS27; NbExp=2; IntAct=EBI-5323863, EBI-356336;
P23396:RPS3; NbExp=2; IntAct=EBI-5323863, EBI-351193;
O15027:SEC16A; NbExp=6; IntAct=EBI-5323863, EBI-357515;
Q99962:SH3GL2; NbExp=4; IntAct=EBI-5323863, EBI-77938;
P12235:SLC25A4; NbExp=2; IntAct=EBI-5323863, EBI-359074;
P05141:SLC25A5; NbExp=2; IntAct=EBI-5323863, EBI-355133;
P12236:SLC25A6; NbExp=2; IntAct=EBI-5323863, EBI-356254;
O95295:SNAPIN; NbExp=5; IntAct=EBI-5323863, EBI-296723;
P37840:SNCA; NbExp=6; IntAct=EBI-5323863, EBI-985879;
Q58A65:Spag9 (xeno); NbExp=2; IntAct=EBI-5323863, EBI-6530207;
P07437:TUBB; NbExp=4; IntAct=EBI-5323863, EBI-350864;
P04350:TUBB4A; NbExp=4; IntAct=EBI-5323863, EBI-355007;
P31946:YWHAB; NbExp=5; IntAct=EBI-5323863, EBI-359815;
P62258:YWHAE; NbExp=6; IntAct=EBI-5323863, EBI-356498;
P61981:YWHAG; NbExp=4; IntAct=EBI-5323863, EBI-359832;
P61983:Ywhag (xeno); NbExp=6; IntAct=EBI-5323863, EBI-359821;
Q04917:YWHAH; NbExp=3; IntAct=EBI-5323863, EBI-306940;
P27348:YWHAQ; NbExp=8; IntAct=EBI-5323863, EBI-359854;
P63104:YWHAZ; NbExp=9; IntAct=EBI-5323863, EBI-347088;
-!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
Cytoplasm. Perikaryon. Mitochondrion. Golgi apparatus. Cell
projection, axon. Cell projection, dendrite. Endoplasmic reticulum
{ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic
vesicle membrane {ECO:0000269|PubMed:24687852}; Peripheral
membrane protein {ECO:0000269|PubMed:24687852}; Cytoplasmic side
{ECO:0000269|PubMed:24687852}. Endosome {ECO:0000250}. Lysosome
{ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}.
Mitochondrion inner membrane {ECO:0000250}. Mitochondrion matrix
{ECO:0000250}. 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. {ECO:0000250}.
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:15541308, ECO:0000269|PubMed:15541309,
ECO:0000269|PubMed:16532471, ECO:0000269|PubMed:17120249}.
-!- DOMAIN: The seven-bladed WD repeat region is critical for synaptic
vesicle trafficking and mediates interaction with multiple
vesicle-associated presynaptic proteins.
{ECO:0000269|PubMed:24687852}.
-!- DOMAIN: The Roc domain mediates homodimerization and regulates
kinase activity. {ECO:0000269|PubMed:18230735}.
-!- PTM: Autophosphorylated.
-!- DISEASE: 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. {ECO:0000269|PubMed:15541308,
ECO:0000269|PubMed:15541309, ECO:0000269|PubMed:15680455,
ECO:0000269|PubMed:15680456, ECO:0000269|PubMed:15680457,
ECO:0000269|PubMed:15726496, ECO:0000269|PubMed:15732108,
ECO:0000269|PubMed:15811454, ECO:0000269|PubMed:15852371,
ECO:0000269|PubMed:15880653, ECO:0000269|PubMed:15925109,
ECO:0000269|PubMed:15929036, ECO:0000269|PubMed:16102999,
ECO:0000269|PubMed:16157901, ECO:0000269|PubMed:16157908,
ECO:0000269|PubMed:16157909, ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:16240353, ECO:0000269|PubMed:16247070,
ECO:0000269|PubMed:16250030, ECO:0000269|PubMed:16251215,
ECO:0000269|PubMed:16269541, ECO:0000269|PubMed:16272164,
ECO:0000269|PubMed:16272257, ECO:0000269|PubMed:16298482,
ECO:0000269|PubMed:16321986, ECO:0000269|PubMed:16333314,
ECO:0000269|PubMed:16533964, ECO:0000269|PubMed:17114044,
ECO:0000269|PubMed:18213618, ECO:0000269|PubMed:21850687,
ECO:0000269|PubMed:22956510, ECO:0000269|PubMed:23395371}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY792511; AAV63975.1; -; mRNA.
EMBL; AC079630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL834529; CAD39185.1; -; mRNA.
CCDS; CCDS31774.1; -.
RefSeq; NP_940980.3; NM_198578.3.
UniGene; Hs.187636; -.
PDB; 2ZEJ; X-ray; 2.00 A; A/B=1333-1516.
PDB; 3D6T; X-ray; 2.43 A; B=1335-1505.
PDB; 5MY9; X-ray; 1.33 A; P=929-941.
PDB; 5MYC; X-ray; 1.46 A; P=904-941.
PDBsum; 2ZEJ; -.
PDBsum; 3D6T; -.
PDBsum; 5MY9; -.
PDBsum; 5MYC; -.
ProteinModelPortal; Q5S007; -.
SMR; Q5S007; -.
BioGrid; 125700; 153.
DIP; DIP-29684N; -.
IntAct; Q5S007; 549.
MINT; MINT-7997594; -.
STRING; 9606.ENSP00000298910; -.
BindingDB; Q5S007; -.
ChEMBL; CHEMBL1075104; -.
GuidetoPHARMACOLOGY; 2059; -.
iPTMnet; Q5S007; -.
PhosphoSitePlus; Q5S007; -.
BioMuta; LRRK2; -.
DMDM; 294862450; -.
MaxQB; Q5S007; -.
PaxDb; Q5S007; -.
PeptideAtlas; Q5S007; -.
PRIDE; Q5S007; -.
Ensembl; ENST00000298910; ENSP00000298910; ENSG00000188906.
GeneID; 120892; -.
KEGG; hsa:120892; -.
UCSC; uc001rmg.5; human.
CTD; 120892; -.
DisGeNET; 120892; -.
GeneCards; LRRK2; -.
GeneReviews; LRRK2; -.
HGNC; HGNC:18618; LRRK2.
HPA; CAB037160; -.
HPA; HPA014293; -.
MalaCards; LRRK2; -.
MIM; 168600; phenotype.
MIM; 607060; phenotype.
MIM; 609007; gene.
neXtProt; NX_Q5S007; -.
OpenTargets; ENSG00000188906; -.
Orphanet; 2828; Young adult-onset Parkinsonism.
PharmGKB; PA134968052; -.
eggNOG; ENOG410IRBK; Eukaryota.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG1100; LUCA.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00530000063477; -.
HOGENOM; HOG000293315; -.
HOVERGEN; HBG081937; -.
InParanoid; Q5S007; -.
KO; K08844; -.
OMA; FKIRDQP; -.
OrthoDB; EOG091G003N; -.
PhylomeDB; Q5S007; -.
TreeFam; TF313679; -.
Reactome; R-HSA-8857538; PTK6 promotes HIF1A stabilization.
SignaLink; Q5S007; -.
SIGNOR; Q5S007; -.
ChiTaRS; LRRK2; human.
EvolutionaryTrace; Q5S007; -.
GeneWiki; LRRK2; -.
GenomeRNAi; 120892; -.
PRO; PR:Q5S007; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000188906; -.
CleanEx; HS_LRRK2; -.
ExpressionAtlas; Q5S007; baseline and differential.
Genevisible; Q5S007; HS.
GO; GO:0044753; C:amphisome; IDA:ParkinsonsUK-UCL.
GO; GO:0044754; C:autolysosome; IDA:ParkinsonsUK-UCL.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0099400; C:caveola neck; IDA:ParkinsonsUK-UCL.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
GO; GO:0005798; C:Golgi-associated vesicle; IDA:ParkinsonsUK-UCL.
GO; GO:0030426; C:growth cone; IDA:ParkinsonsUK-UCL.
GO; GO:0016234; C:inclusion body; IMP:ParkinsonsUK-UCL.
GO; GO:0005622; C:intracellular; IMP:ParkinsonsUK-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0005902; C:microvillus; IDA:ParkinsonsUK-UCL.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0097487; C:multivesicular body, internal vesicle; IDA:ParkinsonsUK-UCL.
GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0043195; C:terminal bouton; TAS:ParkinsonsUK-UCL.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL.
GO; GO:0003779; F:actin binding; IPI:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:1904713; F:beta-catenin destruction complex binding; NAS:ParkinsonsUK-UCL.
GO; GO:0030276; F:clathrin binding; IPI:ParkinsonsUK-UCL.
GO; GO:0039706; F:co-receptor binding; TAS:ParkinsonsUK-UCL.
GO; GO:0001948; F:glycoprotein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0034211; F:GTP-dependent protein kinase activity; IDA:BHF-UCL.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; IDA:BHF-UCL.
GO; GO:0008017; F:microtubule binding; TAS:ParkinsonsUK-UCL.
GO; GO:0036479; F:peroxidase inhibitor activity; IDA:ParkinsonsUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0051018; F:protein kinase A binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0030159; F:receptor signaling complex scaffold activity; IC:ParkinsonsUK-UCL.
GO; GO:0017048; F:Rho GTPase binding; IPI:BHF-UCL.
GO; GO:0000149; F:SNARE binding; IPI:ParkinsonsUK-UCL.
GO; GO:0017075; F:syntaxin-1 binding; IPI:ParkinsonsUK-UCL.
GO; GO:0015631; F:tubulin binding; IDA:BHF-UCL.
GO; GO:0000187; P:activation of MAPK activity; IMP:ParkinsonsUK-UCL.
GO; GO:0000186; P:activation of MAPKK activity; IDA:BHF-UCL.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0019722; P:calcium-mediated signaling; IMP:ParkinsonsUK-UCL.
GO; GO:0060070; P:canonical Wnt signaling pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0034613; P:cellular protein localization; ISS:ParkinsonsUK-UCL.
GO; GO:1903351; P:cellular response to dopamine; IMP:ParkinsonsUK-UCL.
GO; GO:0071287; P:cellular response to manganese ion; IMP:ParkinsonsUK-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:ParkinsonsUK-UCL.
GO; GO:0009267; P:cellular response to starvation; IMP:ParkinsonsUK-UCL.
GO; GO:0008340; P:determination of adult lifespan; IMP:BHF-UCL.
GO; GO:0006897; P:endocytosis; IMP:ParkinsonsUK-UCL.
GO; GO:0060079; P:excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
GO; GO:0035640; P:exploration behavior; IMP:BHF-UCL.
GO; GO:0007030; P:Golgi organization; IMP:ParkinsonsUK-UCL.
GO; GO:0046039; P:GTP metabolic process; IDA:BHF-UCL.
GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; ISS:ParkinsonsUK-UCL.
GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
GO; GO:0007040; P:lysosome organization; IMP:ParkinsonsUK-UCL.
GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
GO; GO:0051646; P:mitochondrion localization; IMP:ParkinsonsUK-UCL.
GO; GO:0007005; P:mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:ParkinsonsUK-UCL.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
GO; GO:0034260; P:negative regulation of GTPase activity; IDA:MGI.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IMP:ParkinsonsUK-UCL.
GO; GO:1902823; P:negative regulation of late endosome to lysosome transport; TAS:ParkinsonsUK-UCL.
GO; GO:0016242; P:negative regulation of macroautophagy; IMP:ParkinsonsUK-UCL.
GO; GO:1901215; P:negative regulation of neuron death; IGI:ParkinsonsUK-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IMP:ParkinsonsUK-UCL.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:ParkinsonsUK-UCL.
GO; GO:0010955; P:negative regulation of protein processing; IDA:ParkinsonsUK-UCL.
GO; GO:1903217; P:negative regulation of protein processing involved in protein targeting to mitochondrion; IC:ParkinsonsUK-UCL.
GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:1903125; P:negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0007528; P:neuromuscular junction development; IMP:BHF-UCL.
GO; GO:0070997; P:neuron death; IMP:BHF-UCL.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
GO; GO:0021772; P:olfactory bulb development; IMP:ParkinsonsUK-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0016310; P:phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IC:ParkinsonsUK-UCL.
GO; GO:0043068; P:positive regulation of programmed cell death; IDA:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:BHF-UCL.
GO; GO:1902499; P:positive regulation of protein autoubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0070585; P:protein localization to mitochondrion; TAS:ParkinsonsUK-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0010506; P:regulation of autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:2000172; P:regulation of branching morphogenesis of a nerve; IMP:ParkinsonsUK-UCL.
GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; IMP:ParkinsonsUK-UCL.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:ParkinsonsUK-UCL.
GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0035564; P:regulation of kidney size; ISS:BHF-UCL.
GO; GO:0040012; P:regulation of locomotion; IMP:BHF-UCL.
GO; GO:0035751; P:regulation of lysosomal lumen pH; IMP:ParkinsonsUK-UCL.
GO; GO:0042391; P:regulation of membrane potential; IMP:BHF-UCL.
GO; GO:0051900; P:regulation of mitochondrial depolarization; IMP:ParkinsonsUK-UCL.
GO; GO:0090140; P:regulation of mitochondrial fission; TAS:ParkinsonsUK-UCL.
GO; GO:1902692; P:regulation of neuroblast proliferation; IMP:ParkinsonsUK-UCL.
GO; GO:1901214; P:regulation of neuron death; IMP:ParkinsonsUK-UCL.
GO; GO:0014041; P:regulation of neuron maturation; IMP:ParkinsonsUK-UCL.
GO; GO:0010738; P:regulation of protein kinase A signaling; ISS:ParkinsonsUK-UCL.
GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IGI:ParkinsonsUK-UCL.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:ParkinsonsUK-UCL.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:ParkinsonsUK-UCL.
GO; GO:1902803; P:regulation of synaptic vesicle transport; ISS:ParkinsonsUK-UCL.
GO; GO:0006979; P:response to oxidative stress; IMP:BHF-UCL.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IMP:ParkinsonsUK-UCL.
GO; GO:1904887; P:Wnt signalosome assembly; IPI:ParkinsonsUK-UCL.
Gene3D; 1.25.10.10; -; 2.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR032171; COR.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR025875; Leu-rich_rpt_4.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR013684; MIRO-like.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR020859; ROC_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
InterPro; IPR017986; WD40_repeat_dom.
Pfam; PF16095; COR; 1.
Pfam; PF12799; LRR_4; 1.
Pfam; PF13855; LRR_8; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF08477; Roc; 1.
SMART; SM00369; LRR_TYP; 7.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF48371; SSF48371; 2.
SUPFAM; SSF50978; SSF50978; 1.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF56112; SSF56112; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51450; LRR; 11.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS51424; ROC; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Autophagy; Cell junction; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Differentiation; Disease mutation; Endoplasmic reticulum; Endosome;
Golgi apparatus; GTP-binding; GTPase activation; Kinase;
Leucine-rich repeat; Lysosome; Membrane; Mitochondrion;
Mitochondrion inner membrane; Mitochondrion outer membrane;
Neurodegeneration; Nucleotide-binding; Parkinson disease;
Parkinsonism; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Serine/threonine-protein kinase; Synapse; Transferase;
WD repeat.
CHAIN 1 2527 Leucine-rich repeat serine/threonine-
protein kinase 2.
/FTId=PRO_0000086238.
REPEAT 983 1004 LRR 1.
REPEAT 1012 1033 LRR 2.
REPEAT 1036 1057 LRR 3.
REPEAT 1059 1080 LRR 4.
REPEAT 1084 1105 LRR 5.
REPEAT 1108 1129 LRR 6.
REPEAT 1130 1150 LRR 7.
REPEAT 1174 1196 LRR 8.
REPEAT 1197 1218 LRR 9.
REPEAT 1221 1241 LRR 10.
REPEAT 1246 1267 LRR 11.
REPEAT 1269 1291 LRR 12.
DOMAIN 1328 1511 Roc. {ECO:0000255|PROSITE-
ProRule:PRU00758}.
DOMAIN 1879 2138 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REPEAT 2139 2183 WD 1.
REPEAT 2188 2228 WD 2.
REPEAT 2233 2276 WD 3.
REPEAT 2281 2327 WD 4.
REPEAT 2333 2377 WD 5.
REPEAT 2402 2438 WD 6.
REPEAT 2443 2497 WD 7.
NP_BIND 1341 1348 GTP. {ECO:0000255|PROSITE-
ProRule:PRU00758,
ECO:0000269|PubMed:18230735}.
NP_BIND 1885 1893 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 2098 2121 GTP. {ECO:0000255|PROSITE-
ProRule:PRU00758}.
NP_BIND 2295 2298 GTP. {ECO:0000255|PROSITE-
ProRule:PRU00758}.
COILED 319 348 {ECO:0000255}.
COMPBIAS 728 731 Poly-Leu.
ACT_SITE 1994 1994 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 1906 1906 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 935 935 Phosphoserine.
{ECO:0000250|UniProtKB:Q5S006}.
VARIANT 50 50 R -> H (in dbSNP:rs2256408).
/FTId=VAR_024931.
VARIANT 119 119 L -> P (in dbSNP:rs33995463).
{ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_024932.
VARIANT 228 228 C -> S (in dbSNP:rs56108242).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054740.
VARIANT 419 419 A -> V (in dbSNP:rs34594498).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_033903.
VARIANT 551 551 N -> K (in dbSNP:rs7308720).
{ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:16251215,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:22415848}.
/FTId=VAR_024933.
VARIANT 712 712 M -> V (in PARK8; dbSNP:rs199566791).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054741.
VARIANT 716 716 A -> V (in dbSNP:rs281865043).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054742.
VARIANT 723 723 I -> V (in dbSNP:rs10878307).
{ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:22415848}.
/FTId=VAR_024934.
VARIANT 755 755 P -> L (in dbSNP:rs34410987).
/FTId=VAR_033904.
VARIANT 793 793 R -> M (in PARK8; unknown pathological
significance; dbSNP:rs35173587).
{ECO:0000269|PubMed:16157908,
ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:16251215}.
/FTId=VAR_024935.
VARIANT 871 871 K -> E (in dbSNP:rs281865044).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054743.
VARIANT 930 930 Q -> R (in PARK8; unknown pathological
significance; dbSNP:rs281865045).
{ECO:0000269|PubMed:16251215}.
/FTId=VAR_024936.
VARIANT 944 944 D -> Y (in dbSNP:rs17519916).
/FTId=VAR_024937.
VARIANT 1067 1067 R -> Q (in PARK8; dbSNP:rs111341148).
{ECO:0000269|PubMed:16247070}.
/FTId=VAR_024938.
VARIANT 1096 1096 S -> C (in PARK8; unknown pathological
significance; dbSNP:rs76535406).
/FTId=VAR_024939.
VARIANT 1122 1122 I -> V (in PARK8; dbSNP:rs34805604).
{ECO:0000269|PubMed:15541309,
ECO:0000269|PubMed:16172858}.
/FTId=VAR_024940.
VARIANT 1228 1228 S -> T (in PARK8; dbSNP:rs60185966).
{ECO:0000269|PubMed:16251215}.
/FTId=VAR_024941.
VARIANT 1262 1262 P -> A (in dbSNP:rs4640000).
{ECO:0000269|PubMed:16172858}.
/FTId=VAR_024942.
VARIANT 1359 1359 K -> I (found in a renal cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064728.
VARIANT 1371 1371 I -> V (in PARK8; unknown pathological
significance; dbSNP:rs17466213).
{ECO:0000269|PubMed:16157901,
ECO:0000269|PubMed:16333314}.
/FTId=VAR_024943.
VARIANT 1375 1375 D -> E (in dbSNP:rs28365226).
/FTId=VAR_047022.
VARIANT 1398 1398 R -> H (in dbSNP:rs7133914).
{ECO:0000269|PubMed:16157901,
ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:22415848}.
/FTId=VAR_024944.
VARIANT 1441 1441 R -> C (in PARK; shows an increase in
activity in both autophosphorylation and
phosphorylation of a generic substrate;
dbSNP:rs33939927).
{ECO:0000269|PubMed:15541309,
ECO:0000269|PubMed:16157909,
ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:16269541,
ECO:0000269|PubMed:16333314,
ECO:0000269|PubMed:16533964}.
/FTId=VAR_024945.
VARIANT 1441 1441 R -> G (in PARK8; shows a progressive
reduction in neurite length and
branching; dbSNP:rs33939927).
{ECO:0000269|PubMed:15541308,
ECO:0000269|PubMed:15925109,
ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:16533964,
ECO:0000269|PubMed:17114044}.
/FTId=VAR_024946.
VARIANT 1441 1441 R -> H (in PARK8; pathogenicity has yet
to be confirmed; dbSNP:rs34995376).
{ECO:0000269|PubMed:16157909,
ECO:0000269|PubMed:16172858}.
/FTId=VAR_024947.
VARIANT 1514 1514 R -> Q (in PARK8; pathogenicity has yet
to be confirmed; might have an effect on
protein structure; dbSNP:rs35507033).
{ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:22415848}.
/FTId=VAR_024948.
VARIANT 1542 1542 P -> S (in PARK8; pathogenicity has yet
to be confirmed; might have an effect on
protein structure; dbSNP:rs33958906).
{ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:22415848}.
/FTId=VAR_024949.
VARIANT 1550 1550 R -> Q (in an ovarian mucinous carcinoma
sample; somatic mutation;
dbSNP:rs200212150).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040678.
VARIANT 1598 1598 V -> E (in PARK8; pathogenicity has yet
to be confirmed; might have an effect on
protein structure; dbSNP:rs721710).
{ECO:0000269|PubMed:16172858}.
/FTId=VAR_024950.
VARIANT 1628 1628 R -> P (may be associated with Parkinson
disease in some populations;
dbSNP:rs33949390).
{ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:21641266,
ECO:0000269|PubMed:22415848}.
/FTId=VAR_024951.
VARIANT 1646 1646 M -> T (in dbSNP:rs35303786).
{ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:22415848}.
/FTId=VAR_024952.
VARIANT 1647 1647 S -> T (in dbSNP:rs11564148).
{ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:22415848}.
/FTId=VAR_024953.
VARIANT 1699 1699 Y -> C (in PARK8; shows no progressive
reduction in neurite length and
branching; dbSNP:rs35801418).
{ECO:0000269|PubMed:15541308,
ECO:0000269|PubMed:15541309,
ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:16272164,
ECO:0000269|PubMed:17114044}.
/FTId=VAR_024954.
VARIANT 1723 1723 R -> P (in an ovarian serous carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040679.
VARIANT 1728 1728 R -> H (in PARK8; dbSNP:rs145364431).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054744.
VARIANT 1728 1728 R -> L (in PARK8; dbSNP:rs145364431).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054745.
VARIANT 1869 1869 M -> T (in PARK8; pathogenicity has yet
to be confirmed; dbSNP:rs35602796).
{ECO:0000269|PubMed:16157908,
ECO:0000269|PubMed:16172858}.
/FTId=VAR_024955.
VARIANT 1870 1870 L -> F (in dbSNP:rs281865053).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054746.
VARIANT 1906 1906 K -> M (does not inhibit interaction with
RAB29; shows a progressive increase in
neurite length and branching).
{ECO:0000269|PubMed:17114044,
ECO:0000269|PubMed:23395371}.
/FTId=VAR_071101.
VARIANT 1941 1941 R -> H (in PARK8; dbSNP:rs77428810).
{ECO:0000269|PubMed:16272164}.
/FTId=VAR_024956.
VARIANT 2012 2012 I -> T (in PARK8; pathogenicity
uncertain; dbSNP:rs34015634).
{ECO:0000269|PubMed:16172858}.
/FTId=VAR_024957.
VARIANT 2019 2019 G -> 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; dbSNP:rs34637584).
{ECO:0000269|PubMed:15680455,
ECO:0000269|PubMed:15680456,
ECO:0000269|PubMed:15680457,
ECO:0000269|PubMed:15726496,
ECO:0000269|PubMed:15732108,
ECO:0000269|PubMed:15811454,
ECO:0000269|PubMed:15852371,
ECO:0000269|PubMed:15929036,
ECO:0000269|PubMed:16001413,
ECO:0000269|PubMed:16102999,
ECO:0000269|PubMed:16157901,
ECO:0000269|PubMed:16157908,
ECO:0000269|PubMed:16157909,
ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:16240353,
ECO:0000269|PubMed:16250030,
ECO:0000269|PubMed:16251215,
ECO:0000269|PubMed:16269541,
ECO:0000269|PubMed:16272164,
ECO:0000269|PubMed:16272257,
ECO:0000269|PubMed:16298482,
ECO:0000269|PubMed:16333314,
ECO:0000269|PubMed:16533964,
ECO:0000269|PubMed:17114044,
ECO:0000269|PubMed:18213618,
ECO:0000269|PubMed:21850687,
ECO:0000269|PubMed:22956510,
ECO:0000269|PubMed:23395371}.
/FTId=VAR_024958.
VARIANT 2020 2020 I -> 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; dbSNP:rs35870237).
{ECO:0000269|PubMed:15541309,
ECO:0000269|PubMed:15880653,
ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:16251215,
ECO:0000269|PubMed:16321986,
ECO:0000269|PubMed:17114044}.
/FTId=VAR_024959.
VARIANT 2081 2081 N -> D (in dbSNP:rs33995883).
{ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:22415848}.
/FTId=VAR_024960.
VARIANT 2119 2119 P -> L (in dbSNP:rs12423862).
{ECO:0000269|PubMed:16172858}.
/FTId=VAR_024961.
VARIANT 2141 2141 T -> M (in PARK8; dbSNP:rs111691891).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054747.
VARIANT 2143 2143 R -> H (in PARK8; dbSNP:rs201271001).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054748.
VARIANT 2261 2261 N -> I (in dbSNP:rs12581902).
{ECO:0000269|PubMed:16172858}.
/FTId=VAR_024962.
VARIANT 2356 2356 T -> I (in PARK8; dbSNP:rs113511708).
{ECO:0000269|PubMed:16272164}.
/FTId=VAR_024963.
VARIANT 2385 2385 G -> 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; reduced binding to synaptic
vesicles; dbSNP:rs34778348).
{ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:17019612,
ECO:0000269|PubMed:24687852}.
/FTId=VAR_024964.
VARIANT 2395 2395 E -> K (in dbSNP:rs78964014).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054749.
VARIANT 2397 2397 M -> T (in dbSNP:rs3761863).
{ECO:0000269|PubMed:16157901,
ECO:0000269|PubMed:16172858,
ECO:0000269|PubMed:22415848}.
/FTId=VAR_024965.
VARIANT 2466 2466 L -> H (in PARK8; dbSNP:rs281865057).
{ECO:0000269|PubMed:18213618}.
/FTId=VAR_054750.
MUTAGEN 1343 1343 T->G: Decreased kinase activity; when
associated with Q-1398.
{ECO:0000269|PubMed:18230735}.
MUTAGEN 1398 1398 R->Q: Decreased kinase activity; when
associated with G-1343.
{ECO:0000269|PubMed:18230735}.
CONFLICT 212 212 L -> S (in Ref. 1; AAV63975).
{ECO:0000305}.
HELIX 913 917 {ECO:0000244|PDB:5MYC}.
STRAND 1336 1341 {ECO:0000244|PDB:2ZEJ}.
HELIX 1347 1354 {ECO:0000244|PDB:2ZEJ}.
STRAND 1370 1377 {ECO:0000244|PDB:2ZEJ}.
STRAND 1389 1395 {ECO:0000244|PDB:2ZEJ}.
HELIX 1398 1402 {ECO:0000244|PDB:2ZEJ}.
HELIX 1406 1411 {ECO:0000244|PDB:2ZEJ}.
STRAND 1412 1420 {ECO:0000244|PDB:2ZEJ}.
HELIX 1421 1423 {ECO:0000244|PDB:2ZEJ}.
HELIX 1425 1429 {ECO:0000244|PDB:2ZEJ}.
HELIX 1431 1441 {ECO:0000244|PDB:2ZEJ}.
STRAND 1446 1452 {ECO:0000244|PDB:2ZEJ}.
HELIX 1454 1456 {ECO:0000244|PDB:2ZEJ}.
HELIX 1459 1472 {ECO:0000244|PDB:2ZEJ}.
TURN 1473 1475 {ECO:0000244|PDB:2ZEJ}.
STRAND 1481 1487 {ECO:0000244|PDB:2ZEJ}.
HELIX 1495 1509 {ECO:0000244|PDB:2ZEJ}.
SEQUENCE 2527 AA; 286103 MW; 26142A0CECBBC3F4 CRC64;
MASGSCQGCE EDEETLKKLI VRLNNVQEGK QIETLVQILE DLLVFTYSER ASKLFQGKNI
HVPLLIVLDS YMRVASVQQV GWSLLCKLIE VCPGTMQSLM GPQDVGNDWE VLGVHQLILK
MLTVHNASVN LSVIGLKTLD LLLTSGKITL LILDEESDIF MLIFDAMHSF PANDEVQKLG
CKALHVLFER VSEEQLTEFV ENKDYMILLS ALTNFKDEEE IVLHVLHCLH SLAIPCNNVE
VLMSGNVRCY NIVVEAMKAF PMSERIQEVS CCLLHRLTLG NFFNILVLNE VHEFVVKAVQ
QYPENAALQI SALSCLALLT ETIFLNQDLE EKNENQENDD EGEEDKLFWL EACYKALTWH
RKNKHVQEAA CWALNNLLMY QNSLHEKIGD EDGHFPAHRE VMLSMLMHSS SKEVFQASAN
ALSTLLEQNV NFRKILLSKG IHLNVLELMQ KHIHSPEVAE SGCKMLNHLF EGSNTSLDIM
AAVVPKILTV MKRHETSLPV QLEALRAILH FIVPGMPEES REDTEFHHKL NMVKKQCFKN
DIHKLVLAAL NRFIGNPGIQ KCGLKVISSI VHFPDALEML SLEGAMDSVL HTLQMYPDDQ
EIQCLGLSLI GYLITKKNVF IGTGHLLAKI LVSSLYRFKD VAEIQTKGFQ TILAILKLSA
SFSKLLVHHS FDLVIFHQMS SNIMEQKDQQ FLNLCCKCFA KVAMDDYLKN VMLERACDQN
NSIMVECLLL LGADANQAKE GSSLICQVCE KESSPKLVEL LLNSGSREQD VRKALTISIG
KGDSQIISLL LRRLALDVAN NSICLGGFCI GKVEPSWLGP LFPDKTSNLR KQTNIASTLA
RMVIRYQMKS AVEEGTASGS DGNFSEDVLS KFDEWTFIPD SSMDSVFAQS DDLDSEGSEG
SFLVKKKSNS ISVGEFYRDA VLQRCSPNLQ RHSNSLGPIF DHEDLLKRKR KILSSDDSLR
SSKLQSHMRH SDSISSLASE REYITSLDLS ANELRDIDAL SQKCCISVHL EHLEKLELHQ
NALTSFPQQL CETLKSLTHL DLHSNKFTSF PSYLLKMSCI ANLDVSRNDI GPSVVLDPTV
KCPTLKQFNL SYNQLSFVPE NLTDVVEKLE QLILEGNKIS GICSPLRLKE LKILNLSKNH
ISSLSENFLE ACPKVESFSA RMNFLAAMPF LPPSMTILKL SQNKFSCIPE AILNLPHLRS
LDMSSNDIQY LPGPAHWKSL NLRELLFSHN QISILDLSEK AYLWSRVEKL HLSHNKLKEI
PPEIGCLENL TSLDVSYNLE LRSFPNEMGK LSKIWDLPLD ELHLNFDFKH IGCKAKDIIR
FLQQRLKKAV PYNRMKLMIV GNTGSGKTTL LQQLMKTKKS DLGMQSATVG IDVKDWPIQI
RDKRKRDLVL NVWDFAGREE FYSTHPHFMT QRALYLAVYD LSKGQAEVDA MKPWLFNIKA
RASSSPVILV GTHLDVSDEK QRKACMSKIT KELLNKRGFP AIRDYHFVNA TEESDALAKL
RKTIINESLN FKIRDQLVVG QLIPDCYVEL EKIILSERKN VPIEFPVIDR KRLLQLVREN
QLQLDENELP HAVHFLNESG VLLHFQDPAL QLSDLYFVEP KWLCKIMAQI LTVKVEGCPK
HPKGIISRRD VEKFLSKKRK FPKNYMSQYF KLLEKFQIAL PIGEEYLLVP SSLSDHRPVI
ELPHCENSEI IIRLYEMPYF PMGFWSRLIN RLLEISPYML SGRERALRPN RMYWRQGIYL
NWSPEAYCLV GSEVLDNHPE SFLKITVPSC RKGCILLGQV VDHIDSLMEE WFPGLLEIDI
CGEGETLLKK WALYSFNDGE EHQKILLDDL MKKAEEGDLL VNPDQPRLTI PISQIAPDLI
LADLPRNIML NNDELEFEQA PEFLLGDGSF GSVYRAAYEG EEVAVKIFNK HTSLRLLRQE
LVVLCHLHHP SLISLLAAGI RPRMLVMELA SKGSLDRLLQ QDKASLTRTL QHRIALHVAD
GLRYLHSAMI IYRDLKPHNV LLFTLYPNAA IIAKIADYGI AQYCCRMGIK TSEGTPGFRA
PEVARGNVIY NQQADVYSFG LLLYDILTTG GRIVEGLKFP NEFDELEIQG KLPDPVKEYG
CAPWPMVEKL IKQCLKENPQ ERPTSAQVFD ILNSAELVCL TRRILLPKNV IVECMVATHH
NSRNASIWLG CGHTDRGQLS FLDLNTEGYT SEEVADSRIL CLALVHLPVE KESWIVSGTQ
SGTLLVINTE DGKKRHTLEK MTDSVTCLYC NSFSKQSKQK NFLLVGTADG KLAIFEDKTV
KLKGAAPLKI LNIGNVSTPL MCLSESTNST ERNVMWGGCG TKIFSFSNDF TIQKLIETRT
SQLFSYAAFS DSNIITVVVD TALYIAKQNS PVVEVWDKKT EKLCGLIDCV HFLREVMVKE
NKESKHKMSY SGRVKTLCLQ KNTALWIGTG GGHILLLDLS TRRLIRVIYN FCNSVRVMMT
AQLGSLKNVM LVLGYNRKNT EGTQKQKEIQ SCLTVWDINL PHEVQNLEKH IEVRKELAEK
MRRTSVE


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