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

 LRRK2_MOUSE             Reviewed;        2527 AA.
Q5S006; E9QNJ2; Q8BWG7; Q8BZJ6; Q8CI84; Q8K062;
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 137.
RecName: Full=Leucine-rich repeat serine/threonine-protein kinase 2;
EC=2.7.11.1;
Name=Lrrk2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Swiss Webster; TISSUE=Embryo;
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].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-946 AND 1162-1707.
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1688-2527.
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
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).
[6]
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).
[7]
TISSUE SPECIFICITY.
PubMed=16487147; DOI=10.1111/j.1460-9568.2006.04616.x;
Simon-Sanchez J., Herranz-Perez V., Olucha-Bordonau F., Perez-Tur J.;
"LRRK2 is expressed in areas affected by Parkinson's disease in the
adult mouse brain.";
Eur. J. Neurosci. 23:659-666(2006).
[8]
TISSUE SPECIFICITY.
PubMed=16504409; DOI=10.1016/j.neuroscience.2006.01.017;
Melrose H., Lincoln S., Tyndall G., Dickson D., Farrer M.;
"Anatomical localization of leucine-rich repeat kinase 2 in mouse
brain.";
Neuroscience 139:791-794(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-935, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
INTERACTION WITH VPS35 AND RAB29.
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).
-!- 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).
Phosphorylates PRDX3. Has GTPase activity (By similarity).
{ECO:0000250|UniProtKB:Q5S007}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Homodimer. Interacts with PRKN, PRDX3 and TPCN2 (By
similarity). Interacts with VPS35 and RAB29. {ECO:0000250,
ECO:0000269|PubMed:23395371}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-2693710, EBI-2693710;
Q9EPJ9:Arfgap1; NbExp=3; IntAct=EBI-2693710, EBI-6288020;
Q8K1M6:Dnm1l; NbExp=4; IntAct=EBI-2693710, EBI-2365792;
P26038:MSN (xeno); NbExp=2; IntAct=EBI-2693710, EBI-528768;
P46460:Nsf; NbExp=3; IntAct=EBI-2693710, EBI-398006;
P31324:Prkar2b; NbExp=3; IntAct=EBI-2693710, EBI-455340;
Q9CQV8:Ywhab; NbExp=3; IntAct=EBI-2693710, EBI-771608;
P62259:Ywhae; NbExp=3; IntAct=EBI-2693710, EBI-356480;
P61982:Ywhag; NbExp=7; IntAct=EBI-2693710, EBI-359843;
P68510:Ywhah; NbExp=4; IntAct=EBI-2693710, EBI-444641;
P68254:Ywhaq; NbExp=3; IntAct=EBI-2693710, EBI-400675;
P63101:Ywhaz; NbExp=4; IntAct=EBI-2693710, EBI-354751;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Perikaryon
{ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell
projection, dendrite {ECO:0000250}. Golgi apparatus
{ECO:0000269|PubMed:17120249}. Endoplasmic reticulum
{ECO:0000269|PubMed:17120249}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5S007,
ECO:0000269|PubMed:17120249}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q5S007}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q5S007}. Endosome
{ECO:0000269|PubMed:17120249}. Lysosome
{ECO:0000269|PubMed:17120249}. Mitochondrion outer membrane
{ECO:0000269|PubMed:17120249}. Mitochondrion inner membrane
{ECO:0000269|PubMed:17120249}. Mitochondrion matrix
{ECO:0000269|PubMed:17120249}. Note=Localized in the cytoplasm and
associated with cellular membrane structures. 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).
Predominantly associated with intracytoplasmic vesicular and
membranous structures. Predominantly associated with the
mitochondrial outer membrane of the mitochondria. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
Detected throughout the adult brain. Expressed in deep cerebral
cortex layers, superficial cingulate cortex layers, the piriform
cortex, hippocampal formation, caudate putamen, substantia nigra,
the basolateral and basomedial anterior amygdala nuclei, reticular
thalamic nucleus and also in the cerebellar granular cell layer.
Highly expressed in the striatum, cortex and olfactory tubercle.
Little or no expression in the substantia nigra, where
dopaminergic neurons preferentially degenerate in Parkinson
disease. Expression is particularly high in brain dopaminoceptive
areas. High and strikingly specific expression in striatum and
parts of cortex and no signals in dopamine neurons.
{ECO:0000269|PubMed:16487147, ECO:0000269|PubMed:16504409,
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:0000250|UniProtKB:Q5S007}.
-!- DOMAIN: The Roc domain mediates homodimerization and regulates
kinase activity. {ECO:0000250|UniProtKB:Q5S007}.
-!- PTM: Autophosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
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EMBL; AY792512; AAV63976.1; -; mRNA.
EMBL; AC099704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC158752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK052591; BAC35052.1; -; mRNA.
EMBL; AK034413; BAC28700.1; -; mRNA.
EMBL; BC034074; AAH34074.1; -; mRNA.
EMBL; BC035949; AAH35949.1; -; mRNA.
CCDS; CCDS37180.1; -.
RefSeq; NP_080006.3; NM_025730.3.
UniGene; Mm.37558; -.
ProteinModelPortal; Q5S006; -.
BioGrid; 211674; 27.
DIP; DIP-58648N; -.
IntAct; Q5S006; 69.
STRING; 10090.ENSMUSP00000052584; -.
ChEMBL; CHEMBL2010622; -.
iPTMnet; Q5S006; -.
PhosphoSitePlus; Q5S006; -.
MaxQB; Q5S006; -.
PaxDb; Q5S006; -.
PeptideAtlas; Q5S006; -.
PRIDE; Q5S006; -.
Ensembl; ENSMUST00000060642; ENSMUSP00000052584; ENSMUSG00000036273.
GeneID; 66725; -.
KEGG; mmu:66725; -.
UCSC; uc007xhz.1; mouse.
CTD; 120892; -.
MGI; MGI:1913975; Lrrk2.
eggNOG; KOG0192; Eukaryota.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG1100; LUCA.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00910000144054; -.
HOGENOM; HOG000293315; -.
HOVERGEN; HBG081937; -.
InParanoid; Q5S006; -.
KO; K08844; -.
OMA; FKIRDQP; -.
OrthoDB; EOG091G003N; -.
TreeFam; TF313679; -.
Reactome; R-MMU-8857538; PTK6 promotes HIF1A stabilization.
PRO; PR:Q5S006; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000036273; Expressed in 171 organ(s), highest expression level in adult mammalian kidney.
CleanEx; MM_LRRK2; -.
Genevisible; Q5S006; MM.
GO; GO:0044753; C:amphisome; ISO:MGI.
GO; GO:0044754; C:autolysosome; ISO:MGI.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0099400; C:caveola neck; ISO:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005798; C:Golgi-associated vesicle; ISO:MGI.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0016234; C:inclusion body; ISO:MGI.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0005902; C:microvillus; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0097487; C:multivesicular body, internal vesicle; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0043195; C:terminal bouton; IC:ParkinsonsUK-UCL.
GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:1904713; F:beta-catenin destruction complex binding; IPI:ParkinsonsUK-UCL.
GO; GO:0030276; F:clathrin binding; ISO:MGI.
GO; GO:0005525; F:GTP binding; ISO:MGI.
GO; GO:0034211; F:GTP-dependent protein kinase activity; ISO:MGI.
GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
GO; GO:0003924; F:GTPase activity; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044325; F:ion channel binding; ISO:MGI.
GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; ISO:MGI.
GO; GO:0036479; F:peroxidase inhibitor activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0051018; F:protein kinase A binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0044877; F:protein-containing complex binding; IC:ParkinsonsUK-UCL.
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; ISO:MGI.
GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
GO; GO:0015631; F:tubulin binding; ISO:MGI.
GO; GO:0000187; P:activation of MAPK activity; ISO:MGI.
GO; GO:0000186; P:activation of MAPKK activity; ISO:MGI.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
GO; GO:0034613; P:cellular protein localization; IMP:ParkinsonsUK-UCL.
GO; GO:1903351; P:cellular response to dopamine; ISO:MGI.
GO; GO:0071287; P:cellular response to manganese ion; ISO:MGI.
GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
GO; GO:0008340; P:determination of adult lifespan; ISO:MGI.
GO; GO:0006897; P:endocytosis; ISO:MGI.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:ParkinsonsUK-UCL.
GO; GO:0035640; P:exploration behavior; ISO:MGI.
GO; GO:0007030; P:Golgi organization; IGI:MGI.
GO; GO:0046039; P:GTP metabolic process; ISO:MGI.
GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IMP:ParkinsonsUK-UCL.
GO; GO:0035641; P:locomotory exploration behavior; IMP:ParkinsonsUK-UCL.
GO; GO:0007040; P:lysosome organization; ISO:MGI.
GO; GO:0000165; P:MAPK cascade; ISO:MGI.
GO; GO:0051646; P:mitochondrion localization; ISO:MGI.
GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
GO; GO:1902902; P:negative regulation of autophagosome assembly; ISO:MGI.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:ParkinsonsUK-UCL.
GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISO:MGI.
GO; GO:0016242; P:negative regulation of macroautophagy; ISO:MGI.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0010955; P:negative regulation of protein processing; ISO:MGI.
GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; ISO:MGI.
GO; GO:1903125; P:negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0007528; P:neuromuscular junction development; ISO:MGI.
GO; GO:0070997; P:neuron death; ISO:MGI.
GO; GO:0140058; P:neuron projection arborization; ISO:MGI.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0021772; P:olfactory bulb development; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0016310; P:phosphorylation; ISO:MGI.
GO; GO:0010508; P:positive regulation of autophagy; IMP:BHF-UCL.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; ISO:MGI.
GO; GO:1901727; P:positive regulation of histone deacetylase activity; IMP:MGI.
GO; GO:1903980; P:positive regulation of microglial cell activation; ISO:MGI.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
GO; GO:0043068; P:positive regulation of programmed cell death; ISO:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:BHF-UCL.
GO; GO:1902499; P:positive regulation of protein autoubiquitination; ISO:MGI.
GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IDA:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
GO; GO:2000172; P:regulation of branching morphogenesis of a nerve; ISO:MGI.
GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; ISO:MGI.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IPI:ParkinsonsUK-UCL.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IGI:ParkinsonsUK-UCL.
GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0035564; P:regulation of kidney size; IMP:BHF-UCL.
GO; GO:0040012; P:regulation of locomotion; ISO:MGI.
GO; GO:0035751; P:regulation of lysosomal lumen pH; ISO:MGI.
GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
GO; GO:0051900; P:regulation of mitochondrial depolarization; ISO:MGI.
GO; GO:1902692; P:regulation of neuroblast proliferation; ISO:MGI.
GO; GO:1901214; P:regulation of neuron death; ISO:MGI.
GO; GO:0014041; P:regulation of neuron maturation; ISO:MGI.
GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:ParkinsonsUK-UCL.
GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; ISO:MGI.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:ParkinsonsUK-UCL.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
GO; GO:1902803; P:regulation of synaptic vesicle transport; IMP:ParkinsonsUK-UCL.
GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0021756; P:striatum development; IEA:Ensembl.
GO; GO:0036465; P:synaptic vesicle recycling; TAS:ParkinsonsUK-UCL.
GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; ISO:MGI.
GO; GO:1904887; P:Wnt signalosome assembly; ISO:MGI.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR032171; COR.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR025875; Leu-rich_rpt_4.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
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_sf.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF16095; COR; 1.
Pfam; PF12799; LRR_4; 1.
Pfam; PF13855; LRR_8; 2.
Pfam; PF00069; Pkinase; 1.
SMART; SM00369; LRR_TYP; 7.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF48371; SSF48371; 2.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF50978; SSF50978; 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;
ATP-binding; Autophagy; Cell junction; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Differentiation;
Endoplasmic reticulum; Endosome; Golgi apparatus; GTP-binding;
GTPase activation; Kinase; Leucine-rich repeat; Lysosome; Membrane;
Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase; Synapse;
Transferase; WD repeat.
CHAIN 1 2527 Leucine-rich repeat serine/threonine-
protein kinase 2.
/FTId=PRO_0000086239.
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 1151 LRR 7.
REPEAT 1174 1195 LRR 8.
REPEAT 1197 1218 LRR 9.
REPEAT 1221 1242 LRR 10.
REPEAT 1246 1267 LRR 11.
REPEAT 1269 1291 LRR 12.
DOMAIN 1328 1511 Roc. {ECO:0000255|PROSITE-
ProRule:PRU00758}.
DOMAIN 1879 2146 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}.
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 9 33 {ECO:0000255}.
COMPBIAS 10 16 Poly-Glu.
COMPBIAS 728 731 Poly-Leu.
COMPBIAS 971 976 Poly-Ser.
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:0000244|PubMed:21183079}.
CONFLICT 343 343 E -> K (in Ref. 3; BAC35052).
{ECO:0000305}.
CONFLICT 777 777 V -> I (in Ref. 1; AAV63976).
{ECO:0000305}.
CONFLICT 863 863 K -> N (in Ref. 1; AAV63976).
{ECO:0000305}.
CONFLICT 925 925 C -> Y (in Ref. 1; AAV63976).
{ECO:0000305}.
CONFLICT 1705 1707 WSR -> GQD (in Ref. 3; BAC28700).
{ECO:0000305}.
SEQUENCE 2527 AA; 284732 MW; 706E25C173E36F98 CRC64;
MASGACQGCE EEEEEEALKK LIVRLNNVQE GKQIETLLQL LEDMLVFTYS DRASKLFEDK
NFHVPLLIVL DSYMRVASVQ QAGWSLLCKL IEVCPGTLQS LIGPQDIGND WEVLGIHRLI
LKMLTVHHAN VNLSIVGLKA LDLLLDSGKL TLLILDEECD IFLLIFDAMH RYSANDEVQK
LGCKALHVLF ERVSEEQLTE FVENKDYTIL LSTFGSFRRD KEIVYHVLCC LHSLAVTCSN
VEVLMSGNVR CYNLVVEAMK AFPTNENIQE VSCSLFQKLT LGNFFNILVL NEVHVFVVKA
VRQYPENAAL QISALSCLAL LTETIFLNQD LEERSETQEQ SEEEDSEKLF WLEPCYKALV
RHRKDKHVQE AACWALNNLL MYQNSLHEKI GDEDGQFPAH REVMLSMLMH SSSKDVFQAA
AHALSTLLEQ NVNFRKILLA KGVYLNVLEL MQKHAHAPEV AESGCKMLSH LFEGSNPSLD
TMAAVVPKIL TVMKAHGTSL SVQLEALRAI LHFVVPGLLE ESREDSQCRP NVLRKQCFRT
DIHKLVLVAL NRFIGNPGIQ KCGLKVISSL AHLPDATETL SLQGAVDSVL HTLQMYPDDQ
EIQCLGLHLM GCLMTKKNFC IGTGHLLAKI LASTLQRFKD VAEVQTTGLQ TTLSILELSV
SFSKLLVHYS FDVVIFHQMS SSVVEQKDEQ FLNLCCKCFA KVAVDDELKN TMLERACDQN
NSIMVECLLL LGADANQVKG ATSLIYQVCE KESSPKLVEL LLNGGCREQD VRKALTVSIQ
KGDSQVISLL LRKLALDLAN NSICLGGFGI GKIDPSWLGP LFPDKSSNLR KQTNTGSVLA
RKVLRYQMRN TLQEGVASGS DGKFSEDALA KFGEWTFIPD SSMDSVFGQS DDLDSEGSES
SFLVKRKSNS ISVGEVYRDL ALQRCSPNAQ RHSNSLGPVF DHEDLLRRKR KILSSDESLR
SSRLPSHMRQ SDSSSSLASE REHITSLDLS ANELKDIDAL SQKCCLSSHL EHLTKLELHQ
NSLTSFPQQL CETLKCLIHL DLHSNKFTSF PSFVLKMPRI TNLDASRNDI GPTVVLDPAM
KCPSLKQLNL SYNQLSSIPE NLAQVVEKLE QLLLEGNKIS GICSPLSLKE LKILNLSKNH
IPSLPGDFLE ACSKVESFSA RMNFLAAMPA LPSSITSLKL SQNSFTCIPE AIFSLPHLRS
LDMSHNNIEC LPGPAHWKSL NLRELIFSKN QISTLDFSEN PHVWSRVEKL HLSHNKLKEI
PPEIGCLENL TSLDVSYNLE LRSFPNEMGK LSKIWDLPLD GLHLNFDFKH VGCKAKDIIR
FLQQRLKKAV PYNRMKLMIV GNTGSGKTTL LQQLMKMKKP ELGMQGATVG IDVRDWSIQI
RGKRRKDLVL NVWDFAGREE FYSTHPHFMT QRALYLAVYD LSKGQAEVDA MKPWLFNIKA
RASSSPVILV GTHLDVSDEK QRKACISKIT KELLNKRGFP TIRDYHFVNA TEESDALAKL
RKTIINESLN FKIRDQPVVG QLIPDCYVEL EKIILSERKA VPTEFPVINR KHLLQLVNEH
QLQLDENELP HAVHFLNESG VLLHFQDPAL QLSDLYFVEP KWLCKVMAQI LTVKVDGCLK
HPKGIISRRD VEKFLSKKKR FPKNYMMQYF KLLEKFQIAL PIGEEYLLVP SSLSDHRPVI
ELPHCENSEI IIRLYEMPYF PMGFWSRLIN RLLEISPFML SGRERALRPN RMYWRQGIYL
NWSPEAYCLV GSEVLDNRPE SFLKITVPSC RKGCILLGRV VDHIDSLMEE WFPGLLEIDI
CGEGETLLKK WALYSFNDGE EHQKILLDEL MKKAEEGDLL INPDQPRLTI PISQIAPDLI
LADLPRNIML NNDELEFEEA PEFLLGDGSF GSVYRAAYEG EEVAVKIFNK HTSLRLLRQE
LVVLCHLHHP SLISLLAAGI RPRMLVMELA SKGSLDRLLQ QDKASLTRTL QHRIALHVAD
GLRYLHSAMI IYRDLKPHNV LLFTLYPNAA IIAKIADYGI AQYCCRMGIK TSEGTPGFRA
PEVARGNVIY NQQADVYSFG LLLHDIWTTG SRIMEGLRFP NEFDELAIQG KLPDPVKEYG
CAPWPMVEKL ITKCLKENPQ ERPTSAQVFD ILNSAELICL MRHILIPKNI IVECMVATNL
NSKSATLWLG CGNTEKGQLS LFDLNTERYS YEEVADSRIL CLALVHLAAE KESWVVCGTQ
SGALLVINVE EETKRHTLEK MTDSVTCLHC NSLAKQSKQS NFLLVGTADG NLMIFEDKAV
KCKGAAPLKT LHIGDVSTPL MCLSESLNSS ERHITWGGCG TKVFSFSNDF TIQKLIETKT
NQLFSYAAFS DSNIIALAVD TALYIAKKNS PVVEVWDKKT EKLCELIDCV HFLKEVMVKL
NKESKHQLSY SGRVKALCLQ KNTALWIGTG GGHILLLDLS TRRVIRTIHN FCDSVRAMAT
AQLGSLKNVM LVLGYKRKST EGIQEQKEIQ SCLSIWDLNL PHEVQNLEKH IEVRTELADK
MRKTSVE


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