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Q5S006

- LRRK2_MOUSE

UniProt

Q5S006 - LRRK2_MOUSE

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Protein
Leucine-rich repeat serine/threonine-protein kinase 2
Gene
Lrrk2
Organism
Mus musculus (Mouse)
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 By similarity.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1906 – 19061ATP By similarity
Active sitei1994 – 19941Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1341 – 13488GTP Reviewed prediction
Nucleotide bindingi1885 – 18939ATP By similarity
Nucleotide bindingi2098 – 212124GTP Reviewed prediction
Add
BLAST
Nucleotide bindingi2295 – 22984GTP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GTP binding Source: MGI
  3. GTP-dependent protein kinase activity Source: MGI
  4. GTPase activator activity Source: UniProtKB-KW
  5. GTPase activity Source: Ensembl
  6. MAP kinase kinase activity Source: Ensembl
  7. Rho GTPase binding Source: BHF-UCL
  8. identical protein binding Source: IntAct
  9. protein binding Source: IntAct
  10. protein kinase A binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. activation of MAPKK activity Source: Ensembl
  2. autophagy Source: UniProtKB-KW
  3. cellular protein localization Source: ParkinsonsUK-UCL
  4. cellular response to organic cyclic compound Source: Ensembl
  5. determination of adult lifespan Source: Ensembl
  6. intracellular distribution of mitochondria Source: Ensembl
  7. intracellular signal transduction Source: ParkinsonsUK-UCL
  8. locomotory exploration behavior Source: ParkinsonsUK-UCL
  9. negative regulation of GTPase activity Source: MGI
  10. negative regulation of branching morphogenesis of a nerve Source: Ensembl
  11. negative regulation of dendritic spine morphogenesis Source: Ensembl
  12. negative regulation of neuroblast proliferation Source: Ensembl
  13. negative regulation of neuron maturation Source: Ensembl
  14. negative regulation of protein phosphorylation Source: ParkinsonsUK-UCL
  15. neuromuscular junction development Source: Ensembl
  16. neuron death Source: Ensembl
  17. peptidyl-serine phosphorylation Source: Ensembl
  18. peptidyl-threonine phosphorylation Source: Ensembl
  19. positive regulation of autophagy Source: BHF-UCL
  20. positive regulation of dopamine receptor signaling pathway Source: Ensembl
  21. positive regulation of programmed cell death Source: Ensembl
  22. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  23. positive regulation of protein ubiquitination Source: Ensembl
  24. protein autophosphorylation Source: MGI
  25. protein phosphorylation Source: MGI
  26. regulation of dendritic spine morphogenesis Source: ParkinsonsUK-UCL
  27. regulation of dopamine receptor signaling pathway Source: ParkinsonsUK-UCL
  28. regulation of excitatory postsynaptic membrane potential Source: ParkinsonsUK-UCL
  29. regulation of kidney size Source: BHF-UCL
  30. regulation of locomotion Source: Ensembl
  31. regulation of protein kinase A signaling Source: ParkinsonsUK-UCL
  32. regulation of synaptic transmission, glutamatergic Source: ParkinsonsUK-UCL
  33. regulation of synaptic vesicle transport Source: ParkinsonsUK-UCL
  34. response to oxidative stress Source: Ensembl
  35. small GTPase mediated signal transduction Source: InterPro
  36. tangential migration from the subventricular zone to the olfactory bulb Source: Ensembl
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

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat serine/threonine-protein kinase 2 (EC:2.7.11.1)
Gene namesi
Name:Lrrk2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1913975. Lrrk2.

Subcellular locationi

Membrane; Peripheral membrane protein By similarity. Cytoplasm By similarity. Perikaryon By similarity. Cell projectionaxon By similarity. Cell projectiondendrite By similarity. Golgi apparatus. Endoplasmic reticulum. Cytoplasmic vesicle. Endosome. Lysosome. Mitochondrion outer membrane. Mitochondrion inner membrane. Mitochondrion matrix
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.

GO - Cellular componenti

  1. cytoplasmic side of mitochondrial outer membrane Source: Ensembl
  2. dendrite Source: ParkinsonsUK-UCL
  3. dendrite cytoplasm Source: Ensembl
  4. membrane raft Source: MGI
  5. neuronal cell body Source: Ensembl
  6. plasma membrane Source: MGI
  7. synapse Source: MGI
  8. synaptic vesicle Source: MGI
  9. terminal bouton Source: ParkinsonsUK-UCL
  10. trans-Golgi network Source: MGI
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25272527Leucine-rich repeat serine/threonine-protein kinase 2
PRO_0000086239Add
BLAST

Post-translational modificationi

Autophosphorylated By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5S006.
PaxDbiQ5S006.
PRIDEiQ5S006.

PTM databases

PhosphoSiteiQ5S006.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ5S006.
CleanExiMM_LRRK2.
GenevestigatoriQ5S006.

Interactioni

Subunit structurei

Homodimer. Interacts with PARK2, PRDX3 and TPCN2 By similarity. Interacts with VPS35 and RAB29.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-2693710,EBI-2693710
Arfgap1Q9EPJ93EBI-2693710,EBI-6288020
Dnm1lQ8K1M64EBI-2693710,EBI-2365792
NsfP464603EBI-2693710,EBI-398006
Prkar2bP313243EBI-2693710,EBI-455340
YwhabQ9CQV83EBI-2693710,EBI-771608
YwhaeP622593EBI-2693710,EBI-356480
YwhagP619827EBI-2693710,EBI-359843
YwhahP685104EBI-2693710,EBI-444641
YwhaqP682543EBI-2693710,EBI-400675
YwhazP631014EBI-2693710,EBI-354751

Protein-protein interaction databases

BioGridi211674. 24 interactions.
DIPiDIP-58648N.
IntActiQ5S006. 61 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ5S006.
SMRiQ5S006. Positions 1335-1512.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati983 – 100422LRR 1
Add
BLAST
Repeati1012 – 103322LRR 2
Add
BLAST
Repeati1036 – 105722LRR 3
Add
BLAST
Repeati1059 – 108022LRR 4
Add
BLAST
Repeati1084 – 110522LRR 5
Add
BLAST
Repeati1108 – 112922LRR 6
Add
BLAST
Repeati1130 – 115122LRR 7
Add
BLAST
Repeati1174 – 119522LRR 8
Add
BLAST
Repeati1197 – 121822LRR 9
Add
BLAST
Repeati1221 – 124222LRR 10
Add
BLAST
Repeati1246 – 126722LRR 11
Add
BLAST
Repeati1269 – 129123LRR 12
Add
BLAST
Domaini1328 – 1511184Roc
Add
BLAST
Domaini1879 – 2146268Protein kinase
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili9 – 3325 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 167Poly-Glu
Compositional biasi728 – 7314Poly-Leu
Compositional biasi971 – 9766Poly-Ser

Sequence similaritiesi

Contains 1 Roc domain.

Keywords - Domaini

Coiled coil, Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063477.
HOGENOMiHOG000293315.
HOVERGENiHBG081937.
InParanoidiQ5S006.
KOiK08844.
OMAiFKIRDQP.
OrthoDBiEOG7R56RK.
TreeFamiTF313679.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
1.25.40.20. 1 hit.
2.130.10.10. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
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.
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.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 1 hit.
PF08477. Miro. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00248. ANK. 2 hits.
SM00320. WD40. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF48403. SSF48403. 1 hit.
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.

Q5S006-1 [UniParc]FASTAAdd to Basket

« Hide

MASGACQGCE EEEEEEALKK LIVRLNNVQE GKQIETLLQL LEDMLVFTYS     50
DRASKLFEDK NFHVPLLIVL DSYMRVASVQ QAGWSLLCKL IEVCPGTLQS 100
LIGPQDIGND WEVLGIHRLI LKMLTVHHAN VNLSIVGLKA LDLLLDSGKL 150
TLLILDEECD IFLLIFDAMH RYSANDEVQK LGCKALHVLF ERVSEEQLTE 200
FVENKDYTIL LSTFGSFRRD KEIVYHVLCC LHSLAVTCSN VEVLMSGNVR 250
CYNLVVEAMK AFPTNENIQE VSCSLFQKLT LGNFFNILVL NEVHVFVVKA 300
VRQYPENAAL QISALSCLAL LTETIFLNQD LEERSETQEQ SEEEDSEKLF 350
WLEPCYKALV RHRKDKHVQE AACWALNNLL MYQNSLHEKI GDEDGQFPAH 400
REVMLSMLMH SSSKDVFQAA AHALSTLLEQ NVNFRKILLA KGVYLNVLEL 450
MQKHAHAPEV AESGCKMLSH LFEGSNPSLD TMAAVVPKIL TVMKAHGTSL 500
SVQLEALRAI LHFVVPGLLE ESREDSQCRP NVLRKQCFRT DIHKLVLVAL 550
NRFIGNPGIQ KCGLKVISSL AHLPDATETL SLQGAVDSVL HTLQMYPDDQ 600
EIQCLGLHLM GCLMTKKNFC IGTGHLLAKI LASTLQRFKD VAEVQTTGLQ 650
TTLSILELSV SFSKLLVHYS FDVVIFHQMS SSVVEQKDEQ FLNLCCKCFA 700
KVAVDDELKN TMLERACDQN NSIMVECLLL LGADANQVKG ATSLIYQVCE 750
KESSPKLVEL LLNGGCREQD VRKALTVSIQ KGDSQVISLL LRKLALDLAN 800
NSICLGGFGI GKIDPSWLGP LFPDKSSNLR KQTNTGSVLA RKVLRYQMRN 850
TLQEGVASGS DGKFSEDALA KFGEWTFIPD SSMDSVFGQS DDLDSEGSES 900
SFLVKRKSNS ISVGEVYRDL ALQRCSPNAQ RHSNSLGPVF DHEDLLRRKR 950
KILSSDESLR SSRLPSHMRQ SDSSSSLASE REHITSLDLS ANELKDIDAL 1000
SQKCCLSSHL EHLTKLELHQ NSLTSFPQQL CETLKCLIHL DLHSNKFTSF 1050
PSFVLKMPRI TNLDASRNDI GPTVVLDPAM KCPSLKQLNL SYNQLSSIPE 1100
NLAQVVEKLE QLLLEGNKIS GICSPLSLKE LKILNLSKNH IPSLPGDFLE 1150
ACSKVESFSA RMNFLAAMPA LPSSITSLKL SQNSFTCIPE AIFSLPHLRS 1200
LDMSHNNIEC LPGPAHWKSL NLRELIFSKN QISTLDFSEN PHVWSRVEKL 1250
HLSHNKLKEI PPEIGCLENL TSLDVSYNLE LRSFPNEMGK LSKIWDLPLD 1300
GLHLNFDFKH VGCKAKDIIR FLQQRLKKAV PYNRMKLMIV GNTGSGKTTL 1350
LQQLMKMKKP ELGMQGATVG IDVRDWSIQI RGKRRKDLVL NVWDFAGREE 1400
FYSTHPHFMT QRALYLAVYD LSKGQAEVDA MKPWLFNIKA RASSSPVILV 1450
GTHLDVSDEK QRKACISKIT KELLNKRGFP TIRDYHFVNA TEESDALAKL 1500
RKTIINESLN FKIRDQPVVG QLIPDCYVEL EKIILSERKA VPTEFPVINR 1550
KHLLQLVNEH QLQLDENELP HAVHFLNESG VLLHFQDPAL QLSDLYFVEP 1600
KWLCKVMAQI LTVKVDGCLK HPKGIISRRD VEKFLSKKKR FPKNYMMQYF 1650
KLLEKFQIAL PIGEEYLLVP SSLSDHRPVI ELPHCENSEI IIRLYEMPYF 1700
PMGFWSRLIN RLLEISPFML SGRERALRPN RMYWRQGIYL NWSPEAYCLV 1750
GSEVLDNRPE SFLKITVPSC RKGCILLGRV VDHIDSLMEE WFPGLLEIDI 1800
CGEGETLLKK WALYSFNDGE EHQKILLDEL MKKAEEGDLL INPDQPRLTI 1850
PISQIAPDLI LADLPRNIML NNDELEFEEA PEFLLGDGSF GSVYRAAYEG 1900
EEVAVKIFNK HTSLRLLRQE LVVLCHLHHP SLISLLAAGI RPRMLVMELA 1950
SKGSLDRLLQ QDKASLTRTL QHRIALHVAD GLRYLHSAMI IYRDLKPHNV 2000
LLFTLYPNAA IIAKIADYGI AQYCCRMGIK TSEGTPGFRA PEVARGNVIY 2050
NQQADVYSFG LLLHDIWTTG SRIMEGLRFP NEFDELAIQG KLPDPVKEYG 2100
CAPWPMVEKL ITKCLKENPQ ERPTSAQVFD ILNSAELICL MRHILIPKNI 2150
IVECMVATNL NSKSATLWLG CGNTEKGQLS LFDLNTERYS YEEVADSRIL 2200
CLALVHLAAE KESWVVCGTQ SGALLVINVE EETKRHTLEK MTDSVTCLHC 2250
NSLAKQSKQS NFLLVGTADG NLMIFEDKAV KCKGAAPLKT LHIGDVSTPL 2300
MCLSESLNSS ERHITWGGCG TKVFSFSNDF TIQKLIETKT NQLFSYAAFS 2350
DSNIIALAVD TALYIAKKNS PVVEVWDKKT EKLCELIDCV HFLKEVMVKL 2400
NKESKHQLSY SGRVKALCLQ KNTALWIGTG GGHILLLDLS TRRVIRTIHN 2450
FCDSVRAMAT AQLGSLKNVM LVLGYKRKST EGIQEQKEIQ SCLSIWDLNL 2500
PHEVQNLEKH IEVRTELADK MRKTSVE 2527
Length:2,527
Mass (Da):284,732
Last modified:July 27, 2011 - v2
Checksum:i706E25C173E36F98
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti343 – 3431E → K in BAC35052. 1 Publication
Sequence conflicti777 – 7771V → I in AAV63976. 1 Publication
Sequence conflicti863 – 8631K → N in AAV63976. 1 Publication
Sequence conflicti925 – 9251C → Y in AAV63976. 1 Publication
Sequence conflicti1705 – 17073WSR → GQD in BAC28700. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY792512 mRNA. Translation: AAV63976.1.
AC099704 Genomic DNA. No translation available.
AC158752 Genomic DNA. No translation available.
AK052591 mRNA. Translation: BAC35052.1.
AK034413 mRNA. Translation: BAC28700.1.
BC034074 mRNA. Translation: AAH34074.1.
BC035949 mRNA. Translation: AAH35949.1.
CCDSiCCDS37180.1.
RefSeqiNP_080006.3. NM_025730.3.
UniGeneiMm.37558.

Genome annotation databases

EnsembliENSMUST00000060642; ENSMUSP00000052584; ENSMUSG00000036273.
GeneIDi66725.
KEGGimmu:66725.
UCSCiuc007xhz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY792512 mRNA. Translation: AAV63976.1 .
AC099704 Genomic DNA. No translation available.
AC158752 Genomic DNA. No translation available.
AK052591 mRNA. Translation: BAC35052.1 .
AK034413 mRNA. Translation: BAC28700.1 .
BC034074 mRNA. Translation: AAH34074.1 .
BC035949 mRNA. Translation: AAH35949.1 .
CCDSi CCDS37180.1.
RefSeqi NP_080006.3. NM_025730.3.
UniGenei Mm.37558.

3D structure databases

ProteinModelPortali Q5S006.
SMRi Q5S006. Positions 1335-1512.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 211674. 24 interactions.
DIPi DIP-58648N.
IntActi Q5S006. 61 interactions.

Chemistry

ChEMBLi CHEMBL2010622.

PTM databases

PhosphoSitei Q5S006.

Proteomic databases

MaxQBi Q5S006.
PaxDbi Q5S006.
PRIDEi Q5S006.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000060642 ; ENSMUSP00000052584 ; ENSMUSG00000036273 .
GeneIDi 66725.
KEGGi mmu:66725.
UCSCi uc007xhz.1. mouse.

Organism-specific databases

CTDi 120892.
MGIi MGI:1913975. Lrrk2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000063477.
HOGENOMi HOG000293315.
HOVERGENi HBG081937.
InParanoidi Q5S006.
KOi K08844.
OMAi FKIRDQP.
OrthoDBi EOG7R56RK.
TreeFami TF313679.

Miscellaneous databases

NextBioi 322485.
PROi Q5S006.
SOURCEi Search...

Gene expression databases

Bgeei Q5S006.
CleanExi MM_LRRK2.
Genevestigatori Q5S006.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
1.25.40.20. 1 hit.
2.130.10.10. 2 hits.
3.40.50.300. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
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.
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.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 1 hit.
PF08477. Miro. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00248. ANK. 2 hits.
SM00320. WD40. 2 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
SSF48403. SSF48403. 1 hit.
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].
    Strain: Swiss Webster.
    Tissue: Embryo.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-946 AND 1162-1707.
    Strain: C57BL/6J.
    Tissue: Kidney.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1688-2527.
    Strain: FVB/N.
    Tissue: Kidney.
  5. Cited for: TISSUE SPECIFICITY.
  6. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "LRRK2 is expressed in areas affected by Parkinson's disease in the adult mouse brain."
    Simon-Sanchez J., Herranz-Perez V., Olucha-Bordonau F., Perez-Tur J.
    Eur. J. Neurosci. 23:659-666(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Anatomical localization of leucine-rich repeat kinase 2 in mouse brain."
    Melrose H., Lincoln S., Tyndall G., Dickson D., Farrer M.
    Neuroscience 139:791-794(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "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: INTERACTION WITH VPS35 AND RAB29.

Entry informationi

Entry nameiLRRK2_MOUSE
AccessioniPrimary (citable) accession number: Q5S006
Secondary accession number(s): E9QNJ2
, Q8BWG7, Q8BZJ6, Q8CI84, Q8K062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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