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Q5S006 (LRRK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine-rich repeat serine/threonine-protein kinase 2

EC=2.7.11.1
Gene names
Name:Lrrk2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2527 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates PRDX3 By similarity. May also have GTPase activity By similarity. Has a regulatory role in autophagy induction through a calcium-dependent activation of the CaMKK/AMPK signaling pathway By similarity. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Homodimer By similarity. Interacts with PARK2 By similarity. Interacts with PRDX3 By similarity. Interacts with TPCN2 By similarity.

Subcellular location

Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity. Mitochondrion By similarity. Note: Localized in the cytoplasm and associated with cellular membrane structures By similarity. Associates with the mitochondrial outer membrane By similarity.

Tissue specificity

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. Ref.5 Ref.6 Ref.7

Post-translational modification

Autophosphorylated By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.

Contains 12 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Contains 1 Roc domain.

Ontologies

Keywords
   Biological processAutophagy
   Cellular componentCytoplasm
Membrane
Mitochondrion
   DomainCoiled coil
Leucine-rich repeat
Repeat
   LigandATP-binding
GTP-binding
Nucleotide-binding
   Molecular functionGTPase activation
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPKK activity

Inferred from electronic annotation. Source: Ensembl

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

determination of adult lifespan

Inferred from electronic annotation. Source: Ensembl

exploration behavior

Inferred from electronic annotation. Source: Ensembl

intracellular distribution of mitochondria

Inferred from electronic annotation. Source: Ensembl

negative regulation of GTPase activity

Inferred from sequence orthology PubMed 22423108. Source: MGI

negative regulation of branching morphogenesis of a nerve

Inferred from electronic annotation. Source: Ensembl

negative regulation of dendritic spine morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron maturation

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction development

Inferred from electronic annotation. Source: Ensembl

neuron death

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of autophagy

Inferred from mutant phenotype PubMed 20457918. Source: BHF-UCL

positive regulation of dopamine receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of programmed cell death

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 20457918. Source: BHF-UCL

positive regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from sequence alignment PubMed 16980962. Source: MGI

protein phosphorylation

Inferred from sequence alignment PubMed 16980962. Source: MGI

regulation of kidney size

Inferred from mutant phenotype PubMed 20457918. Source: BHF-UCL

regulation of locomotion

Inferred from electronic annotation. Source: Ensembl

regulation of membrane potential

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

tangential migration from the subventricular zone to the olfactory bulb

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytoplasmic side of mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

dendrite cytoplasm

Inferred from electronic annotation. Source: Ensembl

membrane raft

Inferred from direct assay PubMed 17341485. Source: MGI

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 17341485. Source: MGI

synapse

Inferred from direct assay PubMed 22423108. Source: MGI

synaptic vesicle

Inferred from direct assay PubMed 17341485. Source: MGI

trans-Golgi network

Inferred from direct assay PubMed 17341485. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP binding

Inferred from sequence alignment PubMed 16980962. Source: MGI

GTP-dependent protein kinase activity

Inferred from sequence alignment PubMed 16980962. Source: MGI

GTPase activator activity

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: Ensembl

MAP kinase kinase activity

Inferred from electronic annotation. Source: Ensembl

Rho GTPase binding

Inferred from physical interaction PubMed 21048939. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 21390248PubMed 22952686. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25272527Leucine-rich repeat serine/threonine-protein kinase 2
PRO_0000086239

Regions

Repeat983 – 100422LRR 1
Repeat1012 – 103322LRR 2
Repeat1036 – 105722LRR 3
Repeat1059 – 108022LRR 4
Repeat1084 – 110522LRR 5
Repeat1108 – 112922LRR 6
Repeat1130 – 115122LRR 7
Repeat1174 – 119522LRR 8
Repeat1197 – 121822LRR 9
Repeat1221 – 124222LRR 10
Repeat1246 – 126722LRR 11
Repeat1269 – 129123LRR 12
Domain1328 – 1511184Roc
Domain1879 – 2146268Protein kinase
Nucleotide binding1341 – 13488GTP Potential
Nucleotide binding1885 – 18939ATP By similarity
Nucleotide binding2098 – 212124GTP Potential
Nucleotide binding2295 – 22984GTP Potential
Coiled coil9 – 3325 Potential
Compositional bias10 – 167Poly-Glu
Compositional bias728 – 7314Poly-Leu
Compositional bias971 – 9766Poly-Ser

Sites

Active site19941Proton acceptor By similarity
Binding site19061ATP By similarity

Experimental info

Sequence conflict3431E → K in BAC35052. Ref.3
Sequence conflict7771V → I in AAV63976. Ref.1
Sequence conflict8631K → N in AAV63976. Ref.1
Sequence conflict9251C → Y in AAV63976. Ref.1
Sequence conflict1705 – 17073WSR → GQD in BAC28700. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q5S006 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 706E25C173E36F98

FASTA2,527284,732
        10         20         30         40         50         60 
MASGACQGCE EEEEEEALKK LIVRLNNVQE GKQIETLLQL LEDMLVFTYS DRASKLFEDK 

        70         80         90        100        110        120 
NFHVPLLIVL DSYMRVASVQ QAGWSLLCKL IEVCPGTLQS LIGPQDIGND WEVLGIHRLI 

       130        140        150        160        170        180 
LKMLTVHHAN VNLSIVGLKA LDLLLDSGKL TLLILDEECD IFLLIFDAMH RYSANDEVQK 

       190        200        210        220        230        240 
LGCKALHVLF ERVSEEQLTE FVENKDYTIL LSTFGSFRRD KEIVYHVLCC LHSLAVTCSN 

       250        260        270        280        290        300 
VEVLMSGNVR CYNLVVEAMK AFPTNENIQE VSCSLFQKLT LGNFFNILVL NEVHVFVVKA 

       310        320        330        340        350        360 
VRQYPENAAL QISALSCLAL LTETIFLNQD LEERSETQEQ SEEEDSEKLF WLEPCYKALV 

       370        380        390        400        410        420 
RHRKDKHVQE AACWALNNLL MYQNSLHEKI GDEDGQFPAH REVMLSMLMH SSSKDVFQAA 

       430        440        450        460        470        480 
AHALSTLLEQ NVNFRKILLA KGVYLNVLEL MQKHAHAPEV AESGCKMLSH LFEGSNPSLD 

       490        500        510        520        530        540 
TMAAVVPKIL TVMKAHGTSL SVQLEALRAI LHFVVPGLLE ESREDSQCRP NVLRKQCFRT 

       550        560        570        580        590        600 
DIHKLVLVAL NRFIGNPGIQ KCGLKVISSL AHLPDATETL SLQGAVDSVL HTLQMYPDDQ 

       610        620        630        640        650        660 
EIQCLGLHLM GCLMTKKNFC IGTGHLLAKI LASTLQRFKD VAEVQTTGLQ TTLSILELSV 

       670        680        690        700        710        720 
SFSKLLVHYS FDVVIFHQMS SSVVEQKDEQ FLNLCCKCFA KVAVDDELKN TMLERACDQN 

       730        740        750        760        770        780 
NSIMVECLLL LGADANQVKG ATSLIYQVCE KESSPKLVEL LLNGGCREQD VRKALTVSIQ 

       790        800        810        820        830        840 
KGDSQVISLL LRKLALDLAN NSICLGGFGI GKIDPSWLGP LFPDKSSNLR KQTNTGSVLA 

       850        860        870        880        890        900 
RKVLRYQMRN TLQEGVASGS DGKFSEDALA KFGEWTFIPD SSMDSVFGQS DDLDSEGSES 

       910        920        930        940        950        960 
SFLVKRKSNS ISVGEVYRDL ALQRCSPNAQ RHSNSLGPVF DHEDLLRRKR KILSSDESLR 

       970        980        990       1000       1010       1020 
SSRLPSHMRQ SDSSSSLASE REHITSLDLS ANELKDIDAL SQKCCLSSHL EHLTKLELHQ 

      1030       1040       1050       1060       1070       1080 
NSLTSFPQQL CETLKCLIHL DLHSNKFTSF PSFVLKMPRI TNLDASRNDI GPTVVLDPAM 

      1090       1100       1110       1120       1130       1140 
KCPSLKQLNL SYNQLSSIPE NLAQVVEKLE QLLLEGNKIS GICSPLSLKE LKILNLSKNH 

      1150       1160       1170       1180       1190       1200 
IPSLPGDFLE ACSKVESFSA RMNFLAAMPA LPSSITSLKL SQNSFTCIPE AIFSLPHLRS 

      1210       1220       1230       1240       1250       1260 
LDMSHNNIEC LPGPAHWKSL NLRELIFSKN QISTLDFSEN PHVWSRVEKL HLSHNKLKEI 

      1270       1280       1290       1300       1310       1320 
PPEIGCLENL TSLDVSYNLE LRSFPNEMGK LSKIWDLPLD GLHLNFDFKH VGCKAKDIIR 

      1330       1340       1350       1360       1370       1380 
FLQQRLKKAV PYNRMKLMIV GNTGSGKTTL LQQLMKMKKP ELGMQGATVG IDVRDWSIQI 

      1390       1400       1410       1420       1430       1440 
RGKRRKDLVL NVWDFAGREE FYSTHPHFMT QRALYLAVYD LSKGQAEVDA MKPWLFNIKA 

      1450       1460       1470       1480       1490       1500 
RASSSPVILV GTHLDVSDEK QRKACISKIT KELLNKRGFP TIRDYHFVNA TEESDALAKL 

      1510       1520       1530       1540       1550       1560 
RKTIINESLN FKIRDQPVVG QLIPDCYVEL EKIILSERKA VPTEFPVINR KHLLQLVNEH 

      1570       1580       1590       1600       1610       1620 
QLQLDENELP HAVHFLNESG VLLHFQDPAL QLSDLYFVEP KWLCKVMAQI LTVKVDGCLK 

      1630       1640       1650       1660       1670       1680 
HPKGIISRRD VEKFLSKKKR FPKNYMMQYF KLLEKFQIAL PIGEEYLLVP SSLSDHRPVI 

      1690       1700       1710       1720       1730       1740 
ELPHCENSEI IIRLYEMPYF PMGFWSRLIN RLLEISPFML SGRERALRPN RMYWRQGIYL 

      1750       1760       1770       1780       1790       1800 
NWSPEAYCLV GSEVLDNRPE SFLKITVPSC RKGCILLGRV VDHIDSLMEE WFPGLLEIDI 

      1810       1820       1830       1840       1850       1860 
CGEGETLLKK WALYSFNDGE EHQKILLDEL MKKAEEGDLL INPDQPRLTI PISQIAPDLI 

      1870       1880       1890       1900       1910       1920 
LADLPRNIML NNDELEFEEA PEFLLGDGSF GSVYRAAYEG EEVAVKIFNK HTSLRLLRQE 

      1930       1940       1950       1960       1970       1980 
LVVLCHLHHP SLISLLAAGI RPRMLVMELA SKGSLDRLLQ QDKASLTRTL QHRIALHVAD 

      1990       2000       2010       2020       2030       2040 
GLRYLHSAMI IYRDLKPHNV LLFTLYPNAA IIAKIADYGI AQYCCRMGIK TSEGTPGFRA 

      2050       2060       2070       2080       2090       2100 
PEVARGNVIY NQQADVYSFG LLLHDIWTTG SRIMEGLRFP NEFDELAIQG KLPDPVKEYG 

      2110       2120       2130       2140       2150       2160 
CAPWPMVEKL ITKCLKENPQ ERPTSAQVFD ILNSAELICL MRHILIPKNI IVECMVATNL 

      2170       2180       2190       2200       2210       2220 
NSKSATLWLG CGNTEKGQLS LFDLNTERYS YEEVADSRIL CLALVHLAAE KESWVVCGTQ 

      2230       2240       2250       2260       2270       2280 
SGALLVINVE EETKRHTLEK MTDSVTCLHC NSLAKQSKQS NFLLVGTADG NLMIFEDKAV 

      2290       2300       2310       2320       2330       2340 
KCKGAAPLKT LHIGDVSTPL MCLSESLNSS ERHITWGGCG TKVFSFSNDF TIQKLIETKT 

      2350       2360       2370       2380       2390       2400 
NQLFSYAAFS DSNIIALAVD TALYIAKKNS PVVEVWDKKT EKLCELIDCV HFLKEVMVKL 

      2410       2420       2430       2440       2450       2460 
NKESKHQLSY SGRVKALCLQ KNTALWIGTG GGHILLLDLS TRRVIRTIHN FCDSVRAMAT 

      2470       2480       2490       2500       2510       2520 
AQLGSLKNVM LVLGYKRKST EGIQEQKEIQ SCLSIWDLNL PHEVQNLEKH IEVRTELADK 


MRKTSVE 

« Hide

References

« Hide 'large scale' references
[1]"Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology."
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. expand/collapse author list , Meitinger T., Strom T.M., Wszolek Z.K., Gasser T.
Neuron 44:601-607(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Swiss Webster.
Tissue: Embryo.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"LRRK2 expression linked to dopamine-innervated areas."
Galter D., Westerlund M., Carmine A., Lindqvist E., Sydow O., Olson L.
Ann. Neurol. 59:714-719(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"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.
[7]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_080006.3. NM_025730.3.
UniGeneMm.37558.

3D structure databases

ProteinModelPortalQ5S006.
SMRQ5S006. Positions 1335-1512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211674. 24 interactions.
DIPDIP-58648N.
IntActQ5S006. 57 interactions.

Chemistry

ChEMBLCHEMBL2010622.

PTM databases

PhosphoSiteQ5S006.

Proteomic databases

PaxDbQ5S006.
PRIDEQ5S006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000060642; ENSMUSP00000052584; ENSMUSG00000036273.
GeneID66725.
KEGGmmu:66725.
UCSCuc007xhz.1. mouse.

Organism-specific databases

CTD120892.
MGIMGI:1913975. Lrrk2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000063477.
HOGENOMHOG000293315.
HOVERGENHBG081937.
InParanoidQ5S006.
KOK08844.
OMAFKIRDQP.
OrthoDBEOG7R56RK.
TreeFamTF313679.

Gene expression databases

BgeeQ5S006.
CleanExMM_LRRK2.
GenevestigatorQ5S006.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
1.25.40.20. 1 hit.
2.130.10.10. 2 hits.
3.40.50.300. 1 hit.
InterProIPR002110. 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]
PfamPF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF08477. Miro. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00248. ANK. 2 hits.
SM00320. WD40. 2 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
SSF48403. SSF48403. 1 hit.
SSF50978. SSF50978. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56112. SSF56112. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51450. 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]
ProtoNetSearch...

Other

NextBio322485.
PROQ5S006.
SOURCESearch...

Entry information

Entry nameLRRK2_MOUSE
AccessionPrimary (citable) accession number: Q5S006
Secondary accession number(s): E9QNJ2 expand/collapse secondary AC list , Q8BWG7, Q8BZJ6, Q8CI84, Q8K062
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot