Reviewed, UniProtKB/Swiss-Prot Q5S007 (LRRK2_HUMAN)

Names and origin

Protein names

Recommended name:
    Leucine-rich repeat serine/threonine-protein kinase 2
    EC=2.7.11.1
Alternative name(s):
    Dardarin

Gene names

Name:	LRRK2
Synonyms:	PARK8

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2527 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probable protein kinase whose role is not yet known. May play a role in the phosphorylation of proteins central to Parkinson disease. May also have GTPase activity. Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with PARK2. Ref.8
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein. Note: Localized in the cytoplasm and associated with cellular membrane structures. Associates with the mitochondrial outer membrane. Ref.8 Ref.5 Ref.7
Tissue specificity	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. Ref.1 Ref.9 Ref.10
Involvement in disease	Defects in LRRK2 are the cause of Parkinson disease type 8 (PARK8) [MIM:607060, 168600]. Parkinson disease (PD) is a complex, multifactorial disorder that typically manifests after the age of 50 years, although early-onset cases (before 50 years) are known. PD generally arises as a sporadic condition but is occasionally inherited as a simple mendelian trait. Although sporadic and familial PD are very similar, inherited forms of the disease usually begin at earlier ages and are associated with atypical clinical features. PD is characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. PARK8 is an autosomal-dominant late-onset parkinsonism, characterized by onset from 50 to 65 years, with slow progression and relatively benign course. Ref.5 Ref.1 Ref.10 Ref.4 Ref.6 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.22 Ref.27 Ref.28 Ref.33 Ref.36
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Contains 16 LRR (leucine-rich) repeats. Contains 1 protein kinase domain. Contains 1 Roc domain.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Parkinson disease
Domain	Coiled coil Leucine-rich repeat Repeat
Ligand	ATP-binding GTP-binding Nucleotide-binding
Molecular function	GTPase activation Kinase Serine/threonine-protein kinase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	activation of MAPKK activity Inferred from direct assay. Source: UniProtKB cell death Inferred from mutant phenotype. Source: UniProtKB determination of adult lifespan Inferred from mutant phenotype. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay. Source: UniProtKB positive regulation of programmed cell death Inferred from direct assay. Source: UniProtKB positive regulation of protein ubiquitination Ref.8 Inferred from direct assay. Source: UniProtKB protein amino acid autophosphorylation Ref.5 Ref.7 Inferred from direct assay. Source: UniProtKB regulation of locomotion Inferred from mutant phenotype. Source: UniProtKB response to oxidative stress Inferred from mutant phenotype. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	external side of mitochondrial outer membrane Ref.7 Inferred from direct assay. Source: UniProtKB extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from direct assay. Source: UniProtKB GTP-dependent protein kinase activity Inferred from mutant phenotype. Source: UniProtKB GTPase activator activity Inferred from direct assay. Source: UniProtKB MAP kinase kinase activity Inferred from direct assay. Source: UniProtKB protein homodimerization activity Ref.5 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5S007-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q5S007-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-401: Missing.
     1260-1271: IPPEIGCLENLT → VRRLLPLKKYTL
     1272-2527: Missing.

Note: May be due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2527

2527

Leucine-rich repeat serine/threonine-protein kinase 2

PRO_0000086238

Regions

Repeat

226 – 249

24

LRR 1

Repeat

791 – 815

25

LRR 2

Repeat

981 – 1004

24

LRR 3

Repeat

1010 – 1033

24

LRR 4

Repeat

1035 – 1057

23

LRR 5

Repeat

1059 – 1081

23

LRR 6

Repeat

1082 – 1105

24

LRR 7

Repeat

1107 – 1127

21

LRR 8

Repeat

1128 – 1151

24

LRR 9

Repeat

1172 – 1194

23

LRR 10

Repeat

1195 – 1219

25

LRR 11

Repeat

1221 – 1243

23

LRR 12

Repeat

1244 – 1268

25

LRR 13

Repeat

1270 – 1291

22

LRR 14

Domain

1328 – 1511

184

Roc

Repeat

1556 – 1579

24

LRR 15

Repeat

1861 – 1887

27

LRR 16

Domain

1879 – 2138

260

Protein kinase

Nucleotide binding

1341 – 1348

8

GTP Potential

Nucleotide binding

1885 – 1893

9

ATP By similarity

Nucleotide binding

2098 – 2121

24

GTP Potential

Nucleotide binding

2295 – 2298

4

GTP Potential

Coiled coil

319 – 348

30

Potential

Compositional bias

728 – 731

4

Poly-Leu

Sites

Active site

1994

1

Proton acceptor By similarity

Binding site

1906

1

ATP By similarity

Natural variations

Alternative sequence

1 – 401

401

Missing in isoform 2.

VSP_036140

Alternative sequence

1260 – 1271

12

IPPEI…LENLT → VRRLLPLKKYTL in isoform 2.

VSP_036141

Alternative sequence

1272 – 2527

1256

Missing in isoform 2.

VSP_036142

Natural variant

50

1

H → R: dbSNP rs2256408.

VAR_024931

Natural variant

119

1

L → P: dbSNP rs33995463. Ref.27 Ref.37

VAR_024932

Natural variant

228

1

C → S: dbSNP rs56108242. Ref.38

VAR_054740

Natural variant

419

1

A → V: dbSNP rs34594498. Ref.37

VAR_033903

Natural variant

551

1

N → K: dbSNP rs7308720. Ref.17 Ref.27 Ref.37

VAR_024933

Natural variant

712

1

M → V in PD. Ref.38

VAR_054741

Natural variant

716

1

A → V

VAR_054742

Natural variant

723

1

I → V: dbSNP rs10878307. Ref.27 Ref.37

VAR_024934

Natural variant

755

1

P → L: dbSNP rs34410987.

VAR_033904

Natural variant

793

1

R → M in PARK8 and PD; idiopathic and late onset sporadic; could be a polymorphism. dbSNP rs35173587. Ref.17 Ref.27 Ref.30

VAR_024935

Natural variant

871

1

K → E

VAR_054743

Natural variant

930

1

Q → R in PARK8; could be a poymorphism. Ref.17

VAR_024936

Natural variant

944

1

D → Y: dbSNP rs17519916.

VAR_024937

Natural variant

1067

1

R → Q in PD; familial nondominant. Ref.29

VAR_024938

Natural variant

1096

1

S → C in PARK8; could be a polymorphism. Ref.17

VAR_024939

Natural variant

1122

1

I → V in PARK8. dbSNP rs34805604. Ref.1 Ref.27

VAR_024940

Natural variant

1228

1

S → T in PARK8. Ref.17

VAR_024941

Natural variant

1262

1

P → A: dbSNP rs4640000. Ref.27

VAR_024942

Natural variant

1371

1

I → V in PARK8 and PD; could be a polymorphism. dbSNP rs17466213. Ref.28 Ref.19

VAR_024943

Natural variant

1375

1

D → E: dbSNP rs28365226.

VAR_047022

Natural variant

1398

1

R → H: dbSNP rs7133914. Ref.27 Ref.28 Ref.37

VAR_024944

Natural variant

1441

1

R → C in PARK8 and PD; autosomal dominant inheritance; show an increase in activity in both autophosphorylation and phosphorylation of a generic substrate. Ref.7 Ref.1 Ref.27 Ref.19 Ref.31 Ref.35

VAR_024945

Natural variant

1441

1

R → G in PARK8 and PD; sporadic late-onset patients. dbSNP rs33939927. Ref.10 Ref.27 Ref.35 Ref.32

VAR_024946

Natural variant

1441

1

R → H in PARK8 and PD; sporadic; pathogenicity has yet to be confirmed. dbSNP rs34995376. Ref.27 Ref.31

VAR_024947

Natural variant

1514

1

R → Q in PARK8; pathogenicity has yet to be confirmed; might have an effect on protein structure. dbSNP rs35507033. Ref.27 Ref.37

VAR_024948

Natural variant

1542

1

P → S in PARK8; pathogenicity has yet to be confirmed; might have an effect on protein structure. dbSNP rs33958906. Ref.27 Ref.37

VAR_024949

Natural variant

1550

1

R → Q in an ovarian mucinous carcinoma sample; somatic mutation. Ref.37

VAR_040678

Natural variant

1598

1

V → E in PARK8; pathogenicity has yet to be confirmed; might have an effect on protein structure. dbSNP rs721710. Ref.27

VAR_024950

Natural variant

1628

1

R → P: dbSNP rs33949390. Ref.27

VAR_024951

Natural variant

1646

1

M → T: dbSNP rs35303786. Ref.27

VAR_024952

Natural variant

1647

1

S → T: dbSNP rs11564148. Ref.27

VAR_024953

Natural variant

1699

1

Y → C in PARK8. dbSNP rs35801418. Ref.1 Ref.10 Ref.18 Ref.27

VAR_024954

Natural variant

1723

1

R → P in an ovarian serous carcinoma sample; somatic mutation. Ref.37

VAR_040679

Natural variant

1728

1

R → H in PD. Ref.38

VAR_054744

Natural variant

1728

1

R → L in PD. Ref.38

VAR_054745

Natural variant

1869

1

M → T in PARK8 and PD; pathogenicity has yet to be confirmed. dbSNP rs35602796. Ref.27 Ref.30

VAR_024955

Natural variant

1870

1

L → F

VAR_054746

Natural variant

1941

1

R → H in PARK8. Ref.18

VAR_024956

Natural variant

2012

1

I → T in PARK8; pathogenicity uncertain. dbSNP rs34015634. Ref.27

VAR_024957

Natural variant

2019

1

G → S in PARK8 and PD; idiopathic or sporadic; the most common genetic determinant of PD identified so far; show an increase in activity in both autophosphorylation and phosphorylation of a generic substrate. dbSNP rs34637584. Ref.7 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.20 Ref.22 Ref.27 Ref.28 Ref.33 Ref.38 Ref.30 Ref.19 Ref.31 Ref.35 Ref.16 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.34

VAR_024958

Natural variant

2020

1

I → T in PARK8; significant increase in autophosphorylation of about 40% in comparison to wild-type protein in vitro. dbSNP rs35870237. Ref.5 Ref.1 Ref.15 Ref.17 Ref.27

VAR_024959

Natural variant

2081

1

N → D: dbSNP rs33995883. Ref.27

VAR_024960

Natural variant

2119

1

P → L: dbSNP rs12423862. Ref.27

VAR_024961

Natural variant

2141

1

T → M in PD. Ref.38

VAR_054747

Natural variant

2143

1

R → H in PD. Ref.38

VAR_054748

Natural variant

2261

1

N → I: dbSNP rs12581902. Ref.27

VAR_024962

Natural variant

2356

1

T → I in PARK8. Ref.18

VAR_024963

Natural variant

2385

1

G → R Associated with PD; both the wild-type and the variant protein localize to the cytoplasm and form aggregates; under conditions of oxidative stress the variant protein is more toxic and is associated with a higher rate of apoptosis. dbSNP rs34778348. Ref.27 Ref.36

VAR_024964

Natural variant

2395

1

E → K

VAR_054749

Natural variant

2397

1

M → T: dbSNP rs3761863. Ref.27 Ref.28

VAR_024965

Natural variant

2466

1

L → H in PD. Ref.38

VAR_054750

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2527

Helix Strand Turn

Details...

Beta strand

1336 – 1341

6

Helix

1347 – 1354

8

Beta strand

1370 – 1377

8

Beta strand

1389 – 1395

7

Helix

1398 – 1402

5

Helix

1406 – 1411

6

Beta strand

1412 – 1420

9

Helix

1421 – 1423

3

Helix

1425 – 1429

5

Helix

1431 – 1441

11

Beta strand

1446 – 1452

7

Helix

1454 – 1456

3

Helix

1459 – 1472

14

Turn

1473 – 1475

3

Beta strand

1481 – 1487

7

Helix

1495 – 1509

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 6F6070F2437B9C06	FASTA	2,527	286,058
	10 20 30 40 50 60 MASGSCQGCE EDEETLKKLI VRLNNVQEGK QIETLVQILE DLLVFTYSEH ASKLFQGKNI 70 80 90 100 110 120 HVPLLIVLDS YMRVASVQQV GWSLLCKLIE VCPGTMQSLM GPQDVGNDWE VLGVHQLILK 130 140 150 160 170 180 MLTVHNASVN LSVIGLKTLD LLLTSGKITL LILDEESDIF MLIFDAMHSF PANDEVQKLG 190 200 210 220 230 240 CKALHVLFER VSEEQLTEFV ENKDYMILLS ASTNFKDEEE IVLHVLHCLH SLAIPCNNVE 250 260 270 280 290 300 VLMSGNVRCY NIVVEAMKAF PMSERIQEVS CCLLHRLTLG NFFNILVLNE VHEFVVKAVQ 310 320 330 340 350 360 QYPENAALQI SALSCLALLT ETIFLNQDLE EKNENQENDD EGEEDKLFWL EACYKALTWH 370 380 390 400 410 420 RKNKHVQEAA CWALNNLLMY QNSLHEKIGD EDGHFPAHRE VMLSMLMHSS SKEVFQASAN 430 440 450 460 470 480 ALSTLLEQNV NFRKILLSKG IHLNVLELMQ KHIHSPEVAE SGCKMLNHLF EGSNTSLDIM 490 500 510 520 530 540 AAVVPKILTV MKRHETSLPV QLEALRAILH FIVPGMPEES REDTEFHHKL NMVKKQCFKN 550 560 570 580 590 600 DIHKLVLAAL NRFIGNPGIQ KCGLKVISSI VHFPDALEML SLEGAMDSVL HTLQMYPDDQ 610 620 630 640 650 660 EIQCLGLSLI GYLITKKNVF IGTGHLLAKI LVSSLYRFKD VAEIQTKGFQ TILAILKLSA 670 680 690 700 710 720 SFSKLLVHHS FDLVIFHQMS SNIMEQKDQQ FLNLCCKCFA KVAMDDYLKN VMLERACDQN 730 740 750 760 770 780 NSIMVECLLL LGADANQAKE GSSLICQVCE KESSPKLVEL LLNSGSREQD VRKALTISIG 790 800 810 820 830 840 KGDSQIISLL LRRLALDVAN NSICLGGFCI GKVEPSWLGP LFPDKTSNLR KQTNIASTLA 850 860 870 880 890 900 RMVIRYQMKS AVEEGTASGS DGNFSEDVLS KFDEWTFIPD SSMDSVFAQS DDLDSEGSEG 910 920 930 940 950 960 SFLVKKKSNS ISVGEFYRDA VLQRCSPNLQ RHSNSLGPIF DHEDLLKRKR KILSSDDSLR 970 980 990 1000 1010 1020 SSKLQSHMRH SDSISSLASE REYITSLDLS ANELRDIDAL SQKCCISVHL EHLEKLELHQ 1030 1040 1050 1060 1070 1080 NALTSFPQQL CETLKSLTHL DLHSNKFTSF PSYLLKMSCI ANLDVSRNDI GPSVVLDPTV 1090 1100 1110 1120 1130 1140 KCPTLKQFNL SYNQLSFVPE NLTDVVEKLE QLILEGNKIS GICSPLRLKE LKILNLSKNH 1150 1160 1170 1180 1190 1200 ISSLSENFLE ACPKVESFSA RMNFLAAMPF LPPSMTILKL SQNKFSCIPE AILNLPHLRS 1210 1220 1230 1240 1250 1260 LDMSSNDIQY LPGPAHWKSL NLRELLFSHN QISILDLSEK AYLWSRVEKL HLSHNKLKEI 1270 1280 1290 1300 1310 1320 PPEIGCLENL TSLDVSYNLE LRSFPNEMGK LSKIWDLPLD ELHLNFDFKH IGCKAKDIIR 1330 1340 1350 1360 1370 1380 FLQQRLKKAV PYNRMKLMIV GNTGSGKTTL LQQLMKTKKS DLGMQSATVG IDVKDWPIQI 1390 1400 1410 1420 1430 1440 RDKRKRDLVL NVWDFAGREE FYSTHPHFMT QRALYLAVYD LSKGQAEVDA MKPWLFNIKA 1450 1460 1470 1480 1490 1500 RASSSPVILV GTHLDVSDEK QRKACMSKIT KELLNKRGFP AIRDYHFVNA TEESDALAKL 1510 1520 1530 1540 1550 1560 RKTIINESLN FKIRDQLVVG QLIPDCYVEL EKIILSERKN VPIEFPVIDR KRLLQLVREN 1570 1580 1590 1600 1610 1620 QLQLDENELP HAVHFLNESG VLLHFQDPAL QLSDLYFVEP KWLCKIMAQI LTVKVEGCPK 1630 1640 1650 1660 1670 1680 HPKGIISRRD VEKFLSKKRK FPKNYMSQYF KLLEKFQIAL PIGEEYLLVP SSLSDHRPVI 1690 1700 1710 1720 1730 1740 ELPHCENSEI IIRLYEMPYF PMGFWSRLIN RLLEISPYML SGRERALRPN RMYWRQGIYL 1750 1760 1770 1780 1790 1800 NWSPEAYCLV GSEVLDNHPE SFLKITVPSC RKGCILLGQV VDHIDSLMEE WFPGLLEIDI 1810 1820 1830 1840 1850 1860 CGEGETLLKK WALYSFNDGE EHQKILLDDL MKKAEEGDLL VNPDQPRLTI PISQIAPDLI 1870 1880 1890 1900 1910 1920 LADLPRNIML NNDELEFEQA 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 LLLYDILTTG GRIVEGLKFP NEFDELEIQG KLPDPVKEYG 2110 2120 2130 2140 2150 2160 CAPWPMVEKL IKQCLKENPQ ERPTSAQVFD ILNSAELVCL TRRILLPKNV IVECMVATHH 2170 2180 2190 2200 2210 2220 NSRNASIWLG CGHTDRGQLS FLDLNTEGYT SEEVADSRIL CLALVHLPVE KESWIVSGTQ 2230 2240 2250 2260 2270 2280 SGTLLVINTE DGKKRHTLEK MTDSVTCLYC NSFSKQSKQK NFLLVGTADG KLAIFEDKTV 2290 2300 2310 2320 2330 2340 KLKGAAPLKI LNIGNVSTPL MCLSESTNST ERNVMWGGCG TKIFSFSNDF TIQKLIETRT 2350 2360 2370 2380 2390 2400 SQLFSYAAFS DSNIITVVVD TALYIAKQNS PVVEVWDKKT EKLCGLIDCV HFLREVMVKE 2410 2420 2430 2440 2450 2460 NKESKHKMSY SGRVKTLCLQ KNTALWIGTG GGHILLLDLS TRRLIRVIYN FCNSVRVMMT 2470 2480 2490 2500 2510 2520 AQLGSLKNVM LVLGYNRKNT EGTQKQKEIQ SCLTVWDINL PHEVQNLEKH IEVRKELAEK MRRTSVE
	Isoform 2. Checksum: 3F8387DBABE294A5	FASTA	870	97,591
	10 20 30 40 50 60 MLSMLMHSSS KEVFQASANA LSTLLEQNVN FRKILLSKGI HLNVLELMQK HIHSPEVAES 70 80 90 100 110 120 GCKMLNHLFE GSNTSLDIMA AVVPKILTVM KRHETSLPVQ LEALRAILHF IVPGMPEESR 130 140 150 160 170 180 EDTEFHHKLN MVKKQCFKND IHKLVLAALN RFIGNPGIQK CGLKVISSIV HFPDALEMLS 190 200 210 220 230 240 LEGAMDSVLH TLQMYPDDQE IQCLGLSLIG YLITKKNVFI GTGHLLAKIL VSSLYRFKDV 250 260 270 280 290 300 AEIQTKGFQT ILAILKLSAS FSKLLVHHSF DLVIFHQMSS NIMEQKDQQF LNLCCKCFAK 310 320 330 340 350 360 VAMDDYLKNV MLERACDQNN SIMVECLLLL GADANQAKEG SSLICQVCEK ESSPKLVELL 370 380 390 400 410 420 LNSGSREQDV RKALTISIGK GDSQIISLLL RRLALDVANN SICLGGFCIG KVEPSWLGPL 430 440 450 460 470 480 FPDKTSNLRK QTNIASTLAR MVIRYQMKSA VEEGTASGSD GNFSEDVLSK FDEWTFIPDS 490 500 510 520 530 540 SMDSVFAQSD DLDSEGSEGS FLVKKKSNSI SVGEFYRDAV LQRCSPNLQR HSNSLGPIFD 550 560 570 580 590 600 HEDLLKRKRK ILSSDDSLRS SKLQSHMRHS DSISSLASER EYITSLDLSA NELRDIDALS 610 620 630 640 650 660 QKCCISVHLE HLEKLELHQN ALTSFPQQLC ETLKSLTHLD LHSNKFTSFP SYLLKMSCIA 670 680 690 700 710 720 NLDVSRNDIG PSVVLDPTVK CPTLKQFNLS YNQLSFVPEN LTDVVEKLEQ LILEGNKISG 730 740 750 760 770 780 ICSPLRLKEL KILNLSKNHI SSLSENFLEA CPKVESFSAR MNFLAAMPFL PPSMTILKLS 790 800 810 820 830 840 QNKFSCIPEA ILNLPHLRSL DMSSNDIQYL PGPAHWKSLN LRELLFSHNQ ISILDLSEKA 850 860 870 YLWSRVEKLH LSHNKLKEVR RLLPLKKYTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in a large multifunctional protein (LRRK2) cause autosomal dominant parkinsonism with pleiomorphic a-synuclein and tau-pathology (PARK8)." 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. Neuron 44:601-607(2004) [PubMed: 15541309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS PARK8 VAL-1122; CYS-1441; CYS-1699 AND THR-2020. Tissue: Brain.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2128-2527 (ISOFORM 1). Tissue: Testis.
[4]	"PET in LRRK2 mutations: comparison to sporadic Parkinson's disease and evidence for presymptomatic compensation." Adams J.R., van Netten H., Schulzer M., Mak E., McKenzie J., Strongosky A., Sossi V., Ruth T.J., Lee C.S., Farrer M., Gasser T., Uitti R.J., Calne D.B., Wszolek Z.K., Stoessl A.J. Brain 128:2777-2785(2005) [PubMed: 16081470] [Abstract] Cited for: DISEASE.
[5]	"The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity." Gloeckner C.J., Kinkl N., Schumacher A., Braun R.J., O'Neill E., Meitinger T., Kolch W., Prokisch H., Ueffing M. Hum. Mol. Genet. 15:223-232(2006) [PubMed: 16321986] [Abstract] Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PARK8 THR-2020.
[6]	"LRRK2 mutations are not common in Alzheimer's disease." Toft M., Sando S.B., Melquist S., Ross O.A., White L.R., Aasly J.O., Farrer M.J. Mech. Ageing Dev. 126:1201-1205(2005) [PubMed: 16087219] [Abstract] Cited for: DISEASE.
[7]	"Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity." West A.B., Moore D.J., Biskup S., Bugayenko A., Smith W.W., Ross C.A., Dawson V.L., Dawson T.M. Proc. Natl. Acad. Sci. U.S.A. 102:16842-16847(2005) [PubMed: 16269541] [Abstract] Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS PD CYS-1441 AND SER-2019.
[8]	"Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin and mutant LRRK2 induces neuronal degeneration." Smith W.W., Pei Z., Jiang H., Moore D.J., Liang Y., West A.B., Dawson V.L., Dawson T.M., Ross C.A. Proc. Natl. Acad. Sci. U.S.A. 102:18676-18681(2005) [PubMed: 16352719] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PARK2, POSSIBLE FUNCTION.
[9]	"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: 16532471] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease." 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. Neuron 44:595-600(2004) [PubMed: 15541308] [Abstract] Cited for: VARIANTS PARK8 GLY-1441 AND CYS-1699, TISSUE SPECIFICITY.
[11]	"Identification of a novel LRRK2 mutation linked to autosomal dominant parkinsonism: evidence of a common founder across European populations." Kachergus J.M., Mata I.F., Hulihan M., Taylor J.P., Lincoln S., Aasly J.O., Gibson J.M., Ross O.A., Lynch T., Wiley J., Payami H., Nutt J., Maraganore D.M., Czyzewski K., Styczynska M., Wszolek Z.K., Farrer M.J., Toft M. Am. J. Hum. Genet. 76:672-680(2005) [PubMed: 15726496] [Abstract] Cited for: VARIANT PARK8/PD SER-2019.
[12]	"Clinical and positron emission tomography of Parkinson's disease caused by LRRK2." 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. Ann. Neurol. 57:453-456(2005) [PubMed: 15732108] [Abstract] Cited for: VARIANT PARK8 SER-2019.
[13]	"Clinical features of LRRK2-associated Parkinson's disease in central Norway." Aasly J.O., Toft M., Fernandez-Mata I., Kachergus J.M., Hulihan M., White L.R., Farrer M.J. Ann. Neurol. 57:762-765(2005) [PubMed: 15852371] [Abstract] Cited for: VARIANT PARK8/PD SER-2019.
[14]	"G2019S LRRK2 mutation in French and North African families with Parkinson's disease." 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. Ann. Neurol. 58:784-787(2005) [PubMed: 16240353] [Abstract] Cited for: VARIANT PARK8 SER-2019.
[15]	"An LRRK2 mutation as a cause for the parkinsonism in the original PARK8 family." Funayama M., Hasegawa K., Ohta E., Kawashima N., Komiyama M., Kowa H., Tsuji S., Obata F. Ann. Neurol. 57:918-921(2005) [PubMed: 15880653] [Abstract] Cited for: VARIANT PARK8 THR-2020.
[16]	"Genetic and clinical identification of Parkinson's disease patients with LRRK2 G2019S mutation." Deng H., Le W., Guo Y., Hunter C.B., Xie W., Jankovic J. Ann. Neurol. 57:933-934(2005) [PubMed: 15929036] [Abstract] Cited for: VARIANT PD SER-2019.
[17]	"Type and frequency of mutations in the LRRK2 gene in familial and sporadic Parkinson's disease." Berg D., Schweitzer K., Leitner P., Zimprich A., Lichtner P., Belcredi P., Bruessel T., Schulte C., Maass S., Naegele T. Brain 128:3000-3011(2005) [PubMed: 16251215] [Abstract] Cited for: VARIANTS PARK8 MET-793; ARG-930; CYS-1096 THR-1228; SER-2019 AND THR-2020, VARIANT LYS-551.
[18]	"Mutations in the gene LRRK2 encoding dardarin (PARK8) cause familial Parkinson's disease: clinical, pathological, olfactory and functional imaging and genetic data." Khan N.L., Jain S., Lynch J.M., Pavese N., Abou-Sleiman P.M., Holton J.L., Healy D.G., Gilks W.P., Sweeney M.G., Ganguly M., Gibbons V., Gandhi S., Vaughan J., Eunson L.H., Katzenschlager R., Gayton J., Lennox G., Revesz T. , Nicholl D., Bhatia K.P., Quinn N., Brooks D., Lees A.J., Davis M.B., Piccini P., Singleton A.B., Wood N.W. Brain 128:2786-2796(2005) [PubMed: 16272164] [Abstract] Cited for: VARIANTS PARK8 CYS-1699; HIS-1941; SER-2019 AND ILE-2356.
[19]	"Comprehensive analysis of the LRRK2 gene in sixty families with Parkinson's disease." 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. Eur. J. Hum. Genet. 14:322-331(2006) [PubMed: 16333314] [Abstract] Cited for: VARIANTS PD VAL-1371; CYS-1441 AND SER-2019.
[20]	"The G6055A (G2019S) mutation in LRRK2 is frequent in both early and late onset Parkinson's disease and originates from a common ancestor." 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. J. Med. Genet. 42:E65-E65(2005) [PubMed: 16272257] [Abstract] Cited for: VARIANT PARK8 SER-2019.
[21]	"Genetic screening for a single common LRRK2 mutation in familial Parkinson's disease." 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. Lancet 365:410-412(2005) [PubMed: 15680455] [Abstract] Cited for: VARIANT PD SER-2019.
[22]	"A frequent LRRK2 gene mutation associated with autosomal dominant Parkinson's disease." 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. Lancet 365:412-415(2005) [PubMed: 15680456] [Abstract] Cited for: VARIANT PARK8 SER-2019.
[23]	"A common LRRK2 mutation in idiopathic Parkinson's disease." 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. Lancet 365:415-416(2005) [PubMed: 15680457] [Abstract] Cited for: VARIANT PD SER-2019.
[24]	"LRRK2 mutations and Parkinsonism." Toft M., Mata I.F., Kachergus J.M., Ross O.A., Farrer M.J. Lancet 365:1229-1230(2005) [PubMed: 15811454] [Abstract] Cited for: VARIANT PD SER-2019.
[25]	"Escaping Parkinson's disease: a neurologically healthy octogenarian with the LRRK2 G2019S mutation." Kay D.M., Kramer P., Higgins D.S., Zabetian C.P., Payami H. Mov. Disord. 20:1077-1078(2005) [PubMed: 16001413] [Abstract] Cited for: VARIANT SER-2019.
[26]	"Parkinson's disease and LRRK2: frequency of a common mutation in U.S. movement disorder clinics." Kay D.M., Zabetian C.P., Factor S.A., Nutt J.G., Samii A., Griffith A., Bird T.D., Kramer P., Higgins D.S., Payami H. Mov. Disord. 21:519-523(2006) [PubMed: 16250030] [Abstract] Cited for: VARIANT PD SER-2019.
[27]	"Lrrk2 pathogenic substitutions in Parkinson's disease." 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. Neurogenetics 6:171-177(2005) [PubMed: 16172858] [Abstract] Cited for: VARIANTS PARK8 CYS-1441; GLY-1441; HIS-1441; GLN-1514; SER-1542; GLU-1598; CYS-1699; THR-1869; THR-2012; SER-2019; THR-2020 AND ARG-2385, VARIANTS PRO-119; LYS-551; VAL-723; MET-793; VAL-1122; ALA-1262; HIS-1398; PRO-1628; THR-1646; THR-1647; ASP-2081; LEU-2119; ILE-2261 AND THR-2397.
[28]	"LRRK2 gene in Parkinson disease: mutation analysis and case control association study." 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. Neurology 65:696-700(2005) [PubMed: 16157901] [Abstract] Cited for: VARIANTS PARK8 VAL-1371 AND SER-2019, VARIANTS HIS-1398 AND THR-2397.
[29]	"Analysis of LRRK2 functional domains in nondominant Parkinson disease." 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. Neurology 65:1319-1321(2005) [PubMed: 16247070] [Abstract] Cited for: VARIANT PD GLN-1067.
[30]	"LRRK2 mutations in Parkinson disease." Farrer M., Stone J., Mata I.F., Lincoln S., Kachergus J., Hulihan M., Strain K.J., Maraganore D.M. Neurology 65:738-740(2005) [PubMed: 16157908] [Abstract] Cited for: VARIANTS PD MET-793; THR-1869 AND SER-2019.
[31]	"A clinic-based study of the LRRK2 gene in Parkinson disease yields new mutations." Zabetian C.P., Samii A., Mosley A.D., Roberts J.W., Leis B.C., Yearout D., Raskind W.H., Griffith A. Neurology 65:741-744(2005) [PubMed: 16157909] [Abstract] Cited for: VARIANTS PD CYS-1441; HIS-1441 AND SER-2019.
[32]	"LRRK2 R1441G in Spanish patients with Parkinson's disease." 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. Neurosci. Lett. 382:309-311(2005) [PubMed: 15925109] [Abstract] Cited for: VARIANT PD GLY-1441.
[33]	"LRRK2 G2019S is a common mutation in Spanish patients with late-onset Parkinson's disease." Infante J., Rodriguez E., Combarros O., Mateo I., Fontalba A., Pascual J., Oterino A., Polo J.M., Leno C., Berciano J. Neurosci. Lett. 395:224-226(2006) [PubMed: 16298482] [Abstract] Cited for: VARIANT PARK8/PD SER-2019.
[34]	"Clinical traits of LRRK2-associated Parkinson's disease in Ireland: a link between familial and idiopathic PD." Gosal D., Ross O.A., Wiley J., Irvine G.B., Johnston J.A., Toft M., Mata I.F., Kachergus J., Hulihan M., Taylor J.P., Lincoln S.J., Farrer M.J., Lynch T., Mark Gibson J. Parkinsonism Relat. Disord. 11:349-352(2005) [PubMed: 16102999] [Abstract] Cited for: VARIANT PD SER-2019.
[35]	"LRRK2 mutations in Spanish patients with Parkinson disease: frequency, clinical features, and incomplete penetrance." Gaig C., Ezquerra M., Marti M.J., Munoz E., Valldeoriola F., Tolosa E. Arch. Neurol. 63:377-382(2006) [PubMed: 16533964] [Abstract] Cited for: VARIANTS PD CYS-1441; GLY-1441 AND SER-2019.
[36]	"The LRRK2 Gly2385Arg variant is associated with Parkinson's disease: genetic and functional evidence." Tan E.K., Zhao Y., Skipper L., Tan M.G., Di Fonzo A., Sun L., Fook-Chong S., Tang S., Chua E., Yuen Y., Tan L., Pavanni R., Wong M.C., Kolatkar P., Lu C.S., Bonifati V., Liu J.J. Hum. Genet. 120:857-863(2007) [PubMed: 17019612] [Abstract] Cited for: CHARACTERIZATION OF VARIANT ARG-2385, ASSOCIATION WITH PARKINSON DISEASE.
[37]	"Patterns of somatic mutation in human cancer genomes." 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. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-119; VAL-419; LYS-551; VAL-723; HIS-1398; GLN-1514; SER-1542; GLN-1550 AND PRO-1723.
[38]	"Comprehensive analysis of LRRK2 in publicly available Parkinson's disease cases and neurologically normal controls." Paisan-Ruiz C., Nath P., Washecka N., Gibbs J.R., Singleton A.B. Hum. Mutat. 29:485-490(2008) [PubMed: 18213618] [Abstract] Cited for: VARIANTS PD VAL-712; LEU-1728; HIS-1728; SER-2019; MET-2141; HIS-2143 AND HIS-2466, VARIANTS SER-228; VAL-716; GLU-871; PHE-1870 AND LYS-2395.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY792511 mRNA. Translation: AAV63975.1.
AK127729 mRNA. No translation available.
AL834529 mRNA. Translation: CAD39185.1.

IPI

IPI00175649.
IPI00794835.

RefSeq

NP_940980.3.

UniGene

Hs.187636

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZEJ	X-ray	2.00	A/B	1333-1516	[»]
3D6T	X-ray	2.43	B	1336-1505	[»]

SMR

Q5S007. Positions 557-584, 1336-1638, 1546-1856, 1870-2134.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29684N.

STRING

Q5S007.

PTM databases

PhosphoSite

Q5S007.

Proteomic databases

PRIDE

Q5S007.

Genome annotation databases

Ensembl

ENST00000298910; ENSP00000298910; ENSG00000188906; Homo sapiens. [Genome view]

GeneID

120892.

KEGG

hsa:120892.

Organism-specific databases

CTD

120892.

GeneCards

GC12P038908.

H-InvDB

HIX0010547.

HGNC

HGNC:18618. LRRK2.

HPA

HPA014293.

MIM

168600. phenotype.
607060. phenotype.
609007. gene.

Orphanet

2828. Parkinson disease, genetic type.

PharmGKB

PA134968052.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG445818.

HOVERGEN

Q5S007.

InParanoid

Q5S007.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Gene expression databases

ArrayExpress

Q5S007.

Bgee

Q5S007.

CleanEx

HS_LRRK2.

Genevestigator

Q5S007.

GermOnline

ENSG00000188906. Homo sapiens.

Family and domain databases

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013684. MIRO-like.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001806. Ras_GTPase.
IPR020859. ROC_GTPase.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR005225. Small_GTP_bd.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
[Graphical view]

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.
G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.

Pfam

PF00560. LRR_1. 3 hits.
PF08477. Miro. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00369. LRR_TYP. 1 hit.
SM00320. WD40. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other Resources

NextBio

80641.

SOURCE

Search...

Entry information

Entry name

LRRK2_HUMAN

Accession

Primary (citable) accession number: Q5S007
Secondary accession number(s): Q6ZS50, Q8NCX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	December 21, 2004
Last modified:	February 9, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.