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Reviewed, UniProtKB/Swiss-Prot Q5S007 (LRRK2_HUMAN)

Last modified February 9, 2010. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Leucine-rich repeat serine/threonine-protein kinase 2
    EC=2.7.11.1
Alternative name(s):
    Dardarin
Gene names
Name: LRRK2
Synonyms: PARK8
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2527 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Parkinson disease
   DomainCoiled coil
Leucine-rich repeat
Repeat
   LigandATP-binding
GTP-binding
Nucleotide-binding
   Molecular functionGTPase activation
Kinase
Serine/threonine-protein kinase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processactivation 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 componentexternal side of mitochondrial outer membrane Ref.7

Inferred from direct assay. Source: UniProtKB

extrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25272527Leucine-rich repeat serine/threonine-protein kinase 2
PRO_0000086238

Regions

Repeat226 – 24924LRR 1
Repeat791 – 81525LRR 2
Repeat981 – 100424LRR 3
Repeat1010 – 103324LRR 4
Repeat1035 – 105723LRR 5
Repeat1059 – 108123LRR 6
Repeat1082 – 110524LRR 7
Repeat1107 – 112721LRR 8
Repeat1128 – 115124LRR 9
Repeat1172 – 119423LRR 10
Repeat1195 – 121925LRR 11
Repeat1221 – 124323LRR 12
Repeat1244 – 126825LRR 13
Repeat1270 – 129122LRR 14
Domain1328 – 1511184Roc
Repeat1556 – 157924LRR 15
Repeat1861 – 188727LRR 16
Domain1879 – 2138260Protein kinase
Nucleotide binding1341 – 13488GTP Potential
Nucleotide binding1885 – 18939ATP By similarity
Nucleotide binding2098 – 212124GTP Potential
Nucleotide binding2295 – 22984GTP Potential
Coiled coil319 – 34830 Potential
Compositional bias728 – 7314Poly-Leu

Sites

Active site19941Proton acceptor By similarity
Binding site19061ATP By similarity

Natural variations

Alternative sequence1 – 401401Missing in isoform 2.
VSP_036140
Alternative sequence1260 – 127112IPPEI…LENLT → VRRLLPLKKYTL in isoform 2.
VSP_036141
Alternative sequence1272 – 25271256Missing in isoform 2.
VSP_036142
Natural variant501H → R: dbSNP rs2256408.
VAR_024931
Natural variant1191L → P: dbSNP rs33995463. Ref.27 Ref.37
VAR_024932
Natural variant2281C → S: dbSNP rs56108242. Ref.38
VAR_054740
Natural variant4191A → V: dbSNP rs34594498. Ref.37
VAR_033903
Natural variant5511N → K: dbSNP rs7308720. Ref.17 Ref.27 Ref.37
VAR_024933
Natural variant7121M → V in PD. Ref.38
VAR_054741
Natural variant7161A → V
VAR_054742
Natural variant7231I → V: dbSNP rs10878307. Ref.27 Ref.37
VAR_024934
Natural variant7551P → L: dbSNP rs34410987.
VAR_033904
Natural variant7931R → 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 variant8711K → E
VAR_054743
Natural variant9301Q → R in PARK8; could be a poymorphism. Ref.17
VAR_024936
Natural variant9441D → Y: dbSNP rs17519916.
VAR_024937
Natural variant10671R → Q in PD; familial nondominant. Ref.29
VAR_024938
Natural variant10961S → C in PARK8; could be a polymorphism. Ref.17
VAR_024939
Natural variant11221I → V in PARK8. dbSNP rs34805604. Ref.1 Ref.27
VAR_024940
Natural variant12281S → T in PARK8. Ref.17
VAR_024941
Natural variant12621P → A: dbSNP rs4640000. Ref.27
VAR_024942
Natural variant13711I → V in PARK8 and PD; could be a polymorphism. dbSNP rs17466213. Ref.28 Ref.19
VAR_024943
Natural variant13751D → E: dbSNP rs28365226.
VAR_047022
Natural variant13981R → H: dbSNP rs7133914. Ref.27 Ref.28 Ref.37
VAR_024944
Natural variant14411R → 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 variant14411R → G in PARK8 and PD; sporadic late-onset patients. dbSNP rs33939927. Ref.10 Ref.27 Ref.35 Ref.32
VAR_024946
Natural variant14411R → H in PARK8 and PD; sporadic; pathogenicity has yet to be confirmed. dbSNP rs34995376. Ref.27 Ref.31
VAR_024947
Natural variant15141R → 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 variant15421P → 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 variant15501R → Q in an ovarian mucinous carcinoma sample; somatic mutation. Ref.37
VAR_040678
Natural variant15981V → E in PARK8; pathogenicity has yet to be confirmed; might have an effect on protein structure. dbSNP rs721710. Ref.27
VAR_024950
Natural variant16281R → P: dbSNP rs33949390. Ref.27
VAR_024951
Natural variant16461M → T: dbSNP rs35303786. Ref.27
VAR_024952
Natural variant16471S → T: dbSNP rs11564148. Ref.27
VAR_024953
Natural variant16991Y → C in PARK8. dbSNP rs35801418. Ref.1 Ref.10 Ref.18 Ref.27
VAR_024954
Natural variant17231R → P in an ovarian serous carcinoma sample; somatic mutation. Ref.37
VAR_040679
Natural variant17281R → H in PD. Ref.38
VAR_054744
Natural variant17281R → L in PD. Ref.38
VAR_054745
Natural variant18691M → T in PARK8 and PD; pathogenicity has yet to be confirmed. dbSNP rs35602796. Ref.27 Ref.30
VAR_024955
Natural variant18701L → F
VAR_054746
Natural variant19411R → H in PARK8. Ref.18
VAR_024956
Natural variant20121I → T in PARK8; pathogenicity uncertain. dbSNP rs34015634. Ref.27
VAR_024957
Natural variant20191G → 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 variant20201I → 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 variant20811N → D: dbSNP rs33995883. Ref.27
VAR_024960
Natural variant21191P → L: dbSNP rs12423862. Ref.27
VAR_024961
Natural variant21411T → M in PD. Ref.38
VAR_054747
Natural variant21431R → H in PD. Ref.38
VAR_054748
Natural variant22611N → I: dbSNP rs12581902. Ref.27
VAR_024962
Natural variant23561T → I in PARK8. Ref.18
VAR_024963
Natural variant23851G → 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 variant23951E → K
VAR_054749
Natural variant23971M → T: dbSNP rs3761863. Ref.27 Ref.28
VAR_024965
Natural variant24661L → H in PD. Ref.38
VAR_054750

Secondary structure

.............................. 2527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 6F6070F2437B9C06

FASTA2,527286,058
        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 

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Isoform 2.

Checksum: 3F8387DBABE294A5
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FASTA87097,591

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY792511 mRNA. Translation: AAV63975.1.
AK127729 mRNA. No translation available.
AL834529 mRNA. Translation: CAD39185.1.
IPIIPI00175649.
IPI00794835.
RefSeqNP_940980.3.
UniGeneHs.187636

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZEJX-ray2.00A/B1333-1516[»]
3D6TX-ray2.43B1336-1505[»]
SMRQ5S007. Positions 557-584, 1336-1638, 1546-1856, 1870-2134.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29684N.
STRINGQ5S007.

PTM databases

PhosphoSiteQ5S007.

Proteomic databases

PRIDEQ5S007.

Genome annotation databases

EnsemblENST00000298910; ENSP00000298910; ENSG00000188906; Homo sapiens. [Genome view]
GeneID120892.
KEGGhsa:120892.

Organism-specific databases

CTD120892.
GeneCardsGC12P038908.
H-InvDBHIX0010547.
HGNCHGNC:18618. LRRK2.
HPAHPA014293.
MIM168600. phenotype.
607060. phenotype.
609007. gene.
Orphanet2828. Parkinson disease, genetic type.
PharmGKBPA134968052.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG445818.
HOVERGENQ5S007.
InParanoidQ5S007.

Enzyme and pathway databases

BRENDA2.7.11.1. 247.

Gene expression databases

ArrayExpressQ5S007.
BgeeQ5S007.
CleanExHS_LRRK2.
GenevestigatorQ5S007.
GermOnlineENSG00000188906. Homo sapiens.

Family and domain databases

InterProIPR011989. 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]
Gene3DG3DSA:1.25.10.10. ARM-like. 1 hit.
G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PfamPF00560. LRR_1. 3 hits.
PF08477. Miro. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00369. LRR_TYP. 1 hit.
SM00320. WD40. 1 hit.
[Graphical view]
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 Resources

NextBio80641.
SOURCESearch...

Entry information

Entry nameLRRK2_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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.

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents