Q38SD2 (LRRK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leucine-rich repeat serine/threonine-protein kinase 1
EC=2.7.11.1

Gene names

Name:	LRRK1
Synonyms:	KIAA1790

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2015 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.3
Cofactor	Magnesium or manganese. Ref.3
Enzyme regulation	Binding of GTP stimulates kinase activity. Ref.3
Subunit structure	Homodimer. Ref.6
Subcellular location	Cytoplasm Ref.3.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. ROCO subfamily. Contains 4 ANK repeats. Contains 13 LRR (leucine-rich) repeats. Contains 1 protein kinase domain. Contains 1 Roc domain.
Sequence caution	The sequence AAY67799.1 differs from that shown. Reason: The cDNA contains a duplication of exon 3. The sequence BAB15547.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC85472.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	ANK repeat Leucine-rich repeat Repeat
Ligand	ATP-binding GTP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-1050422,EBI-1050422
DAPK1	P53355	2	EBI-1050422,EBI-358616
LRRK2	Q5S007	5	EBI-1050422,EBI-5323863

Alternative products

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

Isoform 1 Ref.6 (identifier: Q38SD2-1)

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.

Note: No experimental confirmation available.

Isoform 2 Ref.2 (identifier: Q38SD2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     255-264: ALRVKWSHLR → VSSHCLWSVF
     265-2015: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2015	2015	Leucine-rich repeat serine/threonine-protein kinase 1		PRO_0000233377
Regions
	Repeat	86 – 116	31	ANK 1
	Repeat	119 – 148	30	ANK 2
	Repeat	152 – 182	31	ANK 3
	Repeat	193 – 222	30	ANK 4
	Repeat	279 – 300	22	LRR 1
	Repeat	303 – 324	22	LRR 2
	Repeat	330 – 351	22	LRR 3
	Repeat	353 – 374	22	LRR 4
	Repeat	381 – 402	22	LRR 5
	Repeat	405 – 426	22	LRR 6
	Repeat	427 – 447	21	LRR 7
	Repeat	451 – 472	22	LRR 8
	Repeat	474 – 495	22	LRR 9
	Repeat	498 – 519	22	LRR 10
	Repeat	549 – 570	22	LRR 11
	Repeat	572 – 594	23	LRR 12
	Repeat	596 – 617	22	LRR 13
	Domain	632 – 826	195	Roc
	Domain	1242 – 1525	284	Protein kinase
	Nucleotide binding	1248 – 1256	9	ATP By similarity
Sites
	Active site	1386	1	Proton acceptor By similarity
	Binding site	1270	1	ATP By similarity
Natural variations
	Alternative sequence	255 – 264	10	ALRVKWSHLR → VSSHCLWSVF in isoform 2.		VSP_040119
	Alternative sequence	265 – 2015	1751	Missing in isoform 2.		VSP_040120
	Natural variant	1803	1	A → T. Ref.7		VAR_040674
	Natural variant	1824	1	L → F. Ref.7		VAR_040675
	Natural variant	1847	1	S → N. Ref.7		VAR_040676
	Natural variant	1927	1	D → G. Ref.7		VAR_040677
Experimental info
	Mutagenesis	651	1	K → A: Loss of GTP/GDP-binding. Ref.3
	Mutagenesis	746	1	K → G: No effect on GTP-binding but reduction in subsequent stimulation of kinase activity. Ref.3
	Mutagenesis	1022	1	F → C: No effect on GTP-binding but loss of subsequent stimulation of kinase activity. Ref.3
	Mutagenesis	1270	1	K → W: Loss of autophosphorylation. Ref.3
	Mutagenesis	1412	1	I → T: No effect on GTP-binding but reduction in subsequent stimulation of kinase activity. Ref.3
	Sequence conflict	203	1	K → R in BAC85472. Ref.4
	Sequence conflict	1938	1	G → E in AAH66655. Ref.2
	Sequence conflict	1938	1	G → E in BAB47419. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 30, 2010. Version 3. Checksum: 38E77EDC7C84583B	FASTA	2,015	225,393
	10 20 30 40 50 60 MAGMSQRPPS MYWCVGPEES AVCPERAMET LNGAGDTGGK PSTRGGDPAA RSRRTEGIRA 70 80 90 100 110 120 AYRRGDRGGA RDLLEEACDQ CASQLEKGQL LSIPAAYGDL EMVRYLLSKR LVELPTEPTD 130 140 150 160 170 180 DNPAVVAAYF GHTAVVQELL ESLPGPCSPQ RLLNWMLALA CQRGHLGVVK LLVLTHGADP 190 200 210 220 230 240 ESYAVRKNEF PVIVRLPLYA AIKSGNEDIA IFLLRHGAYF CSYILLDSPD PSKHLLRKYF 250 260 270 280 290 300 IEASPLPSSY PGKTALRVKW SHLRLPWVDL DWLIDISCQI TELDLSANCL ATLPSVIPWG 310 320 330 340 350 360 LINLRKLNLS DNHLGELPGV QSSDEIICSR LLEIDISSNK LSHLPPGFLH LSKLQKLTAS 370 380 390 400 410 420 KNCLEKLFEE ENATNWIGLR KLQELDISDN KLTELPALFL HSFKSLNSLN VSRNNLKVFP 430 440 450 460 470 480 DPWACPLKCC KASRNALECL PDKMAVFWKN HLKDVDFSEN ALKEVPLGLF QLDALMFLRL 490 500 510 520 530 540 QGNQLAALPP QEKWTCRQLK TLDLSRNQLG KNEDGLKTKR IAFFTTRGRQ RSGTEAASVL 550 560 570 580 590 600 EFPAFLSESL EVLCLNDNHL DTVPPSVCLL KSLSELYLGN NPGLRELPPE LGQLGNLWQL 610 620 630 640 650 660 DTEDLTISNV PAEIQKEGPK AMLSYLRAQL RKAEKCKLMK MIIVGPPRQG KSTLLEILQT 670 680 690 700 710 720 GRAPQVVHGE ATIRTTKWEL QRPAGSRAKV ESVEFNVWDI GGPASMATVN QCFFTDKALY 730 740 750 760 770 780 VVVWNLALGE EAVANLQFWL LNIEAKAPNA VVLVVGTHLD LIEAKFRVER IATLRAYVLA 790 800 810 820 830 840 LCRSPSGSRA TGFPDITFKH LHEISCKSLE GQEGLRQLIF HVTCSMKDVG STIGCQRLAG 850 860 870 880 890 900 RLIPRSYLSL QEAVLAEQQR RSRDDDVQYL TDRQLEQLVE QTPDNDIKDY EDLQSAISFL 910 920 930 940 950 960 IETGTLLHFP DTSHGLRNLY FLDPIWLSEC LQRIFNIKGS RSVAKNGVIR AEDLRMLLVG 970 980 990 1000 1010 1020 TGFTQQTEEQ YFQFLAKFEI ALPVANDSYL LPHLLPSKPG LDTHGMRHPT ANTIQRVFKM 1030 1040 1050 1060 1070 1080 SFVPVGFWQR FIARMLISLA EMDLQLFENK KNTKSRNRKV TIYSFTGNQR NRCSTFRVKR 1090 1100 1110 1120 1130 1140 NQTIYWQEGL LVTFDGGYLS VESSDVNWKK KKSGGMKIVC QSEVRDFSAM AFITDHVNSL 1150 1160 1170 1180 1190 1200 IDQWFPALTA TESDGTPLME QYVPCPVCET AWAQHTDPSE KSEDVQYFDM EDCVLTAIER 1210 1220 1230 1240 1250 1260 DFISCPRHPD LPVPLQELVP ELFMTDFPAR LFLENSKLEH SEDEGSVLGQ GGSGTVIYRA 1270 1280 1290 1300 1310 1320 RYQGQPVAVK RFHIKKFKNF ANVPADTMLR HLRATDAMKN FSEFRQEASM LHALQHPCIV 1330 1340 1350 1360 1370 1380 ALIGISIHPL CFALELAPLS SLNTVLSENA RDSSFIPLGH MLTQKIAYQI ASGLAYLHKK 1390 1400 1410 1420 1430 1440 NIIFCDLKSD NILVWSLDVK EHINIKLSDY GISRQSFHEG ALGVEGTPGY QAPEIRPRIV 1450 1460 1470 1480 1490 1500 YDEKVDMFSY GMVLYELLSG QRPALGHHQL QIAKKLSKGI RPVLGQPEEV QFRRLQALMM 1510 1520 1530 1540 1550 1560 ECWDTKPEKR PLALSVVSQM KDPTFATFMY ELCCGKQTAF FSSQGQEYTV VFWDGKEESR 1570 1580 1590 1600 1610 1620 NYTVVNTEKG LMEVQRMCCP GMKVSCQLQV QRSLWTATED QKIYIYTLKG MCPLNTPQQA 1630 1640 1650 1660 1670 1680 LDTPAVVTCF LAVPVIKKNS YLVLAGLADG LVAVFPVVRG TPKDSCSYLC SHTANRSKFS 1690 1700 1710 1720 1730 1740 IADEDARQNP YPVKAMEVVN SGSEVWYSNG PGLLVIDCAS LEICRRLEPY MAPSMVTSVV 1750 1760 1770 1780 1790 1800 CSSEGRGEEV VWCLDDKANS LVMYHSTTYQ LCARYFCGVP SPLRDMFPVR PLDTEPPAAS 1810 1820 1830 1840 1850 1860 HTANPKVPEG DSIADVSIMY SEELGTQILI HQESLTDYCS MSSYSSSPPR QAARSPSSLP 1870 1880 1890 1900 1910 1920 SSPASSSSVP FSTDCEDSDM LHTPGAASDR SEHDLTPMDG ETFSQHLQAV KILAVRDLIW 1930 1940 1950 1960 1970 1980 VPRRGGDVIV IGLEKDSGAQ RGRVIAVLKA RELTPHGVLV DAAVVAKDTV VCTFENENTE 1990 2000 2010 WCLAVWRGWG AREFDIFYQS YEELGRLEAC TRKRR
	Isoform 2 [UniParc]. Checksum: 8E95B1F50F1DB2E4	FASTA	264	28,848
	10 20 30 40 50 60 MAGMSQRPPS MYWCVGPEES AVCPERAMET LNGAGDTGGK PSTRGGDPAA RSRRTEGIRA 70 80 90 100 110 120 AYRRGDRGGA RDLLEEACDQ CASQLEKGQL LSIPAAYGDL EMVRYLLSKR LVELPTEPTD 130 140 150 160 170 180 DNPAVVAAYF GHTAVVQELL ESLPGPCSPQ RLLNWMLALA CQRGHLGVVK LLVLTHGADP 190 200 210 220 230 240 ESYAVRKNEF PVIVRLPLYA AIKSGNEDIA IFLLRHGAYF CSYILLDSPD PSKHLLRKYF 250 260 IEASPLPSSY PGKTVSSHCL WSVF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1576-2015 (ISOFORM 1). Tissue: Pancreas and Skin.
[3]	"LRRK1 protein kinase activity is stimulated upon binding of GTP to its Roc domain." Korr D., Toschi L., Donner P., Pohlenz H.-P., Kreft B., Weiss B. Cell. Signal. 18:910-920(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-2015 (ISOFORM 1), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, GTP-BINDING, MUTAGENESIS OF LYS-651; LYS-746; PHE-1022; LYS-1270 AND ILE-1412.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-364 AND 905-2015 (ISOFORM 1). Tissue: Lung, Macrophage and Spleen.
[5]	"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 646-2015 (ISOFORM 1). Tissue: Brain.
[6]	"Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimers." Civiero L., Vancraenenbroeck R., Belluzzi E., Beilina A., Lobbestael E., Reyniers L., Gao F., Micetic I., De Maeyer M., Bubacco L., Baekelandt V., Cookson M.R., Greggio E., Taymans J.M. PLoS ONE 7:E43472-E43472(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, LACK OF AUTOPHOSPHORYLATION.
[7]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-1803; PHE-1824; ASN-1847 AND GLY-1927.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC090907 Genomic DNA. No translation available. BC066655 mRNA. Translation: AAH66655.1. BC068080 mRNA. Translation: AAH68080.1. DQ013130 mRNA. Translation: AAY67799.1. Sequence problems. AK026772 mRNA. Translation: BAB15547.1. Different initiation. AK130975 mRNA. Translation: BAC85472.1. Different initiation. AK131075 mRNA. Translation: BAC85125.1. AB058693 mRNA. Translation: BAB47419.1.
IPI	IPI00747813. IPI00748762.
RefSeq	NP_078928.3. NM_024652.3.
UniGene	Hs.407918.
3D structure databases
ProteinModelPortal	Q38SD2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q38SD2. 25 interactions.
STRING	9606.ENSP00000373600.
PTM databases
PhosphoSite	Q38SD2.
Polymorphism databases
DMDM	94717653.
Proteomic databases
PaxDb	Q38SD2.
PRIDE	Q38SD2.
Protocols and materials databases
DNASU	79705.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000388948; ENSP00000373600; ENSG00000154237. ENST00000532029; ENSP00000433268; ENSG00000154237.
GeneID	79705.
KEGG	hsa:79705.
UCSC	uc002bwq.1. human. uc002bwr.3. human.
Organism-specific databases
CTD	79705.
GeneCards	GC15P101459.
H-InvDB	HIX0012627.
HGNC	HGNC:18608. LRRK1.
HPA	HPA010537.
MIM	610986. gene.
neXtProt	NX_Q38SD2.
PharmGKB	PA134892363.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1100.
HOVERGEN	HBG081936.
KO	K08843.
OMA	FEEENAT.
Enzyme and pathway databases
SignaLink	Q38SD2.
Gene expression databases
ArrayExpress	Q38SD2.
Bgee	Q38SD2.
CleanEx	HS_LRRK1.
Genevestigator	Q38SD2.
GermOnline	ENSG00000154237. Homo sapiens.
Family and domain databases
Gene3D	1.25.40.20. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR011009. Kinase-like_dom. IPR001611. Leu-rich_rpt. IPR003591. Leu-rich_rpt_typical-subtyp. IPR013684. MIRO-like. IPR027417. P-loop_NTPase. IPR000719. Prot_kinase_cat_dom. IPR020859. ROC_GTPase. IPR017986. WD40_repeat_dom. [Graphical view]
Pfam	PF12796. Ank_2. 1 hit. PF00560. LRR_1. 1 hit. PF08477. Miro. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00248. ANK. 3 hits. SM00369. LRR_TYP. 1 hit. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit. SSF56112. Kinase_like. 1 hit. SSF52540. SSF52540. 1 hit. SSF50978. WD40_like. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. False negative. PS51450. LRR. 11 hits. PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. PS51424. ROC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	79705.
NextBio	69015.
SOURCE	Search...

Entry information

Entry name

LRRK1_HUMAN

Accession

Primary (citable) accession number: Q38SD2
Secondary accession number(s): Q6NVH5 , Q6NYC0, Q6ZNL9, Q6ZNM9, Q96JN5, Q9H5S3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	November 30, 2010
Last modified:	May 29, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.