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UniProtKB - Q5S006 (LRRK2_MOUSE)

Entry version 154 (02 Dec 2020)
Sequence version 2 (27 Jul 2011)
Previous versions | rss
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Protein

Leucine-rich repeat serine/threonine-protein kinase 2

Gene

Lrrk2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, autophagy, and vesicle trafficking (PubMed:26824392, PubMed:29125462, PubMed:28720718, PubMed:30398148, PubMed:29212815). Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation (PubMed:26824392, PubMed:28720718, PubMed:30398148, PubMed:29212815, PubMed:29125462). Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB8A, RAB8B, RAB10, RAB12, RAB35, and RAB43 (PubMed:26824392, PubMed:28720718, PubMed:30398148, PubMed:29212815). Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A (By similarity). Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A (By similarity). Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain (PubMed:29125462, PubMed:30398148). Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose-6-phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (By similarity). Regulates neuronal process morphology in the intact central nervous system (CNS) (By similarity). Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization (PubMed:25201882). Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway (By similarity). The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes (By similarity). Phosphorylates PRDX3 (By similarity). By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis (PubMed:28720718). Independent of its kinase activity, inhibits the proteosomal degradation of MAPT, thus promoting MAPT oligomerization and secretion (By similarity). In addition, has GTPase activity via its Roc domain which regulates LRKK2 kinase activity (By similarity).By similarity6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Kinase activity is regulated by the GTPase activity of the ROC domain (Probable). GTP-bound LLRK2 kinase activity is stimulated by RAB29 (Probable). Inhibited by small molecule inhibitors MLi-2 and LRRK2-IN-1 (PubMed:26824392, PubMed:28720718).1 Publication2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1906ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1994Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1341 – 1348GTPPROSITE-ProRule annotation8
Nucleotide bindingi1885 – 1893ATPPROSITE-ProRule annotation9
Nucleotide bindingi2098 – 2121GTPPROSITE-ProRule annotationAdd BLAST24
Nucleotide bindingi2295 – 2298GTPPROSITE-ProRule annotation4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGTPase activation, Hydrolase, Kinase, Serine/threonine-protein kinase, Transferase
Biological processAutophagy, Differentiation
LigandATP-binding, GTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-8857538, PTK6 promotes HIF1A stabilization

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Leucine-rich repeat serine/threonine-protein kinase 2 (EC:2.7.11.13 Publications, EC:3.6.5.-By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Lrrk2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1913975, Lrrk2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane, Mitochondrion, Mitochondrion outer membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1441R → C: Impaired ability to recruit SEC61A and SEC31A to endoplasmic reticulum exit sites. Impaired ability to regulate ER to Golgi vesicle-mediated transport. 1 Publication1
Mutagenesisi1441R → G: Increases kinase activity. Reduces primary ciliogenesis. Causes fragmentation of the trans-Golgi network. 3 Publications1
Mutagenesisi2016A → T: Does not affect kinase activity and decreases sensitivity towards small molecule kinase inhibitors. 1 Publication1
Mutagenesisi2019G → S: Increases kinase activity. Causes loss of dopaminergic neurons in the substantia nigra of 20-month old mice due to increased phosphorylation of APP. Reduces primary ciliogenesis. 3 Publications1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2010622

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000862391 – 2527Leucine-rich repeat serine/threonine-protein kinase 2Add BLAST2527

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei910PhosphoserineBy similarity1
Modified residuei935PhosphoserineCombined sources1 Publication1
Modified residuei955PhosphoserineBy similarity1
Modified residuei973PhosphoserineBy similarity1
Modified residuei1292PhosphoserineBy similarity1
Modified residuei1444PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated (PubMed:28720718, PubMed:29212815). Phosphorylation of Ser-910 and Ser-935 or Ser-1444 facilitates interaction with YWHAG (By similarity). Phosphorylation of Ser-910 and/or Ser-935 facilitates interaction with SFN (By similarity).By similarity2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q5S006

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q5S006

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q5S006

PeptideAtlas

More...PeptideAtlasi		Q5S006

PRoteomics IDEntifications database

More...PRIDEi		Q5S006

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q5S006

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q5S006

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the brain (at protein level) (PubMed:28720718). Detected throughout the adult brain. Expressed in deep cerebral cortex layers, superficial cingulate cortex layers, the piriform cortex, hippocampal formation, caudate putamen, substantia nigra, the basolateral and basomedial anterior amygdala nuclei, reticular thalamic nucleus and also in the cerebellar granular cell layer. Highly expressed in the striatum, cortex and olfactory tubercle. Little or no expression in the substantia nigra, where dopaminergic neurons preferentially degenerate in Parkinson disease. Expression is particularly high in brain dopaminoceptive areas. High and strikingly specific expression in striatum and parts of cortex and no signals in dopamine neurons.5 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000036273, Expressed in granulocyte and 199 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q5S006, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (By similarity).

Interacts with PRKN, PRDX3 and TPCN2 (By similarity).

Interacts with VPS35 and RAB29 (PubMed:23395371).

Interacts (via ROC domain) with SEC16A (PubMed:25201882).

Interacts with APP; interaction promotes phosphorylation of 'Thr-743' of APP (PubMed:28720718).

Interacts with MAPT (By similarity).

Interacts with RAB8A, RAB10, and RAB12 (By similarity).

Interacts with YWHAG; this interaction is dependent on phosphorylation of Ser-910 and either Ser-935 or Ser-1444 (By similarity).

Interacts with SFN; this interaction is dependent on phosphorylation of Ser-910 and/or Ser-935 (By similarity).

By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		211674, 36 interactors

Database of interacting proteins

More...DIPi		DIP-58648N

Protein interaction database and analysis system

More...IntActi		Q5S006, 76 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000052584

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q5S006, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q5S006

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati983 – 1004LRR 1Add BLAST22
Repeati1012 – 1033LRR 2Add BLAST22
Repeati1036 – 1057LRR 3Add BLAST22
Repeati1059 – 1080LRR 4Add BLAST22
Repeati1084 – 1105LRR 5Add BLAST22
Repeati1108 – 1129LRR 6Add BLAST22
Repeati1130 – 1151LRR 7Add BLAST22
Repeati1174 – 1195LRR 8Add BLAST22
Repeati1197 – 1218LRR 9Add BLAST22
Repeati1221 – 1242LRR 10Add BLAST22
Repeati1246 – 1267LRR 11Add BLAST22
Repeati1269 – 1291LRR 12Add BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1328 – 1511RocPROSITE-ProRule annotationAdd BLAST184
Domaini1879 – 2146Protein kinasePROSITE-ProRule annotationAdd BLAST268
Repeati2139 – 2183WD 1Add BLAST45
Repeati2188 – 2228WD 2Add BLAST41
Repeati2233 – 2276WD 3Add BLAST44
Repeati2281 – 2327WD 4Add BLAST47
Repeati2333 – 2377WD 5Add BLAST45
Repeati2402 – 2438WD 6Add BLAST37
Repeati2443 – 2497WD 7Add BLAST55

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili9 – 33Sequence analysisAdd BLAST25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi10 – 16Poly-Glu7
Compositional biasi728 – 731Poly-Leu4
Compositional biasi971 – 976Poly-Ser6

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The seven-bladed WD repeat region is critical for synaptic vesicle trafficking and mediates interaction with multiple vesicle-associated presynaptic proteins (By similarity). It also mediates homodimerization and regulates kinase activity (By similarity).By similarity
The Roc domain mediates homodimerization and regulates kinase activity.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Leucine-rich repeat, Repeat, WD repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0192, Eukaryota
KOG0619, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158267

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000815_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q5S006

Identification of Orthologs from Complete Genome Data

More...OMAi		CKLIEVC

Database of Orthologous Groups

More...OrthoDBi		14978at2759

TreeFam database of animal gene trees

More...TreeFami		TF313679

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.10.10, 1 hit
1.25.40.20, 1 hit
2.130.10.10, 1 hit
3.80.10.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036770, Ankyrin_rpt-contain_sf
IPR011989, ARM-like
IPR016024, ARM-type_fold
IPR032171, COR
IPR011009, Kinase-like_dom_sf
IPR001611, Leu-rich_rpt
IPR025875, Leu-rich_rpt_4
IPR003591, Leu-rich_rpt_typical-subtyp
IPR032675, LRR_dom_sf
IPR027417, P-loop_NTPase
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR020859, ROC_dom
IPR008271, Ser/Thr_kinase_AS
IPR005225, Small_GTP-bd_dom
IPR015943, WD40/YVTN_repeat-like_dom_sf
IPR036322, WD40_repeat_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16095, COR, 1 hit
PF12799, LRR_4, 1 hit
PF13855, LRR_8, 2 hits
PF00069, Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00369, LRR_TYP, 7 hits
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48371, SSF48371, 2 hits
SSF48403, SSF48403, 1 hit
SSF50978, SSF50978, 1 hit
SSF52540, SSF52540, 1 hit
SSF56112, SSF56112, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00231, small_GTP, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q5S006-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASGACQGCE EEEEEEALKK LIVRLNNVQE GKQIETLLQL LEDMLVFTYS 
        60         70         80         90        100
DRASKLFEDK NFHVPLLIVL DSYMRVASVQ QAGWSLLCKL IEVCPGTLQS 
       110        120        130        140        150
LIGPQDIGND WEVLGIHRLI LKMLTVHHAN VNLSIVGLKA LDLLLDSGKL 
       160        170        180        190        200
TLLILDEECD IFLLIFDAMH RYSANDEVQK LGCKALHVLF ERVSEEQLTE 
       210        220        230        240        250
FVENKDYTIL LSTFGSFRRD KEIVYHVLCC LHSLAVTCSN VEVLMSGNVR 
       260        270        280        290        300
CYNLVVEAMK AFPTNENIQE VSCSLFQKLT LGNFFNILVL NEVHVFVVKA 
       310        320        330        340        350
VRQYPENAAL QISALSCLAL LTETIFLNQD LEERSETQEQ SEEEDSEKLF 
       360        370        380        390        400
WLEPCYKALV RHRKDKHVQE AACWALNNLL MYQNSLHEKI GDEDGQFPAH 
       410        420        430        440        450
REVMLSMLMH SSSKDVFQAA AHALSTLLEQ NVNFRKILLA KGVYLNVLEL 
       460        470        480        490        500
MQKHAHAPEV AESGCKMLSH LFEGSNPSLD TMAAVVPKIL TVMKAHGTSL 
       510        520        530        540        550
SVQLEALRAI LHFVVPGLLE ESREDSQCRP NVLRKQCFRT DIHKLVLVAL 
       560        570        580        590        600
NRFIGNPGIQ KCGLKVISSL AHLPDATETL SLQGAVDSVL HTLQMYPDDQ 
       610        620        630        640        650
EIQCLGLHLM GCLMTKKNFC IGTGHLLAKI LASTLQRFKD VAEVQTTGLQ 
       660        670        680        690        700
TTLSILELSV SFSKLLVHYS FDVVIFHQMS SSVVEQKDEQ FLNLCCKCFA 
       710        720        730        740        750
KVAVDDELKN TMLERACDQN NSIMVECLLL LGADANQVKG ATSLIYQVCE 
       760        770        780        790        800
KESSPKLVEL LLNGGCREQD VRKALTVSIQ KGDSQVISLL LRKLALDLAN 
       810        820        830        840        850
NSICLGGFGI GKIDPSWLGP LFPDKSSNLR KQTNTGSVLA RKVLRYQMRN 
       860        870        880        890        900
TLQEGVASGS DGKFSEDALA KFGEWTFIPD SSMDSVFGQS DDLDSEGSES 
       910        920        930        940        950
SFLVKRKSNS ISVGEVYRDL ALQRCSPNAQ RHSNSLGPVF DHEDLLRRKR 
       960        970        980        990       1000
KILSSDESLR SSRLPSHMRQ SDSSSSLASE REHITSLDLS ANELKDIDAL 
      1010       1020       1030       1040       1050
SQKCCLSSHL EHLTKLELHQ NSLTSFPQQL CETLKCLIHL DLHSNKFTSF 
      1060       1070       1080       1090       1100
PSFVLKMPRI TNLDASRNDI GPTVVLDPAM KCPSLKQLNL SYNQLSSIPE 
      1110       1120       1130       1140       1150
NLAQVVEKLE QLLLEGNKIS GICSPLSLKE LKILNLSKNH IPSLPGDFLE 
      1160       1170       1180       1190       1200
ACSKVESFSA RMNFLAAMPA LPSSITSLKL SQNSFTCIPE AIFSLPHLRS 
      1210       1220       1230       1240       1250
LDMSHNNIEC LPGPAHWKSL NLRELIFSKN QISTLDFSEN PHVWSRVEKL 
      1260       1270       1280       1290       1300
HLSHNKLKEI PPEIGCLENL TSLDVSYNLE LRSFPNEMGK LSKIWDLPLD 
      1310       1320       1330       1340       1350
GLHLNFDFKH VGCKAKDIIR FLQQRLKKAV PYNRMKLMIV GNTGSGKTTL 
      1360       1370       1380       1390       1400
LQQLMKMKKP ELGMQGATVG IDVRDWSIQI RGKRRKDLVL NVWDFAGREE 
      1410       1420       1430       1440       1450
FYSTHPHFMT QRALYLAVYD LSKGQAEVDA MKPWLFNIKA RASSSPVILV 
      1460       1470       1480       1490       1500
GTHLDVSDEK QRKACISKIT KELLNKRGFP TIRDYHFVNA TEESDALAKL 
      1510       1520       1530       1540       1550
RKTIINESLN FKIRDQPVVG QLIPDCYVEL EKIILSERKA VPTEFPVINR 
      1560       1570       1580       1590       1600
KHLLQLVNEH QLQLDENELP HAVHFLNESG VLLHFQDPAL QLSDLYFVEP 
      1610       1620       1630       1640       1650
KWLCKVMAQI LTVKVDGCLK HPKGIISRRD VEKFLSKKKR FPKNYMMQYF 
      1660       1670       1680       1690       1700
KLLEKFQIAL PIGEEYLLVP SSLSDHRPVI ELPHCENSEI IIRLYEMPYF 
      1710       1720       1730       1740       1750
PMGFWSRLIN RLLEISPFML SGRERALRPN RMYWRQGIYL NWSPEAYCLV 
      1760       1770       1780       1790       1800
GSEVLDNRPE SFLKITVPSC RKGCILLGRV VDHIDSLMEE WFPGLLEIDI 
      1810       1820       1830       1840       1850
CGEGETLLKK WALYSFNDGE EHQKILLDEL MKKAEEGDLL INPDQPRLTI 
      1860       1870       1880       1890       1900
PISQIAPDLI LADLPRNIML NNDELEFEEA PEFLLGDGSF GSVYRAAYEG 
      1910       1920       1930       1940       1950
EEVAVKIFNK HTSLRLLRQE LVVLCHLHHP SLISLLAAGI RPRMLVMELA 
      1960       1970       1980       1990       2000
SKGSLDRLLQ QDKASLTRTL QHRIALHVAD GLRYLHSAMI IYRDLKPHNV 
      2010       2020       2030       2040       2050
LLFTLYPNAA IIAKIADYGI AQYCCRMGIK TSEGTPGFRA PEVARGNVIY 
      2060       2070       2080       2090       2100
NQQADVYSFG LLLHDIWTTG SRIMEGLRFP NEFDELAIQG KLPDPVKEYG 
      2110       2120       2130       2140       2150
CAPWPMVEKL ITKCLKENPQ ERPTSAQVFD ILNSAELICL MRHILIPKNI 
      2160       2170       2180       2190       2200
IVECMVATNL NSKSATLWLG CGNTEKGQLS LFDLNTERYS YEEVADSRIL 
      2210       2220       2230       2240       2250
CLALVHLAAE KESWVVCGTQ SGALLVINVE EETKRHTLEK MTDSVTCLHC 
      2260       2270       2280       2290       2300
NSLAKQSKQS NFLLVGTADG NLMIFEDKAV KCKGAAPLKT LHIGDVSTPL 
      2310       2320       2330       2340       2350
MCLSESLNSS ERHITWGGCG TKVFSFSNDF TIQKLIETKT NQLFSYAAFS 
      2360       2370       2380       2390       2400
DSNIIALAVD TALYIAKKNS PVVEVWDKKT EKLCELIDCV HFLKEVMVKL 
      2410       2420       2430       2440       2450
NKESKHQLSY SGRVKALCLQ KNTALWIGTG GGHILLLDLS TRRVIRTIHN 
      2460       2470       2480       2490       2500
FCDSVRAMAT AQLGSLKNVM LVLGYKRKST EGIQEQKEIQ SCLSIWDLNL 
      2510       2520 
PHEVQNLEKH IEVRTELADK MRKTSVE
Length:2,527
Mass (Da):284,732
Last modified:July 27, 2011 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i706E25C173E36F98
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti343E → K in BAC35052 (PubMed:16141072).Curated1
Sequence conflicti777V → I in AAV63976 (PubMed:15541309).Curated1
Sequence conflicti863K → N in AAV63976 (PubMed:15541309).Curated1
Sequence conflicti925C → Y in AAV63976 (PubMed:15541309).Curated1
Sequence conflicti1705 – 1707WSR → GQD in BAC28700 (PubMed:16141072).Curated3

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AY792512 mRNA Translation: AAV63976.1
AC099704 Genomic DNA No translation available.
AC158752 Genomic DNA No translation available.
AK052591 mRNA Translation: BAC35052.1
AK034413 mRNA Translation: BAC28700.1
BC034074 mRNA Translation: AAH34074.1
BC035949 mRNA Translation: AAH35949.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS37180.1

NCBI Reference Sequences

More...RefSeqi		NP_080006.3, NM_025730.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000060642; ENSMUSP00000052584; ENSMUSG00000036273

Database of genes from NCBI RefSeq genomes

More...GeneIDi		66725

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:66725

UCSC genome browser

More...UCSCi		uc007xhz.1, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY792512 mRNA Translation: AAV63976.1
AC099704 Genomic DNA No translation available.
AC158752 Genomic DNA No translation available.
AK052591 mRNA Translation: BAC35052.1
AK034413 mRNA Translation: BAC28700.1
BC034074 mRNA Translation: AAH34074.1
BC035949 mRNA Translation: AAH35949.1
CCDSiCCDS37180.1
RefSeqiNP_080006.3, NM_025730.3

3D structure databases

SMRiQ5S006
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi211674, 36 interactors
DIPiDIP-58648N
IntActiQ5S006, 76 interactors
STRINGi10090.ENSMUSP00000052584

Chemistry databases

ChEMBLiCHEMBL2010622

PTM databases

iPTMnetiQ5S006
PhosphoSitePlusiQ5S006

Proteomic databases

jPOSTiQ5S006
MaxQBiQ5S006
PaxDbiQ5S006
PeptideAtlasiQ5S006
PRIDEiQ5S006

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		Q5S006, 1 sequenced antibody

Antibodypedia a portal for validated antibodies

More...Antibodypediai		2109, 850 antibodies

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		120892
MGIiMGI:1913975, Lrrk2

Phylogenomic databases

eggNOGiKOG0192, Eukaryota
KOG0619, Eukaryota
GeneTreeiENSGT00940000158267
HOGENOMiCLU_000815_0_0_1
InParanoidiQ5S006
OMAiCKLIEVC
OrthoDBi14978at2759
TreeFamiTF313679

Enzyme and pathway databases

ReactomeiR-MMU-8857538, PTK6 promotes HIF1A stabilization

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		66725, 0 hits in 17 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Lrrk2, mouse

Protein Ontology

More...PROi		PR:Q5S006
RNActiQ5S006, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000036273, Expressed in granulocyte and 199 other tissues
GenevisibleiQ5S006, MM

Family and domain databases

Gene3Di1.25.10.10, 1 hit
1.25.40.20, 1 hit
2.130.10.10, 1 hit
3.80.10.10, 2 hits
InterProiView protein in InterPro
IPR036770, Ankyrin_rpt-contain_sf
IPR011989, ARM-like
IPR016024, ARM-type_fold
IPR032171, COR
IPR011009, Kinase-like_dom_sf
IPR001611, Leu-rich_rpt
IPR025875, Leu-rich_rpt_4
IPR003591, Leu-rich_rpt_typical-subtyp
IPR032675, LRR_dom_sf
IPR027417, P-loop_NTPase
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR020859, ROC_dom
IPR008271, Ser/Thr_kinase_AS
IPR005225, Small_GTP-bd_dom
IPR015943, WD40/YVTN_repeat-like_dom_sf
IPR036322, WD40_repeat_dom_sf
PfamiView protein in Pfam
PF16095, COR, 1 hit
PF12799, LRR_4, 1 hit
PF13855, LRR_8, 2 hits
PF00069, Pkinase, 1 hit
SMARTiView protein in SMART
SM00369, LRR_TYP, 7 hits
SM00220, S_TKc, 1 hit
SUPFAMiSSF48371, SSF48371, 2 hits
SSF48403, SSF48403, 1 hit
SSF50978, SSF50978, 1 hit
SSF52540, SSF52540, 1 hit
SSF56112, SSF56112, 1 hit
TIGRFAMsiTIGR00231, small_GTP, 1 hit
PROSITEiView protein in 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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLRRK2_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q5S006
Secondary accession number(s): E9QNJ2
, Q8BWG7, Q8BZJ6, Q8CI84, Q8K062
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: July 27, 2011
Last modified: December 2, 2020
This is version 154 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

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