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Entry version 166 (03 Jul 2019)
Sequence version 2 (20 Apr 2010)
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Protein

Leucine-rich repeat serine/threonine-protein kinase 2

Gene

LRRK2

Organism
Homo sapiens (Human)
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

Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. 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. Regulates neuronal process morphology in the intact central nervous system (CNS). Plays a role in synaptic vesicle trafficking. Phosphorylates PRDX3. Has GTPase activity. May play a role in the phosphorylation of proteins central to Parkinson disease. Plays an important role in recuiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization (PubMed:25201882).8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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_section">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 annotation1 Publication8
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

GO - Biological processi

<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, 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

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Reactomei
R-HSA-8857538 PTK6 promotes HIF1A stabilization

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q5S007

SIGNOR Signaling Network Open Resource

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SIGNORi
Q5S007

<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_and_taxonomy_section">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:2.7.11.1)
Alternative name(s):
Dardarin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
Synonyms:PARK8
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 12

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:18618 LRRK2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
609007 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q5S007

<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, Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane, Mitochondrion, Mitochondrion inner membrane, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Parkinson disease 8 (PARK8)34 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA slowly progressive neurodegenerative disorder characterized by bradykinesia, rigidity, resting tremor, postural instability, neuronal loss in the substantia nigra, and the presence of neurofibrillary MAPT (tau)-positive and Lewy bodies in some patients.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_054741712M → V in PARK8. 1 PublicationCorresponds to variant dbSNP:rs199566791EnsemblClinVar.1
Natural variantiVAR_024935793R → M in PARK8; unknown pathological significance. 3 PublicationsCorresponds to variant dbSNP:rs35173587EnsemblClinVar.1
Natural variantiVAR_024936930Q → R in PARK8; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs281865045EnsemblClinVar.1
Natural variantiVAR_0249381067R → Q in PARK8. 1 PublicationCorresponds to variant dbSNP:rs111341148EnsemblClinVar.1
Natural variantiVAR_0249391096S → C in PARK8; unknown pathological significance. Corresponds to variant dbSNP:rs76535406EnsemblClinVar.1
Natural variantiVAR_0249401122I → V in PARK8. 2 PublicationsCorresponds to variant dbSNP:rs34805604EnsemblClinVar.1
Natural variantiVAR_0249411228S → T in PARK8. 1 PublicationCorresponds to variant dbSNP:rs60185966EnsemblClinVar.1
Natural variantiVAR_0249431371I → V in PARK8; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs17466213EnsemblClinVar.1
Natural variantiVAR_0249451441R → C in PARK8; shows an increase in activity in both autophosphorylation and phosphorylation of a generic substrate; loss of interaction with SEC16A. 7 PublicationsCorresponds to variant dbSNP:rs33939927EnsemblClinVar.1
Natural variantiVAR_0249461441R → G in PARK8; shows a progressive reduction in neurite length and branching. 5 PublicationsCorresponds to variant dbSNP:rs33939927EnsemblClinVar.1
Natural variantiVAR_0249471441R → H in PARK8; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs34995376EnsemblClinVar.1
Natural variantiVAR_0249481514R → Q in PARK8; unknown pathological significance. 3 PublicationsCorresponds to variant dbSNP:rs35507033EnsemblClinVar.1
Natural variantiVAR_0249491542P → S in PARK8; unknown pathological significance. 3 PublicationsCorresponds to variant dbSNP:rs33958906EnsemblClinVar.1
Natural variantiVAR_0249501598V → E in PARK8; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs721710EnsemblClinVar.1
Natural variantiVAR_0249541699Y → C in PARK8; shows no progressive reduction in neurite length and branching; no loss of interaction with SEC16A. 6 PublicationsCorresponds to variant dbSNP:rs35801418EnsemblClinVar.1
Natural variantiVAR_0547441728R → H in PARK8. 1 PublicationCorresponds to variant dbSNP:rs145364431EnsemblClinVar.1
Natural variantiVAR_0547451728R → L in PARK8. 1 PublicationCorresponds to variant dbSNP:rs145364431EnsemblClinVar.1
Natural variantiVAR_0249551869M → T in PARK8; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs35602796EnsemblClinVar.1
Natural variantiVAR_0249561941R → H in PARK8. 1 PublicationCorresponds to variant dbSNP:rs77428810EnsemblClinVar.1
Natural variantiVAR_0249572012I → T in PARK8; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs34015634EnsemblClinVar.1
Natural variantiVAR_0249582019G → S in PARK8; shows an increase in activity in both autophosphorylation and phosphorylation of a generic substrate; results in increased PRDX3 phosphorylation promoting dysregulation of mitochondrial function and oxidative damage; does not inhibit interaction with RAB29; shows a progressive reduction in neurite length and branching; shows distinctive spheroid-like inclusions within both neuronal processes and at intracellular membranous structures; shows lysosomal swelling and reduced retrograde transport of selective cargo between lysosomes and the Golgi apparatus; shows apoptotic mechanism of cell death; no loss of interaction with SEC16A. 29 PublicationsCorresponds to variant dbSNP:rs34637584EnsemblClinVar.1
Natural variantiVAR_0249592020I → T in PARK8; significant increase in autophosphorylation of about 40% in comparison to wild-type protein in vitro; shows a progressive reduction in neurite length and branching. 6 PublicationsCorresponds to variant dbSNP:rs35870237EnsemblClinVar.1
Natural variantiVAR_0547472141T → M in PARK8. 1 PublicationCorresponds to variant dbSNP:rs111691891EnsemblClinVar.1
Natural variantiVAR_0547482143R → H in PARK8. 1 PublicationCorresponds to variant dbSNP:rs201271001EnsemblClinVar.1
Natural variantiVAR_0249632356T → I in PARK8. 1 PublicationCorresponds to variant dbSNP:rs113511708EnsemblClinVar.1
Natural variantiVAR_0547502466L → H in PARK8. 1 PublicationCorresponds to variant dbSNP:rs281865057EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi1343T → G: Decreased kinase activity; when associated with Q-1398. 1 Publication1
Mutagenesisi1347K → A: GTPase-dead mutant. Loss of interaction with SEC16A and impaired ability to recruit SEC16A to endoplasmic reticulum exit sites. 1 Publication1
Mutagenesisi1398R → Q: Decreased kinase activity; when associated with G-1343. 1 Publication1
Mutagenesisi1994D → N: Kinase-dead mutant. No loss of interaction with SEC16A and no loss of ability to recruit SEC16A to endoplasmic reticulum exit sites. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism

Organism-specific databases

DisGeNET

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DisGeNETi
120892

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
LRRK2

MalaCards human disease database

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MalaCardsi
LRRK2
MIMi168600 phenotype
607060 phenotype

Open Targets

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OpenTargetsi
ENSG00000188906

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
411602 Hereditary late-onset Parkinson disease
2828 Young-onset Parkinson disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134968052

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1075104

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2059

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
LRRK2

Domain mapping of disease mutations (DMDM)

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DMDMi
294862450

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000862381 – 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 residuei935PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q5S007

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q5S007

MaxQB - The MaxQuant DataBase

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MaxQBi
Q5S007

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

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PaxDbi
Q5S007

PeptideAtlas

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PeptideAtlasi
Q5S007

PRoteomics IDEntifications database

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PRIDEi
Q5S007

ProteomicsDB human proteome resource

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ProteomicsDBi
63755

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q5S007

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

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PhosphoSitePlusi
Q5S007

<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. Expressed in pyramidal neurons in all cortical laminae of the visual cortex, in neurons of the substantia nigra pars compacta and caudate putamen (at protein level). 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.4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000188906 Expressed in 166 organ(s), highest expression level in visceral pleura

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q5S007 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q5S007 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB037160
HPA014293

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

Interacts with PRKN, PRDX3, RAB29, TPCN2 and VPS35.

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

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself68EBI-5323863,EBI-5323863
AGO2Q9UKV83EBI-5323863,EBI-528269
AHCYL1O438653EBI-5323863,EBI-2371423
AKT1P317496EBI-5323863,EBI-296087
ANKS4BQ8N8V42EBI-5323863,EBI-9658517
ARFGAP1Q8N6T3-26EBI-5323863,EBI-6288865
Arfgap1Q628487EBI-5323863,EBI-4398879From Rattus norvegicus.
ARHGEF7Q141557EBI-5323863,EBI-717515
Atp2a2O5514313EBI-5323863,EBI-770763From Mus musculus.
BAG2O958163EBI-5323863,EBI-355275
BAG3O958172EBI-5323863,EBI-747185
BAG5Q9UL1512EBI-5323863,EBI-356517
BCL2P10415-12EBI-5323863,EBI-4370304
CDC37Q165437EBI-5323863,EBI-295634
CDC42P609533EBI-5323863,EBI-81752
CDC42EP3Q9UKI22EBI-5323863,EBI-723480
CFAP20Q9Y6A43EBI-5323863,EBI-1046872
CHGBP050603EBI-5323863,EBI-712619
Ckmt1P302752EBI-5323863,EBI-773103From Mus musculus.
CSNK1A1P48729-12EBI-5323863,EBI-10106282
CUEDC1Q9NWM32EBI-5323863,EBI-5838167
DAPK1P533552EBI-5323863,EBI-358616
DNM1Q051934EBI-5323863,EBI-713135
Dnm1P390533EBI-5323863,EBI-397785From Mus musculus.
DNM1LO0042911EBI-5323863,EBI-724571
DNM1LO00429-32EBI-5323863,EBI-6896746
DVL1O14640-27EBI-5323863,EBI-6504027
DVL2O146415EBI-5323863,EBI-740850
DVL3Q929974EBI-5323863,EBI-739789
ECHS1P300844EBI-5323863,EBI-719602
EEF1A2Q056393EBI-5323863,EBI-354943
FADDQ131584EBI-5323863,EBI-494804
GAKO1497611EBI-5323863,EBI-714707
GSK3BP498417EBI-5323863,EBI-373586
HSPA8P111425EBI-5323863,EBI-351896
LARP4Q71RC23EBI-5323863,EBI-2878091
LARP7Q4G0J33EBI-5323863,EBI-2371923
LDHBP071952EBI-5323863,EBI-358748
LRP6O755814EBI-5323863,EBI-910915
LRRK1Q38SD25EBI-5323863,EBI-1050422
MAP1BP468215EBI-5323863,EBI-9517186
MAP2K3P467345EBI-5323863,EBI-602462
MAP2K6P525644EBI-5323863,EBI-448135
MAP2K7O147333EBI-5323863,EBI-492605
MAPTP10636-23EBI-5323863,EBI-7796412
MAPTP10636-89EBI-5323863,EBI-366233
MATKP426792EBI-5323863,EBI-751664
MBPP026873EBI-5323863,EBI-908215From Bos taurus.
Mfn1Q811U43EBI-5323863,EBI-9029118From Mus musculus.
MFN2O951403EBI-5323863,EBI-3324756
MRPL19P494063EBI-5323863,EBI-1188518
MSNP2603819EBI-5323863,EBI-528768
NDUFAF7Q7L5922EBI-5323863,EBI-2555519
NEK1Q96PY62EBI-5323863,EBI-373615
NFATC2Q134693EBI-5323863,EBI-716258
NUP133Q8WUM04EBI-5323863,EBI-295695
OPA1O603135EBI-5323863,EBI-1054131
PAK6Q9NQU52EBI-5323863,EBI-1053685
phoAP006342EBI-5323863,EBI-552958From Escherichia coli (strain K12).
PPP1CAP621366EBI-5323863,EBI-357253
PPP1R8Q129723EBI-5323863,EBI-716633
PRDX3P3004814EBI-5323863,EBI-748336
PRKACAP176126EBI-5323863,EBI-476586
Prkar2bP123693EBI-5323863,EBI-6096160From Rattus norvegicus.
PRKNO602603EBI-5323863,EBI-716346
RAB10P610267EBI-5323863,EBI-726075
RAB12Q6IQ222EBI-5323863,EBI-4289591
RAB1BQ9H0U45EBI-5323863,EBI-1045214
RAB29O149667EBI-5323863,EBI-372165
Rab29Q634813EBI-5323863,EBI-6513837From Rattus norvegicus.
RAB32Q136376EBI-5323863,EBI-9837586
RAB5BP610209EBI-5323863,EBI-399401
Rab5bP610212EBI-5323863,EBI-8320093From Mus musculus.
RAB8AP610066EBI-5323863,EBI-722293
RAC1P630005EBI-5323863,EBI-413628
RGS2P412206EBI-5323863,EBI-712388
RPL10AP629064EBI-5323863,EBI-356860
RPL13P263734EBI-5323863,EBI-356849
RPL14P509142EBI-5323863,EBI-356746
RPL23AP627502EBI-5323863,EBI-353254
RPL30P628883EBI-5323863,EBI-353116
RPL34P492073EBI-5323863,EBI-1051893
RPS11P622805EBI-5323863,EBI-1047710
RPS13P622773EBI-5323863,EBI-351850
RPS15P628419EBI-5323863,EBI-372635
RPS16P622494EBI-5323863,EBI-352480
RPS18P622693EBI-5323863,EBI-352451
RPS2P158804EBI-5323863,EBI-443446
RPS20P608664EBI-5323863,EBI-353105
RPS23P622662EBI-5323863,EBI-353072
RPS27P426774EBI-5323863,EBI-356336
RPS3P233964EBI-5323863,EBI-351193
SEC16AO150278EBI-5323863,EBI-357515
SFNP319473EBI-5323863,EBI-476295
SH3GL1Q999613EBI-5323863,EBI-697911
SH3GL2Q999624EBI-5323863,EBI-77938
SLC25A4P122352EBI-5323863,EBI-359074
SLC25A5P051412EBI-5323863,EBI-355133
SLC25A6P122362EBI-5323863,EBI-356254
SNAPINO952955EBI-5323863,EBI-296723
SNCAP378406EBI-5323863,EBI-985879
Spag9Q58A652EBI-5323863,EBI-6530207From Mus musculus.
STUB1Q9UNE74EBI-5323863,EBI-357085
STUB1Q9UNE7-12EBI-5323863,EBI-15687717
Stub1Q9WUD12EBI-5323863,EBI-773027From Mus musculus.
TCF25Q9BQ703EBI-5323863,EBI-745182
TTC27Q6P3X33EBI-5323863,EBI-1057046
TUBBP074376EBI-5323863,EBI-350864
TUBB2AQ138853EBI-5323863,EBI-711595
TUBB4AP043506EBI-5323863,EBI-355007
TUBB4BP683713EBI-5323863,EBI-351356
TUBB6Q9BUF53EBI-5323863,EBI-356735
USP39Q53GS93EBI-5323863,EBI-1044822
VDAC1P217963EBI-5323863,EBI-354158
WSB1Q9Y6I75EBI-5323863,EBI-1171494
YWHABP319465EBI-5323863,EBI-359815
YWHAEP622588EBI-5323863,EBI-356498
YWHAGP619814EBI-5323863,EBI-359832
YwhagP619836EBI-5323863,EBI-359821From Rattus norvegicus.
YWHAHQ049173EBI-5323863,EBI-306940
YWHAQP2734810EBI-5323863,EBI-359854
YWHAZP6310411EBI-5323863,EBI-347088
ZRANB2O952182EBI-5323863,EBI-1051583

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
125700, 266 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q5S007

Database of interacting proteins

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DIPi
DIP-29684N

Protein interaction database and analysis system

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IntActi
Q5S007, 2309 interactors

Molecular INTeraction database

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MINTi
Q5S007

STRING: functional protein association networks

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STRINGi
9606.ENSP00000298910

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q5S007

<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

Secondary structure

12527
Legend: HelixTurnBeta strandPDB Structure known for this area
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