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Entry version 168 (13 Feb 2019)
Sequence version 1 (01 Jan 1998)
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Protein

Muscle, skeletal receptor tyrosine-protein kinase

Gene

MUSK

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

Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle (PubMed:25537362). Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUSK, the kinase of the complex. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. May regulate AChR phosphorylation and clustering through activation of ABL1 and Src family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a ternary complex with MUSK are also important for MUSK-dependent regulation of AChR clustering. May positively regulate Rho family GTPases through FNTA. Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. Other effectors of the MUSK signaling include DNAJA3 which functions downstream of MUSK. May also play a role within the central nervous system by mediating cholinergic responses, synaptic plasticity and memory formation (By similarity).By similarity1 Publication

<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

<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+1 Publication

<p>This subsection of the ‘Function’ 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

Positively regulated by CK2.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei609ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 sitei725Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi581 – 589ATPPROSITE-ProRule annotation9

<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 functionDevelopmental protein, Kinase, Muscle protein, Receptor, Transferase, Tyrosine-protein kinase
Biological processDifferentiation
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3000178 ECM proteoglycans

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

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SignaLinki
O15146

SIGNOR Signaling Network Open Resource

More...
SIGNORi
O15146

<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:
Muscle, skeletal receptor tyrosine-protein kinase (EC:2.7.10.11 Publication)
Alternative name(s):
Muscle-specific tyrosine-protein kinase receptor
Short name:
MuSK
Short name:
Muscle-specific kinase receptor
<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:MUSK
<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 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000030304.13

Human Gene Nomenclature Database

More...
HGNCi
HGNC:7525 MUSK

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
601296 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O15146

<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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini24 – 495ExtracellularSequence analysisAdd BLAST472
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei496 – 516HelicalSequence analysisAdd BLAST21
Topological domaini517 – 869CytoplasmicSequence analysisAdd BLAST353

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell 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

Myasthenic syndrome, congenital, 9, associated with acetylcholine receptor deficiency (CMS9)5 Publications
The disease is caused by mutations affecting the gene represented in this entry. MUSK mutations lead to decreased agrin-dependent AChR aggregation, a critical step in the formation of the neuromuscular junction.
Disease descriptionA form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS9 is a disorder of postsynaptic neuromuscular transmission, due to deficiency of AChR at the endplate that results in low amplitude of the miniature endplate potential and current.
See also OMIM:616325
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_07278538D → E in CMS9. 1 PublicationCorresponds to variant dbSNP:rs775587809Ensembl.1
Natural variantiVAR_072786344P → R in CMS9. 1 PublicationCorresponds to variant dbSNP:rs387906803EnsemblClinVar.1
Natural variantiVAR_066604605M → I in CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 PublicationCorresponds to variant dbSNP:rs766640370Ensembl.1
Natural variantiVAR_066605727A → V in CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 PublicationCorresponds to variant dbSNP:rs397515450EnsemblClinVar.1
Natural variantiVAR_023046790V → M in CMS9; does not affect catalytic kinase activity; reduces protein expression and stability. 1 PublicationCorresponds to variant dbSNP:rs199476083EnsemblClinVar.1
Natural variantiVAR_072788835M → V in CMS9; reduces AChR aggregation in developing neuromuscular junction. 1 Publication1
Fetal akinesia deformation sequence (FADS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA clinically and genetically heterogeneous group of disorders with congenital malformations related to impaired fetal movement. Clinical features include fetal akinesia, intrauterine growth retardation, polyhydramnios, arthrogryposis, pulmonary hypoplasia, craniofacial abnormalities, and cryptorchidism.
See also OMIM:208150
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072787575I → T in FADS; reduces agrin-dependent AChR aggregation and tyrosine kinase activity in developing neuromuscular junction. 1 PublicationCorresponds to variant dbSNP:rs751889864EnsemblClinVar.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>Mutagenesisi584G → C or D: Mild decrease in kinase activity. 1 Publication1
Mutagenesisi609K → R: Severe loss of kinase activity. 1 Publication1
Mutagenesisi743D → N: Severe loss of kinase activity. 1 Publication1

Keywords - Diseasei

Congenital myasthenic syndrome, Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
4593

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

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GeneReviewsi
MUSK

MalaCards human disease database

More...
MalaCardsi
MUSK
MIMi208150 phenotype
616325 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000030304

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

More...
Orphaneti
994 Fetal akinesia deformation sequence
98913 Postsynaptic congenital myasthenic syndromes

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA31326

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5684

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1847

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
MUSK

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Sequence analysisAdd BLAST23
<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_000002444624 – 869Muscle, skeletal receptor tyrosine-protein kinaseAdd BLAST846

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi49 ↔ 99By similarity
Disulfide bondi98 ↔ 112By similarity
Disulfide bondi142 ↔ 190By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi222N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi233 ↔ 282By similarity
Disulfide bondi317 ↔ 382By similarity
Disulfide bondi325 ↔ 375By similarity
Glycosylationi338N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi366 ↔ 406By similarity
Disulfide bondi394 ↔ 447By similarity
Disulfide bondi398 ↔ 434By similarity
<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 residuei554Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei681Phosphoserine; by CK2By similarity1
Modified residuei698Phosphoserine; by CK2By similarity1
Modified residuei755Phosphotyrosine; by autocatalysisBy 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

Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis and lysosomal degradation (By similarity).By similarity
Phosphorylated (By similarity). Phosphorylation is induced by AGRIN in a LRP4-dependent manner (By similarity). Autophosphorylated (PubMed:25029443). Autophosphorylation at Tyr-554 is required for interaction with DOK7 which in turn stimulates the phosphorylation and the activation of MUSK (By similarity).By similarity1 Publication
Neddylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O15146

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

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PaxDbi
O15146

PeptideAtlas

More...
PeptideAtlasi
O15146

PRoteomics IDEntifications database

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PRIDEi
O15146

ProteomicsDB human proteome resource

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ProteomicsDBi
48471
48472 [O15146-2]
48473 [O15146-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O15146

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

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PhosphoSitePlusi
O15146

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000030304 Expressed in 88 organ(s), highest expression level in small intestine Peyer's patch

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O15146 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O15146 HS

<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

Monomer (By similarity). Homodimer (Probable). Interacts with LRP4; the heterodimer forms an AGRIN receptor complex that binds AGRIN resulting in activation of MUSK (By similarity). Forms a heterotetramer composed of 2 DOK7 and 2 MUSK molecules which facilitates MUSK trans-autophosphorylation on tyrosine residue and activation. Interacts (via cytoplasmic part) with DOK7 (via IRS-type PTB domain); requires MUSK phosphorylation. Interacts with DVL1 (via DEP domain); the interaction is direct and mediates the formation of a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering (By similarity). Interacts with PDZRN3; this interaction is enhanced by agrin (By similarity). Interacts with FNTA; the interaction is direct and mediates AGRIN-induced phosphorylation and activation of FNTA (By similarity). Interacts with CSNK2B; mediates regulation by CK2 (By similarity). Interacts (via the cytoplasmic domain) with DNAJA3 (By similarity). Interacts with NSF; may regulate MUSK endocytosis and activity (By similarity). Interacts with CAV3; may regulate MUSK signaling (By similarity). Interacts with RNF31 (By similarity).By similarityCurated

<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
HSP90AB1P082382EBI-6423196,EBI-352572

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110679, 8 interactors

Protein interaction database and analysis system

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IntActi
O15146, 6 interactors

Molecular INTeraction database

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MINTi
O15146

STRING: functional protein association networks

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STRINGi
9606.ENSP00000363571

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O15146

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O15146

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

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SMRi
O15146

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 <a href="http://www.uniprot.org/help/family_and_domains_section">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>Domaini28 – 116Ig-like 1Add BLAST89
Domaini121 – 205Ig-like 2Add BLAST85
Domaini212 – 302Ig-like 3Add BLAST91
Domaini312 – 450FZPROSITE-ProRule annotationAdd BLAST139
Domaini575 – 856Protein kinasePROSITE-ProRule annotationAdd BLAST282

<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. Tyr protein kinase family.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IMMJ Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158226

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000044461

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052539

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O15146

KEGG Orthology (KO)

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KOi
K05129

Identification of Orthologs from Complete Genome Data

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OMAi
CAPYNGK

Database of Orthologous Groups

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OrthoDBi
1576308at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O15146

TreeFam database of animal gene trees

More...
TreeFami
TF106465

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.2000.10, 1 hit
2.60.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR020067 Frizzled_dom
IPR036790 Frizzled_dom_sf
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01392 Fz, 1 hit
PF07679 I-set, 2 hits
PF07714 Pkinase_Tyr, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48726 SSF48726, 3 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50038 FZ, 1 hit
PS50835 IG_LIKE, 3 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O15146-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MRELVNIPLV HILTLVAFSG TEKLPKAPVI TTPLETVDAL VEEVATFMCA
60 70 80 90 100
VESYPQPEIS WTRNKILIKL FDTRYSIREN GQLLTILSVE DSDDGIYCCT
110 120 130 140 150
ANNGVGGAVE SCGALQVKMK PKITRPPINV KIIEGLKAVL PCTTMGNPKP
160 170 180 190 200
SVSWIKGDSP LRENSRIAVL ESGSLRIHNV QKEDAGQYRC VAKNSLGTAY
210 220 230 240 250
SKVVKLEVEV FARILRAPES HNVTFGSFVT LHCTATGIPV PTITWIENGN
260 270 280 290 300
AVSSGSIQES VKDRVIDSRL QLFITKPGLY TCIATNKHGE KFSTAKAAAT
310 320 330 340 350
ISIAEWSKPQ KDNKGYCAQY RGEVCNAVLA KDALVFLNTS YADPEEAQEL
360 370 380 390 400
LVHTAWNELK VVSPVCRPAA EALLCNHIFQ ECSPGVVPTP IPICREYCLA
410 420 430 440 450
VKELFCAKEW LVMEEKTHRG LYRSEMHLLS VPECSKLPSM HWDPTACARL
460 470 480 490 500
PHLDYNKENL KTFPPMTSSK PSVDIPNLPS SSSSSFSVSP TYSMTVIISI
510 520 530 540 550
MSSFAIFVLL TITTLYCCRR RKQWKNKKRE SAAVTLTTLP SELLLDRLHP
560 570 580 590 600
NPMYQRMPLL LNPKLLSLEY PRNNIEYVRD IGEGAFGRVF QARAPGLLPY
610 620 630 640 650
EPFTMVAVKM LKEEASADMQ ADFQREAALM AEFDNPNIVK LLGVCAVGKP
660 670 680 690 700
MCLLFEYMAY GDLNEFLRSM SPHTVCSLSH SDLSMRAQVS SPGPPPLSCA
710 720 730 740 750
EQLCIARQVA AGMAYLSERK FVHRDLATRN CLVGENMVVK IADFGLSRNI
760 770 780 790 800
YSADYYKANE NDAIPIRWMP PESIFYNRYT TESDVWAYGV VLWEIFSYGL
810 820 830 840 850
QPYYGMAHEE VIYYVRDGNI LSCPENCPVE LYNLMRLCWS KLPADRPSFT
860
SIHRILERMC ERAEGTVSV
Length:869
Mass (Da):97,056
Last modified:January 1, 1998 - v1
<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:i3DDC20E179FA010C
GO
Isoform 2 (identifier: O15146-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-209: E → EEESEPEQDTK
     307-394: Missing.
     454-462: DYNKENLKT → A

Show »
Length:783
Mass (Da):87,598
Checksum:i695BD37016C0D980
GO
Isoform 3 (identifier: O15146-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     307-394: Missing.
     454-462: DYNKENLKT → A

Show »
Length:773
Mass (Da):86,425
Checksum:i3BEA481E3C84D000
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WSY1A0A087WSY1_HUMAN
Muscle, skeletal receptor tyrosine-...
MUSK
861Annotation score:

Annotation score:2 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>
Q5T0B5Q5T0B5_HUMAN
Muscle, skeletal receptor tyrosine-...
MUSK
783Annotation score:

Annotation score:2 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>
F6XAJ2F6XAJ2_HUMAN
Muscle, skeletal receptor tyrosine-...
MUSK
132Annotation score:

Annotation score:1 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04174827A → G1 PublicationCorresponds to variant dbSNP:rs56054734Ensembl.1
Natural variantiVAR_07278538D → E in CMS9. 1 PublicationCorresponds to variant dbSNP:rs775587809Ensembl.1
Natural variantiVAR_041749100T → M1 PublicationCorresponds to variant dbSNP:rs35142681EnsemblClinVar.1
Natural variantiVAR_041750107G → E1 PublicationCorresponds to variant dbSNP:rs55786136EnsemblClinVar.1
Natural variantiVAR_041751159S → G1 PublicationCorresponds to variant dbSNP:rs35176182EnsemblClinVar.1
Natural variantiVAR_041752222N → S1 PublicationCorresponds to variant dbSNP:rs55826142EnsemblClinVar.1
Natural variantiVAR_072786344P → R in CMS9. 1 PublicationCorresponds to variant dbSNP:rs387906803EnsemblClinVar.1
Natural variantiVAR_021930413M → I1 PublicationCorresponds to variant dbSNP:rs2274419EnsemblClinVar.1
Natural variantiVAR_072787575I → T in FADS; reduces agrin-dependent AChR aggregation and tyrosine kinase activity in developing neuromuscular junction. 1 PublicationCorresponds to variant dbSNP:rs751889864EnsemblClinVar.1
Natural variantiVAR_066604605M → I in CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 PublicationCorresponds to variant dbSNP:rs766640370Ensembl.1
Natural variantiVAR_041753629L → F1 PublicationCorresponds to variant dbSNP:rs34267283Ensembl.1
Natural variantiVAR_041754644V → A1 PublicationCorresponds to variant dbSNP:rs41279055EnsemblClinVar.1
Natural variantiVAR_041755664N → S1 PublicationCorresponds to variant dbSNP:rs55963442EnsemblClinVar.1
Natural variantiVAR_041756696P → L1 PublicationCorresponds to variant dbSNP:rs56126328Ensembl.1
Natural variantiVAR_066605727A → V in CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 PublicationCorresponds to variant dbSNP:rs397515450EnsemblClinVar.1
Natural variantiVAR_041757782E → D1 PublicationCorresponds to variant dbSNP:rs34614566Ensembl.1
Natural variantiVAR_023046790V → M in CMS9; does not affect catalytic kinase activity; reduces protein expression and stability. 1 PublicationCorresponds to variant dbSNP:rs199476083EnsemblClinVar.1
Natural variantiVAR_041758819N → S in a lung neuroendocrine carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs757577755Ensembl.1
Natural variantiVAR_033837829V → L1 PublicationCorresponds to variant dbSNP:rs578430EnsemblClinVar.1
Natural variantiVAR_072788835M → V in CMS9; reduces AChR aggregation in developing neuromuscular junction. 1 Publication1
Natural variantiVAR_041759858R → H1 PublicationCorresponds to variant dbSNP:rs34115159EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_035958209E → EEESEPEQDTK in isoform 2. 1 Publication1
Alternative sequenceiVSP_035959307 – 394Missing in isoform 2 and isoform 3. 1 PublicationAdd BLAST88
Alternative sequenceiVSP_035960454 – 462DYNKENLKT → A in isoform 2 and isoform 3. 1 Publication9

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
AF006464 mRNA Translation: AAB63044.1
AL157881 Genomic DNA No translation available.
AL513328 Genomic DNA No translation available.
BC109098 mRNA Translation: AAI09099.1
BC109099 mRNA Translation: AAI09100.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS48005.1 [O15146-1]
CCDS75874.1 [O15146-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001159752.1, NM_001166280.1 [O15146-2]
NP_001159753.1, NM_001166281.1 [O15146-3]
NP_005583.1, NM_005592.3 [O15146-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.521653

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000189978; ENSP00000189978; ENSG00000030304 [O15146-2]
ENST00000374448; ENSP00000363571; ENSG00000030304 [O15146-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4593

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4593

UCSC genome browser

More...
UCSCi
uc064vai.1 human [O15146-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

MuSK entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006464 mRNA Translation: AAB63044.1
AL157881 Genomic DNA No translation available.
AL513328 Genomic DNA No translation available.
BC109098 mRNA Translation: AAI09099.1
BC109099 mRNA Translation: AAI09100.1
CCDSiCCDS48005.1 [O15146-1]
CCDS75874.1 [O15146-2]
RefSeqiNP_001159752.1, NM_001166280.1 [O15146-2]
NP_001159753.1, NM_001166281.1 [O15146-3]
NP_005583.1, NM_005592.3 [O15146-1]
UniGeneiHs.521653

3D structure databases

ProteinModelPortaliO15146
SMRiO15146
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110679, 8 interactors
IntActiO15146, 6 interactors
MINTiO15146
STRINGi9606.ENSP00000363571

Chemistry databases

BindingDBiO15146
ChEMBLiCHEMBL5684
GuidetoPHARMACOLOGYi1847

PTM databases

iPTMnetiO15146
PhosphoSitePlusiO15146

Polymorphism and mutation databases

BioMutaiMUSK

Proteomic databases

jPOSTiO15146
PaxDbiO15146
PeptideAtlasiO15146
PRIDEiO15146
ProteomicsDBi48471
48472 [O15146-2]
48473 [O15146-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4593
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000189978; ENSP00000189978; ENSG00000030304 [O15146-2]
ENST00000374448; ENSP00000363571; ENSG00000030304 [O15146-1]
GeneIDi4593
KEGGihsa:4593
UCSCiuc064vai.1 human [O15146-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4593
DisGeNETi4593
EuPathDBiHostDB:ENSG00000030304.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MUSK
GeneReviewsiMUSK
HGNCiHGNC:7525 MUSK
MalaCardsiMUSK
MIMi208150 phenotype
601296 gene
616325 phenotype
neXtProtiNX_O15146
OpenTargetsiENSG00000030304
Orphaneti994 Fetal akinesia deformation sequence
98913 Postsynaptic congenital myasthenic syndromes
PharmGKBiPA31326

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IMMJ Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000158226
HOGENOMiHOG000044461
HOVERGENiHBG052539
InParanoidiO15146
KOiK05129
OMAiCAPYNGK
OrthoDBi1576308at2759
PhylomeDBiO15146
TreeFamiTF106465

Enzyme and pathway databases

ReactomeiR-HSA-3000178 ECM proteoglycans
SignaLinkiO15146
SIGNORiO15146

Miscellaneous databases

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

More...
ChiTaRSi
MUSK human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
4593

Protein Ontology

More...
PROi
PR:O15146

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000030304 Expressed in 88 organ(s), highest expression level in small intestine Peyer's patch
ExpressionAtlasiO15146 baseline and differential
GenevisibleiO15146 HS

Family and domain databases

Gene3Di1.10.2000.10, 1 hit
2.60.40.10, 3 hits
InterProiView protein in InterPro
IPR020067 Frizzled_dom
IPR036790 Frizzled_dom_sf
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF01392 Fz, 1 hit
PF07679 I-set, 2 hits
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 3 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50038 FZ, 1 hit
PS50835 IG_LIKE, 3 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiMUSK_HUMAN
<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: O15146
Secondary accession number(s): Q32MJ8
, Q32MJ9, Q5VZW7, Q5VZW8
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 1, 1998
Last modified: February 13, 2019
This is version 168 of the entry and version 1 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
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.

<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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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