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O15146

- MUSK_HUMAN

UniProt

O15146 - MUSK_HUMAN

Protein

Muscle, skeletal receptor tyrosine-protein kinase

Gene

MUSK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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. 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 similarity

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    Positively regulated by CK2.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei609 – 6091ATPPROSITE-ProRule annotation
    Active sitei725 – 7251Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi581 – 5899ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein tyrosine kinase activity Source: UniProtKB
    4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. extracellular matrix organization Source: Reactome
    3. memory Source: UniProtKB
    4. multicellular organismal development Source: UniProtKB-KW
    5. neuromuscular junction development Source: UniProtKB
    6. peptidyl-tyrosine phosphorylation Source: GOC
    7. positive regulation of gene expression Source: UniProtKB
    8. positive regulation of neuron apoptotic process Source: Ensembl
    9. positive regulation of protein geranylgeranylation Source: UniProtKB
    10. positive regulation of protein phosphorylation Source: UniProtKB
    11. protein autophosphorylation Source: UniProtKB
    12. regulation of synaptic growth at neuromuscular junction Source: UniProtKB
    13. regulation of transcription, DNA-templated Source: Ensembl
    14. skeletal muscle acetylcholine-gated channel clustering Source: UniProtKB
    15. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc

    Keywords - Molecular functioni

    Developmental protein, Kinase, Muscle protein, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Differentiation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_163906. ECM proteoglycans.
    SignaLinkiO15146.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Muscle, skeletal receptor tyrosine-protein kinase (EC:2.7.10.1)
    Alternative name(s):
    Muscle-specific tyrosine-protein kinase receptor
    Short name:
    MuSK
    Short name:
    Muscle-specific kinase receptor
    Gene namesi
    Name:MUSK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:7525. MUSK.

    Subcellular locationi

    Cell junctionsynapsepostsynaptic cell membrane Curated; Single-pass type I membrane protein Curated
    Note: Localizes to the postsynaptic cell membrane of the neuromuscular junction.Curated

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. integral component of plasma membrane Source: UniProtKB
    3. neuromuscular junction Source: UniProtKB
    4. postsynaptic membrane Source: UniProtKB
    5. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    Myasthenic syndrome, congenital, associated with acetylcholine receptor deficiency (CMS-ACHRD) [MIM:608931]: A post-synaptic congenital myasthenic syndrome. Congenital myasthenic syndromes (CMS) are inherited disorders of neuromuscular transmission that stem from mutations in presynaptic, synaptic, or postsynaptic proteins.2 Publications
    Note: 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.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti605 – 6051M → I in CMS-ACHRD; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 Publication
    VAR_066604
    Natural varianti727 – 7271A → V in CMS-ACHRD; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 Publication
    VAR_066605
    Natural varianti790 – 7901V → M in CMS-ACHRD; does not affect catalytic kinase activity; reduces protein expression and stability. 1 Publication
    VAR_023046

    Keywords - Diseasei

    Congenital myasthenic syndrome, Disease mutation

    Organism-specific databases

    MIMi608931. phenotype.
    Orphaneti98913. Postsynaptic congenital myasthenic syndromes.
    PharmGKBiPA31326.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 869846Muscle, skeletal receptor tyrosine-protein kinasePRO_0000024446Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi49 ↔ 99By similarity
    Disulfide bondi98 ↔ 112By similarity
    Disulfide bondi142 ↔ 190By similarity
    Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi233 ↔ 282By similarity
    Disulfide bondi317 ↔ 382By similarity
    Disulfide bondi325 ↔ 375By similarity
    Glycosylationi338 – 3381N-linked (GlcNAc...)By similarity
    Disulfide bondi366 ↔ 406By similarity
    Disulfide bondi394 ↔ 447By similarity
    Disulfide bondi398 ↔ 434By similarity
    Modified residuei554 – 5541Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei681 – 6811Phosphoserine; by CK2By similarity
    Modified residuei698 – 6981Phosphoserine; by CK2By similarity
    Modified residuei755 – 7551Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis and lysosomal degradation By similarity.By similarity
    Phosphorylated. Phosphorylation is induced by AGRIN. Autophosphorylation at Tyr-554 is required for interaction with DOK7 which in turn stimulates the phosphorylation and the activation of MUSK.
    Neddylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO15146.
    PRIDEiO15146.

    PTM databases

    PhosphoSiteiO15146.

    Expressioni

    Gene expression databases

    ArrayExpressiO15146.
    BgeeiO15146.
    CleanExiHS_MUSK.
    GenevestigatoriO15146.

    Interactioni

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSP90AB1P082382EBI-6423196,EBI-352572

    Protein-protein interaction databases

    BioGridi110679. 5 interactions.
    IntActiO15146. 6 interactions.
    MINTiMINT-2983114.
    STRINGi9606.ENSP00000363571.

    Structurei

    3D structure databases

    ProteinModelPortaliO15146.
    SMRiO15146. Positions 25-294, 314-454, 561-861.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 495472ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini517 – 869353CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei496 – 51621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 11689Ig-like 1Add
    BLAST
    Domaini121 – 20585Ig-like 2Add
    BLAST
    Domaini212 – 30291Ig-like 3Add
    BLAST
    Domaini312 – 450139FZPROSITE-ProRule annotationAdd
    BLAST
    Domaini575 – 856282Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
    Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000044461.
    HOVERGENiHBG052539.
    InParanoidiO15146.
    KOiK05129.
    OrthoDBiEOG76739G.
    PhylomeDBiO15146.
    TreeFamiTF106465.

    Family and domain databases

    Gene3Di1.10.2000.10. 1 hit.
    2.60.40.10. 3 hits.
    InterProiIPR020067. Frizzled_dom.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    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.
    [Graphical view]
    PfamiPF01392. Fz. 1 hit.
    PF07679. I-set. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00408. IGc2. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50038. 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.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    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

    MRELVNIPLV HILTLVAFSG TEKLPKAPVI TTPLETVDAL VEEVATFMCA    50
    VESYPQPEIS WTRNKILIKL FDTRYSIREN GQLLTILSVE DSDDGIYCCT 100
    ANNGVGGAVE SCGALQVKMK PKITRPPINV KIIEGLKAVL PCTTMGNPKP 150
    SVSWIKGDSP LRENSRIAVL ESGSLRIHNV QKEDAGQYRC VAKNSLGTAY 200
    SKVVKLEVEV FARILRAPES HNVTFGSFVT LHCTATGIPV PTITWIENGN 250
    AVSSGSIQES VKDRVIDSRL QLFITKPGLY TCIATNKHGE KFSTAKAAAT 300
    ISIAEWSKPQ KDNKGYCAQY RGEVCNAVLA KDALVFLNTS YADPEEAQEL 350
    LVHTAWNELK VVSPVCRPAA EALLCNHIFQ ECSPGVVPTP IPICREYCLA 400
    VKELFCAKEW LVMEEKTHRG LYRSEMHLLS VPECSKLPSM HWDPTACARL 450
    PHLDYNKENL KTFPPMTSSK PSVDIPNLPS SSSSSFSVSP TYSMTVIISI 500
    MSSFAIFVLL TITTLYCCRR RKQWKNKKRE SAAVTLTTLP SELLLDRLHP 550
    NPMYQRMPLL LNPKLLSLEY PRNNIEYVRD IGEGAFGRVF QARAPGLLPY 600
    EPFTMVAVKM LKEEASADMQ ADFQREAALM AEFDNPNIVK LLGVCAVGKP 650
    MCLLFEYMAY GDLNEFLRSM SPHTVCSLSH SDLSMRAQVS SPGPPPLSCA 700
    EQLCIARQVA AGMAYLSERK FVHRDLATRN CLVGENMVVK IADFGLSRNI 750
    YSADYYKANE NDAIPIRWMP PESIFYNRYT TESDVWAYGV VLWEIFSYGL 800
    QPYYGMAHEE VIYYVRDGNI LSCPENCPVE LYNLMRLCWS KLPADRPSFT 850
    SIHRILERMC ERAEGTVSV 869
    Length:869
    Mass (Da):97,056
    Last modified:January 1, 1998 - v1
    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

    Sequence cautioni

    The sequence CAH69977.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAH69978.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI17349.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI17350.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 271A → G.1 Publication
    Corresponds to variant rs56054734 [ dbSNP | Ensembl ].
    VAR_041748
    Natural varianti100 – 1001T → M.1 Publication
    Corresponds to variant rs35142681 [ dbSNP | Ensembl ].
    VAR_041749
    Natural varianti107 – 1071G → E.1 Publication
    Corresponds to variant rs55786136 [ dbSNP | Ensembl ].
    VAR_041750
    Natural varianti159 – 1591S → G.1 Publication
    Corresponds to variant rs35176182 [ dbSNP | Ensembl ].
    VAR_041751
    Natural varianti222 – 2221N → S.1 Publication
    Corresponds to variant rs55826142 [ dbSNP | Ensembl ].
    VAR_041752
    Natural varianti413 – 4131M → I.1 Publication
    Corresponds to variant rs2274419 [ dbSNP | Ensembl ].
    VAR_021930
    Natural varianti605 – 6051M → I in CMS-ACHRD; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 Publication
    VAR_066604
    Natural varianti629 – 6291L → F.1 Publication
    Corresponds to variant rs34267283 [ dbSNP | Ensembl ].
    VAR_041753
    Natural varianti644 – 6441V → A.1 Publication
    Corresponds to variant rs41279055 [ dbSNP | Ensembl ].
    VAR_041754
    Natural varianti664 – 6641N → S.1 Publication
    Corresponds to variant rs55963442 [ dbSNP | Ensembl ].
    VAR_041755
    Natural varianti696 – 6961P → L.1 Publication
    Corresponds to variant rs56126328 [ dbSNP | Ensembl ].
    VAR_041756
    Natural varianti727 – 7271A → V in CMS-ACHRD; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 Publication
    VAR_066605
    Natural varianti782 – 7821E → D.1 Publication
    Corresponds to variant rs34614566 [ dbSNP | Ensembl ].
    VAR_041757
    Natural varianti790 – 7901V → M in CMS-ACHRD; does not affect catalytic kinase activity; reduces protein expression and stability. 1 Publication
    VAR_023046
    Natural varianti819 – 8191N → S in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
    VAR_041758
    Natural varianti829 – 8291V → L.1 Publication
    Corresponds to variant rs578430 [ dbSNP | Ensembl ].
    VAR_033837
    Natural varianti858 – 8581R → H.1 Publication
    Corresponds to variant rs34115159 [ dbSNP | Ensembl ].
    VAR_041759

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei209 – 2091E → EEESEPEQDTK in isoform 2. 1 PublicationVSP_035958
    Alternative sequencei307 – 39488Missing in isoform 2 and isoform 3. 1 PublicationVSP_035959Add
    BLAST
    Alternative sequencei454 – 4629DYNKENLKT → A in isoform 2 and isoform 3. 1 PublicationVSP_035960

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006464 mRNA. Translation: AAB63044.1.
    AL157881, AL513328 Genomic DNA. Translation: CAH69977.1. Sequence problems.
    AL513328, AL157881 Genomic DNA. Translation: CAI17349.1. Sequence problems.
    AL157881, AL513328 Genomic DNA. Translation: CAH69978.1. Sequence problems.
    AL513328, AL157881 Genomic DNA. Translation: CAI17350.1. Sequence problems.
    BC109098 mRNA. Translation: AAI09099.1.
    BC109099 mRNA. Translation: AAI09100.1.
    CCDSiCCDS48005.1. [O15146-1]
    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.

    Genome annotation databases

    EnsembliENST00000374448; ENSP00000363571; ENSG00000030304. [O15146-1]
    GeneIDi4593.
    KEGGihsa:4593.
    UCSCiuc004bez.2. human. [O15146-2]
    uc022blt.1. human. [O15146-1]
    uc022blu.1. human. [O15146-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    MuSK entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006464 mRNA. Translation: AAB63044.1 .
    AL157881 , AL513328 Genomic DNA. Translation: CAH69977.1 . Sequence problems.
    AL513328 , AL157881 Genomic DNA. Translation: CAI17349.1 . Sequence problems.
    AL157881 , AL513328 Genomic DNA. Translation: CAH69978.1 . Sequence problems.
    AL513328 , AL157881 Genomic DNA. Translation: CAI17350.1 . Sequence problems.
    BC109098 mRNA. Translation: AAI09099.1 .
    BC109099 mRNA. Translation: AAI09100.1 .
    CCDSi CCDS48005.1. [O15146-1 ]
    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 ]
    UniGenei Hs.521653.

    3D structure databases

    ProteinModelPortali O15146.
    SMRi O15146. Positions 25-294, 314-454, 561-861.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110679. 5 interactions.
    IntActi O15146. 6 interactions.
    MINTi MINT-2983114.
    STRINGi 9606.ENSP00000363571.

    Chemistry

    BindingDBi O15146.
    ChEMBLi CHEMBL5684.
    GuidetoPHARMACOLOGYi 1847.

    PTM databases

    PhosphoSitei O15146.

    Proteomic databases

    PaxDbi O15146.
    PRIDEi O15146.

    Protocols and materials databases

    DNASUi 4593.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374448 ; ENSP00000363571 ; ENSG00000030304 . [O15146-1 ]
    GeneIDi 4593.
    KEGGi hsa:4593.
    UCSCi uc004bez.2. human. [O15146-2 ]
    uc022blt.1. human. [O15146-1 ]
    uc022blu.1. human. [O15146-3 ]

    Organism-specific databases

    CTDi 4593.
    GeneCardsi GC09P113431.
    GeneReviewsi MUSK.
    HGNCi HGNC:7525. MUSK.
    MIMi 601296. gene.
    608931. phenotype.
    neXtProti NX_O15146.
    Orphaneti 98913. Postsynaptic congenital myasthenic syndromes.
    PharmGKBi PA31326.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000044461.
    HOVERGENi HBG052539.
    InParanoidi O15146.
    KOi K05129.
    OrthoDBi EOG76739G.
    PhylomeDBi O15146.
    TreeFami TF106465.

    Enzyme and pathway databases

    Reactomei REACT_163906. ECM proteoglycans.
    SignaLinki O15146.

    Miscellaneous databases

    ChiTaRSi MUSK. human.
    GenomeRNAii 4593.
    NextBioi 17656.
    PROi O15146.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15146.
    Bgeei O15146.
    CleanExi HS_MUSK.
    Genevestigatori O15146.

    Family and domain databases

    Gene3Di 1.10.2000.10. 1 hit.
    2.60.40.10. 3 hits.
    InterProi IPR020067. Frizzled_dom.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    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.
    [Graphical view ]
    Pfami PF01392. Fz. 1 hit.
    PF07679. I-set. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00408. IGc2. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Receptor tyrosine kinase specific for the skeletal muscle lineage: expression in embryonic muscle, at the neuromuscular junction, and after injury."
      Valenzuela D.M., Stitt T.N., DiStefano P.S., Rojas E., Mattsson K., Compton D.L., Nunez L., Park J.S., Stark J.L., Gies D.R., Thomas S., LeBeau M.M., Fernald A.A., Copeland N.G., Jenkins N.A., Burden S.J., Glass D.J., Yancopoulos G.D.
      Neuron 15:573-584(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 2 AND 3).
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    4. "The cytoplasmic adaptor protein Dok7 activates the receptor tyrosine kinase MuSK via dimerization."
      Bergamin E., Hallock P.T., Burden S.J., Hubbard S.R.
      Mol. Cell 39:100-109(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOK7.
    5. "Development and validation of a method for profiling post-translational modification activities using protein microarrays."
      Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
      PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NEDDYLATION.
    6. Cited for: VARIANT CMS-ACHRD MET-790.
    7. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-27; MET-100; GLU-107; GLY-159; SER-222; ILE-413; PHE-629; ALA-644; SER-664; LEU-696; ASP-782; SER-819; LEU-829 AND HIS-858.
    8. "Mutations in MUSK causing congenital myasthenic syndrome impair MuSK-Dok-7 interaction."
      Maselli R.A., Arredondo J., Cagney O., Ng J.J., Anderson J.A., Williams C., Gerke B.J., Soliven B., Wollmann R.L.
      Hum. Mol. Genet. 19:2370-2379(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CMS-ACHRD ILE-605 AND VAL-727, CHARACTERIZATION OF VARIANTS CMS-ACHRD ILE-605 AND VAL-727.

    Entry informationi

    Entry nameiMUSK_HUMAN
    AccessioniPrimary (citable) accession number: O15146
    Secondary accession number(s): Q32MJ8
    , Q32MJ9, Q5VZW7, Q5VZW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    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.

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

    External Data

    Dasty 3