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Muscle, skeletal receptor tyrosine-protein kinase (EC 2.7.10.1) (Muscle-specific tyrosine-protein kinase receptor) (MuSK) (Muscle-specific kinase receptor)

 MUSK_HUMAN              Reviewed;         869 AA.
O15146; Q32MJ8; Q32MJ9; Q5VZW7; Q5VZW8;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
20-JUN-2018, entry version 162.
RecName: Full=Muscle, skeletal receptor tyrosine-protein kinase;
EC=2.7.10.1 {ECO:0000269|PubMed:25029443};
AltName: Full=Muscle-specific tyrosine-protein kinase receptor;
Short=MuSK;
Short=Muscle-specific kinase receptor;
Flags: Precursor;
Name=MUSK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING
(ISOFORMS 2 AND 3).
PubMed=7546737; DOI=10.1016/0896-6273(95)90146-9;
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.;
"Receptor tyrosine kinase specific for the skeletal muscle lineage:
expression in embryonic muscle, at the neuromuscular junction, and
after injury.";
Neuron 15:573-584(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH DOK7.
PubMed=20603078; DOI=10.1016/j.molcel.2010.06.007;
Bergamin E., Hallock P.T., Burden S.J., Hubbard S.R.;
"The cytoplasmic adaptor protein Dok7 activates the receptor tyrosine
kinase MuSK via dimerization.";
Mol. Cell 39:100-109(2010).
[5]
NEDDYLATION.
PubMed=20596523; DOI=10.1371/journal.pone.0011332;
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B.,
Spruck C.;
"Development and validation of a method for profiling post-
translational modification activities using protein microarrays.";
PLoS ONE 5:E11332-E11332(2010).
[6]
CATALYTIC ACTIVITY, COFACTOR, PHOSPHORYLATION, AND MUTAGENESIS OF
GLY-584; LYS-609 AND ASP-743.
PubMed=25029443; DOI=10.1371/journal.pone.0102695;
Bainbridge T.W., DeAlmeida V.I., Izrael-Tomasevic A., Chalouni C.,
Pan B., Goldsmith J., Schoen A.P., Quinones G.A., Kelly R., Lill J.R.,
Sandoval W., Costa M., Polakis P., Arnott D., Rubinfeld B.,
Ernst J.A.;
"Evolutionary divergence in the catalytic activity of the CAM-1, ROR1
and ROR2 kinase domains.";
PLoS ONE 9:E102695-E102695(2014).
[7]
VARIANT CMS9 MET-790, AND INVOLVEMENT IN CMS9.
PubMed=15496425; DOI=10.1093/hmg/ddh333;
Chevessier F., Faraut B., Ravel-Chapuis A., Richard P., Gaudon K.,
Bauche S., Prioleau C., Herbst R., Goillot E., Ioos C., Azulay J.-P.,
Attarian S., Leroy J.-P., Fournier E., Legay C., Schaeffer L.,
Koenig J., Fardeau M., Eymard B., Pouget J., Hantai D.;
"MUSK, a new target for mutations causing congenital myasthenic
syndrome.";
Hum. Mol. Genet. 13:3229-3240(2004).
[8]
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.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[9]
VARIANT CMS9 ARG-344.
PubMed=19949040; DOI=10.1212/WNL.0b013e3181c3fce9;
Mihaylova V., Salih M.A., Mukhtar M.M., Abuzeid H.A., El-Sadig S.M.,
von der Hagen M., Huebner A., Nurnberg G., Abicht A., Muller J.S.,
Lochmuller H., Guergueltcheva V.;
"Refinement of the clinical phenotype in musk-related congenital
myasthenic syndromes.";
Neurology 73:1926-1928(2009).
[10]
VARIANTS CMS9 ILE-605 AND VAL-727, AND CHARACTERIZATION OF VARIANTS
CMS9 ILE-605 AND VAL-727.
PubMed=20371544; DOI=10.1093/hmg/ddq110;
Maselli R.A., Arredondo J., Cagney O., Ng J.J., Anderson J.A.,
Williams C., Gerke B.J., Soliven B., Wollmann R.L.;
"Mutations in MUSK causing congenital myasthenic syndrome impair MuSK-
Dok-7 interaction.";
Hum. Mol. Genet. 19:2370-2379(2010).
[11]
VARIANT CMS9 VAL-835, AND SUBCELLULAR LOCATION.
PubMed=23326516; DOI=10.1371/journal.pone.0053826;
Ben Ammar A., Soltanzadeh P., Bauche S., Richard P., Goillot E.,
Herbst R., Gaudon K., Huze C., Schaeffer L., Yamanashi Y., Higuchi O.,
Taly A., Koenig J., Leroy J.P., Hentati F., Najmabadi H., Kahrizi K.,
Ilkhani M., Fardeau M., Eymard B., Hantai D.;
"A mutation causes MuSK reduced sensitivity to agrin and congenital
myasthenia.";
PLoS ONE 8:E53826-E53826(2013).
[12]
VARIANT FADS THR-575, INVOLVEMENT IN FADS, CHARACTERIZATION OF VARIANT
FADS THR-575, AND FUNCTION.
PubMed=25537362; DOI=10.1038/ejhg.2014.273;
Tan-Sindhunata M.B., Mathijssen I.B., Smit M., Baas F., de Vries J.I.,
van der Voorn J.P., Kluijt I., Hagen M.A., Blom E.W., Sistermans E.,
Meijers-Heijboer H., Waisfisz Q., Weiss M.M., Groffen A.J.;
"Identification of a Dutch founder mutation in MUSK causing fetal
akinesia deformation sequence.";
Eur. J. Hum. Genet. 23:1151-1157(2015).
[13]
VARIANT CMS9 GLU-38.
PubMed=24183479; DOI=10.1016/j.nmd.2013.08.002;
Gallenmuller C., Muller-Felber W., Dusl M., Stucka R.,
Guergueltcheva V., Blaschek A., von der Hagen M., Huebner A.,
Muller J.S., Lochmuller H., Abicht A.;
"Salbutamol-responsive limb-girdle congenital myasthenic syndrome due
to a novel missense mutation and heteroallelic deletion in MUSK.";
Neuromuscul. Disord. 24:31-35(2014).
[14]
INVOLVEMENT IN FADS.
PubMed=25612909; DOI=10.1136/jmedgenet-2014-102730;
Wilbe M., Ekvall S., Eurenius K., Ericson K., Casar-Borota O.,
Klar J., Dahl N., Ameur A., Anneren G., Bondeson M.L.;
"MuSK: a new target for lethal fetal akinesia deformation sequence
(FADS).";
J. Med. Genet. 52:195-202(2015).
-!- FUNCTION: 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). {ECO:0000250,
ECO:0000269|PubMed:25537362}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:25029443}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:25029443};
-!- ENZYME REGULATION: Positively regulated by CK2. {ECO:0000250}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:Q62838, ECO:0000305}.
-!- INTERACTION:
P08238:HSP90AB1; NbExp=2; IntAct=EBI-6423196, EBI-352572;
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane {ECO:0000269|PubMed:23326516}; Single-pass type I
membrane protein {ECO:0000305}. Note=Colocalizes with
acetylcholine receptors (AChR) to the postsynaptic cell membrane
of the neuromuscular junction. {ECO:0000269|PubMed:23326516}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O15146-1; Sequence=Displayed;
Name=2;
IsoId=O15146-2; Sequence=VSP_035958, VSP_035959, VSP_035960;
Name=3;
IsoId=O15146-3; Sequence=VSP_035959, VSP_035960;
-!- PTM: Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis
and lysosomal degradation (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated. 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).
{ECO:0000250|UniProtKB:Q62838, ECO:0000269|PubMed:25029443}.
-!- PTM: Neddylated. {ECO:0000269|PubMed:20596523}.
-!- DISEASE: Myasthenic syndrome, congenital, 9, associated with
acetylcholine receptor deficiency (CMS9) [MIM:616325]: A 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. {ECO:0000269|PubMed:15496425,
ECO:0000269|PubMed:19949040, ECO:0000269|PubMed:20371544,
ECO:0000269|PubMed:23326516, ECO:0000269|PubMed:24183479}.
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.
-!- DISEASE: Fetal akinesia deformation sequence (FADS) [MIM:208150]:
A 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.
{ECO:0000269|PubMed:25537362, ECO:0000269|PubMed:25612909}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=CAH69977.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH69978.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI17349.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI17350.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=MuSK entry;
URL="https://en.wikipedia.org/wiki/MuSK_protein";
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EMBL; AF006464; AAB63044.1; -; mRNA.
EMBL; AL157881; CAH69977.1; ALT_SEQ; Genomic_DNA.
EMBL; AL513328; CAH69977.1; JOINED; Genomic_DNA.
EMBL; AL513328; CAI17349.1; ALT_SEQ; Genomic_DNA.
EMBL; AL157881; CAI17349.1; JOINED; Genomic_DNA.
EMBL; AL157881; CAH69978.1; ALT_SEQ; Genomic_DNA.
EMBL; AL513328; CAH69978.1; JOINED; Genomic_DNA.
EMBL; AL513328; CAI17350.1; ALT_SEQ; Genomic_DNA.
EMBL; AL157881; CAI17350.1; JOINED; Genomic_DNA.
EMBL; BC109098; AAI09099.1; -; mRNA.
EMBL; BC109099; AAI09100.1; -; mRNA.
CCDS; CCDS48005.1; -. [O15146-1]
CCDS; CCDS75874.1; -. [O15146-2]
RefSeq; NP_001159752.1; NM_001166280.1. [O15146-2]
RefSeq; NP_001159753.1; NM_001166281.1. [O15146-3]
RefSeq; NP_005583.1; NM_005592.3. [O15146-1]
UniGene; Hs.521653; -.
ProteinModelPortal; O15146; -.
SMR; O15146; -.
BioGrid; 110679; 8.
IntAct; O15146; 6.
MINT; O15146; -.
STRING; 9606.ENSP00000363571; -.
BindingDB; O15146; -.
ChEMBL; CHEMBL5684; -.
GuidetoPHARMACOLOGY; 1847; -.
iPTMnet; O15146; -.
PhosphoSitePlus; O15146; -.
BioMuta; MUSK; -.
PaxDb; O15146; -.
PeptideAtlas; O15146; -.
PRIDE; O15146; -.
ProteomicsDB; 48471; -.
ProteomicsDB; 48472; -. [O15146-2]
ProteomicsDB; 48473; -. [O15146-3]
DNASU; 4593; -.
Ensembl; ENST00000189978; ENSP00000189978; ENSG00000030304. [O15146-2]
Ensembl; ENST00000374448; ENSP00000363571; ENSG00000030304. [O15146-1]
GeneID; 4593; -.
KEGG; hsa:4593; -.
UCSC; uc064vai.1; human. [O15146-1]
CTD; 4593; -.
DisGeNET; 4593; -.
EuPathDB; HostDB:ENSG00000030304.13; -.
GeneCards; MUSK; -.
GeneReviews; MUSK; -.
HGNC; HGNC:7525; MUSK.
MalaCards; MUSK; -.
MIM; 208150; phenotype.
MIM; 601296; gene.
MIM; 616325; phenotype.
neXtProt; NX_O15146; -.
OpenTargets; ENSG00000030304; -.
Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
PharmGKB; PA31326; -.
eggNOG; ENOG410IMMJ; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118818; -.
HOGENOM; HOG000044461; -.
HOVERGEN; HBG052539; -.
InParanoid; O15146; -.
KO; K05129; -.
OMA; KGYCAQY; -.
OrthoDB; EOG091G016V; -.
PhylomeDB; O15146; -.
TreeFam; TF106465; -.
Reactome; R-HSA-3000178; ECM proteoglycans.
SignaLink; O15146; -.
SIGNOR; O15146; -.
ChiTaRS; MUSK; human.
GenomeRNAi; 4593; -.
PRO; PR:O15146; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000030304; -.
CleanEx; HS_MUSK; -.
ExpressionAtlas; O15146; baseline and differential.
Genevisible; O15146; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007613; P:memory; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0007528; P:neuromuscular junction development; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:2000541; P:positive regulation of protein geranylgeranylation; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0008582; P:regulation of synaptic growth at neuromuscular junction; ISS:UniProtKB.
GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
Gene3D; 1.10.2000.10; -; 1.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR020067; Frizzled_dom.
InterPro; IPR036790; Frizzled_dom_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF01392; Fz; 1.
Pfam; PF07679; I-set; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50038; FZ; 1.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell junction; Cell membrane;
Complete proteome; Congenital myasthenic syndrome;
Developmental protein; Differentiation; Disease mutation;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase;
Magnesium; Membrane; Metal-binding; Muscle protein;
Nucleotide-binding; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Receptor; Reference proteome; Repeat;
Signal; Synapse; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 869 Muscle, skeletal receptor tyrosine-
protein kinase.
/FTId=PRO_0000024446.
TOPO_DOM 24 495 Extracellular. {ECO:0000255}.
TRANSMEM 496 516 Helical. {ECO:0000255}.
TOPO_DOM 517 869 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 116 Ig-like 1.
DOMAIN 121 205 Ig-like 2.
DOMAIN 212 302 Ig-like 3.
DOMAIN 312 450 FZ. {ECO:0000255|PROSITE-
ProRule:PRU00090}.
DOMAIN 575 856 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 581 589 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 725 725 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 609 609 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 554 554 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q61006}.
MOD_RES 681 681 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:Q61006}.
MOD_RES 698 698 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:Q61006}.
MOD_RES 755 755 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q62838}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 49 99 {ECO:0000250}.
DISULFID 98 112 {ECO:0000250}.
DISULFID 142 190 {ECO:0000250}.
DISULFID 233 282 {ECO:0000250}.
DISULFID 317 382 {ECO:0000250}.
DISULFID 325 375 {ECO:0000250}.
DISULFID 366 406 {ECO:0000250}.
DISULFID 394 447 {ECO:0000250}.
DISULFID 398 434 {ECO:0000250}.
VAR_SEQ 209 209 E -> EEESEPEQDTK (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035958.
VAR_SEQ 307 394 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035959.
VAR_SEQ 454 462 DYNKENLKT -> A (in isoform 2 and isoform
3). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_035960.
VARIANT 27 27 A -> G (in dbSNP:rs56054734).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041748.
VARIANT 38 38 D -> E (in CMS9; dbSNP:rs775587809).
{ECO:0000269|PubMed:24183479}.
/FTId=VAR_072785.
VARIANT 100 100 T -> M (in dbSNP:rs35142681).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041749.
VARIANT 107 107 G -> E (in dbSNP:rs55786136).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041750.
VARIANT 159 159 S -> G (in dbSNP:rs35176182).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041751.
VARIANT 222 222 N -> S (in dbSNP:rs55826142).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041752.
VARIANT 344 344 P -> R (in CMS9; dbSNP:rs387906803).
{ECO:0000269|PubMed:19949040}.
/FTId=VAR_072786.
VARIANT 413 413 M -> I (in dbSNP:rs2274419).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_021930.
VARIANT 575 575 I -> T (in FADS; reduces agrin-dependent
AChR aggregation and tyrosin kinase
activity in developing neuromuscular
junction; dbSNP:rs751889864).
{ECO:0000269|PubMed:25537362}.
/FTId=VAR_072787.
VARIANT 605 605 M -> I (in CMS9; affects interaction with
DOK7 and impairs MUSK phosphorylation;
altered AChR clustering;
dbSNP:rs766640370).
{ECO:0000269|PubMed:20371544}.
/FTId=VAR_066604.
VARIANT 629 629 L -> F (in dbSNP:rs34267283).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041753.
VARIANT 644 644 V -> A (in dbSNP:rs41279055).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041754.
VARIANT 664 664 N -> S (in dbSNP:rs55963442).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041755.
VARIANT 696 696 P -> L (in dbSNP:rs56126328).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041756.
VARIANT 727 727 A -> V (in CMS9; affects interaction with
DOK7 and impairs MUSK phosphorylation;
altered AChR clustering;
dbSNP:rs397515450).
{ECO:0000269|PubMed:20371544}.
/FTId=VAR_066605.
VARIANT 782 782 E -> D (in dbSNP:rs34614566).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041757.
VARIANT 790 790 V -> M (in CMS9; does not affect
catalytic kinase activity; reduces
protein expression and stability;
dbSNP:rs199476083).
{ECO:0000269|PubMed:15496425}.
/FTId=VAR_023046.
VARIANT 819 819 N -> S (in a lung neuroendocrine
carcinoma sample; somatic mutation;
dbSNP:rs757577755).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041758.
VARIANT 829 829 V -> L (in dbSNP:rs578430).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_033837.
VARIANT 835 835 M -> V (in CMS9; reduces AChR aggregation
in developing neuromuscular junction).
{ECO:0000269|PubMed:23326516}.
/FTId=VAR_072788.
VARIANT 858 858 R -> H (in dbSNP:rs34115159).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041759.
MUTAGEN 584 584 G->C,D: Mild decrease in kinase activity.
{ECO:0000269|PubMed:25029443}.
MUTAGEN 609 609 K->R: Severe loss of kinase activity.
{ECO:0000269|PubMed:25029443}.
MUTAGEN 743 743 D->N: Severe loss of kinase activity.
{ECO:0000269|PubMed:25029443}.
SEQUENCE 869 AA; 97056 MW; 3DDC20E179FA010C CRC64;
MRELVNIPLV HILTLVAFSG TEKLPKAPVI TTPLETVDAL VEEVATFMCA VESYPQPEIS
WTRNKILIKL FDTRYSIREN GQLLTILSVE DSDDGIYCCT ANNGVGGAVE SCGALQVKMK
PKITRPPINV KIIEGLKAVL PCTTMGNPKP SVSWIKGDSP LRENSRIAVL ESGSLRIHNV
QKEDAGQYRC VAKNSLGTAY SKVVKLEVEV FARILRAPES HNVTFGSFVT LHCTATGIPV
PTITWIENGN AVSSGSIQES VKDRVIDSRL QLFITKPGLY TCIATNKHGE KFSTAKAAAT
ISIAEWSKPQ KDNKGYCAQY RGEVCNAVLA KDALVFLNTS YADPEEAQEL LVHTAWNELK
VVSPVCRPAA EALLCNHIFQ ECSPGVVPTP IPICREYCLA VKELFCAKEW LVMEEKTHRG
LYRSEMHLLS VPECSKLPSM HWDPTACARL PHLDYNKENL KTFPPMTSSK PSVDIPNLPS
SSSSSFSVSP TYSMTVIISI MSSFAIFVLL TITTLYCCRR RKQWKNKKRE SAAVTLTTLP
SELLLDRLHP NPMYQRMPLL LNPKLLSLEY PRNNIEYVRD IGEGAFGRVF QARAPGLLPY
EPFTMVAVKM LKEEASADMQ ADFQREAALM AEFDNPNIVK LLGVCAVGKP MCLLFEYMAY
GDLNEFLRSM SPHTVCSLSH SDLSMRAQVS SPGPPPLSCA EQLCIARQVA AGMAYLSERK
FVHRDLATRN CLVGENMVVK IADFGLSRNI YSADYYKANE NDAIPIRWMP PESIFYNRYT
TESDVWAYGV VLWEIFSYGL QPYYGMAHEE VIYYVRDGNI LSCPENCPVE LYNLMRLCWS
KLPADRPSFT SIHRILERMC ERAEGTVSV


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