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O15146 (MUSK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MUSK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length869 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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.

Catalytic activity

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

Enzyme regulation

Positively regulated by CK2 By similarity.

Subunit structure

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. Ref.4

Subcellular location

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

Post-translational modification

Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis and lysosomal degradation 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.

Involvement in disease

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.
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. Ref.6 Ref.8

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family.

Contains 1 FZ (frizzled) domain.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processDifferentiation
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCongenital myasthenic syndrome
Disease mutation
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Muscle protein
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix organization

Traceable author statement. Source: Reactome

memory

Inferred from sequence or structural similarity. Source: UniProtKB

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

neuromuscular junction development

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: GOC

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein geranylgeranylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of synaptic growth at neuromuscular junction

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

skeletal muscle acetylcholine-gated channel clustering

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuromuscular junction

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from sequence or structural similarity. Source: UniProtKB

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSP90AB1P082382EBI-6423196,EBI-352572

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15146-1)

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.
Isoform 2 (identifier: O15146-2)

The sequence of this isoform differs from the canonical sequence as follows:
     209-209: E → EEESEPEQDTK
     307-394: Missing.
     454-462: DYNKENLKT → A
Isoform 3 (identifier: O15146-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 869846Muscle, skeletal receptor tyrosine-protein kinase
PRO_0000024446

Regions

Topological domain24 – 495472Extracellular Potential
Transmembrane496 – 51621Helical; Potential
Topological domain517 – 869353Cytoplasmic Potential
Domain28 – 11689Ig-like 1
Domain121 – 20585Ig-like 2
Domain212 – 30291Ig-like 3
Domain312 – 450139FZ
Domain575 – 856282Protein kinase
Nucleotide binding581 – 5899ATP By similarity

Sites

Active site7251Proton acceptor By similarity
Binding site6091ATP By similarity

Amino acid modifications

Modified residue5541Phosphotyrosine; by autocatalysis By similarity
Modified residue6811Phosphoserine; by CK2 By similarity
Modified residue6981Phosphoserine; by CK2 By similarity
Modified residue7551Phosphotyrosine; by autocatalysis By similarity
Glycosylation2221N-linked (GlcNAc...) Potential
Glycosylation3381N-linked (GlcNAc...) By similarity
Disulfide bond49 ↔ 99 By similarity
Disulfide bond98 ↔ 112 By similarity
Disulfide bond142 ↔ 190 By similarity
Disulfide bond233 ↔ 282 By similarity
Disulfide bond317 ↔ 382 By similarity
Disulfide bond325 ↔ 375 By similarity
Disulfide bond366 ↔ 406 By similarity
Disulfide bond394 ↔ 447 By similarity
Disulfide bond398 ↔ 434 By similarity

Natural variations

Alternative sequence2091E → EEESEPEQDTK in isoform 2.
VSP_035958
Alternative sequence307 – 39488Missing in isoform 2 and isoform 3.
VSP_035959
Alternative sequence454 – 4629DYNKENLKT → A in isoform 2 and isoform 3.
VSP_035960
Natural variant271A → G. Ref.7
Corresponds to variant rs56054734 [ dbSNP | Ensembl ].
VAR_041748
Natural variant1001T → M. Ref.7
Corresponds to variant rs35142681 [ dbSNP | Ensembl ].
VAR_041749
Natural variant1071G → E. Ref.7
Corresponds to variant rs55786136 [ dbSNP | Ensembl ].
VAR_041750
Natural variant1591S → G. Ref.7
Corresponds to variant rs35176182 [ dbSNP | Ensembl ].
VAR_041751
Natural variant2221N → S. Ref.7
Corresponds to variant rs55826142 [ dbSNP | Ensembl ].
VAR_041752
Natural variant4131M → I. Ref.7
Corresponds to variant rs2274419 [ dbSNP | Ensembl ].
VAR_021930
Natural variant6051M → I in CMS-ACHRD; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. Ref.8
VAR_066604
Natural variant6291L → F. Ref.7
Corresponds to variant rs34267283 [ dbSNP | Ensembl ].
VAR_041753
Natural variant6441V → A. Ref.7
Corresponds to variant rs41279055 [ dbSNP | Ensembl ].
VAR_041754
Natural variant6641N → S. Ref.7
Corresponds to variant rs55963442 [ dbSNP | Ensembl ].
VAR_041755
Natural variant6961P → L. Ref.7
Corresponds to variant rs56126328 [ dbSNP | Ensembl ].
VAR_041756
Natural variant7271A → V in CMS-ACHRD; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. Ref.8
VAR_066605
Natural variant7821E → D. Ref.7
Corresponds to variant rs34614566 [ dbSNP | Ensembl ].
VAR_041757
Natural variant7901V → M in CMS-ACHRD; does not affect catalytic kinase activity; reduces protein expression and stability. Ref.6
VAR_023046
Natural variant8191N → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.7
VAR_041758
Natural variant8291V → L. Ref.7
Corresponds to variant rs578430 [ dbSNP | Ensembl ].
VAR_033837
Natural variant8581R → H. Ref.7
Corresponds to variant rs34115159 [ dbSNP | Ensembl ].
VAR_041759

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 3DDC20E179FA010C

FASTA86997,056
        10         20         30         40         50         60 
MRELVNIPLV HILTLVAFSG TEKLPKAPVI TTPLETVDAL VEEVATFMCA VESYPQPEIS 

        70         80         90        100        110        120 
WTRNKILIKL FDTRYSIREN GQLLTILSVE DSDDGIYCCT ANNGVGGAVE SCGALQVKMK 

       130        140        150        160        170        180 
PKITRPPINV KIIEGLKAVL PCTTMGNPKP SVSWIKGDSP LRENSRIAVL ESGSLRIHNV 

       190        200        210        220        230        240 
QKEDAGQYRC VAKNSLGTAY SKVVKLEVEV FARILRAPES HNVTFGSFVT LHCTATGIPV 

       250        260        270        280        290        300 
PTITWIENGN AVSSGSIQES VKDRVIDSRL QLFITKPGLY TCIATNKHGE KFSTAKAAAT 

       310        320        330        340        350        360 
ISIAEWSKPQ KDNKGYCAQY RGEVCNAVLA KDALVFLNTS YADPEEAQEL LVHTAWNELK 

       370        380        390        400        410        420 
VVSPVCRPAA EALLCNHIFQ ECSPGVVPTP IPICREYCLA VKELFCAKEW LVMEEKTHRG 

       430        440        450        460        470        480 
LYRSEMHLLS VPECSKLPSM HWDPTACARL PHLDYNKENL KTFPPMTSSK PSVDIPNLPS 

       490        500        510        520        530        540 
SSSSSFSVSP TYSMTVIISI MSSFAIFVLL TITTLYCCRR RKQWKNKKRE SAAVTLTTLP 

       550        560        570        580        590        600 
SELLLDRLHP NPMYQRMPLL LNPKLLSLEY PRNNIEYVRD IGEGAFGRVF QARAPGLLPY 

       610        620        630        640        650        660 
EPFTMVAVKM LKEEASADMQ ADFQREAALM AEFDNPNIVK LLGVCAVGKP MCLLFEYMAY 

       670        680        690        700        710        720 
GDLNEFLRSM SPHTVCSLSH SDLSMRAQVS SPGPPPLSCA EQLCIARQVA AGMAYLSERK 

       730        740        750        760        770        780 
FVHRDLATRN CLVGENMVVK IADFGLSRNI YSADYYKANE NDAIPIRWMP PESIFYNRYT 

       790        800        810        820        830        840 
TESDVWAYGV VLWEIFSYGL QPYYGMAHEE VIYYVRDGNI LSCPENCPVE LYNLMRLCWS 

       850        860 
KLPADRPSFT SIHRILERMC ERAEGTVSV 

« Hide

Isoform 2 [UniParc].

Checksum: 695BD37016C0D980
Show »

FASTA78387,598
Isoform 3 [UniParc].

Checksum: 3BEA481E3C84D000
Show »

FASTA77386,425

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"MUSK, a new target for mutations causing congenital myasthenic syndrome."
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. expand/collapse author list , Eymard B., Pouget J., Hantai D.
Hum. Mol. Genet. 13:3229-3240(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001159752.1. NM_001166280.1.
NP_001159753.1. NM_001166281.1.
NP_005583.1. NM_005592.3.
UniGeneHs.521653.

3D structure databases

ProteinModelPortalO15146.
SMRO15146. Positions 25-294, 314-454, 561-861.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110679. 5 interactions.
IntActO15146. 2 interactions.
MINTMINT-2983114.
STRING9606.ENSP00000363571.

Chemistry

BindingDBO15146.
ChEMBLCHEMBL5684.
GuidetoPHARMACOLOGY1847.

PTM databases

PhosphoSiteO15146.

Proteomic databases

PaxDbO15146.
PRIDEO15146.

Protocols and materials databases

DNASU4593.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374448; ENSP00000363571; ENSG00000030304. [O15146-1]
GeneID4593.
KEGGhsa:4593.
UCSCuc004bez.2. human. [O15146-2]
uc022blt.1. human. [O15146-1]
uc022blu.1. human. [O15146-3]

Organism-specific databases

CTD4593.
GeneCardsGC09P113431.
HGNCHGNC:7525. MUSK.
MIM601296. gene.
608931. phenotype.
neXtProtNX_O15146.
Orphanet98913. Postsynaptic congenital myasthenic syndromes.
PharmGKBPA31326.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000044461.
HOVERGENHBG052539.
InParanoidO15146.
KOK05129.
OrthoDBEOG76739G.
PhylomeDBO15146.
TreeFamTF106465.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
SignaLinkO15146.

Gene expression databases

ArrayExpressO15146.
BgeeO15146.
CleanExHS_MUSK.
GenevestigatorO15146.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
2.60.40.10. 3 hits.
InterProIPR020067. 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]
PfamPF01392. Fz. 1 hit.
PF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50038. 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]
ProtoNetSearch...

Other

ChiTaRSMUSK. human.
GenomeRNAi4593.
NextBio17656.
PROO15146.
SOURCESearch...

Entry information

Entry nameMUSK_HUMAN
AccessionPrimary (citable) accession number: O15146
Secondary accession number(s): Q32MJ8 expand/collapse secondary AC list , Q32MJ9, Q5VZW7, Q5VZW8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM