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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-Experimental evidence at protein leveli

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

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Positively regulated by CK2.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei609ATPPROSITE-ProRule annotation1
Active sitei725Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi581 – 589ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Differentiation

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS00477-MONOMER.
ReactomeiR-HSA-3000178. ECM proteoglycans.
SignaLinkiO15146.
SIGNORiO15146.

Names & Taxonomyi

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
Gene namesi
Name:MUSK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:7525. MUSK.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 495ExtracellularSequence analysisAdd BLAST472
Transmembranei496 – 516HelicalSequence analysisAdd BLAST21
Topological domaini517 – 869CytoplasmicSequence analysisAdd BLAST353

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

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
Natural variantiVAR_07278538D → E in CMS9. 1 PublicationCorresponds to variant rs775587809dbSNPEnsembl.1
Natural variantiVAR_072786344P → R in CMS9. 1 PublicationCorresponds to variant rs387906803dbSNPEnsembl.1
Natural variantiVAR_066604605M → I in CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 PublicationCorresponds to variant rs766640370dbSNPEnsembl.1
Natural variantiVAR_066605727A → V in CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 PublicationCorresponds to variant rs397515450dbSNPEnsembl.1
Natural variantiVAR_023046790V → M in CMS9; does not affect catalytic kinase activity; reduces protein expression and stability. 1 PublicationCorresponds to variant rs199476083dbSNPEnsembl.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 tyrosin kinase activity in developing neuromuscular junction. 1 PublicationCorresponds to variant rs751889864dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi4593.
MalaCardsiMUSK.
MIMi208150. phenotype.
616325. phenotype.
OpenTargetsiENSG00000030304.
Orphaneti98913. Postsynaptic congenital myasthenic syndromes.
PharmGKBiPA31326.

Chemistry databases

ChEMBLiCHEMBL5684.
GuidetoPHARMACOLOGYi1847.

Polymorphism and mutation databases

BioMutaiMUSK.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000002444624 – 869Muscle, skeletal receptor tyrosine-protein kinaseAdd BLAST846

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 99By similarity
Disulfide bondi98 ↔ 112By similarity
Disulfide bondi142 ↔ 190By similarity
Glycosylationi222N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi233 ↔ 282By similarity
Disulfide bondi317 ↔ 382By similarity
Disulfide bondi325 ↔ 375By similarity
Glycosylationi338N-linked (GlcNAc...)By similarity1
Disulfide bondi366 ↔ 406By similarity
Disulfide bondi394 ↔ 447By similarity
Disulfide bondi398 ↔ 434By similarity
Modified residuei554Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei681Phosphoserine; by CK2By similarity1
Modified residuei698Phosphoserine; by CK2By similarity1
Modified residuei755Phosphotyrosine; by autocatalysisBy similarity1

Post-translational modificationi

Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis and lysosomal degradation (By similarity).By similarity
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).By similarity1 Publication
Neddylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO15146.
PeptideAtlasiO15146.
PRIDEiO15146.

PTM databases

iPTMnetiO15146.
PhosphoSitePlusiO15146.

Expressioni

Gene expression databases

BgeeiENSG00000030304.
CleanExiHS_MUSK.
ExpressionAtlasiO15146. baseline and differential.
GenevisibleiO15146. HS.

Organism-specific databases

HPAiCAB019394.

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. 6 interactors.
IntActiO15146. 6 interactors.
MINTiMINT-2983114.
STRINGi9606.ENSP00000363571.

Chemistry databases

BindingDBiO15146.

Structurei

3D structure databases

ProteinModelPortaliO15146.
SMRiO15146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

eggNOGiENOG410IMMJ. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000044461.
HOVERGENiHBG052539.
InParanoidiO15146.
KOiK05129.
OMAiKGYCAQY.
OrthoDBiEOG091G016V.
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.
IPR003599. Ig_sub.
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.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. 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. AlignAdd to basket

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04174827A → G.1 PublicationCorresponds to variant rs56054734dbSNPEnsembl.1
Natural variantiVAR_07278538D → E in CMS9. 1 PublicationCorresponds to variant rs775587809dbSNPEnsembl.1
Natural variantiVAR_041749100T → M.1 PublicationCorresponds to variant rs35142681dbSNPEnsembl.1
Natural variantiVAR_041750107G → E.1 PublicationCorresponds to variant rs55786136dbSNPEnsembl.1
Natural variantiVAR_041751159S → G.1 PublicationCorresponds to variant rs35176182dbSNPEnsembl.1
Natural variantiVAR_041752222N → S.1 PublicationCorresponds to variant rs55826142dbSNPEnsembl.1
Natural variantiVAR_072786344P → R in CMS9. 1 PublicationCorresponds to variant rs387906803dbSNPEnsembl.1
Natural variantiVAR_021930413M → I.1 PublicationCorresponds to variant rs2274419dbSNPEnsembl.1
Natural variantiVAR_072787575I → T in FADS; reduces agrin-dependent AChR aggregation and tyrosin kinase activity in developing neuromuscular junction. 1 PublicationCorresponds to variant rs751889864dbSNPEnsembl.1
Natural variantiVAR_066604605M → I in CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 PublicationCorresponds to variant rs766640370dbSNPEnsembl.1
Natural variantiVAR_041753629L → F.1 PublicationCorresponds to variant rs34267283dbSNPEnsembl.1
Natural variantiVAR_041754644V → A.1 PublicationCorresponds to variant rs41279055dbSNPEnsembl.1
Natural variantiVAR_041755664N → S.1 PublicationCorresponds to variant rs55963442dbSNPEnsembl.1
Natural variantiVAR_041756696P → L.1 PublicationCorresponds to variant rs56126328dbSNPEnsembl.1
Natural variantiVAR_066605727A → V in CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. 1 PublicationCorresponds to variant rs397515450dbSNPEnsembl.1
Natural variantiVAR_041757782E → D.1 PublicationCorresponds to variant rs34614566dbSNPEnsembl.1
Natural variantiVAR_023046790V → M in CMS9; does not affect catalytic kinase activity; reduces protein expression and stability. 1 PublicationCorresponds to variant rs199476083dbSNPEnsembl.1
Natural variantiVAR_041758819N → S in a lung neuroendocrine carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs757577755dbSNPEnsembl.1
Natural variantiVAR_033837829V → L.1 PublicationCorresponds to variant rs578430dbSNPEnsembl.1
Natural variantiVAR_072788835M → V in CMS9; reduces AChR aggregation in developing neuromuscular junction. 1 Publication1
Natural variantiVAR_041759858R → H.1 PublicationCorresponds to variant rs34115159dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
EMBLi
GenBanki
DDBJi
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]
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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

MuSK entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
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. 6 interactors.
IntActiO15146. 6 interactors.
MINTiMINT-2983114.
STRINGi9606.ENSP00000363571.

Chemistry databases

BindingDBiO15146.
ChEMBLiCHEMBL5684.
GuidetoPHARMACOLOGYi1847.

PTM databases

iPTMnetiO15146.
PhosphoSitePlusiO15146.

Polymorphism and mutation databases

BioMutaiMUSK.

Proteomic databases

PaxDbiO15146.
PeptideAtlasiO15146.
PRIDEiO15146.

Protocols and materials databases

DNASUi4593.
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

CTDi4593.
DisGeNETi4593.
GeneCardsiMUSK.
GeneReviewsiMUSK.
HGNCiHGNC:7525. MUSK.
HPAiCAB019394.
MalaCardsiMUSK.
MIMi208150. phenotype.
601296. gene.
616325. phenotype.
neXtProtiNX_O15146.
OpenTargetsiENSG00000030304.
Orphaneti98913. Postsynaptic congenital myasthenic syndromes.
PharmGKBiPA31326.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IMMJ. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000044461.
HOVERGENiHBG052539.
InParanoidiO15146.
KOiK05129.
OMAiKGYCAQY.
OrthoDBiEOG091G016V.
PhylomeDBiO15146.
TreeFamiTF106465.

Enzyme and pathway databases

BioCyciZFISH:HS00477-MONOMER.
ReactomeiR-HSA-3000178. ECM proteoglycans.
SignaLinkiO15146.
SIGNORiO15146.

Miscellaneous databases

ChiTaRSiMUSK. human.
GenomeRNAii4593.
PROiO15146.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000030304.
CleanExiHS_MUSK.
ExpressionAtlasiO15146. baseline and differential.
GenevisibleiO15146. HS.

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.
IPR003599. Ig_sub.
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.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 153 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.