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Protein

Muscle, skeletal receptor tyrosine-protein kinase

Gene

Musk

Organism
Mus musculus (Mouse)
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. 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.5 Publications

Catalytic activityi

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

Cofactori

Mg2+By similarity

Enzyme regulationi

Positively regulated by CK2.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei608 – 6081ATPPROSITE-ProRule annotation
Active sitei724 – 7241Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi580 – 5889ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • PDZ domain binding Source: UniProtKB
  • protein tyrosine kinase activity Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase activity Source: MGI

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • multicellular organism development Source: UniProtKB-KW
  • neuromuscular junction development Source: UniProtKB
  • positive regulation of neuron apoptotic process Source: MGI
  • positive regulation of protein geranylgeranylation Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of skeletal muscle acetylcholine-gated channel clustering Source: UniProtKB
  • receptor clustering Source: MGI
  • regulation of synaptic growth at neuromuscular junction Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • skeletal muscle acetylcholine-gated channel clustering Source: UniProtKB
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

BRENDAi2.7.10.1. 3474.

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
Synonyms:Nsk2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:103581. Musk.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 494473ExtracellularSequence analysisAdd
BLAST
Transmembranei495 – 51521HelicalSequence analysisAdd
BLAST
Topological domaini516 – 868353CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • integral component of plasma membrane Source: UniProtKB
  • membrane Source: MGI
  • neuromuscular junction Source: UniProtKB
  • plasma membrane Source: MGI
  • postsynaptic membrane Source: UniProtKB
  • receptor complex Source: MGI
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Mice die perinatally being unable to take a breath and to respond to tail or leg pinch. Despite the presence of apparently normal skeletal muscle, the absence of differentiated nerve terminals is sufficient to account for this phenotype. Every aspect of NMJ formation examined is absent in these mice. Branches of the main intramuscular nerve do not establish normal contacts with the muscle, do not form correctly positioned or specialized nerve terminals, and are apparently not given appropriate signals to stop their wandering aimlessly across the muscle. Furthermore, postsynaptic differentiation is absent, muscle-derived proteins normally localized to the synaptic basal lamina or the postsynaptic membrane being uniformly distributed in myofibers.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi553 – 5531Y → F: Loss of interaction with DOK7. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 868847Muscle, skeletal receptor tyrosine-protein kinasePRO_0000024447Add
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
Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence analysis
Modified residuei553 – 5531Phosphotyrosine; by autocatalysis2 Publications
Modified residuei680 – 6801Phosphoserine; by CK21 Publication
Modified residuei697 – 6971Phosphoserine; by CK21 Publication
Modified residuei754 – 7541Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis and lysosomal degradation.1 Publication
Phosphorylated (PubMed:16818610). Phosphorylation is induced by AGRIN (PubMed:8653787, PubMed:18848351). Autophosphorylated. Autophosphorylation at Tyr-553 is required for interaction with DOK7 which in turn stimulates the phosphorylation and the activation of MUSK (PubMed:16794080, PubMed:20603078).5 Publications
Neddylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ61006.
PRIDEiQ61006.

PTM databases

iPTMnetiQ61006.
PhosphoSiteiQ61006.

Expressioni

Tissue specificityi

Expressed preferentially in skeletal muscle.1 Publication

Developmental stagei

Skeletal myogenesis is a major site of expression during normal embryogenesis. In addition, the ganglia of the developing peripheral nervous system and various embryonic epithelia, including those of kidney, lung and gut are also sites of expression.1 Publication

Gene expression databases

BgeeiQ61006.
CleanExiMM_MUSK.
ExpressionAtlasiQ61006. baseline and differential.
GenevisibleiQ61006. MM.

Interactioni

Subunit structurei

Monomer. Homodimer (Probable). Interacts with LRP4; the heterodimer forms an AGRIN receptor complex that binds AGRIN resulting in activation of MUSK. 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. Interacts with PDZRN3; this interaction is enhanced by agrin. Interacts with FNTA; the interaction is direct and mediates AGRIN-induced phosphorylation and activation of FNTA. Interacts with CSNK2B; mediates regulation by CK2. Interacts (via the cytoplasmic domain) with DNAJA3. Interacts with NSF; may regulate MUSK endocytosis and activity. Interacts with CAV3; may regulate MUSK signaling. Interacts with RNF31.Curated11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dok7Q18PE03EBI-3989087,EBI-3989091
NsfP464605EBI-6308424,EBI-398006

GO - Molecular functioni

  • PDZ domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi201860. 5 interactions.
IntActiQ61006. 4 interactions.
STRINGi10090.ENSMUSP00000095665.

Structurei

Secondary structure

1
868
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni551 – 5544Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ML4X-ray2.60E/F/G/H544-556[»]
ProteinModelPortaliQ61006.
SMRiQ61006. Positions 25-294, 314-454, 502-862.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61006.

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
Domaini574 – 855282Protein 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

eggNOGiENOG410IMMJ. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000044461.
HOVERGENiHBG052539.
InParanoidiQ61006.
KOiK05129.
OrthoDBiEOG76739G.
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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q61006-1) [UniParc]FASTAAdd to basket

Also known as: MLK2

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
MRELVNIPLL QMLTLVAFSG TEKLPKAPVI TTPLETVDAL VEEVATFMCA
60 70 80 90 100
VESYPQPEIS WTRNKILIKL FDTRYSIREN GQLLTILSVE DSDDGIYCCI
110 120 130 140 150
ANNGVGGAVE SCGALQVKMK PKITRPPINV KIIEGLKAVL PCTTMGNPKP
160 170 180 190 200
SVSWIKGDNA LRENSRIAVL ESGSLRIHNV QKEDAGQYRC VAKNSLGTAY
210 220 230 240 250
SKLVKLEVEV FARILRAPES HNVTFGSFVT LRCTAIGIPV PTISWIENGN
260 270 280 290 300
AVSSGSIQES VKDRVIDSRL QLFITKPGLY TCIATNKHGE KFSTAKAAAT
310 320 330 340 350
VSIAEWSKSQ KDSQGYCAQY RGEVCDAVLA KDALVFFNTS YRDPEDAQEL
360 370 380 390 400
LIHTAWNELK AVSPLCRPAA EALLCNHLFQ ECSPGVVPTP MPICREYCLA
410 420 430 440 450
VKELFCAKEW QAMEGKAHRG LYRSGMHLLP VPECSKLPSM HRDPTACTRL
460 470 480 490 500
PYLDYKKENI TTFPSITSSR PSADIPNLPA STSSFAVSPA YSMTVIISIV
510 520 530 540 550
SSFALFALLT IATLYCCRRR KEWKNKKRES TAVTLTTLPS ELLLDRLHPN
560 570 580 590 600
PMYQRMPLLL NPKLLSLEYP RNNIEYVRDI GEGAFGRVFQ ARAPGLLPYE
610 620 630 640 650
PFTMVAVKML KEEASADMQA DFQREAALMA EFDNPNIVKL LGVCAVGKPM
660 670 680 690 700
CLLFEYMAYG DLNEFLRSMS PHTVCSLSHS DLSTRARVSS PGPPPLSCAE
710 720 730 740 750
QLCIARQVAA GMAYLSERKF VHRDLATRNC LVGETMVVKI ADFGLSRNIY
760 770 780 790 800
SADYYKADGN DAIPIRWMPP ESIFYNRYTT ESDVWAYGVV LWEIFSYGLQ
810 820 830 840 850
PYYGMAHEEV IYYVRDGNIL ACPENCPLEL YNLMRLCWSK LPADRPSFCS
860
IHRILQRMCE RAEGTVGV
Length:868
Mass (Da):96,693
Last modified:November 1, 1996 - v1
Checksum:iAFE4E644C6869933
GO
Isoform 2 (identifier: Q61006-2) [UniParc]FASTAAdd to basket

Also known as: MLK1

The sequence of this isoform differs from the canonical sequence as follows:
     454-462: DYKKENITT → A

Note: No experimental confirmation available.
Show »
Length:860
Mass (Da):95,671
Checksum:iA837F8299BD7494C
GO
Isoform 3 (identifier: Q61006-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     324-338: VCDAVLAKDALVFFN → GVLMQGPGEKMLLVFLPT

Note: No experimental confirmation available.
Show »
Length:871
Mass (Da):96,998
Checksum:iAA8D8D17E2F04722
GO
Isoform 4 (identifier: Q61006-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     866-868: VGV → TDGRAHFFWPHQY

Note: No experimental confirmation available.
Show »
Length:878
Mass (Da):98,081
Checksum:iA08686F5F939B8BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311T → A in CAA60165 (PubMed:7624144).Curated
Sequence conflicti31 – 311T → A in CAA60166 (PubMed:7624144).Curated
Sequence conflicti169 – 1691V → A in CAA60165 (PubMed:7624144).Curated
Sequence conflicti169 – 1691V → A in CAA60166 (PubMed:7624144).Curated
Sequence conflicti211 – 2122FA → LG in CAA60165 (PubMed:7624144).Curated
Sequence conflicti211 – 2122FA → LG in CAA60166 (PubMed:7624144).Curated
Sequence conflicti235 – 2351A → E in CAA60165 (PubMed:7624144).Curated
Sequence conflicti235 – 2351A → E in CAA60166 (PubMed:7624144).Curated
Sequence conflicti341 – 3411Y → H in CAA60165 (PubMed:7624144).Curated
Sequence conflicti341 – 3411Y → H in CAA60166 (PubMed:7624144).Curated
Sequence conflicti376 – 3761N → Y in CAA60165 (PubMed:7624144).Curated
Sequence conflicti376 – 3761N → Y in CAA60166 (PubMed:7624144).Curated
Sequence conflicti380 – 3801Q → L in CAA60165 (PubMed:7624144).Curated
Sequence conflicti380 – 3801Q → L in CAA60166 (PubMed:7624144).Curated
Sequence conflicti435 – 4351S → R in CAA60165 (PubMed:7624144).Curated
Sequence conflicti435 – 4351S → R in CAA60166 (PubMed:7624144).Curated
Sequence conflicti503 – 5031F → L in CAA60165 (PubMed:7624144).Curated
Sequence conflicti503 – 5031F → L in CAA60166 (PubMed:7624144).Curated
Sequence conflicti512 – 5121A → V in CAA60165 (PubMed:7624144).Curated
Sequence conflicti512 – 5121A → V in CAA60166 (PubMed:7624144).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei324 – 33815VCDAV…LVFFN → GVLMQGPGEKMLLVFLPT in isoform 3. 1 PublicationVSP_010785Add
BLAST
Alternative sequencei454 – 4629DYKKENITT → A in isoform 2. 1 PublicationVSP_010784
Alternative sequencei866 – 8683VGV → TDGRAHFFWPHQY in isoform 4. 1 PublicationVSP_010786

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37708 mRNA. Translation: AAA79203.1.
U37709 mRNA. Translation: AAA79204.1.
X86444 mRNA. Translation: CAA60165.1.
X86445 Genomic DNA. Translation: CAA60166.1.
CCDSiCCDS18210.1. [Q61006-2]
CCDS18211.1. [Q61006-1]
PIRiI48696.
I48697.
RefSeqiNP_001032205.1. NM_001037128.1.
NP_001032206.1. NM_001037129.1.
NP_001032207.1. NM_001037130.1. [Q61006-2]
NP_035074.2. NM_010944.2. [Q61006-1]
UniGeneiMm.16148.

Genome annotation databases

EnsembliENSMUST00000084578; ENSMUSP00000081625; ENSMUSG00000057280. [Q61006-1]
ENSMUST00000102893; ENSMUSP00000099957; ENSMUSG00000057280. [Q61006-2]
GeneIDi18198.
KEGGimmu:18198.
UCSCiuc033icg.1. mouse. [Q61006-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37708 mRNA. Translation: AAA79203.1.
U37709 mRNA. Translation: AAA79204.1.
X86444 mRNA. Translation: CAA60165.1.
X86445 Genomic DNA. Translation: CAA60166.1.
CCDSiCCDS18210.1. [Q61006-2]
CCDS18211.1. [Q61006-1]
PIRiI48696.
I48697.
RefSeqiNP_001032205.1. NM_001037128.1.
NP_001032206.1. NM_001037129.1.
NP_001032207.1. NM_001037130.1. [Q61006-2]
NP_035074.2. NM_010944.2. [Q61006-1]
UniGeneiMm.16148.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ML4X-ray2.60E/F/G/H544-556[»]
ProteinModelPortaliQ61006.
SMRiQ61006. Positions 25-294, 314-454, 502-862.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201860. 5 interactions.
IntActiQ61006. 4 interactions.
STRINGi10090.ENSMUSP00000095665.

PTM databases

iPTMnetiQ61006.
PhosphoSiteiQ61006.

Proteomic databases

PaxDbiQ61006.
PRIDEiQ61006.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084578; ENSMUSP00000081625; ENSMUSG00000057280. [Q61006-1]
ENSMUST00000102893; ENSMUSP00000099957; ENSMUSG00000057280. [Q61006-2]
GeneIDi18198.
KEGGimmu:18198.
UCSCiuc033icg.1. mouse. [Q61006-1]

Organism-specific databases

CTDi4593.
MGIiMGI:103581. Musk.

Phylogenomic databases

eggNOGiENOG410IMMJ. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000044461.
HOVERGENiHBG052539.
InParanoidiQ61006.
KOiK05129.
OrthoDBiEOG76739G.
TreeFamiTF106465.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.

Miscellaneous databases

EvolutionaryTraceiQ61006.
PROiQ61006.
SOURCEiSearch...

Gene expression databases

BgeeiQ61006.
CleanExiMM_MUSK.
ExpressionAtlasiQ61006. baseline and differential.
GenevisibleiQ61006. MM.

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...

Publicationsi

  1. Caruso A., Morris J.C., Neben S., Finnerty H., Beier D., Turner K., Wood C.R.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "Cloning and developmental expression of Nsk2, a novel receptor tyrosine kinase implicated in skeletal myogenesis."
    Ganju P., Walls E., Brennan J., Reith A.D.
    Oncogene 11:281-290(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3 AND 4), DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    Tissue: Myoblast.
  3. Cited for: DISRUPTION PHENOTYPE, FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT.
  4. Cited for: IDENTIFICATION OF AGRIN AS LIGAND, IDENTIFICATION OF THE AGRIN RECEPTOR COMPLEX, PHOSPHORYLATION.
  5. "Distinct roles of nerve and muscle in postsynaptic differentiation of the neuromuscular synapse."
    Lin W., Burgess R.W., Dominguez B., Pfaff S.L., Sanes J.R., Lee K.F.
    Nature 410:1057-1064(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACETYLCHOLINE RECEPTOR CLUSTERING.
  6. "Regulation of AChR clustering by Dishevelled interacting with MuSK and PAK1."
    Luo Z.G., Wang Q., Zhou J.Z., Wang J., Luo Z., Liu M., He X., Wynshaw-Boris A., Xiong W.C., Lu B., Mei L.
    Neuron 35:489-505(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DVL1 AND PAK1.
  7. "A novel pathway for MuSK to induce key genes in neuromuscular synapse formation."
    Lacazette E., Le Calvez S., Gajendran N., Brenner H.R.
    J. Cell Biol. 161:727-736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTION REGULATION.
  8. "Implication of geranylgeranyltransferase I in synapse formation."
    Luo Z.G., Je H.S., Wang Q., Yang F., Dobbins G.C., Yang Z.H., Xiong W.C., Lu B., Mei L.
    Neuron 40:703-717(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RAC1 ACTIVATION, FUNCTION IN PHOSPHORYLATION OF FNTA, INTERACTION WITH FNTA.
  9. "A putative ariadne-like E3 ubiquitin ligase (PAUL) that interacts with the muscle-specific kinase (MuSK)."
    Bromann P.A., Weiner J.A., Apel E.D., Lewis R.M., Sanes J.R.
    Gene Expr. Patterns 4:77-84(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF31.
  10. "A single pulse of agrin triggers a pathway that acts to cluster acetylcholine receptors."
    Mittaud P., Camilleri A.A., Willmann R., Erb-Voegtli S., Burden S.J., Fuhrer C.
    Mol. Cell. Biol. 24:7841-7854(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACETYLCHOLINE RECEPTOR CLUSTERING.
  11. "Casein kinase 2-dependent serine phosphorylation of MuSK regulates acetylcholine receptor aggregation at the neuromuscular junction."
    Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T., Jacob G., Sticht H., Allende J., Boldyreff B., Brenner H.R., Hashemolhosseini S.
    Genes Dev. 20:1800-1816(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-680 AND SER-697 BY CK2, INTERACTION WITH CSNK2B.
  12. Cited for: INTERACTION WITH DOK7, PHOSPHORYLATION AT TYR-553, MUTAGENESIS OF TYR-553.
  13. "Regulation of synaptic growth and maturation by a synapse-associated E3 ubiquitin ligase at the neuromuscular junction."
    Lu Z., Je H.S., Young P., Gross J., Lu B., Feng G.
    J. Cell Biol. 177:1077-1089(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDZRN3, UBIQUITINATION.
  14. Cited for: PHOSPHORYLATION, INTERACTION WITH LRP4.
  15. "Muscle-specific receptor tyrosine kinase endocytosis in acetylcholine receptor clustering in response to agrin."
    Zhu D., Yang Z., Luo Z., Luo S., Xiong W.C., Mei L.
    J. Neurosci. 28:1688-1696(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NSF.
  16. "A mammalian homolog of Drosophila tumorous imaginal discs, Tid1, mediates agrin signaling at the neuromuscular junction."
    Linnoila J., Wang Y., Yao Y., Wang Z.Z.
    Neuron 60:625-641(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNAJA3, SUBCELLULAR LOCATION.
  17. "Caveolin-3 promotes nicotinic acetylcholine receptor clustering and regulates neuromuscular junction activity."
    Hezel M., de Groat W.C., Galbiati F.
    Mol. Biol. Cell 21:302-310(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV3.
  18. "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: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 544-556 IN COMPLEX WITH DOK7, INTERACTION WITH DOK7, PHOSPHORYLATION AT TYR-553.

Entry informationi

Entry nameiMUSK_MOUSE
AccessioniPrimary (citable) accession number: Q61006
Secondary accession number(s): Q61005, Q61987, Q61988
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. 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.