O15146 (MUSK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

MUSK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	869 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 junction › synapse › postsynaptic 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.
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.5 Ref.7
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 process	Differentiation
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Congenital myasthenic syndrome Disease mutation
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Muscle protein Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	memory Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of gene expression Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara 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-dependent Inferred from electronic annotation. Source: Compara 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_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to 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
Molecular_function	ATP 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: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AB1	P08238	2	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 869	846	Muscle, skeletal receptor tyrosine-protein kinase		PRO_0000024446
Regions
	Topological domain	24 – 495	472	Extracellular Potential
	Transmembrane	496 – 516	21	Helical; Potential
	Topological domain	517 – 869	353	Cytoplasmic Potential
	Domain	28 – 116	89	Ig-like 1
	Domain	121 – 205	85	Ig-like 2
	Domain	212 – 302	91	Ig-like 3
	Domain	312 – 450	139	FZ
	Domain	575 – 856	282	Protein kinase
	Nucleotide binding	581 – 589	9	ATP By similarity
Sites
	Active site	725	1	Proton acceptor By similarity
	Binding site	609	1	ATP By similarity
Amino acid modifications
	Modified residue	554	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	681	1	Phosphoserine; by CK2 By similarity
	Modified residue	698	1	Phosphoserine; by CK2 By similarity
	Modified residue	755	1	Phosphotyrosine; by autocatalysis By similarity
	Glycosylation	222	1	N-linked (GlcNAc...) Potential
	Glycosylation	338	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	49 ↔ 99		By similarity
	Disulfide bond	98 ↔ 112		By similarity
	Disulfide bond	142 ↔ 190		By similarity
	Disulfide bond	233 ↔ 282		By similarity
	Disulfide bond	317 ↔ 382		By similarity
	Disulfide bond	325 ↔ 375		By similarity
	Disulfide bond	366 ↔ 406		By similarity
	Disulfide bond	394 ↔ 447		By similarity
	Disulfide bond	398 ↔ 434		By similarity
Natural variations
	Alternative sequence	209	1	E → EEESEPEQDTK in isoform 2.		VSP_035958
	Alternative sequence	307 – 394	88	Missing in isoform 2 and isoform 3.		VSP_035959
	Alternative sequence	454 – 462	9	DYNKENLKT → A in isoform 2 and isoform 3.		VSP_035960
	Natural variant	27	1	A → G. Ref.6 Corresponds to variant rs56054734 [ dbSNP | Ensembl ].		VAR_041748
	Natural variant	100	1	T → M. Ref.6 Corresponds to variant rs35142681 [ dbSNP | Ensembl ].		VAR_041749
	Natural variant	107	1	G → E. Ref.6 Corresponds to variant rs55786136 [ dbSNP | Ensembl ].		VAR_041750
	Natural variant	159	1	S → G. Ref.6 Corresponds to variant rs35176182 [ dbSNP | Ensembl ].		VAR_041751
	Natural variant	222	1	N → S. Ref.6 Corresponds to variant rs55826142 [ dbSNP | Ensembl ].		VAR_041752
	Natural variant	413	1	M → I. Ref.6 Corresponds to variant rs2274419 [ dbSNP | Ensembl ].		VAR_021930
	Natural variant	605	1	M → I in CMS-ACHRD; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. Ref.7		VAR_066604
	Natural variant	629	1	L → F. Ref.6 Corresponds to variant rs34267283 [ dbSNP | Ensembl ].		VAR_041753
	Natural variant	644	1	V → A. Ref.6 Corresponds to variant rs41279055 [ dbSNP | Ensembl ].		VAR_041754
	Natural variant	664	1	N → S. Ref.6 Corresponds to variant rs55963442 [ dbSNP | Ensembl ].		VAR_041755
	Natural variant	696	1	P → L. Ref.6 Corresponds to variant rs56126328 [ dbSNP | Ensembl ].		VAR_041756
	Natural variant	727	1	A → V in CMS-ACHRD; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering. Ref.7		VAR_066605
	Natural variant	782	1	E → D. Ref.6 Corresponds to variant rs34614566 [ dbSNP | Ensembl ].		VAR_041757
	Natural variant	790	1	V → M in CMS-ACHRD; does not affect catalytic kinase activity; reduces protein expression and stability. Ref.5		VAR_023046
	Natural variant	819	1	N → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.6		VAR_041758
	Natural variant	829	1	V → L. Ref.6 Corresponds to variant rs578430 [ dbSNP | Ensembl ].		VAR_033837
	Natural variant	858	1	R → H. Ref.6 Corresponds to variant rs34115159 [ dbSNP | Ensembl ].		VAR_041759

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 3DDC20E179FA010C	FASTA	869	97,056
	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
	Isoform 2 [UniParc]. Checksum: 695BD37016C0D980	FASTA	783	87,598
	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 SKVVKLEVEE ESEPEQDTKV FARILRAPES HNVTFGSFVT 250 260 270 280 290 300 LHCTATGIPV PTITWIENGN AVSSGSIQES VKDRVIDSRL QLFITKPGLY TCIATNKHGE 310 320 330 340 350 360 KFSTAKAAAT ISIAEWREYC LAVKELFCAK EWLVMEEKTH RGLYRSEMHL LSVPECSKLP 370 380 390 400 410 420 SMHWDPTACA RLPHLAFPPM TSSKPSVDIP NLPSSSSSSF SVSPTYSMTV IISIMSSFAI 430 440 450 460 470 480 FVLLTITTLY CCRRRKQWKN KKRESAAVTL TTLPSELLLD RLHPNPMYQR MPLLLNPKLL 490 500 510 520 530 540 SLEYPRNNIE YVRDIGEGAF GRVFQARAPG LLPYEPFTMV AVKMLKEEAS ADMQADFQRE 550 560 570 580 590 600 AALMAEFDNP NIVKLLGVCA VGKPMCLLFE YMAYGDLNEF LRSMSPHTVC SLSHSDLSMR 610 620 630 640 650 660 AQVSSPGPPP LSCAEQLCIA RQVAAGMAYL SERKFVHRDL ATRNCLVGEN MVVKIADFGL 670 680 690 700 710 720 SRNIYSADYY KANENDAIPI RWMPPESIFY NRYTTESDVW AYGVVLWEIF SYGLQPYYGM 730 740 750 760 770 780 AHEEVIYYVR DGNILSCPEN CPVELYNLMR LCWSKLPADR PSFTSIHRIL ERMCERAEGT VSV
	Isoform 3 [UniParc]. Checksum: 3BEA481E3C84D000	FASTA	773	86,425
	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 ISIAEWREYC LAVKELFCAK EWLVMEEKTH RGLYRSEMHL LSVPECSKLP SMHWDPTACA 370 380 390 400 410 420 RLPHLAFPPM TSSKPSVDIP NLPSSSSSSF SVSPTYSMTV IISIMSSFAI FVLLTITTLY 430 440 450 460 470 480 CCRRRKQWKN KKRESAAVTL TTLPSELLLD RLHPNPMYQR MPLLLNPKLL SLEYPRNNIE 490 500 510 520 530 540 YVRDIGEGAF GRVFQARAPG LLPYEPFTMV AVKMLKEEAS ADMQADFQRE AALMAEFDNP 550 560 570 580 590 600 NIVKLLGVCA VGKPMCLLFE YMAYGDLNEF LRSMSPHTVC SLSHSDLSMR AQVSSPGPPP 610 620 630 640 650 660 LSCAEQLCIA RQVAAGMAYL SERKFVHRDL ATRNCLVGEN MVVKIADFGL SRNIYSADYY 670 680 690 700 710 720 KANENDAIPI RWMPPESIFY NRYTTESDVW AYGVVLWEIF SYGLQPYYGM AHEEVIYYVR 730 740 750 760 770 DGNILSCPEN CPVELYNLMR LCWSKLPADR PSFTSIHRIL ERMCERAEGT VSV

References

	« Hide 'large scale' referencesShow '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. , 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]	"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. , Eymard B., Pouget J., Hantai D. Hum. Mol. Genet. 13:3229-3240(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMS-ACHRD MET-790.
[6]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-27; MET-100; GLU-107; GLY-159; SER-222; ILE-413; PHE-629; ALA-644; SER-664; LEU-696; ASP-782; SER-819; LEU-829 AND HIS-858.
[7]	"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

GeneReviews

Wikipedia

MuSK entry

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.
IPI	IPI00289243. IPI00655599. IPI00915471.
RefSeq	NP_001159752.1. NM_001166280.1. NP_001159753.1. NM_001166281.1. NP_005583.1. NM_005592.3.
UniGene	Hs.521653.
3D structure databases
ProteinModelPortal	O15146.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15146. 1 interaction.
MINT	MINT-2983114.
STRING	9606.ENSP00000363571.
PTM databases
PhosphoSite	O15146.
Proteomic databases
PaxDb	O15146.
PRIDE	O15146.
Protocols and materials databases
DNASU	4593.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000189978; ENSP00000189978; ENSG00000030304. ENST00000374448; ENSP00000363571; ENSG00000030304. ENST00000416899; ENSP00000393608; ENSG00000030304.
GeneID	4593.
KEGG	hsa:4593.
UCSC	uc004bez.2. human. uc022blt.1. human. uc022blu.1. human.
Organism-specific databases
CTD	4593.
GeneCards	GC09P113431.
HGNC	HGNC:7525. MUSK.
MIM	600878. gene. 601296. gene. 608931. phenotype.
neXtProt	NX_O15146.
Orphanet	98913. Postsynaptic congenital myasthenic syndromes.
PharmGKB	PA31326.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000044461.
HOVERGEN	HBG052539.
InParanoid	O15146.
KO	K05129.
Gene expression databases
ArrayExpress	O15146.
Bgee	O15146.
CleanEx	HS_MUSK.
Genevestigator	O15146.
GermOnline	ENSG00000030304. Homo sapiens.
Family and domain databases
Gene3D	1.10.2000.10. 1 hit. 2.60.40.10. 3 hits.
InterPro	IPR020067. Frizzled_dom. IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR013098. Ig_I-set. IPR003598. Ig_sub2. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. [Graphical view]
Pfam	PF01392. Fz. 1 hit. PF07679. I-set. 2 hits. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
SMART	SM00408. IGc2. 3 hits. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50038. FZ. 1 hit. PS50835. IG_LIKE. 3 hits. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O15146.
ChEMBL	CHEMBL5684.
ChiTaRS	MUSK. human.
GenomeRNAi	4593.
NextBio	17656.
SOURCE	Search...

Entry information

Entry name

MUSK_HUMAN

Accession

Primary (citable) accession number: O15146
Secondary accession number(s): Q32MJ8 , Q32MJ9, Q5VZW7, Q5VZW8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.