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Q62838

- MUSK_RAT

UniProt

Q62838 - MUSK_RAT

Protein

Muscle, skeletal receptor tyrosine protein kinase

Gene

Musk

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.2 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Positively regulated by CK2.By similarity

    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

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: RGD
    3. protein kinase binding Source: RGD
    4. protein tyrosine kinase activity Source: UniProtKB
    5. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. cochlea development Source: RGD
    3. long-term synaptic potentiation Source: RGD
    4. memory Source: RGD
    5. negative regulation of gene expression Source: RGD
    6. neuromuscular junction development Source: RGD
    7. peptidyl-tyrosine phosphorylation Source: GOC
    8. positive regulation of gene expression Source: RGD
    9. positive regulation of peptidyl-tyrosine phosphorylation Source: RGD
    10. positive regulation of protein phosphorylation Source: RGD
    11. positive regulation of synaptic growth at neuromuscular junction Source: RGD
    12. positive regulation of synaptic transmission, cholinergic Source: RGD
    13. protein autophosphorylation Source: RGD
    14. receptor clustering Source: RGD
    15. regulation of synaptic growth at neuromuscular junction Source: UniProtKB
    16. response to axon injury Source: RGD
    17. response to electrical stimulus Source: RGD
    18. response to muscle activity Source: RGD
    19. retina development in camera-type eye Source: RGD

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Differentiation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3211. Musk.

    Subcellular locationi

    Cell junctionsynapsepostsynaptic cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
    Note: Localizes to the postsynaptic cell membrane of the neuromuscular junction.Curated

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell projection Source: RGD
    3. external side of plasma membrane Source: RGD
    4. integral component of membrane Source: UniProtKB-KW
    5. neuromuscular junction Source: RGD
    6. plasma membrane Source: UniProtKB
    7. postsynaptic membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481M → R: Strongly reduced agrin-dependent activation and autophosphorylation. 1 Publication
    Mutagenesisi83 – 831L → R: Abolishes agrin-dependent activation and autophosphorylation. 1 Publication
    Mutagenesisi96 – 961I → A: Abolishes agrin-dependent activation and autophosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 868847Muscle, skeletal receptor tyrosine protein kinasePRO_0000024448Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi49 ↔ 99
    Disulfide bondi98 ↔ 112
    Disulfide bondi142 ↔ 190
    Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi233 ↔ 282By similarity
    Disulfide bondi317 ↔ 382
    Disulfide bondi325 ↔ 375
    Glycosylationi338 – 3381N-linked (GlcNAc...)1 Publication
    Disulfide bondi366 ↔ 406
    Disulfide bondi394 ↔ 447
    Disulfide bondi398 ↔ 434
    Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis
    Modified residuei553 – 5531Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei680 – 6801Phosphoserine; by CK2By similarity
    Modified residuei697 – 6971Phosphoserine; by CK2By similarity
    Modified residuei754 – 7541Phosphotyrosine; by autocatalysis2 Publications

    Post-translational modificationi

    Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis and lysosomal degradation By similarity.By similarity
    Phosphorylated. Phosphorylation is induced by AGRIN. Autophosphorylation at Tyr-553 is required for interaction with DOK7 which in turn stimulates the phosphorylation and the activation of MUSK By similarity.By similarity
    Neddylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ62838.

    PTM databases

    PhosphoSiteiQ62838.

    Expressioni

    Tissue specificityi

    Muscle specific.1 Publication

    Developmental stagei

    From E14.0 day, expressed in developing myotomes. Once the muscle is innervated, localized to the neuromuscular junction (NMJ), where its expression is restricted to synaptic nuclei. Expression drops after birth.1 Publication

    Inductioni

    Up-regulated upon denervation (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriQ62838.

    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. 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. 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

    Protein-protein interaction databases

    IntActiQ62838. 7 interactions.
    STRINGi10116.ENSRNOP00000056324.

    Structurei

    Secondary structure

    1
    868
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 327
    Beta strandi36 – 405
    Beta strandi45 – 484
    Beta strandi51 – 555
    Beta strandi58 – 636
    Beta strandi75 – 784
    Helixi79 – 813
    Beta strandi83 – 886
    Helixi91 – 933
    Beta strandi95 – 1028
    Beta strandi104 – 1063
    Beta strandi109 – 12517
    Beta strandi130 – 1334
    Beta strandi138 – 1403
    Beta strandi143 – 1486
    Beta strandi151 – 1566
    Beta strandi165 – 1695
    Beta strandi175 – 1795
    Helixi182 – 1843
    Beta strandi186 – 1949
    Beta strandi197 – 2004
    Beta strandi204 – 2096
    Beta strandi315 – 3184
    Beta strandi323 – 3253
    Turni326 – 3283
    Beta strandi335 – 3384
    Beta strandi341 – 3433
    Helixi344 – 35916
    Turni364 – 3663
    Helixi367 – 37812
    Beta strandi384 – 3874
    Helixi395 – 4039
    Turni404 – 4096
    Helixi410 – 42415
    Helixi434 – 4363
    Turni440 – 4423
    Beta strandi446 – 4483
    Turni451 – 4533
    Helixi562 – 5665
    Helixi571 – 5733
    Beta strandi575 – 5828
    Beta strandi587 – 5948
    Beta strandi600 – 60910
    Helixi616 – 63015
    Beta strandi640 – 6445
    Beta strandi646 – 6494
    Beta strandi651 – 6555
    Helixi662 – 6687
    Helixi698 – 71720
    Helixi727 – 7293
    Beta strandi730 – 7323
    Helixi734 – 7363
    Beta strandi738 – 7403
    Helixi746 – 7494
    Helixi751 – 7533
    Helixi765 – 7673
    Helixi770 – 7756
    Helixi780 – 79516
    Turni796 – 7983
    Turni801 – 8044
    Helixi807 – 8159
    Helixi828 – 83710
    Helixi842 – 8443
    Helixi848 – 85710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LUFX-ray2.05A529-868[»]
    2IEPX-ray2.21A/B22-212[»]
    3HKLX-ray2.10A/B313-494[»]
    ProteinModelPortaliQ62838.
    SMRiQ62838. Positions 25-211, 560-860.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ62838.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 494473ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini516 – 868353CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei495 – 51521HelicalSequence AnalysisAdd
    BLAST

    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

    eggNOGiCOG0515.
    HOGENOMiHOG000044461.
    HOVERGENiHBG052539.
    KOiK05129.

    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.
    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. 3 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00408. IGc2. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q62838-1 [UniParc]FASTAAdd to Basket

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    MRELVNIPLL QMLTLVAFSG TEKLPKAPVI TTPLETVDAL VEEVATFMCA    50
    VESYPQPEIS WTRNKILIKL FDTRYSIREN GQLLTILSVE DSDDGIYCCT 100
    ANNGVGGAVE SCGALQVKMK PKITRPPINV KIIEGLKAVL PCTTMGNPKP 150
    SVSWIKGDSA LRENSRIAVL ESGSLRIHNV QKEDAGQYRC VAKNSLGTAY 200
    SKLVKLEVEV FARILRAPES HNVTFGSFVT LRCTAIGMPV PTISWIENGN 250
    AVSSGSIQEN VKDRVIDSRL QLFITKPGLY TCIATNKHGE KFSTAKAAAT 300
    VSIAEWSKSQ KESKGYCAQY RGEVCDAVLV KDSLVFFNTS YPDPEEAQEL 350
    LIHTAWNELK AVSPLCRPAA EALLCNHLFQ ECSPGVLPTP MPICREYCLA 400
    VKELFCAKEW LAMEGKTHRG LYRSGMHFLP VPECSKLPSM HQDPTACTRL 450
    PYLDYKKENI TTFPSITSSK PSVDIPNLPA STSSFAVSPA YSMTVIISIM 500
    SCFAVFALLT ITTLYCCRRR REWKNKKRES AAVTLTTLPS ELLLDRLHPN 550
    PMYQRMPLLL NPKLLSLEYP RNNIEYVRDI GEGAFGRVFQ ARAPGLLPYE 600
    PFTMVAVKML KEEASADMQA DFQREAALMA EFDNPNIVKL LGVCAVGKPM 650
    CLLFEYMAYG DLNEFLRSMS PHTVCSLSHS DLSTRARVSS PGPPPLSCAE 700
    QLCIARQVAA GMAYLSERKF VHRDLATRNC LVGENMVVKI ADFGLSRNIY 750
    SADYYKADGN DAIPIRWMPP ESIFYNRYTT ESDVWAYGVV LWEIFSYGLQ 800
    PYYGMAHEEV IYYVRDGNIL ACPENCPLEL YNLMRLCWSK LPADRPSFCS 850
    IHRILQRMCE RAEGTVGV 868
    Length:868
    Mass (Da):96,822
    Last modified:November 1, 1996 - v1
    Checksum:iC146B4E74EE25B24
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34985 mRNA. Translation: AAA90956.1.
    RefSeqiNP_112323.1. NM_031061.1.
    UniGeneiRn.10210.

    Genome annotation databases

    GeneIDi81725.
    KEGGirno:81725.
    UCSCiRGD:3211. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34985 mRNA. Translation: AAA90956.1 .
    RefSeqi NP_112323.1. NM_031061.1.
    UniGenei Rn.10210.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LUF X-ray 2.05 A 529-868 [» ]
    2IEP X-ray 2.21 A/B 22-212 [» ]
    3HKL X-ray 2.10 A/B 313-494 [» ]
    ProteinModelPortali Q62838.
    SMRi Q62838. Positions 25-211, 560-860.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q62838. 7 interactions.
    STRINGi 10116.ENSRNOP00000056324.

    PTM databases

    PhosphoSitei Q62838.

    Proteomic databases

    PRIDEi Q62838.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 81725.
    KEGGi rno:81725.
    UCSCi RGD:3211. rat.

    Organism-specific databases

    CTDi 4593.
    RGDi 3211. Musk.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000044461.
    HOVERGENi HBG052539.
    KOi K05129.

    Miscellaneous databases

    EvolutionaryTracei Q62838.
    NextBioi 615376.
    PROi Q62838.

    Gene expression databases

    Genevestigatori Q62838.

    Family and domain databases

    Gene3Di 1.10.2000.10. 1 hit.
    2.60.40.10. 3 hits.
    InterProi 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_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF01392. Fz. 1 hit.
    PF07679. I-set. 3 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00408. IGc2. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY DENERVATION.
      Tissue: Muscle.
    2. "MuSK expressed in the brain mediates cholinergic responses, synaptic plasticity, and memory formation."
      Garcia-Osta A., Tsokas P., Pollonini G., Landau E.M., Blitzer R., Alberini C.M.
      J. Neurosci. 26:7919-7932(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MEMORY FORMATION.
    3. Cited for: INTERACTION WITH LRP4.
    4. "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.
    5. "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, ENZYME REGULATION, PHOSPHORYLATION AT TYR-754.
    6. "Crystal structure of the MuSK tyrosine kinase: insights into receptor autoregulation."
      Till J.H., Becerra M., Watty A., Lu Y., Ma Y., Neubert T.A., Burden S.J., Hubbard S.R.
      Structure 10:1187-1196(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 560-860.
    7. "Crystal structure of the agrin-responsive immunoglobulin-like domains 1 and 2 of the receptor tyrosine kinase MuSK."
      Stiegler A.L., Burden S.J., Hubbard S.R.
      J. Mol. Biol. 364:424-433(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 22-212, FUNCTION, PHOSPHORYLATION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-48; LEU-83 AND ILE-96, DISULFIDE BONDS.
    8. "Crystal structure of the frizzled-like cysteine-rich domain of the receptor tyrosine kinase MuSK."
      Stiegler A.L., Burden S.J., Hubbard S.R.
      J. Mol. Biol. 393:1-9(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 313-494, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-338.

    Entry informationi

    Entry nameiMUSK_RAT
    AccessioniPrimary (citable) accession number: Q62838
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 123 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3