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Q62838

- MUSK_RAT

UniProt

Q62838 - MUSK_RAT

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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

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 kinase binding Source: RGD
  3. protein tyrosine kinase activity Source: UniProtKB
  4. 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
Complete GO annotation...

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-KW
Complete GO annotation...

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 autocatalysis1 Publication

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.
InParanoidiQ62838.
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

« Hide

        10         20         30         40         50
MRELVNIPLL QMLTLVAFSG 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
SVSWIKGDSA LRENSRIAVL ESGSLRIHNV QKEDAGQYRC VAKNSLGTAY
210 220 230 240 250
SKLVKLEVEV FARILRAPES HNVTFGSFVT LRCTAIGMPV PTISWIENGN
260 270 280 290 300
AVSSGSIQEN VKDRVIDSRL QLFITKPGLY TCIATNKHGE KFSTAKAAAT
310 320 330 340 350
VSIAEWSKSQ KESKGYCAQY RGEVCDAVLV KDSLVFFNTS YPDPEEAQEL
360 370 380 390 400
LIHTAWNELK AVSPLCRPAA EALLCNHLFQ ECSPGVLPTP MPICREYCLA
410 420 430 440 450
VKELFCAKEW LAMEGKTHRG LYRSGMHFLP VPECSKLPSM HQDPTACTRL
460 470 480 490 500
PYLDYKKENI TTFPSITSSK PSVDIPNLPA STSSFAVSPA YSMTVIISIM
510 520 530 540 550
SCFAVFALLT ITTLYCCRRR REWKNKKRES AAVTLTTLPS 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 LVGENMVVKI 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):96,822
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.
InParanoidi Q62838.
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 29, 2014
This is version 124 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