Protein detail
DYSF
Dysferlin (Dystrophy-associated fer-1-like protein) (Fer-1-like protein 1)
Protein symbol DYSF | UniProt ID | EVMP score 0.50 |
Frequency 5 | Transmembrane count 1 | Protein classification Disease related genesHuman disease related genesPotential drug targetsPredicted intracellular proteinsPredicted membrane proteinsTransporters |
Basic Information
Protein Names
Dysferlin (Dystrophy-associated fer-1-like protein) (Fer-1-like protein 1)
Protein Class
Disease related genesHuman disease related genesPotential drug targetsPredicted intracellular proteinsPredicted membrane proteinsTransporters
Protein Function
- Predicted intracellular proteins
- Potential drug targets
- Human disease related genes:Musculoskeletal diseases:Muscular diseases
- Transporters:Transporter channels and pores
- Disease related genes
Transmembrane
2047..2067; Helical; Anchor for type IV membrane protein
Transmembrane Count
1
Ensembl
Entrez Gene Symbol
Gene Synonym
FER1L1LGMD2B
Gene Description
Dysferlin
Chromosome
2
Position
71453561-71686763
Frequency
5
EVMP Score
0.50
Fluorescence & Localization
Tissue Specificlymphoid tissueCell SpecificKupffer cellsSingle-Nuclei Brain Specificleukocyte
Function & Pathway
Protein Function
- Predicted intracellular proteins
- Potential drug targets
- Human disease related genes:Musculoskeletal diseases:Muscular diseases
- Transporters:Transporter channels and pores
- Disease related genes
Cellular Component
- GO:0005768 endosome
- GO:0005769 early endosome
- GO:0005770 late endosome
- GO:0005886 plasma membrane
- GO:0030139 endocytic vesicle
- GO:0030315 T-tubule
- GO:0030659 cytoplasmic vesicle membrane
- GO:0030672 synaptic vesicle membrane
- GO:0034451 centriolar satellite
- GO:0042383 sarcolemma
- GO:0070062 extracellular exosome
Molecular Function
Biological Process
Canonical Pathways
M16801 Sig regulation of the actin cytoskeleton by rho gtpases
Mediation Categories
Clinical-translation mediationFusion and delivery mediationImmune mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
27 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| extracellular | extracellular | OmniPath | No | No | No | No | No |
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
| cell_adhesion | cell_adhesion | Cellinker | Yes | Yes | No | No | No |
| adhesion | adhesion | OmniPath | Yes | Yes | No | No | No |
| cell_adhesion | cell_adhesion | OmniPath | Yes | Yes | No | No | No |
| ferlin | intracellular_intercellular_related | HGNC | Yes | No | No | No | No |
| intracellular_intercellular_related | intracellular_intercellular_related | OmniPath | Yes | No | No | No | No |
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Regulatory Interaction Network
0 records.
Protein Complex Composition
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential UltracentrifugationDensity Gradient CentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographyImmunoaffinity Capture | Western blotting|Immunoelectron MicroscopyMass spectrometryMass spectrometry [LTQ-FT Ultra]Western blotting|Flow cytometric alysis|Mass spectrometry | 14 | 318072373103452030604894297231439685355146339443447350534684727174848802328962025912735357287713618922738335265 |
Sequence, Structure & Domains
Sequences
Length
2,080
Mass
237,295
Sequence
MLRVFILYAENVHTPDTDISDAYCSAVFAGVKKRTKVIKNSVNPVWNEGFEWDLKGIPLDQGSELHVVVKDHETMGRNRFLGEAKVPLREVLATPSLSASFNAPLLDTKKQPTGASLVLQVSYTPLPGAVPLFPPPTPLEPSPTLPDLDVVADTGGEEDTEDQGLTGDEAEPFLDQSGGPGAPTTPRKLPSRPPPHYPGIKRKRSAPTSRKLLSDKPQDFQIRVQVIEGRQLPGVNIKPVVKVTAAGQTKRTRIHKGNSPLFNETLFFNLFDSPGELFDEPIFITVVDSRSLRTDALLGEFRMDVGTIYREPRHAYLRKWLLLSDPDDFSAGARGYLKTSLCVLGPGDEAPLERKDPSEDKEDIESNLLRPTGVALRGAHFCLKVFRAEDLPQMDDAVMDNVKQIFGFESNKKNLVDPFVEVSFAGKMLCSKILEKTANPQWNQNITLPAMFPSMCEKMRIRIIDWDRLTHNDIVATTYLSMSKISAPGGEIEEEPAGAVKPSKASDLDDYLGFLPTFGPCYINLYGSPREFTGFPDPYTELNTGKGEGVAYRGRLLLSLETKLVEHSEQKVEDLPADDILRVEKYLRRRKYSLFAAFYSATMLQDVDDAIQFEVSIGNYGNKFDMTCLPLASTTQYSRAVFDGCHYYYLPWGNVKPVVVLSSYWEDISHRIETQNQLLGIADRLEAGLEQVHLALKAQCSTEDVDSLVAQLTDELIAGCSQPLGDIHETPSATHLDQYLYQLRTHHLSQITEAALALKLGHSELPAALEQAEDWLLRLRALAEEPQNSLPDIVIWMLQGDKRVAYQRVPAHQVLFSRRGANYCGKNCGKLQTIFLKYPMEKVPGARMPVQIRVKLWFGLSVDEKEFNQFAEGKLSVFAETYENETKLALVGNWGTTGLTYPKFSDVTGKIKLPKDSFRPSAGWTWAGDWFVCPEKTLLHDMDAGHLSFVEEVFENQTRLPGGQWIYMSDNYTDVNGEKVLPKDDIECPLGWKWEDEEWSTDLNRAVDEQGWEYSITIPPERKPKHWVPAEKMYYTHRRRRWVRLRRRDLSQMEALKRHRQAEAEGEGWEYASLFGWKFHLEYRKTDAFRRRRWRRRMEPLEKTGPAAVFALEGALGGVMDDKSEDSMSVSTLSFGVNRPTISCIFDYGNRYHLRCYMYQARDLAAMDKDSFSDPYAIVSFLHQSQKTVVVKNTLNPTWDQTLIFYEIEIFGEPATVAEQPPSIVVELYDHDTYGADEFMGRCICQPSLERMPRLAWFPLTRGSQPSGELLASFELIQREKPAIHHIPGFEVQETSRILDESEDTDLPYPPPQREANIYMVPQNIKPALQRTAIEILAWGLRNMKSYQLANISSPSLVVECGGQTVQSCVIRNLRKNPNFDICTLFMEVMLPREELYCPPITVKVIDNRQFGRRPVVGQCTIRSLESFLCDPYSAESPSPQGGPDDVSLLSPGEDVLIDIDDKEPLIPIQEEEFIDWWSKFFASIGEREKCGSYLEKDFDTLKVYDTQLENVEAFEGLSDFCNTFKLYRGKTQEETEDPSVIGEFKGLFKIYPLPEDPAIPMPPRQFHQLAAQGPQECLVRIYIVRAFGLQPKDPNGKCDPYIKISIGKKSVSDQDNYIPCTLEPVFGKMFELTCTLPLEKDLKITLYDYDLLSKDEKIGETVVDLENRLLSKFGARCGLPQTYCVSGPNQWRDQLRPSQLLHLFCQQHRVKAPVYRTDRVMFQDKEYSIEEIEAGRIPNPHLGPVEERLALHVLQQQGLVPEHVESRPLYSPLQPDIEQGKLQMWVDLFPKALGRPGPPFNITPRRARRFFLRCIIWNTRDVILDDLSLTGEKMSDIYVKGWMIGFEEHKQKTDVHYRSLGGEGNFNWRFIFPFDYLPAEQVCTIAKKDAFWRLDKTESKIPARVVFQIWDNDKFSFDDFLGSLQLDLNRMPKPAKTAKKCSLDQLDDAFHPEWFVSLFEQKTVKGWWPCVAEEGEKKILAGKLEMTLEIVAESEHEERPAGQGRDEPNMNPKLEDPRRPDTSFLWFTSPYKTMKFILWRRFRWAIILFIILFILLLFLAIFIYAFPNYAAMKLVKPFS
Alternative Products
Event=Alternative promoter usage, Alternative splicing; Named isoforms=15; Comment=Approximately 23% of the transcripts in skeletal muscle incorporate exon 1a from an alternative promoter and missing the calcium-binding sites of domain C2 1.; Name=1; IsoId=O75923-1; Sequence=Displayed; Name=2; IsoId=O75923-2; Sequence=VSP_035925; Name=3; IsoId=O75923-3; Sequence=VSP_035926; Name=4; IsoId=O75923-4; Sequence=VSP_035927; Name=5; IsoId=O75923-5; Sequence=VSP_035925, VSP_035926; Name=6; IsoId=O75923-6; Sequence=VSP_035926, VSP_035927; Name=7; IsoId=O75923-7; Sequence=VSP_035925, VSP_035926, VSP_035927; Name=8; IsoId=O75923-8; Sequence=VSP_035924, VSP_035925; Name=9; IsoId=O75923-9; Sequence=VSP_035924, VSP_035926; Name=10; IsoId=O75923-10; Sequence=VSP_035924, VSP_035927; Name=11; IsoId=O75923-11; Sequence=VSP_035924, VSP_035925, VSP_035926; Name=12; IsoId=O75923-12; Sequence=VSP_035924, VSP_035926, VSP_035927; Name=13; IsoId=O75923-13; Sequence=VSP_035924, VSP_035925, VSP_035926, VSP_035927; Name=14; Synonyms=Dysferlin_v1, DYSF_v1; IsoId=O75923-14; Sequence=VSP_035924; Name=15; IsoId=O75923-15; Sequence=VSP_035926, VSP_035928, VSP_035929
Alternative Sequence
1..29; MLRVFILYAENVHTPDTDISDAYCSAVFA -> MLCCLLVRASNLPSAKKDRRSDPVASLTFR (in isoform 8, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13 and isoform 14); 152; A -> AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT (in isoform 2, isoform 5, isoform 7, isoform 8, isoform 11 and isoform 13); 494..508; EEPAGAVKPSKASDL -> V (in isoform 3, isoform 5, isoform 6, isoform 7, isoform 9, isoform 11, isoform 12, isoform 13 and isoform 15); 1470; Q -> QLADGLSSLAPTNTASPPSSPH (in isoform 4, isoform 6, isoform 7, isoform 10, isoform 12 and isoform 13); 1934..1968; KPAKTAKKCSLDQLDDAFHPEWFVSLFEQKTVKGW -> SSASSSRPPRPDCPARVGRQTDGPAHTPRVANMEL (in isoform 15); 1969..2080; Missing (in isoform 15)
3D Structural Models
Helix
89..92; 983..985
Beta Strand
1..11; 15..18; 22..28; 31..34; 45..53; 55..57; 64..71; 74..76; 79..87; 98..106; 107..109; 112..123; 946..958; 966..973; 996..998; 1000..1002; 1011..1015; 1021..1023; 1028..1030; 1037..1049
3D Structure
Electron microscopy (3); NMR spectroscopy (2); X-ray crystallography (5)
Domain & Motif Annotations
Compositional Bias
132..144; Pro residues; 155..172; Acidic residues
Domain (CC)
All seven C2 domains associate with lipid membranes in a calcium-dependent manner. Domains C2 1 and 3 have the highest affinity for calcium, the C2 domain 1 seems to be largely unstructured in the absence of bound ligands. The C2 domain 1 from isoform 14 does not bind calcium in the absence of bound phospholipid (PubMed:24239457, PubMed:24461013).
Domain (FT)
1..101; C2 1; 203..321; C2 2; 360..496; C2 3; 1136..1262; C2 4; 1310..1438; C2 5; 1561..1679; C2 6; 1795..1943; C2 7
Region
132..215; Disordered; 1995..2017; Disordered
Protein Families
Ferlin family
Sequence Similarities
Belongs to the ferlin family.
Clinical Relevance
Disease Involvement
Disease variantLimb-girdle muscular dystrophy
Related Diseases
Biomarker
Phase 1
Interaction Protein
ENSG00000036448ENSG00000077044ENSG00000077522ENSG00000101347ENSG00000101605ENSG00000102683ENSG00000105993ENSG00000116127ENSG00000123240ENSG00000128591ENSG00000143553ENSG00000155657ENSG00000157500ENSG00000164309ENSG00000175084
Interaction Count
15
Interaction Dataset
intact_biogrid