UniProtKB - O75923 (DYSF_HUMAN)
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
>sp|O75923|DYSF_HUMAN Dysferlin OS=Homo sapiens OX=9606 GN=DYSF PE=1 SV=1 MLRVFILYAENVHTPDTDISDAYCSAVFAGVKKRTKVIKNSVNPVWNEGFEWDLKGIPLD QGSELHVVVKDHETMGRNRFLGEAKVPLREVLATPSLSASFNAPLLDTKKQPTGASLVLQ VSYTPLPGAVPLFPPPTPLEPSPTLPDLDVVADTGGEEDTEDQGLTGDEAEPFLDQSGGP GAPTTPRKLPSRPPPHYPGIKRKRSAPTSRKLLSDKPQDFQIRVQVIEGRQLPGVNIKPV VKVTAAGQTKRTRIHKGNSPLFNETLFFNLFDSPGELFDEPIFITVVDSRSLRTDALLGE FRMDVGTIYREPRHAYLRKWLLLSDPDDFSAGARGYLKTSLCVLGPGDEAPLERKDPSED KEDIESNLLRPTGVALRGAHFCLKVFRAEDLPQMDDAVMDNVKQIFGFESNKKNLVDPFV EVSFAGKMLCSKILEKTANPQWNQNITLPAMFPSMCEKMRIRIIDWDRLTHNDIVATTYL SMSKISAPGGEIEEEPAGAVKPSKASDLDDYLGFLPTFGPCYINLYGSPREFTGFPDPYT ELNTGKGEGVAYRGRLLLSLETKLVEHSEQKVEDLPADDILRVEKYLRRRKYSLFAAFYS ATMLQDVDDAIQFEVSIGNYGNKFDMTCLPLASTTQYSRAVFDGCHYYYLPWGNVKPVVV LSSYWEDISHRIETQNQLLGIADRLEAGLEQVHLALKAQCSTEDVDSLVAQLTDELIAGC SQPLGDIHETPSATHLDQYLYQLRTHHLSQITEAALALKLGHSELPAALEQAEDWLLRLR ALAEEPQNSLPDIVIWMLQGDKRVAYQRVPAHQVLFSRRGANYCGKNCGKLQTIFLKYPM EKVPGARMPVQIRVKLWFGLSVDEKEFNQFAEGKLSVFAETYENETKLALVGNWGTTGLT YPKFSDVTGKIKLPKDSFRPSAGWTWAGDWFVCPEKTLLHDMDAGHLSFVEEVFENQTRL PGGQWIYMSDNYTDVNGEKVLPKDDIECPLGWKWEDEEWSTDLNRAVDEQGWEYSITIPP ERKPKHWVPAEKMYYTHRRRRWVRLRRRDLSQMEALKRHRQAEAEGEGWEYASLFGWKFH LEYRKTDAFRRRRWRRRMEPLEKTGPAAVFALEGALGGVMDDKSEDSMSVSTLSFGVNRP TISCIFDYGNRYHLRCYMYQARDLAAMDKDSFSDPYAIVSFLHQSQKTVVVKNTLNPTWD QTLIFYEIEIFGEPATVAEQPPSIVVELYDHDTYGADEFMGRCICQPSLERMPRLAWFPL TRGSQPSGELLASFELIQREKPAIHHIPGFEVQETSRILDESEDTDLPYPPPQREANIYM VPQNIKPALQRTAIEILAWGLRNMKSYQLANISSPSLVVECGGQTVQSCVIRNLRKNPNF DICTLFMEVMLPREELYCPPITVKVIDNRQFGRRPVVGQCTIRSLESFLCDPYSAESPSP QGGPDDVSLLSPGEDVLIDIDDKEPLIPIQEEEFIDWWSKFFASIGEREKCGSYLEKDFD TLKVYDTQLENVEAFEGLSDFCNTFKLYRGKTQEETEDPSVIGEFKGLFKIYPLPEDPAI PMPPRQFHQLAAQGPQECLVRIYIVRAFGLQPKDPNGKCDPYIKISIGKKSVSDQDNYIP CTLEPVFGKMFELTCTLPLEKDLKITLYDYDLLSKDEKIGETVVDLENRLLSKFGARCGL PQTYCVSGPNQWRDQLRPSQLLHLFCQQHRVKAPVYRTDRVMFQDKEYSIEEIEAGRIPN PHLGPVEERLALHVLQQQGLVPEHVESRPLYSPLQPDIEQGKLQMWVDLFPKALGRPGPP FNITPRRARRFFLRCIIWNTRDVILDDLSLTGEKMSDIYVKGWMIGFEEHKQKTDVHYRS LGGEGNFNWRFIFPFDYLPAEQVCTIAKKDAFWRLDKTESKIPARVVFQIWDNDKFSFDD FLGSLQLDLNRMPKPAKTAKKCSLDQLDDAFHPEWFVSLFEQKTVKGWWPCVAEEGEKKI LAGKLEMTLEIVAESEHEERPAGQGRDEPNMNPKLEDPRRPDTSFLWFTSPYKTMKFILW RRFRWAIILFIILFILLLFLAIFIYAFPNYAAMKLVKPFSCommunity curation ()Add a publicationFeedback
Dysferlin
DYSF
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 18 | Calcium 11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 19 | Calcium 1; via carbonyl oxygen1 Publication Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 21 | Calcium 11 Publication Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 40 | Calcium 11 Publication Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 1168 | Calcium 2PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 1174 | Calcium 2PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 1230 | Calcium 2PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 1232 | Calcium 2PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 1594 | Calcium 3PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 1600 | Calcium 3PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 1649 | Calcium 3PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 1651 | Calcium 3PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 1914 | Calcium 4PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 1917 | Calcium 4PROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
Metal bindingi | 1920 | Calcium 4PROSITE-ProRule annotation Manual assertion according to rulesi | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- alpha-tubulin binding Source: Ensembl
- calcium-dependent phospholipid binding Source: UniProtKB
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.15"Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains."
Davis D.B., Doherty K.R., Delmonte A.J., McNally E.M.
J. Biol. Chem. 277:22883-22888(2002) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT MMD1 ASP-67.
- calcium ion binding Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.27"Alternate splicing of dysferlin C2A confers Ca(2+)-dependent and Ca(2+)-independent binding for membrane repair."
Fuson K., Rice A., Mahling R., Snow A., Nayak K., Shanbhogue P., Meyer A.G., Redpath G.M., Hinderliter A., Cooper S.T., Sutton R.B.
Structure 22:104-115(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 1-124 IN COMPLEX WITH CALCIUM, CALCIUM-BINDING (ISOFORMS 1 AND 14), SUBCELLULAR LOCATION, DOMAIN, LIPID-BINDING, TISSUE SPECIFICITY.
- microtubule binding Source: Ensembl
- phospholipid binding Source: UniProtKBInferred from direct assayi
- Ref.27"Alternate splicing of dysferlin C2A confers Ca(2+)-dependent and Ca(2+)-independent binding for membrane repair."
Fuson K., Rice A., Mahling R., Snow A., Nayak K., Shanbhogue P., Meyer A.G., Redpath G.M., Hinderliter A., Cooper S.T., Sutton R.B.
Structure 22:104-115(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 1-124 IN COMPLEX WITH CALCIUM, CALCIUM-BINDING (ISOFORMS 1 AND 14), SUBCELLULAR LOCATION, DOMAIN, LIPID-BINDING, TISSUE SPECIFICITY.
GO - Biological processi
- angiogenesis Source: Ensembl
- cellular response to osmotic stress Source: Ensembl
- cytokine secretion Source: Ensembl
- fat cell differentiation Source: Ensembl
- glycerol metabolic process Source: Ensembl
- lipid storage Source: Ensembl
- macrophage activation involved in immune response Source: MGIInferred from mutant phenotypei
- "Dysferlin deficiency enhances monocyte phagocytosis: a model for the inflammatory onset of limb-girdle muscular dystrophy 2B."
Nagaraju K., Rawat R., Veszelovszky E., Thapliyal R., Kesari A., Sparks S., Raben N., Plotz P., Hoffman E.P.
Am J Pathol 172:774-785(2008) [PubMed] [Europe PMC] [Abstract]
- membrane fusion Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- monocyte activation involved in immune response Source: MGIInferred from mutant phenotypei
- "Dysferlin deficiency enhances monocyte phagocytosis: a model for the inflammatory onset of limb-girdle muscular dystrophy 2B."
Nagaraju K., Rawat R., Veszelovszky E., Thapliyal R., Kesari A., Sparks S., Raben N., Plotz P., Hoffman E.P.
Am J Pathol 172:774-785(2008) [PubMed] [Europe PMC] [Abstract]
- muscle contraction Source: Reactome
- muscle fiber development Source: Ensembl
- negative regulation of gene expression Source: Ensembl
- negative regulation of high voltage-gated calcium channel activity Source: Ensembl
- negative regulation of phagocytosis Source: MGIInferred from mutant phenotypei
- "Dysferlin deficiency enhances monocyte phagocytosis: a model for the inflammatory onset of limb-girdle muscular dystrophy 2B."
Nagaraju K., Rawat R., Veszelovszky E., Thapliyal R., Kesari A., Sparks S., Raben N., Plotz P., Hoffman E.P.
Am J Pathol 172:774-785(2008) [PubMed] [Europe PMC] [Abstract]
- negative regulation of protein catabolic process Source: Ensembl
- negative regulation of protein polyubiquitination Source: Ensembl
- plasma membrane organization Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- plasma membrane repair Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- positive regulation of cell adhesion Source: Ensembl
- positive regulation of endothelial cell proliferation Source: Ensembl
- positive regulation of neutrophil chemotaxis Source: Ensembl
- regulation of calcium ion import Source: Ensembl
- skeletal muscle tissue regeneration Source: Ensembl
- T-tubule organization Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- vesicle fusion Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Ligand | Calcium, Lipid-binding, Metal-binding |
Enzyme and pathway databases
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | O75923 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-445355, Smooth Muscle Contraction |
SIGNOR Signaling Network Open Resource More...SIGNORi | O75923 |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.F.1.2.1, the synaptosomal vesicle fusion pore (svf-pore) family |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: DysferlinAlternative name(s): Dystrophy-associated fer-1-like protein Fer-1-like protein 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:DYSF Synonyms:FER1L1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:3097, DYSF |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 603009, gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O75923 |
Eukaryotic Pathogen, Vector and Host Database Resources More...VEuPathDBi | HostDB:ENSG00000135636.13 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
Other locations
- Cytoplasmic vesicle membrane By similarity; Single-pass type II membrane protein By similarity
Note: Colocalizes, during muscle differentiation, with BIN1 in the T-tubule system of myotubules and at the site of contact between two myotubes or a myoblast and a myotube. Wounding of myotubes led to its focal enrichment to the site of injury and to its relocalization in a Ca2+-dependent manner toward the plasma membrane. Colocalizes with AHNAK, AHNAK2 and PARVB at the sarcolemma of skeletal muscle. Detected on the apical plasma membrane of the syncytiotrophoblast. Reaches the plasmma membrane through a caveolin-independent mechanism. Retained by caveolin at the plasmma membrane (By similarity). Colocalizes, during muscle differentiation, with CACNA1S in the T-tubule system of myotubules (By similarity). Accumulates and colocalizes with fusion vesicles at the sarcolemma disruption sites (By similarity).By similarity
Cytoskeleton
- centriolar satellite Source: HPA
- microtubule Source: Ensembl
Endosome
- early endosome Source: UniProtKBInferred from direct assayi
- "Reduced plasma membrane expression of dysferlin mutants is attributed to accelerated endocytosis via a syntaxin-4-associated pathway."
Evesson F.J., Peat R.A., Lek A., Brilot F., Lo H.P., Dale R.C., Parton R.G., North K.N., Cooper S.T.
J Biol Chem 285:28529-28539(2010) [PubMed] [Europe PMC] [Abstract]
- endosome Source: UniProtKBInferred from direct assayi
- "Reduced plasma membrane expression of dysferlin mutants is attributed to accelerated endocytosis via a syntaxin-4-associated pathway."
Evesson F.J., Peat R.A., Lek A., Brilot F., Lo H.P., Dale R.C., Parton R.G., North K.N., Cooper S.T.
J Biol Chem 285:28529-28539(2010) [PubMed] [Europe PMC] [Abstract]
- late endosome Source: UniProtKBInferred from direct assayi
- "Reduced plasma membrane expression of dysferlin mutants is attributed to accelerated endocytosis via a syntaxin-4-associated pathway."
Evesson F.J., Peat R.A., Lek A., Brilot F., Lo H.P., Dale R.C., Parton R.G., North K.N., Cooper S.T.
J Biol Chem 285:28529-28539(2010) [PubMed] [Europe PMC] [Abstract]
- early endosome Source: UniProtKBInferred from direct assayi
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- "Large-scale proteomics and phosphoproteomics of urinary exosomes."
Gonzales P.A., Pisitkun T., Hoffert J.D., Tchapyjnikov D., Star R.A., Kleta R., Wang N.S., Knepper M.A.
J Am Soc Nephrol 20:363-379(2009) [PubMed] [Europe PMC] [Abstract] - "In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine."
Principe S., Jones E.E., Kim Y., Sinha A., Nyalwidhe J.O., Brooks J., Semmes O.J., Troyer D.A., Lance R.S., Kislinger T., Drake R.R.
Proteomics 13:1667-1671(2013) [PubMed] [Europe PMC] [Abstract]
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Golgi apparatus
- Golgi apparatus Source: Ensembl
Nucleus
- nucleus Source: Ensembl
Plasma Membrane
- plasma membrane Source: UniProtKBInferred from direct assayi
- "Reduced plasma membrane expression of dysferlin mutants is attributed to accelerated endocytosis via a syntaxin-4-associated pathway."
Evesson F.J., Peat R.A., Lek A., Brilot F., Lo H.P., Dale R.C., Parton R.G., North K.N., Cooper S.T.
J Biol Chem 285:28529-28539(2010) [PubMed] [Europe PMC] [Abstract] - Ref.27"Alternate splicing of dysferlin C2A confers Ca(2+)-dependent and Ca(2+)-independent binding for membrane repair."
Fuson K., Rice A., Mahling R., Snow A., Nayak K., Shanbhogue P., Meyer A.G., Redpath G.M., Hinderliter A., Cooper S.T., Sutton R.B.
Structure 22:104-115(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 1-124 IN COMPLEX WITH CALCIUM, CALCIUM-BINDING (ISOFORMS 1 AND 14), SUBCELLULAR LOCATION, DOMAIN, LIPID-BINDING, TISSUE SPECIFICITY.
- sarcolemma Source: UniProtKBInferred from direct assayi
- Ref.19"AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration."
Huang Y., Laval S.H., van Remoortere A., Baudier J., Benaud C., Anderson L.V., Straub V., Deelder A., Frants R.R., den Dunnen J.T., Bushby K., van der Maarel S.M.
FASEB J. 21:732-742(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AHNAK AND AHNAK2, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT LGMDR2 ASP-67, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
- T-tubule Source: UniProtKBInferred from direct assayi
- Ref.19"AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration."
Huang Y., Laval S.H., van Remoortere A., Baudier J., Benaud C., Anderson L.V., Straub V., Deelder A., Frants R.R., den Dunnen J.T., Bushby K., van der Maarel S.M.
FASEB J. 21:732-742(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AHNAK AND AHNAK2, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT LGMDR2 ASP-67, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
- plasma membrane Source: UniProtKBInferred from direct assayi
Other locations
- cytoplasmic vesicle Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- cytoplasmic vesicle membrane Source: Reactome
- endocytic vesicle Source: UniProtKBInferred from direct assayi
- "Reduced plasma membrane expression of dysferlin mutants is attributed to accelerated endocytosis via a syntaxin-4-associated pathway."
Evesson F.J., Peat R.A., Lek A., Brilot F., Lo H.P., Dale R.C., Parton R.G., North K.N., Cooper S.T.
J Biol Chem 285:28529-28539(2010) [PubMed] [Europe PMC] [Abstract]
- integral component of membrane Source: UniProtKB-KW
- lamellipodium Source: Ensembl
- membrane microdomain Source: Ensembl
- cytoplasmic vesicle Source: GO_CentralInferred from biological aspect of ancestori
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 2046 | CytoplasmicSequence analysisAdd BLAST | 2046 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 2047 – 2067 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2068 – 2080 | ExtracellularSequence analysisAdd BLAST | 13 |
Keywords - Cellular componenti
Cell membrane, Cytoplasmic vesicle, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Muscular dystrophy, limb-girdle, autosomal recessive 2 (LGMDR2)14 PublicationsManual assertion based on experiment ini
- Ref.1"Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy."
Liu J., Aoki M., Illa I., Wu C., Fardeau M., Angelini C., Serrano C., Urtizberea J.A., Hentati F., Hamida M.B., Bohlega S., Culper E.J., Amato A.A., Bossie K., Oeltjen J., Bejaoui K., McKenna-Yasek D., Hosler B.A. , Schurr E., Arahata K., de Jong P.J., Brown R.H. Jr.
Nat. Genet. 20:31-36(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MMD1 VAL-1298; ARG-1857 AND CYS-2042, VARIANTS LGMDR2 VAL-1298 AND CYS-2042. - Ref.12"Identical mutation in patients with limb girdle muscular dystrophy type 2B or Miyoshi myopathy suggests a role for modifier gene(s)."
Weiler T., Bashir R., Anderson L.V.B., Davison K., Moss J.A., Britton S., Nylen E., Keers S., Vafiadaki E., Greenberg C.R., Bushby K.M.D., Wrogemann K.
Hum. Mol. Genet. 8:871-877(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, VARIANT MMD1 ARG-791, VARIANT LGMDR2 ARG-791. - Ref.19"AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration."
Huang Y., Laval S.H., van Remoortere A., Baudier J., Benaud C., Anderson L.V., Straub V., Deelder A., Frants R.R., den Dunnen J.T., Bushby K., van der Maarel S.M.
FASEB J. 21:732-742(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AHNAK AND AHNAK2, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT LGMDR2 ASP-67, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.21"A new phenotype of dysferlinopathy with congenital onset."
Paradas C., Gonzalez-Quereda L., De Luna N., Gallardo E., Garcia-Consuegra I., Gomez H., Cabello A., Illa I., Gallano P.
Neuromuscul. Disord. 19:21-25(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN LGMDR2. - Ref.29"Identical dysferlin mutation in limb-girdle muscular dystrophy type 2B and distal myopathy."
Illarioshkin S.N., Ivanova-Smolenskaya I.A., Greenberg C.R., Nylen E., Sukhorukov V.S., Poleshchuk V.V., Markova E.D., Wrogemann K.
Neurology 55:1931-1933(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT MMD1 ASP-67, VARIANT LGMDR2 ASP-67. - Ref.32"Molecular analysis of LGMD-2B and MM patients: identification of novel DYSF mutations and possible founder effect in the Italian population."
Cagliani R., Fortunato F., Giorda R., Rodolico C., Bonaglia M.C., Sironi M., D'Angelo M.G., Prelle A., Locatelli F., Toscano A., Bresolin N., Comi G.P.
Neuromuscul. Disord. 13:788-795(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LGMDR2 TRP-959; GLN-1038 AND LYS-1335, VARIANTS GLN-1022; ALA-GLU-1065 INS AND LEU-1331. - Ref.34"Dysferlin mutation analysis in a group of Italian patients with limb-girdle muscular dystrophy and Miyoshi myopathy."
Kawabe K., Goto K., Nishino I., Angelini C., Hayashi Y.K.
Eur. J. Neurol. 11:657-661(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MMD1 ARG-618; CYS-1041; LYS-1335; ARG-1361 AND ARG-1662, VARIANTS LGMDR2 LYS-1335 AND CYS-1505, VARIANTS GLN-1022 AND ALA-GLU-1065 INS. - Ref.37"Dysferlin mutations in LGMD2B, Miyoshi myopathy, and atypical dysferlinopathies."
Nguyen K., Bassez G., Bernard R., Krahn M., Labelle V., Figarella-Branger D., Pouget J., Hammouda el H., Beroud C., Urtizberea A., Eymard B., Leturcq F., Ben-Yaou R., Levy N.
Hum. Mutat. 26:165-165(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLU-170 AND TRP-253, VARIANTS LGMDR2 TRP-555 AND MET-1208, VARIANTS MMD1 GLU-299; TRP-456; TRP-555; HIS-1046 AND GLN-1693, VARIANT PROXIMODISTAL MYOPATHY VAL-1276, VARIANT PSEUDOMETABOLIC MYOPATHY PRO-266, VARIANTS VAL-189; LEU-1331; SER-1351 AND VAL-1748. - Ref.39"Mutation finding in patients with dysferlin deficiency and role of the dysferlin interacting proteins annexin A1 and A2 in muscular dystrophies."
Cagliani R., Magri F., Toscano A., Merlini L., Fortunato F., Lamperti C., Rodolico C., Prelle A., Sironi M., Aguennouz M., Ciscato P., Uncini A., Moggio M., Bresolin N., Comi G.P.
Hum. Mutat. 26:283-283(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MMD1 TRP-959; TRP-1693; ASN-1837 AND GLY-1942 AND CYS-2042, VARIANTS LGMDR2 ARG-621; TRP-959; GLN-1038; LYS-1335 AND CYS-2042, VARIANTS GLU-170; LEU-374 AND SER-1678. - Ref.40"Novel sequence variants in dysferlin-deficient muscular dystrophy leading to mRNA decay and possible C2-domain misfolding."
Wenzel K., Carl M., Perrot A., Zabojszcza J., Assadi M., Ebeling M., Geier C., Robinson P.N., Kress W., Osterziel K.-J., Spuler S.
Hum. Mutat. 27:599-600(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LGMDR2 ARG-299 AND PRO-1341. - Ref.41"Mutation impact on dysferlin inferred from database analysis and computer-based structural predictions."
Therrien C., Dodig D., Karpati G., Sinnreich M.
J. Neurol. Sci. 250:71-78(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LGMDR2 ARG-791; CYS-930; TRP-1768 AND CYS-2042, VARIANT ALA-GLU-1065 INS. - Ref.43"Symptomatic dysferlin gene mutation carriers: characterization of two cases."
Illa I., De Luna N., Dominguez-Perles R., Rojas-Garcia R., Paradas C., Palmer J., Marquez C., Gallano P., Gallardo E.
Neurology 68:1284-1289(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LGMDR2 TYR-625 AND GLY-1734, VARIANT MMD1 ARG-519. - Ref.44"Dysferlin-deficient muscular dystrophy features amyloidosis."
Spuler S., Carl M., Zabojszcza J., Straub V., Bushby K., Moore S.A., Baehring S., Wenzel K., Vinkemeier U., Rocken C.
Ann. Neurol. 63:323-328(2008) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LGMDR2 ARG-299, VARIANT MMD1 TRP-299. - Ref.45"Analysis of the DYSF mutational spectrum in a large cohort of patients."
Krahn M., Beroud C., Labelle V., Nguyen K., Bernard R., Bassez G., Figarella-Branger D., Fernandez C., Bouvenot J., Richard I., Ollagnon-Roman E., Bevilacqua J.A., Salvo E., Attarian S., Chapon F., Pellissier J.-F., Pouget J., Hammouda el H. , Laforet P., Urtizberea J.A., Eymard B., Leturcq F., Levy N.
Hum. Mutat. 30:E345-E375(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LGMDR2 ARG-52; ARG-155; GLU-234; THR-284; TRP-555; ARG-618; ARG-731; CYS-930; PRO-1228; THR-1526; ASP-1543; TRP-1768; SER-1970 AND CYS-2042, VARIANTS MMD1 GLU-299; 386-PHE--ASP-390 DELINS TYR; ARG-426; TRP-456; TRP-555; LEU-1029; HIS-1046; HIS-1046; GLN-1693; 1938-THR-ALA-1939 DEL AND CYS-2042, VARIANTS GLU-170; TRP-253 AND TRP-555, VARIANTS PROXIMODISTAL MYOPATHY ARG-299; ARG-340; VAL-1748; TRP-1768 AND CYS-2042, VARIANT PSEUDOMETABOLIC MYOPATHY PRO-266, VARIANTS VAL-84; VAL-189; ALA-335; LEU-374; ASN-390; GLN-819; GLN-1022; GLN-1038; VAL-1276; VAL-1325; ASN-1837 AND SER-1967.
Liu J., Aoki M., Illa I., Wu C., Fardeau M., Angelini C., Serrano C., Urtizberea J.A., Hentati F., Hamida M.B., Bohlega S., Culper E.J., Amato A.A., Bossie K., Oeltjen J., Bejaoui K., McKenna-Yasek D., Hosler B.A. , Schurr E., Arahata K., de Jong P.J., Brown R.H. Jr.
Nat. Genet. 20:31-36(1998) [PubMed] [Europe PMC] [Abstract]
Weiler T., Bashir R., Anderson L.V.B., Davison K., Moss J.A., Britton S., Nylen E., Keers S., Vafiadaki E., Greenberg C.R., Bushby K.M.D., Wrogemann K.
Hum. Mol. Genet. 8:871-877(1999) [PubMed] [Europe PMC] [Abstract]
Huang Y., Laval S.H., van Remoortere A., Baudier J., Benaud C., Anderson L.V., Straub V., Deelder A., Frants R.R., den Dunnen J.T., Bushby K., van der Maarel S.M.
FASEB J. 21:732-742(2007) [PubMed] [Europe PMC] [Abstract]
Paradas C., Gonzalez-Quereda L., De Luna N., Gallardo E., Garcia-Consuegra I., Gomez H., Cabello A., Illa I., Gallano P.
Neuromuscul. Disord. 19:21-25(2009) [PubMed] [Europe PMC] [Abstract]
Illarioshkin S.N., Ivanova-Smolenskaya I.A., Greenberg C.R., Nylen E., Sukhorukov V.S., Poleshchuk V.V., Markova E.D., Wrogemann K.
Neurology 55:1931-1933(2000) [PubMed] [Europe PMC] [Abstract]
Cagliani R., Fortunato F., Giorda R., Rodolico C., Bonaglia M.C., Sironi M., D'Angelo M.G., Prelle A., Locatelli F., Toscano A., Bresolin N., Comi G.P.
Neuromuscul. Disord. 13:788-795(2003) [PubMed] [Europe PMC] [Abstract]
Kawabe K., Goto K., Nishino I., Angelini C., Hayashi Y.K.
Eur. J. Neurol. 11:657-661(2004) [PubMed] [Europe PMC] [Abstract]
Nguyen K., Bassez G., Bernard R., Krahn M., Labelle V., Figarella-Branger D., Pouget J., Hammouda el H., Beroud C., Urtizberea A., Eymard B., Leturcq F., Ben-Yaou R., Levy N.
Hum. Mutat. 26:165-165(2005) [PubMed] [Europe PMC] [Abstract]
Cagliani R., Magri F., Toscano A., Merlini L., Fortunato F., Lamperti C., Rodolico C., Prelle A., Sironi M., Aguennouz M., Ciscato P., Uncini A., Moggio M., Bresolin N., Comi G.P.
Hum. Mutat. 26:283-283(2005) [PubMed] [Europe PMC] [Abstract]
Wenzel K., Carl M., Perrot A., Zabojszcza J., Assadi M., Ebeling M., Geier C., Robinson P.N., Kress W., Osterziel K.-J., Spuler S.
Hum. Mutat. 27:599-600(2006) [PubMed] [Europe PMC] [Abstract]
Therrien C., Dodig D., Karpati G., Sinnreich M.
J. Neurol. Sci. 250:71-78(2006) [PubMed] [Europe PMC] [Abstract]
Illa I., De Luna N., Dominguez-Perles R., Rojas-Garcia R., Paradas C., Palmer J., Marquez C., Gallano P., Gallardo E.
Neurology 68:1284-1289(2007) [PubMed] [Europe PMC] [Abstract]
Spuler S., Carl M., Zabojszcza J., Straub V., Bushby K., Moore S.A., Baehring S., Wenzel K., Vinkemeier U., Rocken C.
Ann. Neurol. 63:323-328(2008) [PubMed] [Europe PMC] [Abstract]
Krahn M., Beroud C., Labelle V., Nguyen K., Bernard R., Bassez G., Figarella-Branger D., Fernandez C., Bouvenot J., Richard I., Ollagnon-Roman E., Bevilacqua J.A., Salvo E., Attarian S., Chapon F., Pellissier J.-F., Pouget J., Hammouda el H. , Laforet P., Urtizberea J.A., Eymard B., Leturcq F., Levy N.
Hum. Mutat. 30:E345-E375(2009) [PubMed] [Europe PMC] [Abstract]
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_057834 | 52 | W → R in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057835 | 67 | V → D in MMD1 and LGMDR2; Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057837 | 155 | G → R in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057838 | 234 | G → E in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057839 | 284 | I → T in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057840 | 299 | G → R in LGMDR2 and proximodistal myopathy. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024859 | 555 | R → W in LGMDR2 and MMD1; also found in patients with isolated hyperCKemia. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057851 | 618 | G → R in MMD1 and LGMDR2. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057852 | 621 | G → R in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057853 | 625 | D → Y in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057854 | 731 | P → R in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_012308 | 791 | P → R in MMD1 and LGMDR2. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057856 | 930 | W → C in LGMDR2; unknown pathological significance. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024860 | 959 | R → W in MMD1 and LGMDR2. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024862 | 1038 | R → Q in LGMDR2. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024865 | 1208 | I → M in LGMDR2; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057860 | 1228 | L → P in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_012309 | 1298 | I → V in MMD1 and LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024868 | 1335 | E → K in MMD1 and LGMDR2. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057862 | 1341 | L → P in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057864 | 1505 | Y → C in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057865 | 1526 | K → T in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057866 | 1543 | G → D in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057872 | 1734 | E → G in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057873 | 1768 | R → W in LGMDR2 and proximodistal myopathy; unknown pathological significance. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057880 | 1970 | P → S in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 |
Miyoshi muscular dystrophy 1 (MMD1)16 PublicationsManual assertion based on experiment ini
- Ref.1"Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy."
Liu J., Aoki M., Illa I., Wu C., Fardeau M., Angelini C., Serrano C., Urtizberea J.A., Hentati F., Hamida M.B., Bohlega S., Culper E.J., Amato A.A., Bossie K., Oeltjen J., Bejaoui K., McKenna-Yasek D., Hosler B.A. , Schurr E., Arahata K., de Jong P.J., Brown R.H. Jr.
Nat. Genet. 20:31-36(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MMD1 VAL-1298; ARG-1857 AND CYS-2042, VARIANTS LGMDR2 VAL-1298 AND CYS-2042. - Ref.12"Identical mutation in patients with limb girdle muscular dystrophy type 2B or Miyoshi myopathy suggests a role for modifier gene(s)."
Weiler T., Bashir R., Anderson L.V.B., Davison K., Moss J.A., Britton S., Nylen E., Keers S., Vafiadaki E., Greenberg C.R., Bushby K.M.D., Wrogemann K.
Hum. Mol. Genet. 8:871-877(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, VARIANT MMD1 ARG-791, VARIANT LGMDR2 ARG-791. - Ref.15"Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains."
Davis D.B., Doherty K.R., Delmonte A.J., McNally E.M.
J. Biol. Chem. 277:22883-22888(2002) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT MMD1 ASP-67. - Ref.28"Molecular genetic analysis of dysferlin in Japanese patients with Miyoshi myopathy."
Matsumura T., Aoki M., Nagano A., Hayashi Y.K., Asada C., Ogawa M., Yamanaka G., Goto K., Nakagawa M., Oka H., Sahashi K., Kouhara N., Saito Y., Brown R.H. Jr., Nonaka I., Arahata K.
Proc. Jpn. Acad. 75B:207-212(1999)Cited for: VARIANT MMD1 CYS-999. - Ref.29"Identical dysferlin mutation in limb-girdle muscular dystrophy type 2B and distal myopathy."
Illarioshkin S.N., Ivanova-Smolenskaya I.A., Greenberg C.R., Nylen E., Sukhorukov V.S., Poleshchuk V.V., Markova E.D., Wrogemann K.
Neurology 55:1931-1933(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT MMD1 ASP-67, VARIANT LGMDR2 ASP-67. - Ref.30"Genomic organization of the dysferlin gene and novel mutations in Miyoshi myopathy."
Aoki M., Liu J., Richard I., Bashir R., Britton S., Keers S.M., Oeltjen J., Brown H.E.V., Marchand S., Bourg N., Beley C., McKenna-Yasek D., Arahata K., Bohlega S., Cupler E., Illa I., Majneh I., Barohn R.J. , Urtizberea J.A., Fardeau M., Amato A., Angelini C., Bushby K., Beckmann J.S., Brown R.H. Jr.
Neurology 57:271-278(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MMD1 HIS-1046 AND GLN-2000. - Ref.31"Dysferlin mutations in Japanese Miyoshi myopathy: relationship to phenotype."
Takahashi T., Aoki M., Tateyama M., Kondo E., Mizuno T., Onodera Y., Takano R., Kawai H., Kamakura K., Mochizuki H., Shizuka-Ikeda M., Nakagawa M., Yoshida Y., Akanuma J., Hoshino K., Saito H., Nishizawa M., Kato S. , Saito K., Miyachi T., Yamashita H., Kawai M., Matsumura T., Kuzuhara S., Ibi T., Sahashi K., Nakai H., Kohnosu T., Nonaka I., Arahata K., Brown R.H. Jr., Saito H., Itoyama Y.
Neurology 60:1799-1804(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MMD1 CYS-999 AND GLU-1679, VARIANT HIS-1581. - Ref.33"Phenotypic features and genetic findings in 2 Chinese families with Miyoshi distal myopathy."
Ro L.-S., Lee-Chen G.-J., Lin T.-C., Wu Y.-R., Chen C.-M., Lin C.-Y., Chen S.-T.
Arch. Neurol. 61:1594-1599(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MMD1 VAL-426 AND LEU-2068. - Ref.34"Dysferlin mutation analysis in a group of Italian patients with limb-girdle muscular dystrophy and Miyoshi myopathy."
Kawabe K., Goto K., Nishino I., Angelini C., Hayashi Y.K.
Eur. J. Neurol. 11:657-661(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MMD1 ARG-618; CYS-1041; LYS-1335; ARG-1361 AND ARG-1662, VARIANTS LGMDR2 LYS-1335 AND CYS-1505, VARIANTS GLN-1022 AND ALA-GLU-1065 INS. - Ref.35"Novel dysferlin mutations and characteristic muscle atrophy in late-onset Miyoshi myopathy."
Suzuki N., Aoki M., Takahashi T., Takano D., Asano M., Shiga Y., Onodera Y., Tateyama M., Itoyama Y.
Muscle Nerve 29:721-723(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MMD1 ASP-1842 AND PRO-1922. - Ref.36"Identification of a dysferlin gene mutation in a Korean case with Miyoshi myopathy."
Oh S.-H., Kim T.-S., Choi Y.-C.
Yonsei Med. J. 45:927-930(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT MMD1 GLN-389. - Ref.37"Dysferlin mutations in LGMD2B, Miyoshi myopathy, and atypical dysferlinopathies."
Nguyen K., Bassez G., Bernard R., Krahn M., Labelle V., Figarella-Branger D., Pouget J., Hammouda el H., Beroud C., Urtizberea A., Eymard B., Leturcq F., Ben-Yaou R., Levy N.
Hum. Mutat. 26:165-165(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLU-170 AND TRP-253, VARIANTS LGMDR2 TRP-555 AND MET-1208, VARIANTS MMD1 GLU-299; TRP-456; TRP-555; HIS-1046 AND GLN-1693, VARIANT PROXIMODISTAL MYOPATHY VAL-1276, VARIANT PSEUDOMETABOLIC MYOPATHY PRO-266, VARIANTS VAL-189; LEU-1331; SER-1351 AND VAL-1748. - Ref.39"Mutation finding in patients with dysferlin deficiency and role of the dysferlin interacting proteins annexin A1 and A2 in muscular dystrophies."
Cagliani R., Magri F., Toscano A., Merlini L., Fortunato F., Lamperti C., Rodolico C., Prelle A., Sironi M., Aguennouz M., Ciscato P., Uncini A., Moggio M., Bresolin N., Comi G.P.
Hum. Mutat. 26:283-283(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS MMD1 TRP-959; TRP-1693; ASN-1837 AND GLY-1942 AND CYS-2042, VARIANTS LGMDR2 ARG-621; TRP-959; GLN-1038; LYS-1335 AND CYS-2042, VARIANTS GLU-170; LEU-374 AND SER-1678. - Ref.43"Symptomatic dysferlin gene mutation carriers: characterization of two cases."
Illa I., De Luna N., Dominguez-Perles R., Rojas-Garcia R., Paradas C., Palmer J., Marquez C., Gallano P., Gallardo E.
Neurology 68:1284-1289(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LGMDR2 TYR-625 AND GLY-1734, VARIANT MMD1 ARG-519. - Ref.44"Dysferlin-deficient muscular dystrophy features amyloidosis."
Spuler S., Carl M., Zabojszcza J., Straub V., Bushby K., Moore S.A., Baehring S., Wenzel K., Vinkemeier U., Rocken C.
Ann. Neurol. 63:323-328(2008) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LGMDR2 ARG-299, VARIANT MMD1 TRP-299. - Ref.45"Analysis of the DYSF mutational spectrum in a large cohort of patients."
Krahn M., Beroud C., Labelle V., Nguyen K., Bernard R., Bassez G., Figarella-Branger D., Fernandez C., Bouvenot J., Richard I., Ollagnon-Roman E., Bevilacqua J.A., Salvo E., Attarian S., Chapon F., Pellissier J.-F., Pouget J., Hammouda el H. , Laforet P., Urtizberea J.A., Eymard B., Leturcq F., Levy N.
Hum. Mutat. 30:E345-E375(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LGMDR2 ARG-52; ARG-155; GLU-234; THR-284; TRP-555; ARG-618; ARG-731; CYS-930; PRO-1228; THR-1526; ASP-1543; TRP-1768; SER-1970 AND CYS-2042, VARIANTS MMD1 GLU-299; 386-PHE--ASP-390 DELINS TYR; ARG-426; TRP-456; TRP-555; LEU-1029; HIS-1046; HIS-1046; GLN-1693; 1938-THR-ALA-1939 DEL AND CYS-2042, VARIANTS GLU-170; TRP-253 AND TRP-555, VARIANTS PROXIMODISTAL MYOPATHY ARG-299; ARG-340; VAL-1748; TRP-1768 AND CYS-2042, VARIANT PSEUDOMETABOLIC MYOPATHY PRO-266, VARIANTS VAL-84; VAL-189; ALA-335; LEU-374; ASN-390; GLN-819; GLN-1022; GLN-1038; VAL-1276; VAL-1325; ASN-1837 AND SER-1967.
Liu J., Aoki M., Illa I., Wu C., Fardeau M., Angelini C., Serrano C., Urtizberea J.A., Hentati F., Hamida M.B., Bohlega S., Culper E.J., Amato A.A., Bossie K., Oeltjen J., Bejaoui K., McKenna-Yasek D., Hosler B.A. , Schurr E., Arahata K., de Jong P.J., Brown R.H. Jr.
Nat. Genet. 20:31-36(1998) [PubMed] [Europe PMC] [Abstract]
Weiler T., Bashir R., Anderson L.V.B., Davison K., Moss J.A., Britton S., Nylen E., Keers S., Vafiadaki E., Greenberg C.R., Bushby K.M.D., Wrogemann K.
Hum. Mol. Genet. 8:871-877(1999) [PubMed] [Europe PMC] [Abstract]
Davis D.B., Doherty K.R., Delmonte A.J., McNally E.M.
J. Biol. Chem. 277:22883-22888(2002) [PubMed] [Europe PMC] [Abstract]
Matsumura T., Aoki M., Nagano A., Hayashi Y.K., Asada C., Ogawa M., Yamanaka G., Goto K., Nakagawa M., Oka H., Sahashi K., Kouhara N., Saito Y., Brown R.H. Jr., Nonaka I., Arahata K.
Proc. Jpn. Acad. 75B:207-212(1999)
Illarioshkin S.N., Ivanova-Smolenskaya I.A., Greenberg C.R., Nylen E., Sukhorukov V.S., Poleshchuk V.V., Markova E.D., Wrogemann K.
Neurology 55:1931-1933(2000) [PubMed] [Europe PMC] [Abstract]
Aoki M., Liu J., Richard I., Bashir R., Britton S., Keers S.M., Oeltjen J., Brown H.E.V., Marchand S., Bourg N., Beley C., McKenna-Yasek D., Arahata K., Bohlega S., Cupler E., Illa I., Majneh I., Barohn R.J. , Urtizberea J.A., Fardeau M., Amato A., Angelini C., Bushby K., Beckmann J.S., Brown R.H. Jr.
Neurology 57:271-278(2001) [PubMed] [Europe PMC] [Abstract]
Takahashi T., Aoki M., Tateyama M., Kondo E., Mizuno T., Onodera Y., Takano R., Kawai H., Kamakura K., Mochizuki H., Shizuka-Ikeda M., Nakagawa M., Yoshida Y., Akanuma J., Hoshino K., Saito H., Nishizawa M., Kato S. , Saito K., Miyachi T., Yamashita H., Kawai M., Matsumura T., Kuzuhara S., Ibi T., Sahashi K., Nakai H., Kohnosu T., Nonaka I., Arahata K., Brown R.H. Jr., Saito H., Itoyama Y.
Neurology 60:1799-1804(2003) [PubMed] [Europe PMC] [Abstract]
Ro L.-S., Lee-Chen G.-J., Lin T.-C., Wu Y.-R., Chen C.-M., Lin C.-Y., Chen S.-T.
Arch. Neurol. 61:1594-1599(2004) [PubMed] [Europe PMC] [Abstract]
Kawabe K., Goto K., Nishino I., Angelini C., Hayashi Y.K.
Eur. J. Neurol. 11:657-661(2004) [PubMed] [Europe PMC] [Abstract]
Suzuki N., Aoki M., Takahashi T., Takano D., Asano M., Shiga Y., Onodera Y., Tateyama M., Itoyama Y.
Muscle Nerve 29:721-723(2004) [PubMed] [Europe PMC] [Abstract]
Oh S.-H., Kim T.-S., Choi Y.-C.
Yonsei Med. J. 45:927-930(2004) [PubMed] [Europe PMC] [Abstract]
Nguyen K., Bassez G., Bernard R., Krahn M., Labelle V., Figarella-Branger D., Pouget J., Hammouda el H., Beroud C., Urtizberea A., Eymard B., Leturcq F., Ben-Yaou R., Levy N.
Hum. Mutat. 26:165-165(2005) [PubMed] [Europe PMC] [Abstract]
Cagliani R., Magri F., Toscano A., Merlini L., Fortunato F., Lamperti C., Rodolico C., Prelle A., Sironi M., Aguennouz M., Ciscato P., Uncini A., Moggio M., Bresolin N., Comi G.P.
Hum. Mutat. 26:283-283(2005) [PubMed] [Europe PMC] [Abstract]
Illa I., De Luna N., Dominguez-Perles R., Rojas-Garcia R., Paradas C., Palmer J., Marquez C., Gallano P., Gallardo E.
Neurology 68:1284-1289(2007) [PubMed] [Europe PMC] [Abstract]
Spuler S., Carl M., Zabojszcza J., Straub V., Bushby K., Moore S.A., Baehring S., Wenzel K., Vinkemeier U., Rocken C.
Ann. Neurol. 63:323-328(2008) [PubMed] [Europe PMC] [Abstract]
Krahn M., Beroud C., Labelle V., Nguyen K., Bernard R., Bassez G., Figarella-Branger D., Fernandez C., Bouvenot J., Richard I., Ollagnon-Roman E., Bevilacqua J.A., Salvo E., Attarian S., Chapon F., Pellissier J.-F., Pouget J., Hammouda el H. , Laforet P., Urtizberea J.A., Eymard B., Leturcq F., Levy N.
Hum. Mutat. 30:E345-E375(2009) [PubMed] [Europe PMC] [Abstract]
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_057835 | 67 | V → D in MMD1 and LGMDR2; Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024857 | 299 | G → E in MMD1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057841 | 299 | G → W in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057845 | 386 – 390 | FRAED → Y in MMD1. 1 Publication Manual assertion based on experiment ini
| 5 | |
Natural variantiVAR_057846 | 389 | E → Q in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057848 | 426 | G → R in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057849 | 426 | G → V in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024858 | 456 | C → W in MMD1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057850 | 519 | G → R in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024859 | 555 | R → W in LGMDR2 and MMD1; also found in patients with isolated hyperCKemia. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057851 | 618 | G → R in MMD1 and LGMDR2. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_012308 | 791 | P → R in MMD1 and LGMDR2. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024860 | 959 | R → W in MMD1 and LGMDR2. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057857 | 999 | W → C in MMD1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057858 | 1029 | P → L in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057859 | 1041 | R → C in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024863 | 1046 | R → H in MMD1; dbNP:28939700. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_012309 | 1298 | I → V in MMD1 and LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024868 | 1335 | E → K in MMD1 and LGMDR2. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057863 | 1361 | C → R in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057868 | 1662 | T → R in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057870 | 1679 | G → E in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024870 | 1693 | R → Q in MMD1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057871 | 1693 | R → W in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057874 | 1837 | D → N in MMD1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057875 | 1842 | G → D in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_012310 | 1857 | H → R in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057876 | 1922 | L → P in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057877 | 1938 – 1939 | Missing in MMD1. 1 Publication Manual assertion based on experiment ini
| 2 | |
Natural variantiVAR_057878 | 1942 | C → G in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024872 | 2000 | R → Q in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_012311 | 2042 | R → C in MMD1, LGMDR2 and proximodistal myopathy. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057881 | 2068 | P → L in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 |
Distal myopathy with anterior tibial onset (DMAT)1 PublicationManual assertion based on experiment ini
- Ref.13"Distal anterior compartment myopathy: a dysferlin mutation causing a new muscular dystrophy phenotype."
Illa I., Serrano-Munuera C., Gallardo E., Lasa A., Rojas-Garcia R., Palmer J., Gallano P., Baiget M., Matsuda C., Brown R.H.
Ann. Neurol. 49:130-134(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN DMAT.
Illa I., Serrano-Munuera C., Gallardo E., Lasa A., Rojas-Garcia R., Palmer J., Gallano P., Baiget M., Matsuda C., Brown R.H.
Ann. Neurol. 49:130-134(2001) [PubMed] [Europe PMC] [Abstract]
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 16 | D → A: Fails to bind calcium. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 21 | D → A: Fails to bind calcium. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 71 | D → A: Fails to bind calcium. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 79 | R → D: Moderately increased calcium affinity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 80 | F → A: Reduced calcium affinity. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease variant, Limb-girdle muscular dystrophyOrganism-specific databases
DisGeNET More...DisGeNETi | 8291 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | DYSF |
MalaCards human disease database More...MalaCardsi | DYSF |
MIMi | 253601, phenotype 254130, phenotype 606768, phenotype |
Open Targets More...OpenTargetsi | ENSG00000135636 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 199329, Congenital myopathy, Paradas type 178400, Distal myopathy with anterior tibial onset 268, Dysferlin-related limb-girdle muscular dystrophy R2 45448, Miyoshi myopathy |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27554 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | O75923, Tbio |
Genetic variation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | DYSF |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000057879 | 1 – 2080 | DysferlinAdd BLAST | 2080 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
---|---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 166 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Isoform 2 (identifier: O75923-2) | |||||
Modified residuei | 166 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Modified residuei | 197 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Isoform 5 (identifier: O75923-5) | |||||
Modified residuei | 166 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Modified residuei | 197 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Isoform 7 (identifier: O75923-7) | |||||
Modified residuei | 166 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Modified residuei | 197 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Isoform 8 (identifier: O75923-8) | |||||
Modified residuei | 167 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Modified residuei | 198 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Isoform 11 (identifier: O75923-11) | |||||
Modified residuei | 167 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Modified residuei | 198 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Isoform 13 (identifier: O75923-13) | |||||
Modified residuei | 167 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
Modified residuei | 198 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O75923 |
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | O75923 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | O75923 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O75923 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O75923 |
PeptideAtlas More...PeptideAtlasi | O75923 |
PRoteomics IDEntifications database More...PRIDEi | O75923 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 50278 [O75923-1] 50279 [O75923-10] 50280 [O75923-11] 50281 [O75923-12] 50282 [O75923-13] 50283 [O75923-14] 50284 [O75923-15] 50285 [O75923-2] 50286 [O75923-3] 50287 [O75923-4] 50288 [O75923-5] 50289 [O75923-6] 50290 [O75923-7] 50291 [O75923-8] 50292 [O75923-9] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O75923 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O75923 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Manual assertion based on experiment ini
- Ref.2"Identification and characterization of a novel human dysferlin transcript: dysferlin_v1."
Pramono Z.A.D., Lai P.S., Tan C.L., Takeda S., Yee W.C.
Hum. Genet. 120:410-419(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14), TISSUE SPECIFICITY. - Ref.9"Dysferlin is a plasma membrane protein and is expressed early in human development."
Anderson L.V.B., Davison K., Moss J.A., Young C., Cullen M.J., Walsh J., Johnson M.A., Bashir R., Britton S., Keers S., Argov Z., Mahjneh I., Fougerousse F., Beckmann J.S., Bushby K.M.D.
Hum. Mol. Genet. 8:855-861(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY. - Ref.14"The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle."
Matsuda C., Hayashi Y.K., Ogawa M., Aoki M., Murayama K., Nishino I., Nonaka I., Arahata K., Brown R.H. Jr.
Hum. Mol. Genet. 10:1761-1766(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CAV3, TISSUE SPECIFICITY. - Ref.15"Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains."
Davis D.B., Doherty K.R., Delmonte A.J., McNally E.M.
J. Biol. Chem. 277:22883-22888(2002) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT MMD1 ASP-67. - Ref.16"Developmental and tissue-specific regulation of a novel dysferlin isoform."
Salani S., Lucchiari S., Fortunato F., Crimi M., Corti S., Locatelli F., Bossolasco P., Bresolin N., Comi G.P.
Muscle Nerve 30:366-374(2004) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY. - Ref.18"Dysferlin is expressed in human placenta but does not associate with caveolin."
Vandre D.D., Ackerman W.E., Kniss D.A., Tewari A.K., Mori M., Takizawa T., Robinson J.M.
Biol. Reprod. 77:533-542(2007) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.19"AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration."
Huang Y., Laval S.H., van Remoortere A., Baudier J., Benaud C., Anderson L.V., Straub V., Deelder A., Frants R.R., den Dunnen J.T., Bushby K., van der Maarel S.M.
FASEB J. 21:732-742(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AHNAK AND AHNAK2, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT LGMDR2 ASP-67, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.20"From T-tubule to sarcolemma: damage-induced dysferlin translocation in early myogenesis."
Klinge L., Laval S., Keers S., Haldane F., Straub V., Barresi R., Bushby K.
FASEB J. 21:1768-1776(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.27"Alternate splicing of dysferlin C2A confers Ca(2+)-dependent and Ca(2+)-independent binding for membrane repair."
Fuson K., Rice A., Mahling R., Snow A., Nayak K., Shanbhogue P., Meyer A.G., Redpath G.M., Hinderliter A., Cooper S.T., Sutton R.B.
Structure 22:104-115(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 1-124 IN COMPLEX WITH CALCIUM, CALCIUM-BINDING (ISOFORMS 1 AND 14), SUBCELLULAR LOCATION, DOMAIN, LIPID-BINDING, TISSUE SPECIFICITY.
<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei
Manual assertion based on experiment ini
- Ref.9"Dysferlin is a plasma membrane protein and is expressed early in human development."
Anderson L.V.B., Davison K., Moss J.A., Young C., Cullen M.J., Walsh J., Johnson M.A., Bashir R., Britton S., Keers S., Argov Z., Mahjneh I., Fougerousse F., Beckmann J.S., Bushby K.M.D.
Hum. Mol. Genet. 8:855-861(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000135636, Expressed in blood and 232 other tissues |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O75923, HS |
Organism-specific databases
Human Protein Atlas More...HPAi | ENSG00000135636, Tissue enhanced (placenta, skeletal muscle) |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Interacts with CACNA1S.
Interacts with ANXA1; the interaction is Ca2+- and injury state-dependent.
Interacts with ANXA2; the interaction is Ca2+- and injury state-dependent.
Interacts with CACNA1S and PARVB.
Interacts with TRIM72/MG53; interaction is required for transport to sites of cell injury during repair patch formation (By similarity).
Interacts with RIPOR2; this interaction occurs during early myogenic differentiation (PubMed:24687993).
Interacts with CAV3 and PARVB.
Interacts with AHNAK; the interaction is direct and Ca2+-independent.
Interacts with AHNAK2; the interaction is direct and Ca2+-independent.
By similarity5 PublicationsManual assertion based on experiment ini
- Ref.14"The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle."
Matsuda C., Hayashi Y.K., Ogawa M., Aoki M., Murayama K., Nishino I., Nonaka I., Arahata K., Brown R.H. Jr.
Hum. Mol. Genet. 10:1761-1766(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CAV3, TISSUE SPECIFICITY. - Ref.17"Dysferlin interacts with affixin (beta-parvin) at the sarcolemma."
Matsuda C., Kameyama K., Tagawa K., Ogawa M., Suzuki A., Yamaji S., Okamoto H., Nishino I., Hayashi Y.K.
J. Neuropathol. Exp. Neurol. 64:334-340(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PARVB, SUBCELLULAR LOCATION. - Ref.19"AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration."
Huang Y., Laval S.H., van Remoortere A., Baudier J., Benaud C., Anderson L.V., Straub V., Deelder A., Frants R.R., den Dunnen J.T., Bushby K., van der Maarel S.M.
FASEB J. 21:732-742(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AHNAK AND AHNAK2, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT LGMDR2 ASP-67, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.24"Fam65b is important for formation of the HDAC6-dysferlin protein complex during myogenic cell differentiation."
Balasubramanian A., Kawahara G., Gupta V.A., Rozkalne A., Beauvais A., Kunkel L.M., Gussoni E.
FASEB J. 28:2955-2969(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RIPOR2. - Ref.27"Alternate splicing of dysferlin C2A confers Ca(2+)-dependent and Ca(2+)-independent binding for membrane repair."
Fuson K., Rice A., Mahling R., Snow A., Nayak K., Shanbhogue P., Meyer A.G., Redpath G.M., Hinderliter A., Cooper S.T., Sutton R.B.
Structure 22:104-115(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 1-124 IN COMPLEX WITH CALCIUM, CALCIUM-BINDING (ISOFORMS 1 AND 14), SUBCELLULAR LOCATION, DOMAIN, LIPID-BINDING, TISSUE SPECIFICITY.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
Show more detailsHide detailsO75923
Isoform 13 [O75923-13]
With | #Exp. | IntAct |
---|---|---|
PLP1 - isoform DM-20 [P60201-2] | 3 | EBI-19949386,EBI-12188331 |
GO - Molecular functioni
- alpha-tubulin binding Source: Ensembl
- microtubule binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 113896, 11 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O75923 |
Protein interaction database and analysis system More...IntActi | O75923, 52 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000386881 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | O75923, protein |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1 – 11 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Beta strandi | 22 – 28 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 31 – 34 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 45 – 53 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 64 – 71 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 74 – 76 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 79 – 87 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 89 – 92 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 98 – 106 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 112 – 123 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Beta strandi | 946 – 958 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
Beta strandi | 966 – 973 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 983 – 985 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 996 – 998 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 1000 – 1002 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 1011 – 1015 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 1021 – 1023 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 1028 – 1030 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 1037 – 1049 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O75923 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 1 – 101 | C2 1PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 101 | |
Domaini | 203 – 321 | C2 2PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 119 | |
Domaini | 360 – 496 | C2 3PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 137 | |
Domaini | 1136 – 1262 | C2 4PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 127 | |
Domaini | 1310 – 1438 | C2 5PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 129 | |
Domaini | 1561 – 1679 | C2 6PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 119 | |
Domaini | 1795 – 1943 | C2 7PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 149 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 1038 – 1097 | Arg-richAdd BLAST | 60 |
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
Manual assertion based on experiment ini
- Ref.23"Quantitation of the calcium and membrane binding properties of the c2 domains of dysferlin."
Abdullah N., Padmanarayana M., Marty N.J., Johnson C.P.
Biophys. J. 106:382-389(2014) [PubMed] [Europe PMC] [Abstract]Cited for: DOMAIN C2, CALCIUM-BINDING, MUTAGENESIS OF ASP-16; ASP-21; ASP-71; ARG-79 AND PHE-80. - Ref.27"Alternate splicing of dysferlin C2A confers Ca(2+)-dependent and Ca(2+)-independent binding for membrane repair."
Fuson K., Rice A., Mahling R., Snow A., Nayak K., Shanbhogue P., Meyer A.G., Redpath G.M., Hinderliter A., Cooper S.T., Sutton R.B.
Structure 22:104-115(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 1-124 IN COMPLEX WITH CALCIUM, CALCIUM-BINDING (ISOFORMS 1 AND 14), SUBCELLULAR LOCATION, DOMAIN, LIPID-BINDING, TISSUE SPECIFICITY.
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Keywords - Domaini
Repeat, Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1326, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT00940000156187 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_001183_2_1_1 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O75923 |
Identification of Orthologs from Complete Genome Data More...OMAi | WEEVEWS |
Database of Orthologous Groups More...OrthoDBi | 20162at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | O75923 |
TreeFam database of animal gene trees More...TreeFami | TF316871 |
Family and domain databases
Conserved Domains Database More...CDDi | cd08373, C2A_Ferlin, 1 hit cd04011, C2B_Ferlin, 1 hit cd04018, C2C_Ferlin, 1 hit cd04017, C2D_Ferlin, 1 hit cd04037, C2E_Ferlin, 1 hit cd08374, C2F_Ferlin, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.150, 6 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000008, C2_dom IPR035892, C2_domain_sf IPR037726, C2A_Ferlin IPR037720, C2B_Ferlin IPR037722, C2C_Ferlin IPR037723, C2D_Ferlin IPR037724, C2E_Ferlin IPR037725, C2F_Ferlin IPR029998, Dysferlin IPR012968, FerIin_dom IPR037721, Ferlin IPR012560, Ferlin_A-domain IPR012561, Ferlin_B-domain IPR032362, Ferlin_C IPR006614, Peroxin/Ferlin |
The PANTHER Classification System More...PANTHERi | PTHR12546, PTHR12546, 1 hit PTHR12546:SF44, PTHR12546:SF44, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00168, C2, 7 hits PF08165, FerA, 1 hit PF08150, FerB, 1 hit PF08151, FerI, 1 hit PF16165, Ferlin_C, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00239, C2, 7 hits SM00694, DysFC, 2 hits SM00693, DysFN, 2 hits SM01200, FerA, 1 hit SM01201, FerB, 1 hit SM01202, FerI, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50004, C2, 7 hits |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (15)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 15 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basketAdded to basketThis isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MLRVFILYAE NVHTPDTDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF
60 70 80 90 100
EWDLKGIPLD QGSELHVVVK DHETMGRNRF LGEAKVPLRE VLATPSLSAS
110 120 130 140 150
FNAPLLDTKK QPTGASLVLQ VSYTPLPGAV PLFPPPTPLE PSPTLPDLDV
160 170 180 190 200
VADTGGEEDT EDQGLTGDEA EPFLDQSGGP GAPTTPRKLP SRPPPHYPGI
210 220 230 240 250
KRKRSAPTSR KLLSDKPQDF QIRVQVIEGR QLPGVNIKPV VKVTAAGQTK
260 270 280 290 300
RTRIHKGNSP LFNETLFFNL FDSPGELFDE PIFITVVDSR SLRTDALLGE
310 320 330 340 350
FRMDVGTIYR EPRHAYLRKW LLLSDPDDFS AGARGYLKTS LCVLGPGDEA
360 370 380 390 400
PLERKDPSED KEDIESNLLR PTGVALRGAH FCLKVFRAED LPQMDDAVMD
410 420 430 440 450
NVKQIFGFES NKKNLVDPFV EVSFAGKMLC SKILEKTANP QWNQNITLPA
460 470 480 490 500
MFPSMCEKMR IRIIDWDRLT HNDIVATTYL SMSKISAPGG EIEEEPAGAV
510 520 530 540 550
KPSKASDLDD YLGFLPTFGP CYINLYGSPR EFTGFPDPYT ELNTGKGEGV
560 570 580 590 600
AYRGRLLLSL ETKLVEHSEQ KVEDLPADDI LRVEKYLRRR KYSLFAAFYS
610 620 630 640 650
ATMLQDVDDA IQFEVSIGNY GNKFDMTCLP LASTTQYSRA VFDGCHYYYL
660 670 680 690 700
PWGNVKPVVV LSSYWEDISH RIETQNQLLG IADRLEAGLE QVHLALKAQC
710 720 730 740 750
STEDVDSLVA QLTDELIAGC SQPLGDIHET PSATHLDQYL YQLRTHHLSQ
760 770 780 790 800
ITEAALALKL GHSELPAALE QAEDWLLRLR ALAEEPQNSL PDIVIWMLQG
810 820 830 840 850
DKRVAYQRVP AHQVLFSRRG ANYCGKNCGK LQTIFLKYPM EKVPGARMPV
860 870 880 890 900
QIRVKLWFGL SVDEKEFNQF AEGKLSVFAE TYENETKLAL VGNWGTTGLT
910 920 930 940 950
YPKFSDVTGK IKLPKDSFRP SAGWTWAGDW FVCPEKTLLH DMDAGHLSFV
960 970 980 990 1000
EEVFENQTRL PGGQWIYMSD NYTDVNGEKV LPKDDIECPL GWKWEDEEWS
1010 1020 1030 1040 1050
TDLNRAVDEQ GWEYSITIPP ERKPKHWVPA EKMYYTHRRR RWVRLRRRDL
1060 1070 1080 1090 1100
SQMEALKRHR QAEAEGEGWE YASLFGWKFH LEYRKTDAFR RRRWRRRMEP
1110 1120 1130 1140 1150
LEKTGPAAVF ALEGALGGVM DDKSEDSMSV STLSFGVNRP TISCIFDYGN
1160 1170 1180 1190 1200
RYHLRCYMYQ ARDLAAMDKD SFSDPYAIVS FLHQSQKTVV VKNTLNPTWD
1210 1220 1230 1240 1250
QTLIFYEIEI FGEPATVAEQ PPSIVVELYD HDTYGADEFM GRCICQPSLE
1260 1270 1280 1290 1300
RMPRLAWFPL TRGSQPSGEL LASFELIQRE KPAIHHIPGF EVQETSRILD
1310 1320 1330 1340 1350
ESEDTDLPYP PPQREANIYM VPQNIKPALQ RTAIEILAWG LRNMKSYQLA
1360 1370 1380 1390 1400
NISSPSLVVE CGGQTVQSCV IRNLRKNPNF DICTLFMEVM LPREELYCPP
1410 1420 1430 1440 1450
ITVKVIDNRQ FGRRPVVGQC TIRSLESFLC DPYSAESPSP QGGPDDVSLL
1460 1470 1480 1490 1500
SPGEDVLIDI DDKEPLIPIQ EEEFIDWWSK FFASIGEREK CGSYLEKDFD
1510 1520 1530 1540 1550
TLKVYDTQLE NVEAFEGLSD FCNTFKLYRG KTQEETEDPS VIGEFKGLFK
1560 1570 1580 1590 1600
IYPLPEDPAI PMPPRQFHQL AAQGPQECLV RIYIVRAFGL QPKDPNGKCD
1610 1620 1630 1640 1650
PYIKISIGKK SVSDQDNYIP CTLEPVFGKM FELTCTLPLE KDLKITLYDY
1660 1670 1680 1690 1700
DLLSKDEKIG ETVVDLENRL LSKFGARCGL PQTYCVSGPN QWRDQLRPSQ
1710 1720 1730 1740 1750
LLHLFCQQHR VKAPVYRTDR VMFQDKEYSI EEIEAGRIPN PHLGPVEERL
1760 1770 1780 1790 1800
ALHVLQQQGL VPEHVESRPL YSPLQPDIEQ GKLQMWVDLF PKALGRPGPP
1810 1820 1830 1840 1850
FNITPRRARR FFLRCIIWNT RDVILDDLSL TGEKMSDIYV KGWMIGFEEH
1860 1870 1880 1890 1900
KQKTDVHYRS LGGEGNFNWR FIFPFDYLPA EQVCTIAKKD AFWRLDKTES
1910 1920 1930 1940 1950
KIPARVVFQI WDNDKFSFDD FLGSLQLDLN RMPKPAKTAK KCSLDQLDDA
1960 1970 1980 1990 2000
FHPEWFVSLF EQKTVKGWWP CVAEEGEKKI LAGKLEMTLE IVAESEHEER
2010 2020 2030 2040 2050
PAGQGRDEPN MNPKLEDPRR PDTSFLWFTS PYKTMKFILW RRFRWAIILF
2060 2070 2080
IILFILLLFL AIFIYAFPNY AAMKLVKPFS
The sequence of this isoform differs from the canonical sequence as follows:
152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT
10 20 30 40 50
MLRVFILYAE NVHTPDTDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF
60 70 80 90 100
EWDLKGIPLD QGSELHVVVK DHETMGRNRF LGEAKVPLRE VLATPSLSAS
110 120 130 140 150
FNAPLLDTKK QPTGASLVLQ VSYTPLPGAV PLFPPPTPLE PSPTLPDLDV
160 170 180 190 200
VAGGGQSRAE TWSLLSDSTM DTRYSGKKWP APTDTGGEED TEDQGLTGDE
210 220 230 240 250
AEPFLDQSGG PGAPTTPRKL PSRPPPHYPG IKRKRSAPTS RKLLSDKPQD
260 270 280 290 300
FQIRVQVIEG RQLPGVNIKP VVKVTAAGQT KRTRIHKGNS PLFNETLFFN
310 320 330 340 350
LFDSPGELFD EPIFITVVDS RSLRTDALLG EFRMDVGTIY REPRHAYLRK
360 370 380 390 400
WLLLSDPDDF SAGARGYLKT SLCVLGPGDE APLERKDPSE DKEDIESNLL
410 420 430 440 450
RPTGVALRGA HFCLKVFRAE DLPQMDDAVM DNVKQIFGFE SNKKNLVDPF
460 470 480 490 500
VEVSFAGKML CSKILEKTAN PQWNQNITLP AMFPSMCEKM RIRIIDWDRL
510 520 530 540 550
THNDIVATTY LSMSKISAPG GEIEEEPAGA VKPSKASDLD DYLGFLPTFG
560 570 580 590 600
PCYINLYGSP REFTGFPDPY TELNTGKGEG VAYRGRLLLS LETKLVEHSE
610 620 630 640 650
QKVEDLPADD ILRVEKYLRR RKYSLFAAFY SATMLQDVDD AIQFEVSIGN
660 670 680 690 700
YGNKFDMTCL PLASTTQYSR AVFDGCHYYY LPWGNVKPVV VLSSYWEDIS
710 720 730 740 750
HRIETQNQLL GIADRLEAGL EQVHLALKAQ CSTEDVDSLV AQLTDELIAG
760 770 780 790 800
CSQPLGDIHE TPSATHLDQY LYQLRTHHLS QITEAALALK LGHSELPAAL
810 820 830 840 850
EQAEDWLLRL RALAEEPQNS LPDIVIWMLQ GDKRVAYQRV PAHQVLFSRR
860 870 880 890 900
GANYCGKNCG KLQTIFLKYP MEKVPGARMP VQIRVKLWFG LSVDEKEFNQ
910 920 930 940 950
FAEGKLSVFA ETYENETKLA LVGNWGTTGL TYPKFSDVTG KIKLPKDSFR
960 970 980 990 1000
PSAGWTWAGD WFVCPEKTLL HDMDAGHLSF VEEVFENQTR LPGGQWIYMS
1010 1020 1030 1040 1050
DNYTDVNGEK VLPKDDIECP LGWKWEDEEW STDLNRAVDE QGWEYSITIP
1060 1070 1080 1090 1100
PERKPKHWVP AEKMYYTHRR RRWVRLRRRD LSQMEALKRH RQAEAEGEGW
1110 1120 1130 1140 1150
EYASLFGWKF HLEYRKTDAF RRRRWRRRME PLEKTGPAAV FALEGALGGV
1160 1170 1180 1190 1200
MDDKSEDSMS VSTLSFGVNR PTISCIFDYG NRYHLRCYMY QARDLAAMDK
1210 1220 1230 1240 1250
DSFSDPYAIV SFLHQSQKTV VVKNTLNPTW DQTLIFYEIE IFGEPATVAE
1260 1270 1280 1290 1300
QPPSIVVELY DHDTYGADEF MGRCICQPSL ERMPRLAWFP LTRGSQPSGE
1310 1320 1330 1340 1350
LLASFELIQR EKPAIHHIPG FEVQETSRIL DESEDTDLPY PPPQREANIY
1360 1370 1380 1390 1400
MVPQNIKPAL QRTAIEILAW GLRNMKSYQL ANISSPSLVV ECGGQTVQSC
1410 1420 1430 1440 1450
VIRNLRKNPN FDICTLFMEV MLPREELYCP PITVKVIDNR QFGRRPVVGQ
1460 1470 1480 1490 1500
CTIRSLESFL CDPYSAESPS PQGGPDDVSL LSPGEDVLID IDDKEPLIPI
1510 1520 1530 1540 1550
QEEEFIDWWS KFFASIGERE KCGSYLEKDF DTLKVYDTQL ENVEAFEGLS
1560 1570 1580 1590 1600
DFCNTFKLYR GKTQEETEDP SVIGEFKGLF KIYPLPEDPA IPMPPRQFHQ
1610 1620 1630 1640 1650
LAAQGPQECL VRIYIVRAFG LQPKDPNGKC DPYIKISIGK KSVSDQDNYI
1660 1670 1680 1690 1700
PCTLEPVFGK MFELTCTLPL EKDLKITLYD YDLLSKDEKI GETVVDLENR
1710 1720 1730 1740 1750
LLSKFGARCG LPQTYCVSGP NQWRDQLRPS QLLHLFCQQH RVKAPVYRTD
1760 1770 1780 1790 1800
RVMFQDKEYS IEEIEAGRIP NPHLGPVEER LALHVLQQQG LVPEHVESRP
1810 1820 1830 1840 1850
LYSPLQPDIE QGKLQMWVDL FPKALGRPGP PFNITPRRAR RFFLRCIIWN
1860 1870 1880 1890 1900
TRDVILDDLS LTGEKMSDIY VKGWMIGFEE HKQKTDVHYR SLGGEGNFNW
1910 1920 1930 1940 1950
RFIFPFDYLP AEQVCTIAKK DAFWRLDKTE SKIPARVVFQ IWDNDKFSFD
1960 1970 1980 1990 2000
DFLGSLQLDL NRMPKPAKTA KKCSLDQLDD AFHPEWFVSL FEQKTVKGWW
2010 2020 2030 2040 2050
PCVAEEGEKK ILAGKLEMTL EIVAESEHEE RPAGQGRDEP NMNPKLEDPR
2060 2070 2080 2090 2100
RPDTSFLWFT SPYKTMKFIL WRRFRWAIIL FIILFILLLF LAIFIYAFPN
2110
YAAMKLVKPF S
The sequence of this isoform differs from the canonical sequence as follows:
494-508: EEPAGAVKPSKASDL → V
10 20 30 40 50
MLRVFILYAE NVHTPDTDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF
60 70 80 90 100
EWDLKGIPLD QGSELHVVVK DHETMGRNRF LGEAKVPLRE VLATPSLSAS
110 120 130 140 150
FNAPLLDTKK QPTGASLVLQ VSYTPLPGAV PLFPPPTPLE PSPTLPDLDV
160 170 180 190 200
VADTGGEEDT EDQGLTGDEA EPFLDQSGGP GAPTTPRKLP SRPPPHYPGI
210 220 230 240 250
KRKRSAPTSR KLLSDKPQDF QIRVQVIEGR QLPGVNIKPV VKVTAAGQTK
260 270 280 290 300
RTRIHKGNSP LFNETLFFNL FDSPGELFDE PIFITVVDSR SLRTDALLGE
310 320 330 340 350
FRMDVGTIYR EPRHAYLRKW LLLSDPDDFS AGARGYLKTS LCVLGPGDEA
360 370 380 390 400
PLERKDPSED KEDIESNLLR PTGVALRGAH FCLKVFRAED LPQMDDAVMD
410 420 430 440 450
NVKQIFGFES NKKNLVDPFV EVSFAGKMLC SKILEKTANP QWNQNITLPA
460 470 480 490 500
MFPSMCEKMR IRIIDWDRLT HNDIVATTYL SMSKISAPGG EIEVDDYLGF
510 520 530 540 550
LPTFGPCYIN LYGSPREFTG FPDPYTELNT GKGEGVAYRG RLLLSLETKL
560 570 580 590 600
VEHSEQKVED LPADDILRVE KYLRRRKYSL FAAFYSATML QDVDDAIQFE
610 620 630 640 650
VSIGNYGNKF DMTCLPLAST TQYSRAVFDG CHYYYLPWGN VKPVVVLSSY
660 670 680 690 700
WEDISHRIET QNQLLGIADR LEAGLEQVHL ALKAQCSTED VDSLVAQLTD
710 720 730 740 750
ELIAGCSQPL GDIHETPSAT HLDQYLYQLR THHLSQITEA ALALKLGHSE
760 770 780 790 800
LPAALEQAED WLLRLRALAE EPQNSLPDIV IWMLQGDKRV AYQRVPAHQV
810 820 830 840 850
LFSRRGANYC GKNCGKLQTI FLKYPMEKVP GARMPVQIRV KLWFGLSVDE
860 870 880 890 900
KEFNQFAEGK LSVFAETYEN ETKLALVGNW GTTGLTYPKF SDVTGKIKLP
910 920 930 940 950
KDSFRPSAGW TWAGDWFVCP EKTLLHDMDA GHLSFVEEVF ENQTRLPGGQ
960 970 980 990 1000
WIYMSDNYTD VNGEKVLPKD DIECPLGWKW EDEEWSTDLN RAVDEQGWEY
1010 1020 1030 1040 1050
SITIPPERKP KHWVPAEKMY YTHRRRRWVR LRRRDLSQME ALKRHRQAEA
1060 1070 1080 1090 1100
EGEGWEYASL FGWKFHLEYR KTDAFRRRRW RRRMEPLEKT GPAAVFALEG
1110 1120 1130 1140 1150
ALGGVMDDKS EDSMSVSTLS FGVNRPTISC IFDYGNRYHL RCYMYQARDL
1160 1170 1180 1190 1200
AAMDKDSFSD PYAIVSFLHQ SQKTVVVKNT LNPTWDQTLI FYEIEIFGEP
1210 1220 1230 1240 1250
ATVAEQPPSI VVELYDHDTY GADEFMGRCI CQPSLERMPR LAWFPLTRGS
1260 1270 1280 1290 1300
QPSGELLASF ELIQREKPAI HHIPGFEVQE TSRILDESED TDLPYPPPQR
1310 1320 1330 1340 1350
EANIYMVPQN IKPALQRTAI EILAWGLRNM KSYQLANISS PSLVVECGGQ
1360 1370 1380 1390 1400
TVQSCVIRNL RKNPNFDICT LFMEVMLPRE ELYCPPITVK VIDNRQFGRR
1410 1420 1430 1440 1450
PVVGQCTIRS LESFLCDPYS AESPSPQGGP DDVSLLSPGE DVLIDIDDKE
1460 1470 1480 1490 1500
PLIPIQEEEF IDWWSKFFAS IGEREKCGSY LEKDFDTLKV YDTQLENVEA
1510 1520 1530 1540 1550
FEGLSDFCNT FKLYRGKTQE ETEDPSVIGE FKGLFKIYPL PEDPAIPMPP
1560 1570 1580 1590 1600
RQFHQLAAQG PQECLVRIYI VRAFGLQPKD PNGKCDPYIK ISIGKKSVSD
1610 1620 1630 1640 1650
QDNYIPCTLE PVFGKMFELT CTLPLEKDLK ITLYDYDLLS KDEKIGETVV
1660 1670 1680 1690 1700
DLENRLLSKF GARCGLPQTY CVSGPNQWRD QLRPSQLLHL FCQQHRVKAP
1710 1720 1730 1740 1750
VYRTDRVMFQ DKEYSIEEIE AGRIPNPHLG PVEERLALHV LQQQGLVPEH
1760 1770 1780 1790 1800
VESRPLYSPL QPDIEQGKLQ MWVDLFPKAL GRPGPPFNIT PRRARRFFLR
1810 1820 1830 1840 1850
CIIWNTRDVI LDDLSLTGEK MSDIYVKGWM IGFEEHKQKT DVHYRSLGGE
1860 1870 1880 1890 1900
GNFNWRFIFP FDYLPAEQVC TIAKKDAFWR LDKTESKIPA RVVFQIWDND
1910 1920 1930 1940 1950
KFSFDDFLGS LQLDLNRMPK PAKTAKKCSL DQLDDAFHPE WFVSLFEQKT
1960 1970 1980 1990 2000
VKGWWPCVAE EGEKKILAGK LEMTLEIVAE SEHEERPAGQ GRDEPNMNPK
2010 2020 2030 2040 2050
LEDPRRPDTS FLWFTSPYKT MKFILWRRFR WAIILFIILF ILLLFLAIFI
2060
YAFPNYAAMK LVKPFS
The sequence of this isoform differs from the canonical sequence as follows:
1470-1470: Q → QLADGLSSLAPTNTASPPSSPH
10 20 30 40 50
MLRVFILYAE NVHTPDTDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF
60 70 80 90 100
EWDLKGIPLD QGSELHVVVK DHETMGRNRF LGEAKVPLRE VLATPSLSAS
110 120 130 140 150
FNAPLLDTKK QPTGASLVLQ VSYTPLPGAV PLFPPPTPLE PSPTLPDLDV
160 170 180 190 200
VADTGGEEDT EDQGLTGDEA EPFLDQSGGP GAPTTPRKLP SRPPPHYPGI
210 220 230 240 250
KRKRSAPTSR KLLSDKPQDF QIRVQVIEGR QLPGVNIKPV VKVTAAGQTK
260 270 280 290 300
RTRIHKGNSP LFNETLFFNL FDSPGELFDE PIFITVVDSR SLRTDALLGE
310 320 330 340 350
FRMDVGTIYR EPRHAYLRKW LLLSDPDDFS AGARGYLKTS LCVLGPGDEA
360 370 380 390 400
PLERKDPSED KEDIESNLLR PTGVALRGAH FCLKVFRAED LPQMDDAVMD
410 420 430 440 450
NVKQIFGFES NKKNLVDPFV EVSFAGKMLC SKILEKTANP QWNQNITLPA
460 470 480 490 500
MFPSMCEKMR IRIIDWDRLT HNDIVATTYL SMSKISAPGG EIEEEPAGAV
510 520 530 540 550
KPSKASDLDD YLGFLPTFGP CYINLYGSPR EFTGFPDPYT ELNTGKGEGV
560 570 580 590 600
AYRGRLLLSL ETKLVEHSEQ KVEDLPADDI LRVEKYLRRR KYSLFAAFYS
610 620 630 640 650
ATMLQDVDDA IQFEVSIGNY GNKFDMTCLP LASTTQYSRA VFDGCHYYYL
660 670 680 690 700
PWGNVKPVVV LSSYWEDISH RIETQNQLLG IADRLEAGLE QVHLALKAQC
710 720 730 740 750
STEDVDSLVA QLTDELIAGC SQPLGDIHET PSATHLDQYL YQLRTHHLSQ
760 770 780 790 800
ITEAALALKL GHSELPAALE QAEDWLLRLR ALAEEPQNSL PDIVIWMLQG
810 820 830 840 850
DKRVAYQRVP AHQVLFSRRG ANYCGKNCGK LQTIFLKYPM EKVPGARMPV
860 870 880 890 900
QIRVKLWFGL SVDEKEFNQF AEGKLSVFAE TYENETKLAL VGNWGTTGLT
910 920 930 940 950
YPKFSDVTGK IKLPKDSFRP SAGWTWAGDW FVCPEKTLLH DMDAGHLSFV
960 970 980 990 1000
EEVFENQTRL PGGQWIYMSD NYTDVNGEKV LPKDDIECPL GWKWEDEEWS
1010 1020 1030 1040 1050
TDLNRAVDEQ GWEYSITIPP ERKPKHWVPA EKMYYTHRRR RWVRLRRRDL
1060 1070 1080 1090 1100
SQMEALKRHR QAEAEGEGWE YASLFGWKFH LEYRKTDAFR RRRWRRRMEP
1110 1120 1130 1140 1150
LEKTGPAAVF ALEGALGGVM DDKSEDSMSV STLSFGVNRP TISCIFDYGN
1160 1170 1180 1190 1200
RYHLRCYMYQ ARDLAAMDKD SFSDPYAIVS FLHQSQKTVV VKNTLNPTWD
1210 1220 1230 1240 1250
QTLIFYEIEI FGEPATVAEQ PPSIVVELYD HDTYGADEFM GRCICQPSLE
1260 1270 1280 1290 1300
RMPRLAWFPL TRGSQPSGEL LASFELIQRE KPAIHHIPGF EVQETSRILD
1310 1320 1330 1340 1350
ESEDTDLPYP PPQREANIYM VPQNIKPALQ RTAIEILAWG LRNMKSYQLA
1360 1370 1380 1390 1400
NISSPSLVVE CGGQTVQSCV IRNLRKNPNF DICTLFMEVM LPREELYCPP
1410 1420 1430 1440 1450
ITVKVIDNRQ FGRRPVVGQC TIRSLESFLC DPYSAESPSP QGGPDDVSLL
1460 1470 1480 1490 1500
SPGEDVLIDI DDKEPLIPIQ LADGLSSLAP TNTASPPSSP HEEEFIDWWS
1510 1520 1530 1540 1550
KFFASIGERE KCGSYLEKDF DTLKVYDTQL ENVEAFEGLS DFCNTFKLYR
1560 1570 1580 1590 1600
GKTQEETEDP SVIGEFKGLF KIYPLPEDPA IPMPPRQFHQ LAAQGPQECL
1610 1620 1630 1640 1650
VRIYIVRAFG LQPKDPNGKC DPYIKISIGK KSVSDQDNYI PCTLEPVFGK
1660 1670 1680 1690 1700
MFELTCTLPL EKDLKITLYD YDLLSKDEKI GETVVDLENR LLSKFGARCG
1710 1720 1730 1740 1750
LPQTYCVSGP NQWRDQLRPS QLLHLFCQQH RVKAPVYRTD RVMFQDKEYS
1760 1770 1780 1790 1800
IEEIEAGRIP NPHLGPVEER LALHVLQQQG LVPEHVESRP LYSPLQPDIE
1810 1820 1830 1840 1850
QGKLQMWVDL FPKALGRPGP PFNITPRRAR RFFLRCIIWN TRDVILDDLS
1860 1870 1880 1890 1900
LTGEKMSDIY VKGWMIGFEE HKQKTDVHYR SLGGEGNFNW RFIFPFDYLP
1910 1920 1930 1940 1950
AEQVCTIAKK DAFWRLDKTE SKIPARVVFQ IWDNDKFSFD DFLGSLQLDL
1960 1970 1980 1990 2000
NRMPKPAKTA KKCSLDQLDD AFHPEWFVSL FEQKTVKGWW PCVAEEGEKK
2010 2020 2030 2040 2050
ILAGKLEMTL EIVAESEHEE RPAGQGRDEP NMNPKLEDPR RPDTSFLWFT
2060 2070 2080 2090 2100
SPYKTMKFIL WRRFRWAIIL FIILFILLLF LAIFIYAFPN YAAMKLVKPF
S
The sequence of this isoform differs from the canonical sequence as follows:
152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT
494-508: EEPAGAVKPSKASDL → V
10 20 30 40 50
MLRVFILYAE NVHTPDTDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF
60 70 80 90 100
EWDLKGIPLD QGSELHVVVK DHETMGRNRF LGEAKVPLRE VLATPSLSAS
110 120 130 140 150
FNAPLLDTKK QPTGASLVLQ VSYTPLPGAV PLFPPPTPLE PSPTLPDLDV
160 170 180 190 200
VAGGGQSRAE TWSLLSDSTM DTRYSGKKWP APTDTGGEED TEDQGLTGDE
210 220 230 240 250
AEPFLDQSGG PGAPTTPRKL PSRPPPHYPG IKRKRSAPTS RKLLSDKPQD
260 270 280 290 300
FQIRVQVIEG RQLPGVNIKP VVKVTAAGQT KRTRIHKGNS PLFNETLFFN
310 320 330 340 350
LFDSPGELFD EPIFITVVDS RSLRTDALLG EFRMDVGTIY REPRHAYLRK
360 370 380 390 400
WLLLSDPDDF SAGARGYLKT SLCVLGPGDE APLERKDPSE DKEDIESNLL
410 420 430 440 450
RPTGVALRGA HFCLKVFRAE DLPQMDDAVM DNVKQIFGFE SNKKNLVDPF
460 470 480 490 500
VEVSFAGKML CSKILEKTAN PQWNQNITLP AMFPSMCEKM RIRIIDWDRL
510 520 530 540 550
THNDIVATTY LSMSKISAPG GEIEVDDYLG FLPTFGPCYI NLYGSPREFT
560 570 580 590 600
GFPDPYTELN TGKGEGVAYR GRLLLSLETK LVEHSEQKVE DLPADDILRV
610 620 630 640 650
EKYLRRRKYS LFAAFYSATM LQDVDDAIQF EVSIGNYGNK FDMTCLPLAS
660 670 680 690 700
TTQYSRAVFD GCHYYYLPWG NVKPVVVLSS YWEDISHRIE TQNQLLGIAD
710 720 730 740 750
RLEAGLEQVH LALKAQCSTE DVDSLVAQLT DELIAGCSQP LGDIHETPSA
760 770 780 790 800
THLDQYLYQL RTHHLSQITE AALALKLGHS ELPAALEQAE DWLLRLRALA
810 820 830 840 850
EEPQNSLPDI VIWMLQGDKR VAYQRVPAHQ VLFSRRGANY CGKNCGKLQT
860 870 880 890 900
IFLKYPMEKV PGARMPVQIR VKLWFGLSVD EKEFNQFAEG KLSVFAETYE
910 920 930 940 950
NETKLALVGN WGTTGLTYPK FSDVTGKIKL PKDSFRPSAG WTWAGDWFVC
960 970 980 990 1000
PEKTLLHDMD AGHLSFVEEV FENQTRLPGG QWIYMSDNYT DVNGEKVLPK
1010 1020 1030 1040 1050
DDIECPLGWK WEDEEWSTDL NRAVDEQGWE YSITIPPERK PKHWVPAEKM
1060 1070 1080 1090 1100
YYTHRRRRWV RLRRRDLSQM EALKRHRQAE AEGEGWEYAS LFGWKFHLEY
1110 1120 1130 1140 1150
RKTDAFRRRR WRRRMEPLEK TGPAAVFALE GALGGVMDDK SEDSMSVSTL
1160 1170 1180 1190 1200
SFGVNRPTIS CIFDYGNRYH LRCYMYQARD LAAMDKDSFS DPYAIVSFLH
1210 1220 1230 1240 1250
QSQKTVVVKN TLNPTWDQTL IFYEIEIFGE PATVAEQPPS IVVELYDHDT
1260 1270 1280 1290 1300
YGADEFMGRC ICQPSLERMP RLAWFPLTRG SQPSGELLAS FELIQREKPA
1310 1320 1330 1340 1350
IHHIPGFEVQ ETSRILDESE DTDLPYPPPQ REANIYMVPQ NIKPALQRTA
1360 1370 1380 1390 1400
IEILAWGLRN MKSYQLANIS SPSLVVECGG QTVQSCVIRN LRKNPNFDIC
1410 1420 1430 1440 1450
TLFMEVMLPR EELYCPPITV KVIDNRQFGR RPVVGQCTIR SLESFLCDPY
1460 1470 1480 1490 1500
SAESPSPQGG PDDVSLLSPG EDVLIDIDDK EPLIPIQEEE FIDWWSKFFA
1510 1520 1530 1540 1550
SIGEREKCGS YLEKDFDTLK VYDTQLENVE AFEGLSDFCN TFKLYRGKTQ
1560 1570 1580 1590 1600
EETEDPSVIG EFKGLFKIYP LPEDPAIPMP PRQFHQLAAQ GPQECLVRIY
1610 1620 1630 1640 1650
IVRAFGLQPK DPNGKCDPYI KISIGKKSVS DQDNYIPCTL EPVFGKMFEL
1660 1670 1680 1690 1700
TCTLPLEKDL KITLYDYDLL SKDEKIGETV VDLENRLLSK FGARCGLPQT
1710 1720 1730 1740 1750
YCVSGPNQWR DQLRPSQLLH LFCQQHRVKA PVYRTDRVMF QDKEYSIEEI
1760 1770 1780 1790 1800
EAGRIPNPHL GPVEERLALH VLQQQGLVPE HVESRPLYSP LQPDIEQGKL
1810 1820 1830 1840 1850
QMWVDLFPKA LGRPGPPFNI TPRRARRFFL RCIIWNTRDV ILDDLSLTGE
1860 1870 1880 1890 1900
KMSDIYVKGW MIGFEEHKQK TDVHYRSLGG EGNFNWRFIF PFDYLPAEQV
1910 1920 1930 1940 1950
CTIAKKDAFW RLDKTESKIP ARVVFQIWDN DKFSFDDFLG SLQLDLNRMP
1960 1970 1980 1990 2000
KPAKTAKKCS LDQLDDAFHP EWFVSLFEQK TVKGWWPCVA EEGEKKILAG
2010 2020 2030 2040 2050
KLEMTLEIVA ESEHEERPAG QGRDEPNMNP KLEDPRRPDT SFLWFTSPYK
2060 2070 2080 2090
TMKFILWRRF RWAIILFIIL FILLLFLAIF IYAFPNYAAM KLVKPFS
The sequence of this isoform differs from the canonical sequence as follows:
494-508: EEPAGAVKPSKASDL → V
1470-1470: Q → QLADGLSSLAPTNTASPPSSPH
10 20 30 40 50
MLRVFILYAE NVHTPDTDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF
60 70 80 90 100
EWDLKGIPLD QGSELHVVVK DHETMGRNRF LGEAKVPLRE VLATPSLSAS
110 120 130 140 150
FNAPLLDTKK QPTGASLVLQ VSYTPLPGAV PLFPPPTPLE PSPTLPDLDV
160 170 180 190 200
VADTGGEEDT EDQGLTGDEA EPFLDQSGGP GAPTTPRKLP SRPPPHYPGI
210 220 230 240 250
KRKRSAPTSR KLLSDKPQDF QIRVQVIEGR QLPGVNIKPV VKVTAAGQTK
260 270 280 290 300
RTRIHKGNSP LFNETLFFNL FDSPGELFDE PIFITVVDSR SLRTDALLGE
310 320 330 340 350
FRMDVGTIYR EPRHAYLRKW LLLSDPDDFS AGARGYLKTS LCVLGPGDEA
360 370 380 390 400
PLERKDPSED KEDIESNLLR PTGVALRGAH FCLKVFRAED LPQMDDAVMD
410 420 430 440 450
NVKQIFGFES NKKNLVDPFV EVSFAGKMLC SKILEKTANP QWNQNITLPA
460 470 480 490 500
MFPSMCEKMR IRIIDWDRLT HNDIVATTYL SMSKISAPGG EIEVDDYLGF
510 520 530 540 550
LPTFGPCYIN LYGSPREFTG FPDPYTELNT GKGEGVAYRG RLLLSLETKL
560 570 580 590 600
VEHSEQKVED LPADDILRVE KYLRRRKYSL FAAFYSATML QDVDDAIQFE
610 620 630 640 650
VSIGNYGNKF DMTCLPLAST TQYSRAVFDG CHYYYLPWGN VKPVVVLSSY
660 670 680 690 700
WEDISHRIET QNQLLGIADR LEAGLEQVHL ALKAQCSTED VDSLVAQLTD
710 720 730 740 750
ELIAGCSQPL GDIHETPSAT HLDQYLYQLR THHLSQITEA ALALKLGHSE
760 770 780 790 800
LPAALEQAED WLLRLRALAE EPQNSLPDIV IWMLQGDKRV AYQRVPAHQV
810 820 830 840 850
LFSRRGANYC GKNCGKLQTI FLKYPMEKVP GARMPVQIRV KLWFGLSVDE
860 870 880 890 900
KEFNQFAEGK LSVFAETYEN ETKLALVGNW GTTGLTYPKF SDVTGKIKLP
910 920 930 940 950
KDSFRPSAGW TWAGDWFVCP EKTLLHDMDA GHLSFVEEVF ENQTRLPGGQ
960 970 980 990 1000
WIYMSDNYTD VNGEKVLPKD DIECPLGWKW EDEEWSTDLN RAVDEQGWEY
1010 1020 1030 1040 1050
SITIPPERKP KHWVPAEKMY YTHRRRRWVR LRRRDLSQME ALKRHRQAEA
1060 1070 1080 1090 1100
EGEGWEYASL FGWKFHLEYR KTDAFRRRRW RRRMEPLEKT GPAAVFALEG
1110 1120 1130 1140 1150
ALGGVMDDKS EDSMSVSTLS FGVNRPTISC IFDYGNRYHL RCYMYQARDL
1160 1170 1180 1190 1200
AAMDKDSFSD PYAIVSFLHQ SQKTVVVKNT LNPTWDQTLI FYEIEIFGEP
1210 1220 1230 1240 1250
ATVAEQPPSI VVELYDHDTY GADEFMGRCI CQPSLERMPR LAWFPLTRGS
1260 1270 1280 1290 1300
QPSGELLASF ELIQREKPAI HHIPGFEVQE TSRILDESED TDLPYPPPQR
1310 1320 1330 1340 1350
EANIYMVPQN IKPALQRTAI EILAWGLRNM KSYQLANISS PSLVVECGGQ
1360 1370 1380 1390 1400
TVQSCVIRNL RKNPNFDICT LFMEVMLPRE ELYCPPITVK VIDNRQFGRR
1410 1420 1430 1440 1450
PVVGQCTIRS LESFLCDPYS AESPSPQGGP DDVSLLSPGE DVLIDIDDKE
1460 1470 1480 1490 1500
PLIPIQLADG LSSLAPTNTA SPPSSPHEEE FIDWWSKFFA SIGEREKCGS
1510 1520 1530 1540 1550
YLEKDFDTLK VYDTQLENVE AFEGLSDFCN TFKLYRGKTQ EETEDPSVIG
1560 1570 1580 1590 1600
EFKGLFKIYP LPEDPAIPMP PRQFHQLAAQ GPQECLVRIY IVRAFGLQPK
1610 1620 1630 1640 1650
DPNGKCDPYI KISIGKKSVS DQDNYIPCTL EPVFGKMFEL TCTLPLEKDL
1660 1670 1680 1690 1700
KITLYDYDLL SKDEKIGETV VDLENRLLSK FGARCGLPQT YCVSGPNQWR
1710 1720 1730 1740 1750
DQLRPSQLLH LFCQQHRVKA PVYRTDRVMF QDKEYSIEEI EAGRIPNPHL
1760 1770 1780 1790 1800
GPVEERLALH VLQQQGLVPE HVESRPLYSP LQPDIEQGKL QMWVDLFPKA
1810 1820 1830 1840 1850
LGRPGPPFNI TPRRARRFFL RCIIWNTRDV ILDDLSLTGE KMSDIYVKGW
1860 1870 1880 1890 1900
MIGFEEHKQK TDVHYRSLGG EGNFNWRFIF PFDYLPAEQV CTIAKKDAFW
1910 1920 1930 1940 1950
RLDKTESKIP ARVVFQIWDN DKFSFDDFLG SLQLDLNRMP KPAKTAKKCS
1960 1970 1980 1990 2000
LDQLDDAFHP EWFVSLFEQK TVKGWWPCVA EEGEKKILAG KLEMTLEIVA
2010 2020 2030 2040 2050
ESEHEERPAG QGRDEPNMNP KLEDPRRPDT SFLWFTSPYK TMKFILWRRF
2060 2070 2080
RWAIILFIIL FILLLFLAIF IYAFPNYAAM KLVKPFS
The sequence of this isoform differs from the canonical sequence as follows:
152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT
494-508: EEPAGAVKPSKASDL → V
1470-1470: Q → QLADGLSSLAPTNTASPPSSPH
10 20 30 40 50
MLRVFILYAE NVHTPDTDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF
60 70 80 90 100
EWDLKGIPLD QGSELHVVVK DHETMGRNRF LGEAKVPLRE VLATPSLSAS
110 120 130 140 150
FNAPLLDTKK QPTGASLVLQ VSYTPLPGAV PLFPPPTPLE PSPTLPDLDV
160 170 180 190 200
VAGGGQSRAE TWSLLSDSTM DTRYSGKKWP APTDTGGEED TEDQGLTGDE
210 220 230 240 250
AEPFLDQSGG PGAPTTPRKL PSRPPPHYPG IKRKRSAPTS RKLLSDKPQD
260 270 280 290 300
FQIRVQVIEG RQLPGVNIKP VVKVTAAGQT KRTRIHKGNS PLFNETLFFN
310 320 330 340 350
LFDSPGELFD EPIFITVVDS RSLRTDALLG EFRMDVGTIY REPRHAYLRK
360 370 380 390 400
WLLLSDPDDF SAGARGYLKT SLCVLGPGDE APLERKDPSE DKEDIESNLL
410 420 430 440 450
RPTGVALRGA HFCLKVFRAE DLPQMDDAVM DNVKQIFGFE SNKKNLVDPF
460 470 480 490 500
VEVSFAGKML CSKILEKTAN PQWNQNITLP AMFPSMCEKM RIRIIDWDRL
510 520 530 540 550
THNDIVATTY LSMSKISAPG GEIEVDDYLG FLPTFGPCYI NLYGSPREFT
560 570 580 590 600
GFPDPYTELN TGKGEGVAYR GRLLLSLETK LVEHSEQKVE DLPADDILRV
610 620 630 640 650
EKYLRRRKYS LFAAFYSATM LQDVDDAIQF EVSIGNYGNK FDMTCLPLAS
660 670 680 690 700
TTQYSRAVFD GCHYYYLPWG NVKPVVVLSS YWEDISHRIE TQNQLLGIAD
710 720 730 740 750
RLEAGLEQVH LALKAQCSTE DVDSLVAQLT DELIAGCSQP LGDIHETPSA
760 770 780 790 800
THLDQYLYQL RTHHLSQITE AALALKLGHS ELPAALEQAE DWLLRLRALA
810 820 830 840 850
EEPQNSLPDI VIWMLQGDKR VAYQRVPAHQ VLFSRRGANY CGKNCGKLQT
860 870 880 890 900
IFLKYPMEKV PGARMPVQIR VKLWFGLSVD EKEFNQFAEG KLSVFAETYE
910 920 930 940 950
NETKLALVGN WGTTGLTYPK FSDVTGKIKL PKDSFRPSAG WTWAGDWFVC
960 970 980 990 1000
PEKTLLHDMD AGHLSFVEEV FENQTRLPGG QWIYMSDNYT DVNGEKVLPK
1010 1020 1030 1040 1050
DDIECPLGWK WEDEEWSTDL NRAVDEQGWE YSITIPPERK PKHWVPAEKM
1060 1070 1080 1090 1100
YYTHRRRRWV RLRRRDLSQM EALKRHRQAE AEGEGWEYAS LFGWKFHLEY
1110 1120 1130 1140 1150
RKTDAFRRRR WRRRMEPLEK TGPAAVFALE GALGGVMDDK SEDSMSVSTL
1160 1170 1180 1190 1200
SFGVNRPTIS CIFDYGNRYH LRCYMYQARD LAAMDKDSFS DPYAIVSFLH
1210 1220 1230 1240 1250
QSQKTVVVKN TLNPTWDQTL IFYEIEIFGE PATVAEQPPS IVVELYDHDT
1260 1270 1280 1290 1300
YGADEFMGRC ICQPSLERMP RLAWFPLTRG SQPSGELLAS FELIQREKPA
1310 1320 1330 1340 1350
IHHIPGFEVQ ETSRILDESE DTDLPYPPPQ REANIYMVPQ NIKPALQRTA
1360 1370 1380 1390 1400
IEILAWGLRN MKSYQLANIS SPSLVVECGG QTVQSCVIRN LRKNPNFDIC
1410 1420 1430 1440 1450
TLFMEVMLPR EELYCPPITV KVIDNRQFGR RPVVGQCTIR SLESFLCDPY
1460 1470 1480 1490 1500
SAESPSPQGG PDDVSLLSPG EDVLIDIDDK EPLIPIQLAD GLSSLAPTNT
1510 1520 1530 1540 1550
ASPPSSPHEE EFIDWWSKFF ASIGEREKCG SYLEKDFDTL KVYDTQLENV
1560 1570 1580 1590 1600
EAFEGLSDFC NTFKLYRGKT QEETEDPSVI GEFKGLFKIY PLPEDPAIPM
1610 1620 1630 1640 1650
PPRQFHQLAA QGPQECLVRI YIVRAFGLQP KDPNGKCDPY IKISIGKKSV
1660 1670 1680 1690 1700
SDQDNYIPCT LEPVFGKMFE LTCTLPLEKD LKITLYDYDL LSKDEKIGET
1710 1720 1730 1740 1750
VVDLENRLLS KFGARCGLPQ TYCVSGPNQW RDQLRPSQLL HLFCQQHRVK
1760 1770 1780 1790 1800
APVYRTDRVM FQDKEYSIEE IEAGRIPNPH LGPVEERLAL HVLQQQGLVP
1810 1820 1830 1840 1850
EHVESRPLYS PLQPDIEQGK LQMWVDLFPK ALGRPGPPFN ITPRRARRFF
1860 1870 1880 1890 1900
LRCIIWNTRD VILDDLSLTG EKMSDIYVKG WMIGFEEHKQ KTDVHYRSLG
1910 1920 1930 1940 1950
GEGNFNWRFI FPFDYLPAEQ VCTIAKKDAF WRLDKTESKI PARVVFQIWD
1960 1970 1980 1990 2000
NDKFSFDDFL GSLQLDLNRM PKPAKTAKKC SLDQLDDAFH PEWFVSLFEQ
2010 2020 2030 2040 2050
KTVKGWWPCV AEEGEKKILA GKLEMTLEIV AESEHEERPA GQGRDEPNMN
2060 2070 2080 2090 2100
PKLEDPRRPD TSFLWFTSPY KTMKFILWRR FRWAIILFII LFILLLFLAI
2110
FIYAFPNYAA MKLVKPFS
The sequence of this isoform differs from the canonical sequence as follows:
1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT
10 20 30 40 50
MLCCLLVRAS NLPSAKKDRR SDPVASLTFR GVKKRTKVIK NSVNPVWNEG
60 70 80 90 100
FEWDLKGIPL DQGSELHVVV KDHETMGRNR FLGEAKVPLR EVLATPSLSA
110 120 130 140 150
SFNAPLLDTK KQPTGASLVL QVSYTPLPGA VPLFPPPTPL EPSPTLPDLD
160 170 180 190 200
VVAGGGQSRA ETWSLLSDST MDTRYSGKKW PAPTDTGGEE DTEDQGLTGD
210 220 230 240 250
EAEPFLDQSG GPGAPTTPRK LPSRPPPHYP GIKRKRSAPT SRKLLSDKPQ
260 270 280 290 300
DFQIRVQVIE GRQLPGVNIK PVVKVTAAGQ TKRTRIHKGN SPLFNETLFF
310 320 330 340 350
NLFDSPGELF DEPIFITVVD SRSLRTDALL GEFRMDVGTI YREPRHAYLR
360 370 380 390 400
KWLLLSDPDD FSAGARGYLK TSLCVLGPGD EAPLERKDPS EDKEDIESNL
410 420 430 440 450
LRPTGVALRG AHFCLKVFRA EDLPQMDDAV MDNVKQIFGF ESNKKNLVDP
460 470 480 490 500
FVEVSFAGKM LCSKILEKTA NPQWNQNITL PAMFPSMCEK MRIRIIDWDR
510 520 530 540 550
LTHNDIVATT YLSMSKISAP GGEIEEEPAG AVKPSKASDL DDYLGFLPTF
560 570 580 590 600
GPCYINLYGS PREFTGFPDP YTELNTGKGE GVAYRGRLLL SLETKLVEHS
610 620 630 640 650
EQKVEDLPAD DILRVEKYLR RRKYSLFAAF YSATMLQDVD DAIQFEVSIG
660 670 680 690 700
NYGNKFDMTC LPLASTTQYS RAVFDGCHYY YLPWGNVKPV VVLSSYWEDI
710 720 730 740 750
SHRIETQNQL LGIADRLEAG LEQVHLALKA QCSTEDVDSL VAQLTDELIA
760 770 780 790 800
GCSQPLGDIH ETPSATHLDQ YLYQLRTHHL SQITEAALAL KLGHSELPAA
810 820 830 840 850
LEQAEDWLLR LRALAEEPQN SLPDIVIWML QGDKRVAYQR VPAHQVLFSR
860 870 880 890 900
RGANYCGKNC GKLQTIFLKY PMEKVPGARM PVQIRVKLWF GLSVDEKEFN
910 920 930 940 950
QFAEGKLSVF AETYENETKL ALVGNWGTTG LTYPKFSDVT GKIKLPKDSF
960 970 980 990 1000
RPSAGWTWAG DWFVCPEKTL LHDMDAGHLS FVEEVFENQT RLPGGQWIYM
1010 1020 1030 1040 1050
SDNYTDVNGE KVLPKDDIEC PLGWKWEDEE WSTDLNRAVD EQGWEYSITI
1060 1070 1080 1090 1100
PPERKPKHWV PAEKMYYTHR RRRWVRLRRR DLSQMEALKR HRQAEAEGEG
1110 1120 1130 1140 1150
WEYASLFGWK FHLEYRKTDA FRRRRWRRRM EPLEKTGPAA VFALEGALGG
1160 1170 1180 1190 1200
VMDDKSEDSM SVSTLSFGVN RPTISCIFDY GNRYHLRCYM YQARDLAAMD
1210 1220 1230 1240 1250
KDSFSDPYAI VSFLHQSQKT VVVKNTLNPT WDQTLIFYEI EIFGEPATVA
1260 1270 1280 1290 1300
EQPPSIVVEL YDHDTYGADE FMGRCICQPS LERMPRLAWF PLTRGSQPSG
1310 1320 1330 1340 1350
ELLASFELIQ REKPAIHHIP GFEVQETSRI LDESEDTDLP YPPPQREANI
1360 1370 1380 1390 1400
YMVPQNIKPA LQRTAIEILA WGLRNMKSYQ LANISSPSLV VECGGQTVQS
1410 1420 1430 1440 1450
CVIRNLRKNP NFDICTLFME VMLPREELYC PPITVKVIDN RQFGRRPVVG
1460 1470 1480 1490 1500
QCTIRSLESF LCDPYSAESP SPQGGPDDVS LLSPGEDVLI DIDDKEPLIP
1510 1520 1530 1540 1550
IQEEEFIDWW SKFFASIGER EKCGSYLEKD FDTLKVYDTQ LENVEAFEGL
1560 1570 1580 1590 1600
SDFCNTFKLY RGKTQEETED PSVIGEFKGL FKIYPLPEDP AIPMPPRQFH
1610 1620 1630 1640 1650
QLAAQGPQEC LVRIYIVRAF GLQPKDPNGK CDPYIKISIG KKSVSDQDNY
1660 1670 1680 1690 1700
IPCTLEPVFG KMFELTCTLP LEKDLKITLY DYDLLSKDEK IGETVVDLEN
1710 1720 1730 1740 1750
RLLSKFGARC GLPQTYCVSG PNQWRDQLRP SQLLHLFCQQ HRVKAPVYRT
1760 1770 1780 1790 1800
DRVMFQDKEY SIEEIEAGRI PNPHLGPVEE RLALHVLQQQ GLVPEHVESR
1810 1820 1830 1840 1850
PLYSPLQPDI EQGKLQMWVD LFPKALGRPG PPFNITPRRA RRFFLRCIIW
1860 1870 1880 1890 1900
NTRDVILDDL SLTGEKMSDI YVKGWMIGFE EHKQKTDVHY RSLGGEGNFN
1910 1920 1930 1940 1950
WRFIFPFDYL PAEQVCTIAK KDAFWRLDKT ESKIPARVVF QIWDNDKFSF
1960 1970 1980 1990 2000
DDFLGSLQLD LNRMPKPAKT AKKCSLDQLD DAFHPEWFVS LFEQKTVKGW
2010 2020 2030 2040 2050
WPCVAEEGEK KILAGKLEMT LEIVAESEHE ERPAGQGRDE PNMNPKLEDP
2060 2070 2080 2090 2100
RRPDTSFLWF TSPYKTMKFI LWRRFRWAII LFIILFILLL FLAIFIYAFP
2110
NYAAMKLVKP FS
The sequence of this isoform differs from the canonical sequence as follows:
1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
494-508: EEPAGAVKPSKASDL → V
10 20 30 40 50
MLCCLLVRAS NLPSAKKDRR SDPVASLTFR GVKKRTKVIK NSVNPVWNEG
60 70 80 90 100
FEWDLKGIPL DQGSELHVVV KDHETMGRNR FLGEAKVPLR EVLATPSLSA
110 120 130 140 150
SFNAPLLDTK KQPTGASLVL QVSYTPLPGA VPLFPPPTPL EPSPTLPDLD
160 170 180 190 200
VVADTGGEED TEDQGLTGDE AEPFLDQSGG PGAPTTPRKL PSRPPPHYPG
210 220 230 240 250
IKRKRSAPTS RKLLSDKPQD FQIRVQVIEG RQLPGVNIKP VVKVTAAGQT
260 270 280 290 300
KRTRIHKGNS PLFNETLFFN LFDSPGELFD EPIFITVVDS RSLRTDALLG
310 320 330 340 350
EFRMDVGTIY REPRHAYLRK WLLLSDPDDF SAGARGYLKT SLCVLGPGDE
360 370 380 390 400
APLERKDPSE DKEDIESNLL RPTGVALRGA HFCLKVFRAE DLPQMDDAVM
410 420 430 440 450
DNVKQIFGFE SNKKNLVDPF VEVSFAGKML CSKILEKTAN PQWNQNITLP
460 470 480 490 500
AMFPSMCEKM RIRIIDWDRL THNDIVATTY LSMSKISAPG GEIEVDDYLG
510 520 530 540 550
FLPTFGPCYI NLYGSPREFT GFPDPYTELN TGKGEGVAYR GRLLLSLETK
560 570 580 590 600
LVEHSEQKVE DLPADDILRV EKYLRRRKYS LFAAFYSATM LQDVDDAIQF
610 620 630 640 650
EVSIGNYGNK FDMTCLPLAS TTQYSRAVFD GCHYYYLPWG NVKPVVVLSS
660 670 680 690 700
YWEDISHRIE TQNQLLGIAD RLEAGLEQVH LALKAQCSTE DVDSLVAQLT
710 720 730 740 750
DELIAGCSQP LGDIHETPSA THLDQYLYQL RTHHLSQITE AALALKLGHS
760 770 780 790 800
ELPAALEQAE DWLLRLRALA EEPQNSLPDI VIWMLQGDKR VAYQRVPAHQ
810 820 830 840 850
VLFSRRGANY CGKNCGKLQT IFLKYPMEKV PGARMPVQIR VKLWFGLSVD
860 870 880 890 900
EKEFNQFAEG KLSVFAETYE NETKLALVGN WGTTGLTYPK FSDVTGKIKL
910 920 930 940 950
PKDSFRPSAG WTWAGDWFVC PEKTLLHDMD AGHLSFVEEV FENQTRLPGG
960 970 980 990 1000
QWIYMSDNYT DVNGEKVLPK DDIECPLGWK WEDEEWSTDL NRAVDEQGWE
1010 1020 1030 1040 1050
YSITIPPERK PKHWVPAEKM YYTHRRRRWV RLRRRDLSQM EALKRHRQAE
1060 1070 1080 1090 1100
AEGEGWEYAS LFGWKFHLEY RKTDAFRRRR WRRRMEPLEK TGPAAVFALE
1110 1120 1130 1140 1150
GALGGVMDDK SEDSMSVSTL SFGVNRPTIS CIFDYGNRYH LRCYMYQARD
1160 1170 1180 1190 1200
LAAMDKDSFS DPYAIVSFLH QSQKTVVVKN TLNPTWDQTL IFYEIEIFGE
1210 1220 1230 1240 1250
PATVAEQPPS IVVELYDHDT YGADEFMGRC ICQPSLERMP RLAWFPLTRG
1260 1270 1280 1290 1300
SQPSGELLAS FELIQREKPA IHHIPGFEVQ ETSRILDESE DTDLPYPPPQ
1310 1320 1330 1340 1350
REANIYMVPQ NIKPALQRTA IEILAWGLRN MKSYQLANIS SPSLVVECGG
1360 1370 1380 1390 1400
QTVQSCVIRN LRKNPNFDIC TLFMEVMLPR EELYCPPITV KVIDNRQFGR
1410 1420 1430 1440 1450
RPVVGQCTIR SLESFLCDPY SAESPSPQGG PDDVSLLSPG EDVLIDIDDK
1460 1470 1480 1490 1500
EPLIPIQEEE FIDWWSKFFA SIGEREKCGS YLEKDFDTLK VYDTQLENVE
1510 1520 1530 1540 1550
AFEGLSDFCN TFKLYRGKTQ EETEDPSVIG EFKGLFKIYP LPEDPAIPMP
1560 1570 1580 1590 1600
PRQFHQLAAQ GPQECLVRIY IVRAFGLQPK DPNGKCDPYI KISIGKKSVS
1610 1620 1630 1640 1650
DQDNYIPCTL EPVFGKMFEL TCTLPLEKDL KITLYDYDLL SKDEKIGETV
1660 1670 1680 1690 1700
VDLENRLLSK FGARCGLPQT YCVSGPNQWR DQLRPSQLLH LFCQQHRVKA
1710 1720 1730 1740 1750
PVYRTDRVMF QDKEYSIEEI EAGRIPNPHL GPVEERLALH VLQQQGLVPE
1760 1770 1780 1790 1800
HVESRPLYSP LQPDIEQGKL QMWVDLFPKA LGRPGPPFNI TPRRARRFFL
1810 1820 1830 1840 1850
RCIIWNTRDV ILDDLSLTGE KMSDIYVKGW MIGFEEHKQK TDVHYRSLGG
1860 1870 1880 1890 1900
EGNFNWRFIF PFDYLPAEQV CTIAKKDAFW RLDKTESKIP ARVVFQIWDN
1910 1920 1930 1940 1950
DKFSFDDFLG SLQLDLNRMP KPAKTAKKCS LDQLDDAFHP EWFVSLFEQK
1960 1970 1980 1990 2000
TVKGWWPCVA EEGEKKILAG KLEMTLEIVA ESEHEERPAG QGRDEPNMNP
2010 2020 2030 2040 2050
KLEDPRRPDT SFLWFTSPYK TMKFILWRRF RWAIILFIIL FILLLFLAIF
2060
IYAFPNYAAM KLVKPFS
The sequence of this isoform differs from the canonical sequence as follows:
1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
1470-1470: Q → QLADGLSSLAPTNTASPPSSPH
10 20 30 40 50
MLCCLLVRAS NLPSAKKDRR SDPVASLTFR GVKKRTKVIK NSVNPVWNEG
60 70 80 90 100
FEWDLKGIPL DQGSELHVVV KDHETMGRNR FLGEAKVPLR EVLATPSLSA
110 120 130 140 150
SFNAPLLDTK KQPTGASLVL QVSYTPLPGA VPLFPPPTPL EPSPTLPDLD
160 170 180 190 200
VVADTGGEED TEDQGLTGDE AEPFLDQSGG PGAPTTPRKL PSRPPPHYPG
210 220 230 240 250
IKRKRSAPTS RKLLSDKPQD FQIRVQVIEG RQLPGVNIKP VVKVTAAGQT
260 270 280 290 300
KRTRIHKGNS PLFNETLFFN LFDSPGELFD EPIFITVVDS RSLRTDALLG
310 320 330 340 350
EFRMDVGTIY REPRHAYLRK WLLLSDPDDF SAGARGYLKT SLCVLGPGDE
360 370 380 390 400
APLERKDPSE DKEDIESNLL RPTGVALRGA HFCLKVFRAE DLPQMDDAVM
410 420 430 440 450
DNVKQIFGFE SNKKNLVDPF VEVSFAGKML CSKILEKTAN PQWNQNITLP
460 470 480 490 500
AMFPSMCEKM RIRIIDWDRL THNDIVATTY LSMSKISAPG GEIEEEPAGA
510 520 530 540 550
VKPSKASDLD DYLGFLPTFG PCYINLYGSP REFTGFPDPY TELNTGKGEG
560 570 580 590 600
VAYRGRLLLS LETKLVEHSE QKVEDLPADD ILRVEKYLRR RKYSLFAAFY
610 620 630 640 650
SATMLQDVDD AIQFEVSIGN YGNKFDMTCL PLASTTQYSR AVFDGCHYYY
660 670 680 690 700
LPWGNVKPVV VLSSYWEDIS HRIETQNQLL GIADRLEAGL EQVHLALKAQ
710 720 730 740 750
CSTEDVDSLV AQLTDELIAG CSQPLGDIHE TPSATHLDQY LYQLRTHHLS
760 770 780 790 800
QITEAALALK LGHSELPAAL EQAEDWLLRL RALAEEPQNS LPDIVIWMLQ
810 820 830 840 850
GDKRVAYQRV PAHQVLFSRR GANYCGKNCG KLQTIFLKYP MEKVPGARMP
860 870 880 890 900
VQIRVKLWFG LSVDEKEFNQ FAEGKLSVFA ETYENETKLA LVGNWGTTGL
910 920 930 940 950
TYPKFSDVTG KIKLPKDSFR PSAGWTWAGD WFVCPEKTLL HDMDAGHLSF
960 970 980 990 1000
VEEVFENQTR LPGGQWIYMS DNYTDVNGEK VLPKDDIECP LGWKWEDEEW
1010 1020 1030 1040 1050
STDLNRAVDE QGWEYSITIP PERKPKHWVP AEKMYYTHRR RRWVRLRRRD
1060 1070 1080 1090 1100
LSQMEALKRH RQAEAEGEGW EYASLFGWKF HLEYRKTDAF RRRRWRRRME
1110 1120 1130 1140 1150
PLEKTGPAAV FALEGALGGV MDDKSEDSMS VSTLSFGVNR PTISCIFDYG
1160 1170 1180 1190 1200
NRYHLRCYMY QARDLAAMDK DSFSDPYAIV SFLHQSQKTV VVKNTLNPTW
1210 1220 1230 1240 1250
DQTLIFYEIE IFGEPATVAE QPPSIVVELY DHDTYGADEF MGRCICQPSL
1260 1270 1280 1290 1300
ERMPRLAWFP LTRGSQPSGE LLASFELIQR EKPAIHHIPG FEVQETSRIL
1310 1320 1330 1340 1350
DESEDTDLPY PPPQREANIY MVPQNIKPAL QRTAIEILAW GLRNMKSYQL
1360 1370 1380 1390 1400
ANISSPSLVV ECGGQTVQSC VIRNLRKNPN FDICTLFMEV MLPREELYCP
1410 1420 1430 1440 1450
PITVKVIDNR QFGRRPVVGQ CTIRSLESFL CDPYSAESPS PQGGPDDVSL
1460 1470 1480 1490 1500
LSPGEDVLID IDDKEPLIPI QLADGLSSLA PTNTASPPSS PHEEEFIDWW
1510 1520 1530 1540 1550
SKFFASIGER EKCGSYLEKD FDTLKVYDTQ LENVEAFEGL SDFCNTFKLY
1560 1570 1580 1590 1600
RGKTQEETED PSVIGEFKGL FKIYPLPEDP AIPMPPRQFH QLAAQGPQEC
1610 1620 1630 1640 1650
LVRIYIVRAF GLQPKDPNGK CDPYIKISIG KKSVSDQDNY IPCTLEPVFG
1660 1670 1680 1690 1700
KMFELTCTLP LEKDLKITLY DYDLLSKDEK IGETVVDLEN RLLSKFGARC
1710 1720 1730 1740 1750
GLPQTYCVSG PNQWRDQLRP SQLLHLFCQQ HRVKAPVYRT DRVMFQDKEY
1760 1770 1780 1790 1800
SIEEIEAGRI PNPHLGPVEE RLALHVLQQQ GLVPEHVESR PLYSPLQPDI
1810 1820 1830 1840 1850
EQGKLQMWVD LFPKALGRPG PPFNITPRRA RRFFLRCIIW NTRDVILDDL
1860 1870 1880 1890 1900
SLTGEKMSDI YVKGWMIGFE EHKQKTDVHY RSLGGEGNFN WRFIFPFDYL
1910 1920 1930 1940 1950
PAEQVCTIAK KDAFWRLDKT ESKIPARVVF QIWDNDKFSF DDFLGSLQLD
1960 1970 1980 1990 2000
LNRMPKPAKT AKKCSLDQLD DAFHPEWFVS LFEQKTVKGW WPCVAEEGEK
2010 2020 2030 2040 2050
KILAGKLEMT LEIVAESEHE ERPAGQGRDE PNMNPKLEDP RRPDTSFLWF
2060 2070 2080 2090 2100
TSPYKTMKFI LWRRFRWAII LFIILFILLL FLAIFIYAFP NYAAMKLVKP
FS
The sequence of this isoform differs from the canonical sequence as follows:
1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT
494-508: EEPAGAVKPSKASDL → V
10 20 30 40 50
MLCCLLVRAS NLPSAKKDRR SDPVASLTFR GVKKRTKVIK NSVNPVWNEG
60 70 80 90 100
FEWDLKGIPL DQGSELHVVV KDHETMGRNR FLGEAKVPLR EVLATPSLSA
110 120 130 140 150
SFNAPLLDTK KQPTGASLVL QVSYTPLPGA VPLFPPPTPL EPSPTLPDLD
160 170 180 190 200
VVAGGGQSRA ETWSLLSDST MDTRYSGKKW PAPTDTGGEE DTEDQGLTGD
210 220 230 240 250
EAEPFLDQSG GPGAPTTPRK LPSRPPPHYP GIKRKRSAPT SRKLLSDKPQ
260 270 280 290 300
DFQIRVQVIE GRQLPGVNIK PVVKVTAAGQ TKRTRIHKGN SPLFNETLFF
310 320 330 340 350
NLFDSPGELF DEPIFITVVD SRSLRTDALL GEFRMDVGTI YREPRHAYLR
360 370 380 390 400
KWLLLSDPDD FSAGARGYLK TSLCVLGPGD EAPLERKDPS EDKEDIESNL
410 420 430 440 450
LRPTGVALRG AHFCLKVFRA EDLPQMDDAV MDNVKQIFGF ESNKKNLVDP
460 470 480 490 500
FVEVSFAGKM LCSKILEKTA NPQWNQNITL PAMFPSMCEK MRIRIIDWDR
510 520 530 540 550
LTHNDIVATT YLSMSKISAP GGEIEVDDYL GFLPTFGPCY INLYGSPREF
560 570 580 590 600
TGFPDPYTEL NTGKGEGVAY RGRLLLSLET KLVEHSEQKV EDLPADDILR
610 620 630 640 650
VEKYLRRRKY SLFAAFYSAT MLQDVDDAIQ FEVSIGNYGN KFDMTCLPLA
660 670 680 690 700
STTQYSRAVF DGCHYYYLPW GNVKPVVVLS SYWEDISHRI ETQNQLLGIA
710 720 730 740 750
DRLEAGLEQV HLALKAQCST EDVDSLVAQL TDELIAGCSQ PLGDIHETPS
760 770 780 790 800
ATHLDQYLYQ LRTHHLSQIT EAALALKLGH SELPAALEQA EDWLLRLRAL
810 820 830 840 850
AEEPQNSLPD IVIWMLQGDK RVAYQRVPAH QVLFSRRGAN YCGKNCGKLQ
860 870 880 890 900
TIFLKYPMEK VPGARMPVQI RVKLWFGLSV DEKEFNQFAE GKLSVFAETY
910 920 930 940 950
ENETKLALVG NWGTTGLTYP KFSDVTGKIK LPKDSFRPSA GWTWAGDWFV
960 970 980 990 1000
CPEKTLLHDM DAGHLSFVEE VFENQTRLPG GQWIYMSDNY TDVNGEKVLP
1010 1020 1030 1040 1050
KDDIECPLGW KWEDEEWSTD LNRAVDEQGW EYSITIPPER KPKHWVPAEK
1060 1070 1080 1090 1100
MYYTHRRRRW VRLRRRDLSQ MEALKRHRQA EAEGEGWEYA SLFGWKFHLE
1110 1120 1130 1140 1150
YRKTDAFRRR RWRRRMEPLE KTGPAAVFAL EGALGGVMDD KSEDSMSVST
1160 1170 1180 1190 1200
LSFGVNRPTI SCIFDYGNRY HLRCYMYQAR DLAAMDKDSF SDPYAIVSFL
1210 1220 1230 1240 1250
HQSQKTVVVK NTLNPTWDQT LIFYEIEIFG EPATVAEQPP SIVVELYDHD
1260 1270 1280 1290 1300
TYGADEFMGR CICQPSLERM PRLAWFPLTR GSQPSGELLA SFELIQREKP
1310 1320 1330 1340 1350
AIHHIPGFEV QETSRILDES EDTDLPYPPP QREANIYMVP QNIKPALQRT
1360 1370 1380 1390 1400
AIEILAWGLR NMKSYQLANI SSPSLVVECG GQTVQSCVIR NLRKNPNFDI
1410 1420 1430 1440 1450
CTLFMEVMLP REELYCPPIT VKVIDNRQFG RRPVVGQCTI RSLESFLCDP
1460 1470 1480 1490 1500
YSAESPSPQG GPDDVSLLSP GEDVLIDIDD KEPLIPIQEE EFIDWWSKFF
1510 1520 1530 1540 1550
ASIGEREKCG SYLEKDFDTL KVYDTQLENV EAFEGLSDFC NTFKLYRGKT
1560 1570 1580 1590 1600
QEETEDPSVI GEFKGLFKIY PLPEDPAIPM PPRQFHQLAA QGPQECLVRI
1610 1620 1630 1640 1650
YIVRAFGLQP KDPNGKCDPY IKISIGKKSV SDQDNYIPCT LEPVFGKMFE
1660 1670 1680 1690 1700
LTCTLPLEKD LKITLYDYDL LSKDEKIGET VVDLENRLLS KFGARCGLPQ
1710 1720 1730 1740 1750
TYCVSGPNQW RDQLRPSQLL HLFCQQHRVK APVYRTDRVM FQDKEYSIEE
1760 1770 1780 1790 1800
IEAGRIPNPH LGPVEERLAL HVLQQQGLVP EHVESRPLYS PLQPDIEQGK
1810 1820 1830 1840 1850
LQMWVDLFPK ALGRPGPPFN ITPRRARRFF LRCIIWNTRD VILDDLSLTG
1860 1870 1880 1890 1900
EKMSDIYVKG WMIGFEEHKQ KTDVHYRSLG GEGNFNWRFI FPFDYLPAEQ
1910 1920 1930 1940 1950
VCTIAKKDAF WRLDKTESKI PARVVFQIWD NDKFSFDDFL GSLQLDLNRM
1960 1970 1980 1990 2000
PKPAKTAKKC SLDQLDDAFH PEWFVSLFEQ KTVKGWWPCV AEEGEKKILA
2010 2020 2030 2040 2050
GKLEMTLEIV AESEHEERPA GQGRDEPNMN PKLEDPRRPD TSFLWFTSPY
2060 2070 2080 2090
KTMKFILWRR FRWAIILFII LFILLLFLAI FIYAFPNYAA MKLVKPFS
The sequence of this isoform differs from the canonical sequence as follows:
1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
494-508: EEPAGAVKPSKASDL → V
1470-1470: Q → QLADGLSSLAPTNTASPPSSPH
10 20 30 40 50
MLCCLLVRAS NLPSAKKDRR SDPVASLTFR GVKKRTKVIK NSVNPVWNEG
60 70 80 90 100
FEWDLKGIPL DQGSELHVVV KDHETMGRNR FLGEAKVPLR EVLATPSLSA
110 120 130 140 150
SFNAPLLDTK KQPTGASLVL QVSYTPLPGA VPLFPPPTPL EPSPTLPDLD
160 170 180 190 200
VVADTGGEED TEDQGLTGDE AEPFLDQSGG PGAPTTPRKL PSRPPPHYPG
210 220 230 240 250
IKRKRSAPTS RKLLSDKPQD FQIRVQVIEG RQLPGVNIKP VVKVTAAGQT
260 270 280 290 300
KRTRIHKGNS PLFNETLFFN LFDSPGELFD EPIFITVVDS RSLRTDALLG
310 320 330 340 350
EFRMDVGTIY REPRHAYLRK WLLLSDPDDF SAGARGYLKT SLCVLGPGDE
360 370 380 390 400
APLERKDPSE DKEDIESNLL RPTGVALRGA HFCLKVFRAE DLPQMDDAVM
410 420 430 440 450
DNVKQIFGFE SNKKNLVDPF VEVSFAGKML CSKILEKTAN PQWNQNITLP
460 470 480 490 500
AMFPSMCEKM RIRIIDWDRL THNDIVATTY LSMSKISAPG GEIEVDDYLG
510 520 530 540 550
FLPTFGPCYI NLYGSPREFT GFPDPYTELN TGKGEGVAYR GRLLLSLETK
560 570 580 590 600
LVEHSEQKVE DLPADDILRV EKYLRRRKYS LFAAFYSATM LQDVDDAIQF
610 620 630 640 650
EVSIGNYGNK FDMTCLPLAS TTQYSRAVFD GCHYYYLPWG NVKPVVVLSS
660 670 680 690 700
YWEDISHRIE TQNQLLGIAD RLEAGLEQVH LALKAQCSTE DVDSLVAQLT
710 720 730 740 750
DELIAGCSQP LGDIHETPSA THLDQYLYQL RTHHLSQITE AALALKLGHS
760 770 780 790 800
ELPAALEQAE DWLLRLRALA EEPQNSLPDI VIWMLQGDKR VAYQRVPAHQ
810 820 830 840 850
VLFSRRGANY CGKNCGKLQT IFLKYPMEKV PGARMPVQIR VKLWFGLSVD
860 870 880 890 900
EKEFNQFAEG KLSVFAETYE NETKLALVGN WGTTGLTYPK FSDVTGKIKL
910 920 930 940 950
PKDSFRPSAG WTWAGDWFVC PEKTLLHDMD AGHLSFVEEV FENQTRLPGG
960 970 980 990 1000
QWIYMSDNYT DVNGEKVLPK DDIECPLGWK WEDEEWSTDL NRAVDEQGWE
1010 1020 1030 1040 1050
YSITIPPERK PKHWVPAEKM YYTHRRRRWV RLRRRDLSQM EALKRHRQAE
1060 1070 1080 1090 1100
AEGEGWEYAS LFGWKFHLEY RKTDAFRRRR WRRRMEPLEK TGPAAVFALE
1110 1120 1130 1140 1150
GALGGVMDDK SEDSMSVSTL SFGVNRPTIS CIFDYGNRYH LRCYMYQARD
1160 1170 1180 1190 1200
LAAMDKDSFS DPYAIVSFLH QSQKTVVVKN TLNPTWDQTL IFYEIEIFGE
1210 1220 1230 1240 1250
PATVAEQPPS IVVELYDHDT YGADEFMGRC ICQPSLERMP RLAWFPLTRG
1260 1270 1280 1290 1300
SQPSGELLAS FELIQREKPA IHHIPGFEVQ ETSRILDESE DTDLPYPPPQ
1310 1320 1330 1340 1350
REANIYMVPQ NIKPALQRTA IEILAWGLRN MKSYQLANIS SPSLVVECGG
1360 1370 1380 1390 1400
QTVQSCVIRN LRKNPNFDIC TLFMEVMLPR EELYCPPITV KVIDNRQFGR
1410 1420 1430 1440 1450
RPVVGQCTIR SLESFLCDPY SAESPSPQGG PDDVSLLSPG EDVLIDIDDK
1460 1470 1480 1490 1500
EPLIPIQLAD GLSSLAPTNT ASPPSSPHEE EFIDWWSKFF ASIGEREKCG
1510 1520 1530 1540 1550
SYLEKDFDTL KVYDTQLENV EAFEGLSDFC NTFKLYRGKT QEETEDPSVI
1560 1570 1580 1590 1600
GEFKGLFKIY PLPEDPAIPM PPRQFHQLAA QGPQECLVRI YIVRAFGLQP
1610 1620 1630 1640 1650
KDPNGKCDPY IKISIGKKSV SDQDNYIPCT LEPVFGKMFE LTCTLPLEKD
1660 1670 1680 1690 1700
LKITLYDYDL LSKDEKIGET VVDLENRLLS KFGARCGLPQ TYCVSGPNQW
1710 1720 1730 1740 1750
RDQLRPSQLL HLFCQQHRVK APVYRTDRVM FQDKEYSIEE IEAGRIPNPH
1760 1770 1780 1790 1800
LGPVEERLAL HVLQQQGLVP EHVESRPLYS PLQPDIEQGK LQMWVDLFPK
1810 1820 1830 1840 1850
ALGRPGPPFN ITPRRARRFF LRCIIWNTRD VILDDLSLTG EKMSDIYVKG
1860 1870 1880 1890 1900
WMIGFEEHKQ KTDVHYRSLG GEGNFNWRFI FPFDYLPAEQ VCTIAKKDAF
1910 1920 1930 1940 1950
WRLDKTESKI PARVVFQIWD NDKFSFDDFL GSLQLDLNRM PKPAKTAKKC
1960 1970 1980 1990 2000
SLDQLDDAFH PEWFVSLFEQ KTVKGWWPCV AEEGEKKILA GKLEMTLEIV
2010 2020 2030 2040 2050
AESEHEERPA GQGRDEPNMN PKLEDPRRPD TSFLWFTSPY KTMKFILWRR
2060 2070 2080
FRWAIILFII LFILLLFLAI FIYAFPNYAA MKLVKPFS
The sequence of this isoform differs from the canonical sequence as follows:
1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT
494-508: EEPAGAVKPSKASDL → V
1470-1470: Q → QLADGLSSLAPTNTASPPSSPH
10 20 30 40 50
MLCCLLVRAS NLPSAKKDRR SDPVASLTFR GVKKRTKVIK NSVNPVWNEG
60 70 80 90 100
FEWDLKGIPL DQGSELHVVV KDHETMGRNR FLGEAKVPLR EVLATPSLSA
110 120 130 140 150
SFNAPLLDTK KQPTGASLVL QVSYTPLPGA VPLFPPPTPL EPSPTLPDLD
160 170 180 190 200
VVAGGGQSRA ETWSLLSDST MDTRYSGKKW PAPTDTGGEE DTEDQGLTGD
210 220 230 240 250
EAEPFLDQSG GPGAPTTPRK LPSRPPPHYP GIKRKRSAPT SRKLLSDKPQ
260 270 280 290 300
DFQIRVQVIE GRQLPGVNIK PVVKVTAAGQ TKRTRIHKGN SPLFNETLFF
310 320 330 340 350
NLFDSPGELF DEPIFITVVD SRSLRTDALL GEFRMDVGTI YREPRHAYLR
360 370 380 390 400
KWLLLSDPDD FSAGARGYLK TSLCVLGPGD EAPLERKDPS EDKEDIESNL
410 420 430 440 450
LRPTGVALRG AHFCLKVFRA EDLPQMDDAV MDNVKQIFGF ESNKKNLVDP
460 470 480 490 500
FVEVSFAGKM LCSKILEKTA NPQWNQNITL PAMFPSMCEK MRIRIIDWDR
510 520 530 540 550
LTHNDIVATT YLSMSKISAP GGEIEVDDYL GFLPTFGPCY INLYGSPREF
560 570 580 590 600
TGFPDPYTEL NTGKGEGVAY RGRLLLSLET KLVEHSEQKV EDLPADDILR
610 620 630 640 650
VEKYLRRRKY SLFAAFYSAT MLQDVDDAIQ FEVSIGNYGN KFDMTCLPLA
660 670 680 690 700
STTQYSRAVF DGCHYYYLPW GNVKPVVVLS SYWEDISHRI ETQNQLLGIA
710 720 730 740 750
DRLEAGLEQV HLALKAQCST EDVDSLVAQL TDELIAGCSQ PLGDIHETPS
760 770 780 790 800
ATHLDQYLYQ LRTHHLSQIT EAALALKLGH SELPAALEQA EDWLLRLRAL
810 820 830 840 850
AEEPQNSLPD IVIWMLQGDK RVAYQRVPAH QVLFSRRGAN YCGKNCGKLQ
860 870 880 890 900
TIFLKYPMEK VPGARMPVQI RVKLWFGLSV DEKEFNQFAE GKLSVFAETY
910 920 930 940 950
ENETKLALVG NWGTTGLTYP KFSDVTGKIK LPKDSFRPSA GWTWAGDWFV
960 970 980 990 1000
CPEKTLLHDM DAGHLSFVEE VFENQTRLPG GQWIYMSDNY TDVNGEKVLP
1010 1020 1030 1040 1050
KDDIECPLGW KWEDEEWSTD LNRAVDEQGW EYSITIPPER KPKHWVPAEK
1060 1070 1080 1090 1100
MYYTHRRRRW VRLRRRDLSQ MEALKRHRQA EAEGEGWEYA SLFGWKFHLE
1110 1120 1130 1140 1150
YRKTDAFRRR RWRRRMEPLE KTGPAAVFAL EGALGGVMDD KSEDSMSVST
1160 1170 1180 1190 1200
LSFGVNRPTI SCIFDYGNRY HLRCYMYQAR DLAAMDKDSF SDPYAIVSFL
1210 1220 1230 1240 1250
HQSQKTVVVK NTLNPTWDQT LIFYEIEIFG EPATVAEQPP SIVVELYDHD
1260 1270 1280 1290 1300
TYGADEFMGR CICQPSLERM PRLAWFPLTR GSQPSGELLA SFELIQREKP
1310 1320 1330 1340 1350
AIHHIPGFEV QETSRILDES EDTDLPYPPP QREANIYMVP QNIKPALQRT
1360 1370 1380 1390 1400
AIEILAWGLR NMKSYQLANI SSPSLVVECG GQTVQSCVIR NLRKNPNFDI
1410 1420 1430 1440 1450
CTLFMEVMLP REELYCPPIT VKVIDNRQFG RRPVVGQCTI RSLESFLCDP
1460 1470 1480 1490 1500
YSAESPSPQG GPDDVSLLSP GEDVLIDIDD KEPLIPIQLA DGLSSLAPTN
1510 1520 1530 1540 1550
TASPPSSPHE EEFIDWWSKF FASIGEREKC GSYLEKDFDT LKVYDTQLEN
1560 1570 1580 1590 1600
VEAFEGLSDF CNTFKLYRGK TQEETEDPSV IGEFKGLFKI YPLPEDPAIP
1610 1620 1630 1640 1650
MPPRQFHQLA AQGPQECLVR IYIVRAFGLQ PKDPNGKCDP YIKISIGKKS
1660 1670 1680 1690 1700
VSDQDNYIPC TLEPVFGKMF ELTCTLPLEK DLKITLYDYD LLSKDEKIGE
1710 1720 1730 1740 1750
TVVDLENRLL SKFGARCGLP QTYCVSGPNQ WRDQLRPSQL LHLFCQQHRV
1760 1770 1780 1790 1800
KAPVYRTDRV MFQDKEYSIE EIEAGRIPNP HLGPVEERLA LHVLQQQGLV
1810 1820 1830 1840 1850
PEHVESRPLY SPLQPDIEQG KLQMWVDLFP KALGRPGPPF NITPRRARRF
1860 1870 1880 1890 1900
FLRCIIWNTR DVILDDLSLT GEKMSDIYVK GWMIGFEEHK QKTDVHYRSL
1910 1920 1930 1940 1950
GGEGNFNWRF IFPFDYLPAE QVCTIAKKDA FWRLDKTESK IPARVVFQIW
1960 1970 1980 1990 2000
DNDKFSFDDF LGSLQLDLNR MPKPAKTAKK CSLDQLDDAF HPEWFVSLFE
2010 2020 2030 2040 2050
QKTVKGWWPC VAEEGEKKIL AGKLEMTLEI VAESEHEERP AGQGRDEPNM
2060 2070 2080 2090 2100
NPKLEDPRRP DTSFLWFTSP YKTMKFILWR RFRWAIILFI ILFILLLFLA
2110
IFIYAFPNYA AMKLVKPFS
The sequence of this isoform differs from the canonical sequence as follows:
1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR
10 20 30 40 50
MLCCLLVRAS NLPSAKKDRR SDPVASLTFR GVKKRTKVIK NSVNPVWNEG
60 70 80 90 100
FEWDLKGIPL DQGSELHVVV KDHETMGRNR FLGEAKVPLR EVLATPSLSA
110 120 130 140 150
SFNAPLLDTK KQPTGASLVL QVSYTPLPGA VPLFPPPTPL EPSPTLPDLD
160 170 180 190 200
VVADTGGEED TEDQGLTGDE AEPFLDQSGG PGAPTTPRKL PSRPPPHYPG
210 220 230 240 250
IKRKRSAPTS RKLLSDKPQD FQIRVQVIEG RQLPGVNIKP VVKVTAAGQT
260 270 280 290 300
KRTRIHKGNS PLFNETLFFN LFDSPGELFD EPIFITVVDS RSLRTDALLG
310 320 330 340 350
EFRMDVGTIY REPRHAYLRK WLLLSDPDDF SAGARGYLKT SLCVLGPGDE
360 370 380 390 400
APLERKDPSE DKEDIESNLL RPTGVALRGA HFCLKVFRAE DLPQMDDAVM
410 420 430 440 450
DNVKQIFGFE SNKKNLVDPF VEVSFAGKML CSKILEKTAN PQWNQNITLP
460 470 480 490 500
AMFPSMCEKM RIRIIDWDRL THNDIVATTY LSMSKISAPG GEIEEEPAGA
510 520 530 540 550
VKPSKASDLD DYLGFLPTFG PCYINLYGSP REFTGFPDPY TELNTGKGEG
560 570 580 590 600
VAYRGRLLLS LETKLVEHSE QKVEDLPADD ILRVEKYLRR RKYSLFAAFY
610 620 630 640 650
SATMLQDVDD AIQFEVSIGN YGNKFDMTCL PLASTTQYSR AVFDGCHYYY
660 670 680 690 700
LPWGNVKPVV VLSSYWEDIS HRIETQNQLL GIADRLEAGL EQVHLALKAQ
710 720 730 740 750
CSTEDVDSLV AQLTDELIAG CSQPLGDIHE TPSATHLDQY LYQLRTHHLS
760 770 780 790 800
QITEAALALK LGHSELPAAL EQAEDWLLRL RALAEEPQNS LPDIVIWMLQ
810 820 830 840 850
GDKRVAYQRV PAHQVLFSRR GANYCGKNCG KLQTIFLKYP MEKVPGARMP
860 870 880 890 900
VQIRVKLWFG LSVDEKEFNQ FAEGKLSVFA ETYENETKLA LVGNWGTTGL
910 920 930 940 950
TYPKFSDVTG KIKLPKDSFR PSAGWTWAGD WFVCPEKTLL HDMDAGHLSF
960 970 980 990 1000
VEEVFENQTR LPGGQWIYMS DNYTDVNGEK VLPKDDIECP LGWKWEDEEW
1010 1020 1030 1040 1050
STDLNRAVDE QGWEYSITIP PERKPKHWVP AEKMYYTHRR RRWVRLRRRD
1060 1070 1080 1090 1100
LSQMEALKRH RQAEAEGEGW EYASLFGWKF HLEYRKTDAF RRRRWRRRME
1110 1120 1130 1140 1150
PLEKTGPAAV FALEGALGGV MDDKSEDSMS VSTLSFGVNR PTISCIFDYG
1160 1170 1180 1190 1200
NRYHLRCYMY QARDLAAMDK DSFSDPYAIV SFLHQSQKTV VVKNTLNPTW
1210 1220 1230 1240 1250
DQTLIFYEIE IFGEPATVAE QPPSIVVELY DHDTYGADEF MGRCICQPSL
1260 1270 1280 1290 1300
ERMPRLAWFP LTRGSQPSGE LLASFELIQR EKPAIHHIPG FEVQETSRIL
1310 1320 1330 1340 1350
DESEDTDLPY PPPQREANIY MVPQNIKPAL QRTAIEILAW GLRNMKSYQL
1360 1370 1380 1390 1400
ANISSPSLVV ECGGQTVQSC VIRNLRKNPN FDICTLFMEV MLPREELYCP
1410 1420 1430 1440 1450
PITVKVIDNR QFGRRPVVGQ CTIRSLESFL CDPYSAESPS PQGGPDDVSL
1460 1470 1480 1490 1500
LSPGEDVLID IDDKEPLIPI QEEEFIDWWS KFFASIGERE KCGSYLEKDF
1510 1520 1530 1540 1550
DTLKVYDTQL ENVEAFEGLS DFCNTFKLYR GKTQEETEDP SVIGEFKGLF
1560 1570 1580 1590 1600
KIYPLPEDPA IPMPPRQFHQ LAAQGPQECL VRIYIVRAFG LQPKDPNGKC
1610 1620 1630 1640 1650
DPYIKISIGK KSVSDQDNYI PCTLEPVFGK MFELTCTLPL EKDLKITLYD
1660 1670 1680 1690 1700
YDLLSKDEKI GETVVDLENR LLSKFGARCG LPQTYCVSGP NQWRDQLRPS
1710 1720 1730 1740 1750
QLLHLFCQQH RVKAPVYRTD RVMFQDKEYS IEEIEAGRIP NPHLGPVEER
1760 1770 1780 1790 1800
LALHVLQQQG LVPEHVESRP LYSPLQPDIE QGKLQMWVDL FPKALGRPGP
1810 1820 1830 1840 1850
PFNITPRRAR RFFLRCIIWN TRDVILDDLS LTGEKMSDIY VKGWMIGFEE
1860 1870 1880 1890 1900
HKQKTDVHYR SLGGEGNFNW RFIFPFDYLP AEQVCTIAKK DAFWRLDKTE
1910 1920 1930 1940 1950
SKIPARVVFQ IWDNDKFSFD DFLGSLQLDL NRMPKPAKTA KKCSLDQLDD
1960 1970 1980 1990 2000
AFHPEWFVSL FEQKTVKGWW PCVAEEGEKK ILAGKLEMTL EIVAESEHEE
2010 2020 2030 2040 2050
RPAGQGRDEP NMNPKLEDPR RPDTSFLWFT SPYKTMKFIL WRRFRWAIIL
2060 2070 2080
FIILFILLLF LAIFIYAFPN YAAMKLVKPF S
The sequence of this isoform differs from the canonical sequence as follows:
494-508: EEPAGAVKPSKASDL → V
1934-1968: KPAKTAKKCSLDQLDDAFHPEWFVSLFEQKTVKGW → SSASSSRPPRPDCPARVGRQTDGPAHTPRVANMEL
1969-2080: Missing.
10 20 30 40 50
MLRVFILYAE NVHTPDTDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF
60 70 80 90 100
EWDLKGIPLD QGSELHVVVK DHETMGRNRF LGEAKVPLRE VLATPSLSAS
110 120 130 140 150
FNAPLLDTKK QPTGASLVLQ VSYTPLPGAV PLFPPPTPLE PSPTLPDLDV
160 170 180 190 200
VADTGGEEDT EDQGLTGDEA EPFLDQSGGP GAPTTPRKLP SRPPPHYPGI
210 220 230 240 250
KRKRSAPTSR KLLSDKPQDF QIRVQVIEGR QLPGVNIKPV VKVTAAGQTK
260 270 280 290 300
RTRIHKGNSP LFNETLFFNL FDSPGELFDE PIFITVVDSR SLRTDALLGE
310 320 330 340 350
FRMDVGTIYR EPRHAYLRKW LLLSDPDDFS AGARGYLKTS LCVLGPGDEA
360 370 380 390 400
PLERKDPSED KEDIESNLLR PTGVALRGAH FCLKVFRAED LPQMDDAVMD
410 420 430 440 450
NVKQIFGFES NKKNLVDPFV EVSFAGKMLC SKILEKTANP QWNQNITLPA
460 470 480 490 500
MFPSMCEKMR IRIIDWDRLT HNDIVATTYL SMSKISAPGG EIEVDDYLGF
510 520 530 540 550
LPTFGPCYIN LYGSPREFTG FPDPYTELNT GKGEGVAYRG RLLLSLETKL
560 570 580 590 600
VEHSEQKVED LPADDILRVE KYLRRRKYSL FAAFYSATML QDVDDAIQFE
610 620 630 640 650
VSIGNYGNKF DMTCLPLAST TQYSRAVFDG CHYYYLPWGN VKPVVVLSSY
660 670 680 690 700
WEDISHRIET QNQLLGIADR LEAGLEQVHL ALKAQCSTED VDSLVAQLTD
710 720 730 740 750
ELIAGCSQPL GDIHETPSAT HLDQYLYQLR THHLSQITEA ALALKLGHSE
760 770 780 790 800
LPAALEQAED WLLRLRALAE EPQNSLPDIV IWMLQGDKRV AYQRVPAHQV
810 820 830 840 850
LFSRRGANYC GKNCGKLQTI FLKYPMEKVP GARMPVQIRV KLWFGLSVDE
860 870 880 890 900
KEFNQFAEGK LSVFAETYEN ETKLALVGNW GTTGLTYPKF SDVTGKIKLP
910 920 930 940 950
KDSFRPSAGW TWAGDWFVCP EKTLLHDMDA GHLSFVEEVF ENQTRLPGGQ
960 970 980 990 1000
WIYMSDNYTD VNGEKVLPKD DIECPLGWKW EDEEWSTDLN RAVDEQGWEY
1010 1020 1030 1040 1050
SITIPPERKP KHWVPAEKMY YTHRRRRWVR LRRRDLSQME ALKRHRQAEA
1060 1070 1080 1090 1100
EGEGWEYASL FGWKFHLEYR KTDAFRRRRW RRRMEPLEKT GPAAVFALEG
1110 1120 1130 1140 1150
ALGGVMDDKS EDSMSVSTLS FGVNRPTISC IFDYGNRYHL RCYMYQARDL
1160 1170 1180 1190 1200
AAMDKDSFSD PYAIVSFLHQ SQKTVVVKNT LNPTWDQTLI FYEIEIFGEP
1210 1220 1230 1240 1250
ATVAEQPPSI VVELYDHDTY GADEFMGRCI CQPSLERMPR LAWFPLTRGS
1260 1270 1280 1290 1300
QPSGELLASF ELIQREKPAI HHIPGFEVQE TSRILDESED TDLPYPPPQR
1310 1320 1330 1340 1350
EANIYMVPQN IKPALQRTAI EILAWGLRNM KSYQLANISS PSLVVECGGQ
1360 1370 1380 1390 1400
TVQSCVIRNL RKNPNFDICT LFMEVMLPRE ELYCPPITVK VIDNRQFGRR
1410 1420 1430 1440 1450
PVVGQCTIRS LESFLCDPYS AESPSPQGGP DDVSLLSPGE DVLIDIDDKE
1460 1470 1480 1490 1500
PLIPIQEEEF IDWWSKFFAS IGEREKCGSY LEKDFDTLKV YDTQLENVEA
1510 1520 1530 1540 1550
FEGLSDFCNT FKLYRGKTQE ETEDPSVIGE FKGLFKIYPL PEDPAIPMPP
1560 1570 1580 1590 1600
RQFHQLAAQG PQECLVRIYI VRAFGLQPKD PNGKCDPYIK ISIGKKSVSD
1610 1620 1630 1640 1650
QDNYIPCTLE PVFGKMFELT CTLPLEKDLK ITLYDYDLLS KDEKIGETVV
1660 1670 1680 1690 1700
DLENRLLSKF GARCGLPQTY CVSGPNQWRD QLRPSQLLHL FCQQHRVKAP
1710 1720 1730 1740 1750
VYRTDRVMFQ DKEYSIEEIE AGRIPNPHLG PVEERLALHV LQQQGLVPEH
1760 1770 1780 1790 1800
VESRPLYSPL QPDIEQGKLQ MWVDLFPKAL GRPGPPFNIT PRRARRFFLR
1810 1820 1830 1840 1850
CIIWNTRDVI LDDLSLTGEK MSDIYVKGWM IGFEEHKQKT DVHYRSLGGE
1860 1870 1880 1890 1900
GNFNWRFIFP FDYLPAEQVC TIAKKDAFWR LDKTESKIPA RVVFQIWDND
1910 1920 1930 1940 1950
KFSFDDFLGS LQLDLNRMPS SASSSRPPRP DCPARVGRQT DGPAHTPRVA
NMEL
<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_057834 | 52 | W → R in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057835 | 67 | V → D in MMD1 and LGMDR2; Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057836 | 84 | A → V1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057837 | 155 | G → R in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024853 | 170 | A → E3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024854 | 189 | L → V2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057838 | 234 | G → E in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024855 | 253 | R → W Found in patients with isolated hyperCKemia. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024856 | 266 | L → P in pseudometabolic myopathy. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057839 | 284 | I → T in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024857 | 299 | G → E in MMD1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057840 | 299 | G → R in LGMDR2 and proximodistal myopathy. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057841 | 299 | G → W in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057842 | 335 | G → A1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057843 | 340 | S → R in proximodistal myopathy. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057844 | 374 | V → L2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057845 | 386 – 390 | FRAED → Y in MMD1. 1 Publication Manual assertion based on experiment ini
| 5 | |
Natural variantiVAR_057846 | 389 | E → Q in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057847 | 390 | D → N1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057848 | 426 | G → R in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057849 | 426 | G → V in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024858 | 456 | C → W in MMD1. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057850 | 519 | G → R in MMD1. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024859 | 555 | R → W in LGMDR2 and MMD1; also found in patients with isolated hyperCKemia. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057851 | 618 | G → R in MMD1 and LGMDR2. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057852 | 621 | G → R in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057853 | 625 | D → Y in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057854 | 731 | P → R in LGMDR2. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_012308 | 791 | P → R in MMD1 and LGMDR2. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_057855 | 819 | R → Q1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_049055 | 834 | I → V. Corresponds to variant dbSNP:rs34671418Ensembl. | 1 | |
Natural variantiVAR_057856 | 930 | W → C in LGMDR2; unknown pathological significance. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_024860 | 959 | R → W in MMD1 and LGMDR2. 2 Publications Manual assertion based on experiment ini
|