O75923 (DYSF_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 127.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Dysferlin Alternative name(s): Dystrophy-associated fer-1-like protein Fer-1-like protein 1 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 2080 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Key calcium ion sensor involved in the Ca2+-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress By similarity. |
| Subunit structure | 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 CAV3 and PARVB. Interacts with AHNAK; the interaction is direct and Ca2+-independent. Interacts with AHNAK2; the interaction is direct and Ca2+-independent. Ref.15 Ref.18 Ref.20 |
| Subcellular location | Cell membrane › sarcolemma; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; 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. Ref.10 Ref.12 Ref.13 Ref.18 Ref.19 Ref.20 Ref.21 |
| Tissue specificity | Expressed in skeletal muscle, myoblast, myotube and in the syncytiotrophoblast (STB) of the placenta (at protein level). Highly expressed in skeletal muscle. Also found in heart, brain, spleen, intestine, placenta and at lower levels in liver, lung, kidney and pancreas. Ref.2 Ref.10 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 |
| Developmental stage | Expression in limb tissue from 5-6 weeks embryos; persists throughout development. Ref.10 |
| Domain | The C2 domain 1 associates with lipid membranes in a calcium-dependent manner. |
| Involvement in disease | Limb-girdle muscular dystrophy 2B (LGMD2B) [MIM:253601]: An autosomal recessive degenerative myopathy characterized by weakness and atrophy starting in the proximal pelvifemoral muscles, with onset in the late teens or later, massive elevation of serum creatine kinase levels and slow progression. Scapular muscle involvement is minor and not present at onset. Upper limb girdle involvement follows some years after the onset in lower limbs. Miyoshi muscular dystrophy 1 (MMD1) [MIM:254130]: A late-onset muscular dystrophy involving the distal lower limb musculature. It is characterized by weakness that initially affects the gastrocnemius muscle during early adulthood. Distal myopathy with anterior tibial onset (DMAT) [MIM:606768]: Onset of the disorder is between 14 and 28 years of age and the anterior tibial muscles are the first muscle group to be involved. Inheritance is autosomal recessive. |
| Sequence similarities | Belongs to the ferlin family. Contains 5 C2 domains. |
| Sequence caution | The sequence BAG51981.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA07603.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA07603.1 differs from that shown. Reason: Frameshift at position 1972. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Cytoplasmic vesicle Membrane |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Disease | Disease mutation Limb-girdle muscular dystrophy |
| Domain | Repeat Signal-anchor Transmembrane Transmembrane helix |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | plasma membrane repair Inferred from electronic annotation. Source: Compara vesicle fusionInferred from electronic annotation. Source: Compara |
| Cellular_component | T-tubule Inferred from electronic annotation. Source: Compara cytoplasmic vesicle membraneInferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW lamellipodiumInferred from electronic annotation. Source: Compara plasma membraneTraceable author statement Ref.12. Source: ProtInc |
| Molecular_function | calcium-dependent phospholipid binding Inferred from mutant phenotype Ref.16. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ACTN2 | P35609 | 2 | EBI-2799016,EBI-77797 | |
| ALMS1 | Q8TCU4 | 3 | EBI-2799016,EBI-308651 | |
| APPL1 | Q9UKG1 | 2 | EBI-2799016,EBI-741243 | |
| CMYA5 | Q8N3K9 | 3 | EBI-2799016,EBI-2323272 | |
| DES | P17661 | 3 | EBI-2799016,EBI-1055572 | |
| DGKD | Q16760 | 3 | EBI-2799016,EBI-719333 | |
| DNAJB6 | O75190 | 2 | EBI-2799016,EBI-1053164 | |
| FLNC | Q14315 | 3 | EBI-2799016,EBI-489954 | |
| MYBPC1 | Q00872 | 4 | EBI-2799016,EBI-5652924 | |
| MYOM1 | P52179 | 3 | EBI-2799016,EBI-5353249 | |
| MYOM2 | P54296 | 3 | EBI-2799016,EBI-5357134 | |
| NEB | P20929 | 6 | EBI-2799016,EBI-1049657 | |
| OPTN | Q96CV9 | 3 | EBI-2799016,EBI-748974 | |
| SAMHD1 | Q9Y3Z3 | 2 | EBI-2799016,EBI-1054601 | |
| SGCG | Q13326 | 3 | EBI-2799016,EBI-5357343 | |
| SNAPIN | O95295 | 3 | EBI-2799016,EBI-296723 | |
| TTN | Q8WZ42 | 17 | EBI-2799016,EBI-681210 |
Alternative products
| This entry describes 15 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: O75923-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: O75923-2) The sequence of this isoform differs from the canonical sequence as follows: 152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT | ||||||
| Isoform 3 (identifier: O75923-3) The sequence of this isoform differs from the canonical sequence as follows: 494-508: EEPAGAVKPSKASDL → V | ||||||
| Isoform 4 (identifier: O75923-4) The sequence of this isoform differs from the canonical sequence as follows: 1470-1470: Q → QLADGLSSLAPTNTASPPSSPH | ||||||
| Isoform 5 (identifier: O75923-5) The sequence of this isoform differs from the canonical sequence as follows: 152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT 494-508: EEPAGAVKPSKASDL → V | ||||||
| Isoform 6 (identifier: O75923-6) The sequence of this isoform differs from the canonical sequence as follows: 494-508: EEPAGAVKPSKASDL → V 1470-1470: Q → QLADGLSSLAPTNTASPPSSPH | ||||||
| Isoform 7 (identifier: O75923-7) The sequence of this isoform differs from the canonical sequence as follows: 152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT 494-508: EEPAGAVKPSKASDL → V 1470-1470: Q → QLADGLSSLAPTNTASPPSSPH | ||||||
| Isoform 8 (identifier: O75923-8) The sequence of this isoform differs from the canonical sequence as follows: 1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR 152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT | ||||||
| Isoform 9 (identifier: O75923-9) The sequence of this isoform differs from the canonical sequence as follows: 1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR 494-508: EEPAGAVKPSKASDL → V | ||||||
| Isoform 10 (identifier: O75923-10) The sequence of this isoform differs from the canonical sequence as follows: 1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR 1470-1470: Q → QLADGLSSLAPTNTASPPSSPH | ||||||
| Isoform 11 (identifier: O75923-11) The sequence of this isoform differs from the canonical sequence as follows: 1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR 152-152: A → AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT 494-508: EEPAGAVKPSKASDL → V | ||||||
| Isoform 12 (identifier: O75923-12) The sequence of this isoform differs from the canonical sequence as follows: 1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR 494-508: EEPAGAVKPSKASDL → V 1470-1470: Q → QLADGLSSLAPTNTASPPSSPH | ||||||
| Isoform 13 (identifier: O75923-13) 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 | ||||||
| Isoform 14 (identifier: O75923-14) Also known as: Dysferlin_v1; DYSF_v1; The sequence of this isoform differs from the canonical sequence as follows: 1-29: MLRVFILYAENVHTPDTDISDAYCSAVFA → MLCCLLVRASNLPSAKKDRRSDPVASLTFR | ||||||
| Isoform 15 (identifier: O75923-15) The sequence of this isoform differs from the canonical sequence as follows: 494-508: EEPAGAVKPSKASDL → V 1934-1968: KPAKTAKKCSLDQLDDAFHPEWFVSLFEQKTVKGW → SSASSSRPPRPDCPARVGRQTDGPAHTPRVANMEL 1969-2080: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2080 | 2080 | Dysferlin | PRO_0000057879 | |||||
Regions | |||||||||
| Topological domain | 1 – 2046 | 2046 | Cytoplasmic Potential | ||||||
| Transmembrane | 2047 – 2067 | 21 | Helical; Potential | ||||||
| Topological domain | 2068 – 2080 | 13 | Extracellular Potential | ||||||
| Domain | 1 – 85 | 85 | C2 1 | ||||||
| Domain | 207 – 302 | 96 | C2 2 | ||||||
| Domain | 366 – 479 | 114 | C2 3 | ||||||
| Domain | 1139 – 1244 | 106 | C2 4 | ||||||
| Domain | 1565 – 1663 | 99 | C2 5 | ||||||
| Compositional bias | 1038 – 1097 | 60 | Arg-rich | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 29 | 29 | MLRVF…SAVFA → MLCCLLVRASNLPSAKKDRR SDPVASLTFR in isoform 8, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13 and isoform 14. | VSP_035924 | |||||
| Alternative sequence | 152 | 1 | A → AGGGQSRAETWSLLSDSTMD TRYSGKKWPAPT in isoform 2, isoform 5, isoform 7, isoform 8, isoform 11 and isoform 13. | VSP_035925 | |||||
| Alternative sequence | 494 – 508 | 15 | EEPAG…KASDL → V in isoform 3, isoform 5, isoform 6, isoform 7, isoform 9, isoform 11, isoform 12, isoform 13 and isoform 15. | VSP_035926 | |||||
| Alternative sequence | 1470 | 1 | Q → QLADGLSSLAPTNTASPPSS PH in isoform 4, isoform 6, isoform 7, isoform 10, isoform 12 and isoform 13. | VSP_035927 | |||||
| Alternative sequence | 1934 – 1968 | 35 | KPAKT…TVKGW → SSASSSRPPRPDCPARVGRQ TDGPAHTPRVANMEL in isoform 15. | VSP_035928 | |||||
| Alternative sequence | 1969 – 2080 | 112 | Missing in isoform 15. | VSP_035929 | |||||
| Natural variant | 52 | 1 | W → R in LGMD2B. Ref.40 | VAR_057834 | |||||
| Natural variant | 67 | 1 | V → D in MMD1 and LGMD2B; Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2. Ref.16 Ref.24 | VAR_057835 | |||||
| Natural variant | 84 | 1 | A → V. Ref.40 | VAR_057836 | |||||
| Natural variant | 155 | 1 | G → R in LGMD2B. Ref.40 | VAR_057837 | |||||
| Natural variant | 170 | 1 | A → E in MMD1, LGMD2B and isolated hyperCKemia. Ref.32 Ref.34 Ref.40 Corresponds to variant rs34999029 [ dbSNP | Ensembl ]. | VAR_024853 | |||||
| Natural variant | 189 | 1 | L → V. Ref.32 Ref.40 Corresponds to variant rs13407355 [ dbSNP | Ensembl ]. | VAR_024854 | |||||
| Natural variant | 234 | 1 | G → E in LGMD2B. Ref.40 | VAR_057838 | |||||
| Natural variant | 253 | 1 | R → W in isolated hyperCKemia. Ref.32 Ref.40 | VAR_024855 | |||||
| Natural variant | 266 | 1 | L → P in pseudometabolic myopathy. Ref.32 Ref.40 | VAR_024856 | |||||
| Natural variant | 284 | 1 | I → T in LGMD2B. Ref.40 | VAR_057839 | |||||
| Natural variant | 299 | 1 | G → E in MMD1. Ref.32 Ref.40 | VAR_024857 | |||||
| Natural variant | 299 | 1 | G → R in LGMD2B and proximodistal myopathy. Ref.35 Ref.39 Ref.40 | VAR_057840 | |||||
| Natural variant | 299 | 1 | G → W in MMD1. Ref.39 | VAR_057841 | |||||
| Natural variant | 335 | 1 | G → A. Ref.40 | VAR_057842 | |||||
| Natural variant | 340 | 1 | S → R in proximodistal myopathy. Ref.40 | VAR_057843 | |||||
| Natural variant | 374 | 1 | V → L in MMD1; uncertain pathogenicity. Ref.34 Ref.40 | VAR_057844 | |||||
| Natural variant | 386 – 390 | 5 | FRAED → Y in MMD1. | VAR_057845 | |||||
| Natural variant | 389 | 1 | E → Q in MMD1. Ref.31 | VAR_057846 | |||||
| Natural variant | 390 | 1 | D → N. Ref.40 | VAR_057847 | |||||
| Natural variant | 426 | 1 | G → R in MMD1. Ref.40 | VAR_057848 | |||||
| Natural variant | 426 | 1 | G → V in MMD1. Ref.28 | VAR_057849 | |||||
| Natural variant | 456 | 1 | C → W in MMD1. Ref.32 Ref.40 | VAR_024858 | |||||
| Natural variant | 519 | 1 | G → R in MMD1. Ref.38 | VAR_057850 | |||||
| Natural variant | 555 | 1 | R → W in isolated hyperCKemia, LGMD2B and MMD1. Ref.32 Ref.40 | VAR_024859 | |||||
| Natural variant | 618 | 1 | G → R in MMD1 and LGMD2B. Ref.29 Ref.40 | VAR_057851 | |||||
| Natural variant | 621 | 1 | G → R in LGMD2B. Ref.34 | VAR_057852 | |||||
| Natural variant | 625 | 1 | D → Y in LGMD2B. Ref.38 | VAR_057853 | |||||
| Natural variant | 731 | 1 | P → R in LGMD2B. Ref.40 | VAR_057854 | |||||
| Natural variant | 791 | 1 | P → R in MMD1 and LGMD2B. Ref.13 Ref.36 | VAR_012308 | |||||
| Natural variant | 819 | 1 | R → Q. Ref.40 | VAR_057855 | |||||
| Natural variant | 834 | 1 | I → V. Corresponds to variant rs34671418 [ dbSNP | Ensembl ]. | VAR_049055 | |||||
| Natural variant | 930 | 1 | W → C in LGMD2B; uncetain pathogenicity. Ref.36 Ref.40 | VAR_057856 | |||||
| Natural variant | 959 | 1 | R → W in MMD1 and LGMD2B. Ref.27 Ref.34 | VAR_024860 | |||||
| Natural variant | 999 | 1 | W → C in MMD1. Ref.23 Ref.26 Corresponds to variant rs28937581 [ dbSNP | Ensembl ]. | VAR_057857 | |||||
| Natural variant | 1022 | 1 | R → Q in LGMD2B; uncertain pathogenicity. Ref.27 Ref.29 Ref.40 Corresponds to variant rs34211915 [ dbSNP | Ensembl ]. | VAR_024861 | |||||
| Natural variant | 1029 | 1 | P → L in MMD1. Ref.40 | VAR_057858 | |||||
| Natural variant | 1038 | 1 | R → Q in LGMD2B; uncertain pathogenicity. Ref.27 Ref.34 Ref.40 | VAR_024862 | |||||
| Natural variant | 1041 | 1 | R → C in MMD1. Ref.29 | VAR_057859 | |||||
| Natural variant | 1046 | 1 | R → H in MMD1; dbNP:28939700. Ref.25 Ref.32 Ref.40 Corresponds to variant rs28939700 [ dbSNP | Ensembl ]. | VAR_024863 | |||||
| Natural variant | 1065 | 1 | E → EAE. | VAR_024864 | |||||
| Natural variant | 1072 | 1 | A → P. Corresponds to variant rs34660230 [ dbSNP | Ensembl ]. | VAR_049056 | |||||
| Natural variant | 1096 | 1 | R → H. Corresponds to variant rs59915619 [ dbSNP | Ensembl ]. | VAR_061170 | |||||
| Natural variant | 1208 | 1 | I → M in LGMD2B. Ref.32 | VAR_024865 | |||||
| Natural variant | 1228 | 1 | L → P in LGMD2B. Ref.40 | VAR_057860 | |||||
| Natural variant | 1242 | 1 | R → H. Corresponds to variant rs2303603 [ dbSNP | Ensembl ]. | VAR_020308 | |||||
| Natural variant | 1276 | 1 | L → V in proximodistal myopathy. Ref.32 Ref.40 | VAR_024866 | |||||
| Natural variant | 1298 | 1 | I → V in MMD1 and LGMD2B. Ref.1 | VAR_012309 | |||||
| Natural variant | 1325 | 1 | I → M in a breast cancer sample; somatic mutation. Ref.37 | VAR_035893 | |||||
| Natural variant | 1325 | 1 | I → V. Ref.40 | VAR_057861 | |||||
| Natural variant | 1331 | 1 | R → L. Ref.27 Ref.32 Corresponds to variant rs61742872 [ dbSNP | Ensembl ]. | VAR_024867 | |||||
| Natural variant | 1335 | 1 | E → K in MMD1 and LGMD2B. Ref.27 Ref.29 Ref.34 | VAR_024868 | |||||
| Natural variant | 1341 | 1 | L → P in LGMD2B. Ref.35 | VAR_057862 | |||||
| Natural variant | 1349 | 1 | L → V in a breast cancer sample; somatic mutation. Ref.37 | VAR_035894 | |||||
| Natural variant | 1351 | 1 | N → S. Ref.32 | VAR_024869 | |||||
| Natural variant | 1361 | 1 | C → R in MMD1. Ref.29 | VAR_057863 | |||||
| Natural variant | 1505 | 1 | Y → C in LGMD2B. Ref.29 | VAR_057864 | |||||
| Natural variant | 1526 | 1 | K → T in LGMD2B. Ref.40 | VAR_057865 | |||||
| Natural variant | 1543 | 1 | G → D in LGMD2B. Ref.40 | VAR_057866 | |||||
| Natural variant | 1581 | 1 | R → H. Ref.26 | VAR_057867 | |||||
| Natural variant | 1662 | 1 | T → R in MMD1. Ref.29 | VAR_057868 | |||||
| Natural variant | 1678 | 1 | C → S in isolated hyperCKemia. Ref.34 | VAR_057869 | |||||
| Natural variant | 1679 | 1 | G → E in MMD1. Ref.26 | VAR_057870 | |||||
| Natural variant | 1693 | 1 | R → Q in MMD1. Ref.32 Ref.40 | VAR_024870 | |||||
| Natural variant | 1693 | 1 | R → W in MMD1. Ref.34 | VAR_057871 | |||||
| Natural variant | 1734 | 1 | E → G in LGMD2B. Ref.38 | VAR_057872 | |||||
| Natural variant | 1748 | 1 | E → V in proximodistal myopathy. Ref.32 Ref.40 | VAR_024871 | |||||
| Natural variant | 1768 | 1 | R → W in LGMD2B and proximodistal myopathy; uncetain pathogenicity. Ref.36 Ref.40 | VAR_057873 | |||||
| Natural variant | 1837 | 1 | D → N in MMD1. Ref.34 Ref.40 | VAR_057874 | |||||
| Natural variant | 1842 | 1 | G → D in MMD1. Ref.30 | VAR_057875 | |||||
| Natural variant | 1857 | 1 | H → R in MMD1. Ref.1 | VAR_012310 | |||||
| Natural variant | 1922 | 1 | L → P in MMD1. Ref.30 | VAR_057876 | |||||
| Natural variant | 1938 – 1939 | 2 | Missing in MMD1. | VAR_057877 | |||||
| Natural variant | 1942 | 1 | C → G in MMD1. Ref.34 | VAR_057878 | |||||
| Natural variant | 1967 | 1 | G → S. Ref.40 | VAR_057879 | |||||
| Natural variant | 1970 | 1 | P → S in LGMD2B. Ref.40 | VAR_057880 | |||||
| Natural variant | 2000 | 1 | R → Q in MMD1. Ref.25 | VAR_024872 | |||||
| Natural variant | 2042 | 1 | R → C in MMD1, LGMD2B and proximodistal myopathy. Ref.1 Ref.34 Ref.36 Ref.40 | VAR_012311 | |||||
| Natural variant | 2068 | 1 | P → L in MMD1. Ref.28 | VAR_057881 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. 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 LGMD2B VAL-1298 AND CYS-2042. Tissue: Skeletal muscle. |
| [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. |
| [3] | "Human dysferlin variants from alternative splicing: implications for dysferlin mutational screening and isoforms." Pramono Z.A.D., Kam S.Y., Ho M.F., Tan C.L., Lim C.C., See J.S.L., Lai P.S., Yee W.C. Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8; 9; 10; 11; 12 AND 13). |
| [4] | "Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K.Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "Spectrum of dysferlin transcripts in human skeletal muscle and blood." Pramono Z.A.D., Tan C.L., Lim C.C., See J.S.L., Seah I., Ho M.F., Yee W.C., Lai P.S. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 115-221 (ISOFORMS 2/5/7/8/11/13). |
| [7] | "A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B." Bashir R., Britton S., Strachan T., Keers S., Vafiadaki E., Lako M., Richard I., Marchand S., Bourg N., Argov Z., Sadeh M., Mahjneh I., Marconi G., Passos-Bueno M.R., de Sa Moreira E., Zatz M., Beckmann J.S., Bushby K.M.D. Nat. Genet. 20:37-42(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 569-2080 (ISOFORMS 1/2/3/5/8/9/11), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1471-1628 (ISOFORMS 1/2/3/5/8/9/11). Tissue: Placenta and Skeletal muscle. |
| [8] | "The nucleotide sequence of a long cDNA clone isolated from human spleen." Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 439-2080 (ISOFORM 15). Tissue: Spleen. |
| [9] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1497-2080 (ISOFORMS 1/2/3/4/5/6/7/8/9/10/11/12/13/14). Tissue: Mammary gland. |
| [10] | "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. |
| [11] | Erratum 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. 8:1141-1141(1999) |
| [12] | "Dysferlin is a surface membrane-associated protein that is absent in Miyoshi myopathy." Matsuda C., Aoki M., Hayashi Y.K., Ho M.F., Arahata K., Brown R.H. Jr. Neurology 53:1119-1122(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [13] | "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 LGMD2B ARG-791. |
| [14] | "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 DYSTAL MYOPATHY. |
| [15] | "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. |
| [16] | "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. |
| [17] | "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. |
| [18] | "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. |
| [19] | "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. |
| [20] | "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, TISSUE SPECIFICITY, MUTAGENESIS OF VAL-67, MASS SPECTROMETRY. |
| [21] | "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. |
| [22] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [23] | "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. |
| [24] | "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 LGMD2B ASP-67. |
| [25] | "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. Brown R.H. Jr.Neurology 57:271-278(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MMD1 HIS-1046 AND GLN-2000. |
| [26] | "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. Itoyama Y.Neurology 60:1799-1804(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MMD1 CYS-999 AND GLU-1679, VARIANT HIS-1581. |
| [27] | "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 LGMD2B TRP-959; GLN-1038 AND LYS-1335, VARIANTS GLN-1022; ALA-GLU-1065 INS AND LEU-1331. |
| [28] | "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. |
| [29] | "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 LGMD2B LYS-1335 AND CYS-1505, VARIANTS GLN-1022 AND ALA-GLU-1065 INS. |
| [30] | "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. |
| [31] | "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. |
| [32] | "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 ISOLATED HYPERCKEMIA GLU-170 AND TRP-253, VARIANTS LGMD2B 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. |
| [33] | Erratum 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., Levy N. Hum. Mutat. 26:592-592(2005) |
| [34] | "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 GLU-170; LEU-374; TRP-959; TRP-1693; ASN-1837 AND GLY-1942 AND CYS-2042, VARIANTS LGMD2B ARG-621; TRP-959; GLN-1038; LYS-1335 AND CYS-2042, VARIANT ISOLATED HYPERCKEMIA SER-1678. |
| [35] | "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 LGMD2B ARG-299 AND PRO-1341. |
| [36] | "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 LGMD2B ARG-791; CYS-930; TRP-1768 AND CYS-2042, VARIANT ALA-GLU-1065 INS. |
| [37] | "The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E.Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-1325 AND VAL-1349. |
| [38] | "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 LGMD2B TYR-625 AND GLY-1734, VARIANT MMD1 ARG-519. |
| [39] | "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 LGMD2B ARG-299, VARIANT MMD1 TRP-299. |
| [40] | "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. Levy N.Hum. Mutat. 30:E345-E375(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LGMD2B ARG-52; ARG-155; GLU-170; GLU-234; THR-284; TRP-555; ARG-618; ARG-731; CYS-930; GLN-1022; 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 ISOLATED HYPERCKEMIA 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-1038; VAL-1276; VAL-1325; ASN-1837 AND SER-1967. |
| + | Additional computationally mapped references. |
Web resources
| Leiden Muscular Dystrophy pages Dysferlin |
| GeneReviews |
| Wikipedia Dysferlin entry |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF075575 mRNA. Translation: AAC63519.1. DQ267935 mRNA. Translation: ABB89736.1. EU515155 mRNA. Translation: ACB12752.1. EU515156 mRNA. Translation: ACB12753.1. EU515157 mRNA. Translation: ACB12754.1. EU515158 mRNA. Translation: ACB12755.1. EU515159 mRNA. Translation: ACB12756.1. EU515160 mRNA. Translation: ACB12757.1. EU515161 mRNA. Translation: ACB12758.1. EU515162 mRNA. Translation: ACB12759.1. EU515163 mRNA. Translation: ACB12760.1. EU515164 mRNA. Translation: ACB12761.1. EU515165 mRNA. Translation: ACB12762.1. EU515166 mRNA. Translation: ACB12763.1. AC010147 Genomic DNA. Translation: AAY14954.1. AC104084 Genomic DNA. Translation: AAY24199.1. CH471053 Genomic DNA. Translation: EAW99763.1. DQ976379 Genomic DNA. Translation: ABI75150.1. AJ007670 mRNA. Translation: CAA07603.1. Sequence problems. AJ007973 Genomic DNA. Translation: CAA07800.1. AK074104 mRNA. Translation: BAB84930.1. AK074649 mRNA. Translation: BAG51981.1. Different initiation. |
| IPI | IPI00020210. IPI00793867. IPI00871702. IPI00890768. IPI00890779. IPI00908443. IPI00908579. IPI00908658. IPI00908764. IPI00908826. IPI00908936. IPI00910445. IPI00910624. IPI00911101. IPI00915417. |
| RefSeq | NP_001123927.1. NM_001130455.1. NP_001124448.1. NM_001130976.1. NP_001124449.1. NM_001130977.1. NP_001124450.1. NM_001130978.1. NP_001124451.1. NM_001130979.1. NP_001124452.1. NM_001130980.1. NP_001124453.1. NM_001130981.1. NP_001124454.1. NM_001130982.1. NP_001124455.1. NM_001130983.1. NP_001124456.1. NM_001130984.1. NP_001124457.1. NM_001130985.1. NP_001124458.1. NM_001130986.1. NP_001124459.1. NM_001130987.1. NP_003485.1. NM_003494.3. |
| UniGene | Hs.252180. |
3D structure databases | |
| ProteinModelPortal | O75923. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O75923. 44 interactions. |
PTM databases | |
| PhosphoSite | O75923. |
Proteomic databases | |
| PaxDb | O75923. |
| PRIDE | O75923. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000258104; ENSP00000258104; ENSG00000135636. ENST00000394120; ENSP00000377678; ENSG00000135636. ENST00000409366; ENSP00000386512; ENSG00000135636. ENST00000409582; ENSP00000386547; ENSG00000135636. ENST00000409651; ENSP00000386683; ENSG00000135636. ENST00000409744; ENSP00000386285; ENSG00000135636. ENST00000409762; ENSP00000387137; ENSG00000135636. ENST00000410020; ENSP00000386881; ENSG00000135636. ENST00000410041; ENSP00000386617; ENSG00000135636. ENST00000413539; ENSP00000407046; ENSG00000135636. ENST00000429174; ENSP00000398305; ENSG00000135636. |
| GeneID | 8291. |
| KEGG | hsa:8291. |
| UCSC | uc002sie.3. human. uc002sif.3. human. uc002sig.4. human. uc010fee.3. human. uc010fef.3. human. uc010feg.3. human. uc010feh.3. human. uc010fei.3. human. uc010fej.3. human. uc010fek.3. human. uc010fel.3. human. uc010fem.3. human. uc010fen.3. human. uc010feo.3. human. |
Organism-specific databases | |
| CTD | 8291. |
| GeneCards | GC02P071680. |
| HGNC | HGNC:3097. DYSF. |
| HPA | CAB002510. HPA017071. HPA021945. |
| MIM | 253601. phenotype. 254130. phenotype. 603009. gene. 606768. phenotype. |
| neXtProt | NX_O75923. |
| Orphanet | 268. Autosomal recessive limb-girdle muscular dystrophy type 2B. 199329. Congenital myopathy, Paradas type. 178400. Distal myopathy with anterior tibial onset. 45448. Miyoshi myopathy. |
| PharmGKB | PA27554. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG330124. |
| HOVERGEN | HBG018972. |
| OMA | KRHRQAE. |
| PhylomeDB | O75923. |
Gene expression databases | |
| ArrayExpress | O75923. |
| Bgee | O75923. |
| Genevestigator | O75923. |
| GermOnline | ENSG00000135636. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR012968. FerIin-domain. IPR012560. Ferlin_A-domain. IPR012561. Ferlin_B-domain. IPR010482. Peroxin/Dysferlin. IPR006614. Peroxin/Ferlin. [Graphical view] |
| Pfam | PF00168. C2. 7 hits. PF08165. FerA. 1 hit. PF08150. FerB. 1 hit. PF08151. FerI. 1 hit. PF06398. Pex24p. 1 hit. [Graphical view] |
| SMART | SM00239. C2. 7 hits. SM00694. DysFC. 2 hits. SM00693. DysFN. 2 hits. [Graphical view] |
| SUPFAM | SSF49562. C2_CaLB. 7 hits. |
| PROSITE | PS50004. C2. 5 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| GenomeRNAi | 8291. |
| NextBio | 31071. |
| SOURCE | Search... |
Entry information
| Entry name | DYSF_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O75923 Secondary accession number(s): B1PZ70 Q9UEN7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 2 Human chromosome 2: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
