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O75923 (DYSF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dysferlin
Alternative name(s):
Dystrophy-associated fer-1-like protein
Fer-1-like protein 1
Gene names
Name:DYSF
Synonyms:FER1L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2080 AA.
Sequence statusComplete.
Protein existenceEvidence 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 membranesarcolemma; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; Single-pass type II membrane protein By similarity. Cell membrane. 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 Ref.23

Tissue specificity

Expressed in skeletal muscle, myoblast, myotube and in the syncytiotrophoblast (STB) of the placenta (at protein level). Ubiquitous. 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 Ref.23

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. The C2 domain 1 seems to be largely unstructured in the absence of bound ligands. The C2 domain 1 from isoform 1 contains one high-affinity calcium binding site; calcium binding leads to a more ordered conformation and increases protein stability. The C2 domain 1 from isoform 14 does not bind calcium in the absence of bound phospholipid. Ref.23

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.13 Ref.25 Ref.28 Ref.30 Ref.33 Ref.35 Ref.36 Ref.37 Ref.39 Ref.40 Ref.41

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.13 Ref.16 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.39 Ref.40 Ref.41

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20802080Dysferlin
PRO_0000057879

Regions

Topological domain1 – 20462046Cytoplasmic Potential
Transmembrane2047 – 206721Helical; Potential
Topological domain2068 – 208013Extracellular Potential
Domain1 – 8585C2 1
Domain207 – 30296C2 2
Domain366 – 479114C2 3
Domain1139 – 1244106C2 4
Domain1565 – 166399C2 5
Compositional bias1038 – 109760Arg-rich

Sites

Metal binding181Calcium
Metal binding191Calcium; via carbonyl oxygen
Metal binding211Calcium
Metal binding401Calcium

Natural variations

Alternative sequence1 – 2929MLRVF…SAVFA → MLCCLLVRASNLPSAKKDRR SDPVASLTFR in isoform 8, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13 and isoform 14.
VSP_035924
Alternative sequence1521A → AGGGQSRAETWSLLSDSTMD TRYSGKKWPAPT in isoform 2, isoform 5, isoform 7, isoform 8, isoform 11 and isoform 13.
VSP_035925
Alternative sequence494 – 50815EEPAG…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 sequence14701Q → QLADGLSSLAPTNTASPPSS PH in isoform 4, isoform 6, isoform 7, isoform 10, isoform 12 and isoform 13.
VSP_035927
Alternative sequence1934 – 196835KPAKT…TVKGW → SSASSSRPPRPDCPARVGRQ TDGPAHTPRVANMEL in isoform 15.
VSP_035928
Alternative sequence1969 – 2080112Missing in isoform 15.
VSP_035929
Natural variant521W → R in LGMD2B. Ref.41
VAR_057834
Natural variant671V → D in MMD1 and LGMD2B; Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2. Ref.16 Ref.25
VAR_057835
Natural variant841A → V. Ref.41
VAR_057836
Natural variant1551G → R in LGMD2B. Ref.41
VAR_057837
Natural variant1701A → E in MMD1, LGMD2B and isolated hyperCKemia. Ref.33 Ref.35 Ref.41
Corresponds to variant rs34999029 [ dbSNP | Ensembl ].
VAR_024853
Natural variant1891L → V. Ref.33 Ref.41
Corresponds to variant rs13407355 [ dbSNP | Ensembl ].
VAR_024854
Natural variant2341G → E in LGMD2B. Ref.41
VAR_057838
Natural variant2531R → W in isolated hyperCKemia. Ref.33 Ref.41
VAR_024855
Natural variant2661L → P in pseudometabolic myopathy. Ref.33 Ref.41
VAR_024856
Natural variant2841I → T in LGMD2B. Ref.41
VAR_057839
Natural variant2991G → E in MMD1. Ref.33 Ref.41
VAR_024857
Natural variant2991G → R in LGMD2B and proximodistal myopathy. Ref.36 Ref.40 Ref.41
VAR_057840
Natural variant2991G → W in MMD1. Ref.40
VAR_057841
Natural variant3351G → A. Ref.41
VAR_057842
Natural variant3401S → R in proximodistal myopathy. Ref.41
VAR_057843
Natural variant3741V → L in MMD1; unknown pathological significance. Ref.35 Ref.41
Corresponds to variant rs150724610 [ dbSNP | Ensembl ].
VAR_057844
Natural variant386 – 3905FRAED → Y in MMD1.
VAR_057845
Natural variant3891E → Q in MMD1. Ref.32
VAR_057846
Natural variant3901D → N. Ref.41
VAR_057847
Natural variant4261G → R in MMD1. Ref.41
VAR_057848
Natural variant4261G → V in MMD1. Ref.29
VAR_057849
Natural variant4561C → W in MMD1. Ref.33 Ref.41
VAR_024858
Natural variant5191G → R in MMD1. Ref.39
VAR_057850
Natural variant5551R → W in isolated hyperCKemia, LGMD2B and MMD1. Ref.33 Ref.41
VAR_024859
Natural variant6181G → R in MMD1 and LGMD2B. Ref.30 Ref.41
VAR_057851
Natural variant6211G → R in LGMD2B. Ref.35
VAR_057852
Natural variant6251D → Y in LGMD2B. Ref.39
VAR_057853
Natural variant7311P → R in LGMD2B. Ref.41
VAR_057854
Natural variant7911P → R in MMD1 and LGMD2B. Ref.13 Ref.37
VAR_012308
Natural variant8191R → Q. Ref.41
VAR_057855
Natural variant8341I → V.
Corresponds to variant rs34671418 [ dbSNP | Ensembl ].
VAR_049055
Natural variant9301W → C in LGMD2B; uncetain pathogenicity. Ref.37 Ref.41
VAR_057856
Natural variant9591R → W in MMD1 and LGMD2B. Ref.28 Ref.35
VAR_024860
Natural variant9991W → C in MMD1. Ref.24 Ref.27
Corresponds to variant rs28937581 [ dbSNP | Ensembl ].
VAR_057857
Natural variant10221R → Q in LGMD2B; unknown pathological significance. Ref.28 Ref.30 Ref.41
Corresponds to variant rs34211915 [ dbSNP | Ensembl ].
VAR_024861
Natural variant10291P → L in MMD1. Ref.41
VAR_057858
Natural variant10381R → Q in LGMD2B; unknown pathological significance. Ref.28 Ref.35 Ref.41
VAR_024862
Natural variant10411R → C in MMD1. Ref.30
VAR_057859
Natural variant10461R → H in MMD1; dbNP:28939700. Ref.26 Ref.33 Ref.41
Corresponds to variant rs28939700 [ dbSNP | Ensembl ].
VAR_024863
Natural variant10651E → EAE.
VAR_024864
Natural variant10721A → P.
Corresponds to variant rs34660230 [ dbSNP | Ensembl ].
VAR_049056
Natural variant10961R → H.
Corresponds to variant rs59915619 [ dbSNP | Ensembl ].
VAR_061170
Natural variant12081I → M in LGMD2B. Ref.33
Corresponds to variant rs148858485 [ dbSNP | Ensembl ].
VAR_024865
Natural variant12281L → P in LGMD2B. Ref.41
VAR_057860
Natural variant12421R → H.
Corresponds to variant rs2303603 [ dbSNP | Ensembl ].
VAR_020308
Natural variant12761L → V in proximodistal myopathy. Ref.33 Ref.41
VAR_024866
Natural variant12981I → V in MMD1 and LGMD2B. Ref.1
Corresponds to variant rs121908954 [ dbSNP | Ensembl ].
VAR_012309
Natural variant13251I → M in a breast cancer sample; somatic mutation. Ref.38
VAR_035893
Natural variant13251I → V. Ref.41
Corresponds to variant rs145401010 [ dbSNP | Ensembl ].
VAR_057861
Natural variant13311R → L. Ref.28 Ref.33
Corresponds to variant rs61742872 [ dbSNP | Ensembl ].
VAR_024867
Natural variant13351E → K in MMD1 and LGMD2B. Ref.28 Ref.30 Ref.35
VAR_024868
Natural variant13411L → P in LGMD2B. Ref.36
VAR_057862
Natural variant13491L → V in a breast cancer sample; somatic mutation. Ref.38
VAR_035894
Natural variant13511N → S. Ref.33
VAR_024869
Natural variant13611C → R in MMD1. Ref.30
VAR_057863
Natural variant15051Y → C in LGMD2B. Ref.30
VAR_057864
Natural variant15261K → T in LGMD2B. Ref.41
Corresponds to variant rs76086153 [ dbSNP | Ensembl ].
VAR_057865
Natural variant15431G → D in LGMD2B. Ref.41
VAR_057866
Natural variant15811R → H. Ref.27
Corresponds to variant rs185596534 [ dbSNP | Ensembl ].
VAR_057867
Natural variant16621T → R in MMD1. Ref.30
VAR_057868
Natural variant16781C → S in isolated hyperCKemia. Ref.35
VAR_057869
Natural variant16791G → E in MMD1. Ref.27
VAR_057870
Natural variant16931R → Q in MMD1. Ref.33 Ref.41
VAR_024870
Natural variant16931R → W in MMD1. Ref.35
VAR_057871
Natural variant17341E → G in LGMD2B. Ref.39
VAR_057872
Natural variant17481E → V in proximodistal myopathy. Ref.33 Ref.41
VAR_024871
Natural variant17681R → W in LGMD2B and proximodistal myopathy; uncetain pathogenicity. Ref.37 Ref.41
VAR_057873
Natural variant18371D → N in MMD1. Ref.35 Ref.41
VAR_057874
Natural variant18421G → D in MMD1. Ref.31
VAR_057875
Natural variant18571H → R in MMD1. Ref.1
VAR_012310
Natural variant19221L → P in MMD1. Ref.31
VAR_057876
Natural variant1938 – 19392Missing in MMD1.
VAR_057877
Natural variant19421C → G in MMD1. Ref.35
VAR_057878
Natural variant19671G → S. Ref.41
VAR_057879
Natural variant19701P → S in LGMD2B. Ref.41
VAR_057880
Natural variant20001R → Q in MMD1. Ref.26
Corresponds to variant rs115407852 [ dbSNP | Ensembl ].
VAR_024872
Natural variant20421R → C in MMD1, LGMD2B and proximodistal myopathy. Ref.1 Ref.35 Ref.37 Ref.41
VAR_012311
Natural variant20681P → L in MMD1. Ref.29
VAR_057881

Secondary structure

...................................... 2080
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 376E25A5AB9BE398

FASTA2,080237,295
        10         20         30         40         50         60 
MLRVFILYAE NVHTPDTDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF EWDLKGIPLD 

        70         80         90        100        110        120 
QGSELHVVVK DHETMGRNRF LGEAKVPLRE VLATPSLSAS FNAPLLDTKK QPTGASLVLQ 

       130        140        150        160        170        180 
VSYTPLPGAV PLFPPPTPLE PSPTLPDLDV VADTGGEEDT EDQGLTGDEA EPFLDQSGGP 

       190        200        210        220        230        240 
GAPTTPRKLP SRPPPHYPGI KRKRSAPTSR KLLSDKPQDF QIRVQVIEGR QLPGVNIKPV 

       250        260        270        280        290        300 
VKVTAAGQTK RTRIHKGNSP LFNETLFFNL FDSPGELFDE PIFITVVDSR SLRTDALLGE 

       310        320        330        340        350        360 
FRMDVGTIYR EPRHAYLRKW LLLSDPDDFS AGARGYLKTS LCVLGPGDEA PLERKDPSED 

       370        380        390        400        410        420 
KEDIESNLLR PTGVALRGAH FCLKVFRAED LPQMDDAVMD NVKQIFGFES NKKNLVDPFV 

       430        440        450        460        470        480 
EVSFAGKMLC SKILEKTANP QWNQNITLPA MFPSMCEKMR IRIIDWDRLT HNDIVATTYL 

       490        500        510        520        530        540 
SMSKISAPGG EIEEEPAGAV KPSKASDLDD YLGFLPTFGP CYINLYGSPR EFTGFPDPYT 

       550        560        570        580        590        600 
ELNTGKGEGV AYRGRLLLSL ETKLVEHSEQ KVEDLPADDI LRVEKYLRRR KYSLFAAFYS 

       610        620        630        640        650        660 
ATMLQDVDDA IQFEVSIGNY GNKFDMTCLP LASTTQYSRA VFDGCHYYYL PWGNVKPVVV 

       670        680        690        700        710        720 
LSSYWEDISH RIETQNQLLG IADRLEAGLE QVHLALKAQC STEDVDSLVA QLTDELIAGC 

       730        740        750        760        770        780 
SQPLGDIHET PSATHLDQYL YQLRTHHLSQ ITEAALALKL GHSELPAALE QAEDWLLRLR 

       790        800        810        820        830        840 
ALAEEPQNSL PDIVIWMLQG DKRVAYQRVP AHQVLFSRRG ANYCGKNCGK LQTIFLKYPM 

       850        860        870        880        890        900 
EKVPGARMPV QIRVKLWFGL SVDEKEFNQF AEGKLSVFAE TYENETKLAL VGNWGTTGLT 

       910        920        930        940        950        960 
YPKFSDVTGK IKLPKDSFRP SAGWTWAGDW FVCPEKTLLH DMDAGHLSFV EEVFENQTRL 

       970        980        990       1000       1010       1020 
PGGQWIYMSD NYTDVNGEKV LPKDDIECPL GWKWEDEEWS TDLNRAVDEQ GWEYSITIPP 

      1030       1040       1050       1060       1070       1080 
ERKPKHWVPA EKMYYTHRRR RWVRLRRRDL SQMEALKRHR QAEAEGEGWE YASLFGWKFH 

      1090       1100       1110       1120       1130       1140 
LEYRKTDAFR RRRWRRRMEP LEKTGPAAVF ALEGALGGVM DDKSEDSMSV STLSFGVNRP 

      1150       1160       1170       1180       1190       1200 
TISCIFDYGN RYHLRCYMYQ ARDLAAMDKD SFSDPYAIVS FLHQSQKTVV VKNTLNPTWD 

      1210       1220       1230       1240       1250       1260 
QTLIFYEIEI FGEPATVAEQ PPSIVVELYD HDTYGADEFM GRCICQPSLE RMPRLAWFPL 

      1270       1280       1290       1300       1310       1320 
TRGSQPSGEL LASFELIQRE KPAIHHIPGF EVQETSRILD ESEDTDLPYP PPQREANIYM 

      1330       1340       1350       1360       1370       1380 
VPQNIKPALQ RTAIEILAWG LRNMKSYQLA NISSPSLVVE CGGQTVQSCV IRNLRKNPNF 

      1390       1400       1410       1420       1430       1440 
DICTLFMEVM LPREELYCPP ITVKVIDNRQ FGRRPVVGQC TIRSLESFLC DPYSAESPSP 

      1450       1460       1470       1480       1490       1500 
QGGPDDVSLL SPGEDVLIDI DDKEPLIPIQ EEEFIDWWSK FFASIGEREK CGSYLEKDFD 

      1510       1520       1530       1540       1550       1560 
TLKVYDTQLE NVEAFEGLSD FCNTFKLYRG KTQEETEDPS VIGEFKGLFK IYPLPEDPAI 

      1570       1580       1590       1600       1610       1620 
PMPPRQFHQL AAQGPQECLV RIYIVRAFGL QPKDPNGKCD PYIKISIGKK SVSDQDNYIP 

      1630       1640       1650       1660       1670       1680 
CTLEPVFGKM FELTCTLPLE KDLKITLYDY DLLSKDEKIG ETVVDLENRL LSKFGARCGL 

      1690       1700       1710       1720       1730       1740 
PQTYCVSGPN QWRDQLRPSQ LLHLFCQQHR VKAPVYRTDR VMFQDKEYSI EEIEAGRIPN 

      1750       1760       1770       1780       1790       1800 
PHLGPVEERL ALHVLQQQGL VPEHVESRPL YSPLQPDIEQ GKLQMWVDLF PKALGRPGPP 

      1810       1820       1830       1840       1850       1860 
FNITPRRARR FFLRCIIWNT RDVILDDLSL TGEKMSDIYV KGWMIGFEEH KQKTDVHYRS 

      1870       1880       1890       1900       1910       1920 
LGGEGNFNWR FIFPFDYLPA EQVCTIAKKD AFWRLDKTES KIPARVVFQI WDNDKFSFDD 

      1930       1940       1950       1960       1970       1980 
FLGSLQLDLN RMPKPAKTAK KCSLDQLDDA FHPEWFVSLF EQKTVKGWWP CVAEEGEKKI 

      1990       2000       2010       2020       2030       2040 
LAGKLEMTLE IVAESEHEER PAGQGRDEPN MNPKLEDPRR PDTSFLWFTS PYKTMKFILW 

      2050       2060       2070       2080 
RRFRWAIILF IILFILLLFL AIFIYAFPNY AAMKLVKPFS 

« Hide

Isoform 2 [UniParc].

Checksum: AE2E2536294E3F8E
Show »

FASTA2,111240,649
Isoform 3 [UniParc].

Checksum: BB177D29C6673190
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FASTA2,066235,913
Isoform 4 [UniParc].

Checksum: 26EEDCF011956BE1
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FASTA2,101239,297
Isoform 5 [UniParc].

Checksum: 5E5A7D7DC399343D
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FASTA2,097239,267
Isoform 6 [UniParc].

Checksum: E225F74E3A033173
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FASTA2,087237,916
Isoform 7 [UniParc].

Checksum: 8E253645F2D76F4A
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FASTA2,118241,269
Isoform 8 [UniParc].

Checksum: 65D105E2EA06A54E
Show »

FASTA2,112240,735
Isoform 9 [UniParc].

Checksum: 5BE7B5C3285A6CBD
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FASTA2,067236,000
Isoform 10 [UniParc].

Checksum: EBD1B370E34EF3E7
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FASTA2,102239,383
Isoform 11 [UniParc].

Checksum: 3C81E57B591C23C2
Show »

FASTA2,098239,353
Isoform 12 [UniParc].

Checksum: C068B3393FEBAEBA
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FASTA2,088238,002
Isoform 13 [UniParc].

Checksum: 1E839F33439A3B81
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FASTA2,119241,356
Isoform 14 (Dysferlin_v1) (DYSF_v1) [UniParc].

Checksum: CE55314169D4B801
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FASTA2,081237,381
Isoform 15 [UniParc].

Checksum: 99D137284A468A65
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FASTA1,954222,315

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. expand/collapse author list , 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 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. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., 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, IDENTIFICATION BY 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]"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.
[24]"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.
[25]"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.
[26]"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. expand/collapse author list , 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.
[27]"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. expand/collapse author list , 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.
[28]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]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)
[35]"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.
[36]"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.
[37]"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.
[38]"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. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-1325 AND VAL-1349.
[39]"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.
[40]"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.
[41]"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. expand/collapse author list , Laforet P., Urtizberea J.A., Eymard B., Leturcq F., 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

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.
RefSeqNP_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.
UniGeneHs.252180.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4CAHX-ray1.90B942-1052[»]
4CAIX-ray2.20A/B/C942-1052[»]
4IHBX-ray2.04A/B/C/D/E/F1-124[»]
4IQHX-ray1.76A/B/C28-124[»]
ProteinModelPortalO75923.
SMRO75923. Positions 1-128, 218-325, 380-486, 943-1052, 1153-1269, 1330-1424, 1574-1696, 1808-1933.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113896. 4 interactions.
IntActO75923. 44 interactions.

PTM databases

PhosphoSiteO75923.

Proteomic databases

PaxDbO75923.
PRIDEO75923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258104; ENSP00000258104; ENSG00000135636. [O75923-1]
ENST00000394120; ENSP00000377678; ENSG00000135636. [O75923-14]
ENST00000409366; ENSP00000386512; ENSG00000135636. [O75923-10]
ENST00000409582; ENSP00000386547; ENSG00000135636. [O75923-7]
ENST00000409651; ENSP00000386683; ENSG00000135636. [O75923-8]
ENST00000409744; ENSP00000386285; ENSG00000135636. [O75923-12]
ENST00000409762; ENSP00000387137; ENSG00000135636. [O75923-5]
ENST00000410020; ENSP00000386881; ENSG00000135636. [O75923-13]
ENST00000410041; ENSP00000386617; ENSG00000135636. [O75923-11]
ENST00000413539; ENSP00000407046; ENSG00000135636. [O75923-2]
ENST00000429174; ENSP00000398305; ENSG00000135636. [O75923-4]
GeneID8291.
KEGGhsa:8291.
UCSCuc002sie.3. human. [O75923-1]
uc002sif.3. human. [O75923-14]
uc002sig.4. human. [O75923-3]
uc010fee.3. human. [O75923-4]
uc010fef.3. human. [O75923-7]
uc010feg.3. human. [O75923-2]
uc010feh.3. human. [O75923-6]
uc010fei.3. human. [O75923-5]
uc010fej.3. human. [O75923-12]
uc010fek.3. human. [O75923-11]
uc010fel.3. human. [O75923-9]
uc010fem.3. human. [O75923-10]
uc010fen.3. human. [O75923-13]
uc010feo.3. human. [O75923-8]

Organism-specific databases

CTD8291.
GeneCardsGC02P071680.
HGNCHGNC:3097. DYSF.
HPACAB002510.
HPA017071.
HPA021945.
MIM253601. phenotype.
254130. phenotype.
603009. gene.
606768. phenotype.
neXtProtNX_O75923.
Orphanet268. Autosomal recessive limb-girdle muscular dystrophy type 2B.
199329. Congenital myopathy, Paradas type.
178400. Distal myopathy with anterior tibial onset.
45448. Miyoshi myopathy.
PharmGKBPA27554.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG330124.
HOVERGENHBG018972.
OMAQVHLALK.
OrthoDBEOG7CVPWR.
PhylomeDBO75923.
TreeFamTF316871.

Gene expression databases

ArrayExpressO75923.
BgeeO75923.
GenevestigatorO75923.

Family and domain databases

Gene3D2.60.40.150. 8 hits.
InterProIPR000008. C2_dom.
IPR012968. FerIin-domain.
IPR012560. Ferlin_A-domain.
IPR012561. Ferlin_B-domain.
IPR010482. Peroxin/Dysferlin.
IPR006614. Peroxin/Ferlin.
[Graphical view]
PfamPF00168. C2. 7 hits.
PF08165. FerA. 1 hit.
PF08150. FerB. 1 hit.
PF08151. FerI. 1 hit.
PF06398. Pex24p. 1 hit.
[Graphical view]
SMARTSM00239. C2. 7 hits.
SM00694. DysFC. 2 hits.
SM00693. DysFN. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 8 hits.
PROSITEPS50004. C2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDysferlin.
GenomeRNAi8291.
NextBio31071.
PROO75923.
SOURCESearch...

Entry information

Entry nameDYSF_HUMAN
AccessionPrimary (citable) accession number: O75923
Secondary accession number(s): B1PZ70 expand/collapse secondary AC list , B1PZ71, B1PZ72, B1PZ73, B1PZ74, B1PZ75, B1PZ76, B1PZ77, B1PZ78, B1PZ79, B1PZ80, B1PZ81, B3KQB9, O75696, Q09EX5, Q0H395, Q53QY3, Q53TD2, Q8TEL8, Q9UEN7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM