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Q9ESD7

- DYSF_MOUSE

UniProt

Q9ESD7 - DYSF_MOUSE

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Protein

Dysferlin

Gene
Dysf, Fer1l1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Calcium By similarity
Metal bindingi19 – 191Calcium; via carbonyl oxygen By similarity
Metal bindingi21 – 211Calcium By similarity
Metal bindingi40 – 401Calcium By similarity

GO - Molecular functioni

  1. calcium-dependent phospholipid binding Source: Ensembl
  2. calcium ion binding Source: UniProtKB
  3. phospholipid binding Source: UniProtKB
  4. protein binding Source: UniProt

GO - Biological processi

  1. plasma membrane repair Source: UniProtKB
  2. vesicle fusion Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Lipid-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Dysferlin
Alternative name(s):
Dystrophy-associated fer-1-like protein
Fer-1-like protein 1
Gene namesi
Name:Dysf
Synonyms:Fer1l1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1349385. Dysf.

Subcellular locationi

Cell membranesarcolemma; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; Single-pass type II membrane protein. Cell membrane 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 By similarity. Accumulates and colocalizes with fusion vesicles at the sarcolemma disruption sites. 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 By similarity. Colocalizes with ANXA1 and ANXA2 at the sarcolemma in skeletal muscle. Colocalizes with PARVB at the sarcolemma of skeletal muscle By similarity. Retained by caveolin at the plasmma membrane. Reaches the plasmma membrane through a caveolin-independent mechanism. Colocalizes, during muscle differentiation, with CACNA1S in the T-tubule system of myotubules. Detected on the apical plasma membrane of the syncytiotrophoblast By similarity.5 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 20562056Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei2057 – 207721Helical; Reviewed predictionAdd
BLAST
Topological domaini2078 – 209013Extracellular Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cytoplasmic vesicle Source: UniProtKB
  2. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. lamellipodium Source: UniProtKB
  5. plasma membrane Source: UniProtKB
  6. sarcolemma Source: UniProtKB
  7. T-tubule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in Dysf are the cause of a slowly progressive muscular dystrophy observed in SJL mice. It affects primarily the proximal muscles and it is inherited as autosomal recessive trait.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20902090DysferlinPRO_0000057880Add
BLAST

Proteomic databases

MaxQBiQ9ESD7.
PaxDbiQ9ESD7.
PRIDEiQ9ESD7.

PTM databases

PhosphoSiteiQ9ESD7.

Expressioni

Tissue specificityi

Expressed in skeletal and cardiac muscles (at protein level). Expressed in skeletal muscle and heart. Also found in brain, liver and kidney.2 Publications

Gene expression databases

ArrayExpressiQ9ESD7.
BgeeiQ9ESD7.
CleanExiMM_DYSF.
GenevestigatoriQ9ESD7.

Interactioni

Subunit structurei

Interacts with CAV3. Interacts with AHNAK; the interaction is direct and Ca2+-independent. Interacts with AHNAK2; the interaction is direct and Ca2+-independent By similarity. 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.4 Publications

Protein-protein interaction databases

BioGridi205052. 2 interactions.
IntActiQ9ESD7. 4 interactions.
MINTiMINT-4998243.

Structurei

3D structure databases

ProteinModelPortaliQ9ESD7.
SMRiQ9ESD7. Positions 1-124, 223-489, 883-945, 953-1061, 1074-1110, 1156-1275, 1584-1675.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8585C2 1Add
BLAST
Domaini209 – 30496C2 2Add
BLAST
Domaini368 – 486119C2 3Add
BLAST
Domaini1149 – 1254106C2 4Add
BLAST
Domaini1346 – 143388C2 5Add
BLAST
Domaini1575 – 167399C2 6Add
BLAST
Domaini1823 – 1936114C2 7Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1048 – 110760Arg-richAdd
BLAST

Domaini

All seven C2 domains associate with lipid membranes in a calcium-dependent manner. Domains C2 1 and 3 have the highest affinity for calcium, the C2 domain 1 seems to be largely unstructured in the absence of bound ligands By similarity.

Sequence similaritiesi

Belongs to the ferlin family.
Contains 7 C2 domains.

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG330124.
GeneTreeiENSGT00550000074414.
HOGENOMiHOG000006771.
HOVERGENiHBG018972.
InParanoidiQ6KAR3.
KOiK18261.
OMAiQVHLALK.
TreeFamiTF316871.

Family and domain databases

Gene3Di2.60.40.150. 8 hits.
InterProiIPR000008. C2_dom.
IPR012968. FerIin-domain.
IPR012560. Ferlin_A-domain.
IPR012561. Ferlin_B-domain.
IPR010482. Peroxin/Dysferlin.
IPR006614. Peroxin/Ferlin.
[Graphical view]
PfamiPF00168. C2. 7 hits.
PF08165. FerA. 1 hit.
PF08150. FerB. 1 hit.
PF08151. FerI. 1 hit.
PF06398. Pex24p. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 7 hits.
SM00694. DysFC. 2 hits.
SM00693. DysFN. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 7 hits.
PROSITEiPS50004. C2. 5 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9ESD7-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MLRVFILFAE NVHTPDSDIS DAYCSAVFAG VKKRTKVIKN SVNPVWNEGF     50
EWDLKGIPLD QSSELLVVVK DHETMGRNRF LGEAKIPLQE VLATPSLSAS 100
FNAPLLDAKQ QPTGASLVLQ VSYTPPPGAV PLFPPPASLA PSPTLPDMDL 150
VPDTGGEEDT EDQGLTGDEA EPFLDQSAAV GPGGPTTPRK PPSHPPPHYP 200
GAKRKRSSAP PRKLLSDKPQ DFQIRVQVIE GRQLPGVNIK PVVKVTAAGQ 250
TKRTRIQKGN SPLFNETLFF NVFDSPLELF DEPIFITVVD SRSLRTDALL 300
GEFRMDVGTV YREPRHAYLR KWLLLSDPDD FSAGARGYLK ASLCVLGPGD 350
EAPLDKKDPS EDKEDIEGNL LRPTGVALRG AHFCLKLFRA EDLPQMDDAV 400
MDNVKQIFGF DSNKKNLVDP FVEVSFAGKM LCSKILEKTA NPQWNQNITL 450
PAMFPSMCEK MRIRVMDWDR LTHNDTVATT YLGMSKISAT GGEIEEEPAG 500
VLKSPQATDL DDNLGFLPTF GPCYVNLYGS PREFTGFPDP YAELNTGKGE 550
GVAYRGRVLL SLETKLVEHS EQKVEDLPAD DILRVEKYLR RRKYSLFAAF 600
YSATMLQDVD DAIQFEVSIG NYGNKFDTTC LPLASTTQYS RAVFDGGSLP 650
LPVGCHYYYL PWGNVKPVVV LSSYWEDISH RIEIQNQLLR VADRLEANLE 700
QVHLALKAQC SSEDVDALVA QLTDELLADC SQPLCDIHEI PSATHLDQYL 750
LRLRTRHLSQ IKEAALALKL GHSELSTALE QAEDWLLHLR ALAEEPQNSL 800
PDIIIWMLQG DKRVAYQRVP AHEVLFSRRG PSYCGRNCGK LQTIFLKYPM 850
EGMPGARMPV QIRIKLWFGL SVDEKEFNQF AEGKLSVFAE TYENQTKLAL 900
VGNWGTTGLT YPKFSDVTGK IKLPKDSFRP SAGWAWAGDW FVCPEKTLLH 950
DADAGHLSFV EEVFENQTRL PGGQWIYMSD NYTDVNGEKV LPKDDIECPL 1000
GWKWEDEEWS TDLNRAVDEQ GWEYSITIPP DRKPKHWVPV EKMYYTHRRR 1050
RWVRLRRRDL SQMEALKRHR QAEAEGEGWE YASLFGWKFH LEYRKTDAFR 1100
RRRWRRRMEP LEKTGPAAVF ALEGALGGMV DDKSEDSMSV STLSFGVNRP 1150
TISCIFDYGN RYHLRCYLYQ ARDLPAMDKD SFSDPYAIVS FLHQSQKTVV 1200
EKNTLNPTWD QTLIFYEIEI FGEPASIAEH PPCIVVELYD HDTYGADEFM 1250
GRCICQPSLE RMPRLAWFPL TRGSQPAGEL LAAFELIQRE KPAIHHIPGF 1300
EMHETSRILD ETEDTDLPYP PPQREANIYM VPQNIKPALQ RTAIEILAWG 1350
LRNMKSYQMA SISSPSLVVE CGGQTVQSCV IRNLRKNPNF DVCTLFMEVM 1400
LPREDLYCPP IVVKVIDNRQ FGRRPVVGQC TIRSLENFLC DPYSAESPSP 1450
QGGPDDVSLL SPGEDVLIDI DDKEPLIPVQ EEEFIDWWSK FFASVGEREK 1500
CGSYLEKDFD TLKVYDTQLE NVEAFGGLSD FCNTFKLYRG RTQEETDDPS 1550
VIGEFKGLFK IYPLPEDPAI PMPPRQFHQL AAQGPQECLV RIYIVRAFGL 1600
QPKDPNGKCD PYIKISIGKK SVSDQDNYIP CTLEPVFGKM FELTCTLPLE 1650
KDLKITLYDY DLLSKDEKIG ETVIDLENRL LSKFGARCGL PQTYCVSGPN 1700
QWRDQLRPSQ LLHLFCQQHR IKAPVYRTDR VTFQDKDYTI EEIEAGRLPN 1750
PHLGPVEERL ALHVLQQQGL VPEHVESRPL YSPLQPDIEQ GKLQMWIDIF 1800
PKVLGRPGPP FNITPRKARR FFLRCIIWNT KDVILDDLSL TGEKMSDIYV 1850
KGWMVGFEEH KQKTDVHYRS LGGEGNFNWR FVFPFDYLPA EQVCAVAKKD 1900
AFWRLDKTES KIPARVVFQI WDNDKFSFDD FLGSLQLDLN RMPKPAKTAE 1950
KCSLDQLDDT FHPEWFVSLF EQKTVKGWWP CVTEEGEKKM LAGKLEMTLE 2000
IVAESEHEER PAGQGRDEPN MNPKLEDPRR PDTSFLWFTS PYKTMKFILW 2050
RRFRCAIILF IILFILLLFL GVFVYAFPNY AAMKLVKPFR 2090
Length:2,090
Mass (Da):237,911
Last modified:December 16, 2008 - v3
Checksum:i0EBD1E2353946143
GO
Isoform 2 (identifier: Q9ESD7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MLRVFILFAENVHTPDSDISDAYCSAVFA → MLCCLLARASNLPNVKKDRRSDPVASLIFR
     152-152: P → PGGGQSRAETWSLLSDSTMDTRYSGKKWPVPT
     496-510: EEPAGVLKSPQATDL → V
     647-654: Missing.

Show »
Length:2,100
Mass (Da):239,289
Checksum:i3C8A7837C2F78273
GO
Isoform 3 (identifier: Q9ESD7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MLRVFILFAENVHTPDSDISDAYCSAVFA → MLCCLLARASNLPNVKKDRRSDPVASLIFR
     496-510: EEPAGVLKSPQATDL → V
     647-654: Missing.

Show »
Length:2,069
Mass (Da):235,908
Checksum:iBA9E838D870C6396
GO

Sequence cautioni

The sequence CAB63111.1 differs from that shown. Reason: The sequence differs significantly from amino acid position 1855.
The sequence BAD21394.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929MLRVF…SAVFA → MLCCLLARASNLPNVKKDRR SDPVASLIFR in isoform 2 and isoform 3. VSP_035930Add
BLAST
Alternative sequencei152 – 1521P → PGGGQSRAETWSLLSDSTMD TRYSGKKWPVPT in isoform 2. VSP_035931
Alternative sequencei496 – 51015EEPAG…QATDL → V in isoform 2 and isoform 3. VSP_035932Add
BLAST
Alternative sequencei647 – 6548Missing in isoform 2 and isoform 3. VSP_035933

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti467 – 4671D → G in CAB63111. 1 Publication
Sequence conflicti476 – 4761T → I in AAG17046. 1 Publication
Sequence conflicti510 – 5101L → V in CAB63111. 1 Publication
Sequence conflicti684 – 6841I → T in AAG17046. 1 Publication
Sequence conflicti690 – 6912RV → GI in AAG17046. 1 Publication
Sequence conflicti698 – 6981N → G in AAG17046. 1 Publication
Sequence conflicti712 – 7121S → T in AAG17046. 1 Publication
Sequence conflicti717 – 7171A → S in AAG17046. 1 Publication
Sequence conflicti727 – 7271L → I in AAG17046. 1 Publication
Sequence conflicti885 – 8851L → F in AAG17046. 1 Publication
Sequence conflicti909 – 9102LT → FS in AAG17046. 1 Publication
Sequence conflicti931 – 9311S → T in AAG17046. 1 Publication
Sequence conflicti953 – 9531D → A in AAG17046. 1 Publication
Sequence conflicti1175 – 11751P → A in AAG17046. 1 Publication
Sequence conflicti1187 – 11871A → S in CAB63111. 1 Publication
Sequence conflicti1694 – 16941Y → C in AAG17046. 1 Publication
Sequence conflicti1701 – 17011Q → K in AAG17046. 1 Publication
Sequence conflicti1705 – 17051Q → K in AAG17046. 1 Publication
Sequence conflicti1806 – 18061R → Q in AAG17046. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF188290 mRNA. Translation: AAG17046.2.
AK131144 mRNA. Translation: BAD21394.1. Different initiation.
AC153607 Genomic DNA. No translation available.
AC153608 Genomic DNA. No translation available.
AJ242954 mRNA. Translation: CAB63111.1. Sequence problems.
BC043692 mRNA. Translation: AAH43692.1.
CCDSiCCDS39536.1. [Q9ESD7-2]
RefSeqiNP_001071162.1. NM_001077694.2.
NP_067444.2. NM_021469.3. [Q9ESD7-2]
XP_006506243.1. XM_006506180.1. [Q9ESD7-3]
UniGeneiMm.220982.

Genome annotation databases

EnsembliENSMUST00000081904; ENSMUSP00000080579; ENSMUSG00000033788. [Q9ESD7-2]
ENSMUST00000113818; ENSMUSP00000109449; ENSMUSG00000033788. [Q9ESD7-3]
ENSMUST00000168387; ENSMUSP00000132297; ENSMUSG00000033788. [Q9ESD7-1]
GeneIDi26903.
KEGGimmu:26903.
UCSCiuc009cos.2. mouse. [Q9ESD7-3]
uc009cot.1. mouse. [Q9ESD7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF188290 mRNA. Translation: AAG17046.2 .
AK131144 mRNA. Translation: BAD21394.1 . Different initiation.
AC153607 Genomic DNA. No translation available.
AC153608 Genomic DNA. No translation available.
AJ242954 mRNA. Translation: CAB63111.1 . Sequence problems.
BC043692 mRNA. Translation: AAH43692.1 .
CCDSi CCDS39536.1. [Q9ESD7-2 ]
RefSeqi NP_001071162.1. NM_001077694.2.
NP_067444.2. NM_021469.3. [Q9ESD7-2 ]
XP_006506243.1. XM_006506180.1. [Q9ESD7-3 ]
UniGenei Mm.220982.

3D structure databases

ProteinModelPortali Q9ESD7.
SMRi Q9ESD7. Positions 1-124, 223-489, 883-945, 953-1061, 1074-1110, 1156-1275, 1584-1675.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205052. 2 interactions.
IntActi Q9ESD7. 4 interactions.
MINTi MINT-4998243.

PTM databases

PhosphoSitei Q9ESD7.

Proteomic databases

MaxQBi Q9ESD7.
PaxDbi Q9ESD7.
PRIDEi Q9ESD7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000081904 ; ENSMUSP00000080579 ; ENSMUSG00000033788 . [Q9ESD7-2 ]
ENSMUST00000113818 ; ENSMUSP00000109449 ; ENSMUSG00000033788 . [Q9ESD7-3 ]
ENSMUST00000168387 ; ENSMUSP00000132297 ; ENSMUSG00000033788 . [Q9ESD7-1 ]
GeneIDi 26903.
KEGGi mmu:26903.
UCSCi uc009cos.2. mouse. [Q9ESD7-3 ]
uc009cot.1. mouse. [Q9ESD7-2 ]

Organism-specific databases

CTDi 8291.
MGIi MGI:1349385. Dysf.

Phylogenomic databases

eggNOGi NOG330124.
GeneTreei ENSGT00550000074414.
HOGENOMi HOG000006771.
HOVERGENi HBG018972.
InParanoidi Q6KAR3.
KOi K18261.
OMAi QVHLALK.
TreeFami TF316871.

Miscellaneous databases

NextBioi 304757.
PROi Q9ESD7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ESD7.
Bgeei Q9ESD7.
CleanExi MM_DYSF.
Genevestigatori Q9ESD7.

Family and domain databases

Gene3Di 2.60.40.150. 8 hits.
InterProi IPR000008. C2_dom.
IPR012968. FerIin-domain.
IPR012560. Ferlin_A-domain.
IPR012561. Ferlin_B-domain.
IPR010482. Peroxin/Dysferlin.
IPR006614. Peroxin/Ferlin.
[Graphical view ]
Pfami PF00168. C2. 7 hits.
PF08165. FerA. 1 hit.
PF08150. FerB. 1 hit.
PF08151. FerI. 1 hit.
PF06398. Pex24p. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 7 hits.
SM00694. DysFC. 2 hits.
SM00693. DysFN. 2 hits.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 7 hits.
PROSITEi PS50004. C2. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the mouse dysferlin gene and genomic characterization of the SJL-Dysf mutation."
    Vafiadaki E., Reis A., Keers S., Harrison R., Anderson L.V.B., Raffelsberger T., Ivanova S., Hoeger H., Bittner R.E., Bushby K.M.D., Bashir R.
    NeuroReport 12:625-629(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
    Strain: BALB/c, C57BL/10 and SJL/J.
    Tissue: Skeletal muscle.
  2. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
    DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 467-1854 (ISOFORMS 1/2).
    Strain: B6C3FE, BALB/c, C3H, C57BL/10 and C57BL/6.
    Tissue: Muscle.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1490-2090 (ISOFORMS 1/2/3).
    Tissue: Mammary tumor.
  6. "Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing."
    Lennon N.J., Kho A., Bacskai B.J., Perlmutter S.L., Hyman B.T., Brown R.H. Jr.
    J. Biol. Chem. 278:50466-50473(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ANXA1 AND ANXA2, SUBCELLULAR LOCATION.
  7. "Defective membrane repair in dysferlin-deficient muscular dystrophy."
    Bansal D., Miyake K., Vogel S.S., Groh S., Chen C.C., Williamson R., McNeil P.L., Campbell K.P.
    Nature 423:168-172(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Intracellular localization of dysferlin and its association with the dihydropyridine receptor."
    Ampong B.N., Imamura M., Matsumiya T., Yoshida M., Takeda S.
    Acta Myol. 24:134-144(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CACNA1S, SUBCELLULAR LOCATION.
  9. "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.
  10. "Dysferlin-mediated membrane repair protects the heart from stress-induced left ventricular injury."
    Han R., Bansal D., Miyake K., Muniz V.P., Weiss R.M., McNeil P.L., Campbell K.P.
    J. Clin. Invest. 117:1805-1813(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "Caveolin regulates endocytosis of the muscle repair protein, dysferlin."
    Hernandez-Deviez D.J., Howes M.T., Laval S.H., Bushby K., Hancock J.F., Parton R.G.
    J. Biol. Chem. 283:6476-6488(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin."
    Cai C., Weisleder N., Ko J.-K., Komazaki S., Sunada Y., Nishi M., Takeshima H., Ma J.
    J. Biol. Chem. 284:15894-15902(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM72.

Entry informationi

Entry nameiDYSF_MOUSE
AccessioniPrimary (citable) accession number: Q9ESD7
Secondary accession number(s): Q6KAR3, Q80VT0, Q9QXC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Mice lacking Dysf maintain a functional dystrophin glycoprotein complex (DGC) but their muscle cells are defective in repairing the plasma membrane disruptions and accumulates vesicles at the sarcolemma. They develop a progressive muscular dystrophy and cardiomyopathy.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi