MGP Database

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MGP004641

UniProt Annotations

Entry Information
Gene Namespectrin repeat containing, nuclear envelope 1
Protein EntrySYNE1_HUMAN
UniProt IDQ8NF91
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=9; Name=1; Synonyms=Nesprin-1 Giant, Enaptin; IsoId=Q8NF91-1; Sequence=Displayed; Name=2; Synonyms=Beta; IsoId=Q8NF91-2; Sequence=VSP_007130; Name=3; Synonyms=Alpha; IsoId=Q8NF91-3; Sequence=VSP_007132, VSP_007144; Name=4; IsoId=Q8NF91-4; Sequence=VSP_007134, VSP_007139, VSP_007140, VSP_007144; Name=5; IsoId=Q8NF91-5; Sequence=VSP_007135, VSP_007136; Note=No experimental confirmation available.; Name=6; IsoId=Q8NF91-6; Sequence=VSP_007137, VSP_007138; Note=No experimental confirmation available.; Name=7; IsoId=Q8NF91-7; Sequence=VSP_007141, VSP_007142; Note=No experimental confirmation available.; Name=8; Synonyms=Beta 2; IsoId=Q8NF91-8; Sequence=VSP_007131; Name=9; Synonyms=Alpha 2; IsoId=Q8NF91-9; Sequence=VSP_007133, VSP_007143, VSP_007144;
DiseaseEmery-Dreifuss muscular dystrophy 4, autosomal dominant (EDMD4) [MIM:612998]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. {ECO:0000269|PubMed:17761684}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseSpinocerebellar ataxia, autosomal recessive, 8 (SCAR8) [MIM:610743]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR8 is an autosomal recessive form. {ECO:0000269|PubMed:17159980}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DomainThe KASH domain, which contains a transmembrane domain, mediates the nuclear envelope targeting and is involved in the binding to SUN1 and SUN2 through recognition of their SUN domains. {ECO:0000269|PubMed:18396275}.
FunctionMulti-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. Component of SUN-protein- containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. May be involved in the maintenance of nuclear organization and structural integrity. Connects nuclei to the cytoskeleton by interacting with the nuclear envelope and with F- actin in the cytoplasm. May be required for centrosome migration to the apical cell surface during early ciliogenesis. {ECO:0000269|PubMed:11792814, ECO:0000269|PubMed:18396275}.
InteractionQ9NRI5:DISC1; NbExp=6; IntAct=EBI-928867, EBI-529989; O94901:SUN1; NbExp=2; IntAct=EBI-6170938, EBI-2796904; Q9UH99:SUN2; NbExp=3; IntAct=EBI-928867, EBI-1044964;
Sequence CautionSequence=AAC02992.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=AAL38031.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=AAM95335.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin.; Evidence={ECO:0000305}; Sequence=BAB71097.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305}; Sequence=BAC04284.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=CAD28486.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
SimilarityBelongs to the nesprin family. {ECO:0000305}.
SimilarityContains 12 HAT repeats. {ECO:0000305}.
SimilarityContains 1 actin-binding domain. {ECO:0000305}.
SimilarityContains 1 KASH domain. {ECO:0000255|PROSITE- ProRule:PRU00385}.
SimilarityContains 2 CH (calponin-homology) domains. {ECO:0000255|PROSITE-ProRule:PRU00044}.
SimilarityContains 31 spectrin repeats. {ECO:0000305}.
Subcellular LocationNucleus outer membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus. Nucleus envelope. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere. Note=The largest part of the protein is cytoplasmic, while its C-terminal part is associated with the nuclear envelope, most probably the outer nuclear membrane. In skeletal and smooth muscles, a significant amount is found in the sarcomeres. In myoblasts, relocalized from the nuclear envelope to the nucleus and cytoplasm during cell differentiation.
SubunitDimer. Core component of the LINC complex which is composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN domain-containing proteins interact with A-type lamins of the nuclear lamina, while at the other end of the complex, nesprins interact with unique cytoskeletal components. Interacts with SYNE3. May interact with MUSK (By similarity). Interacts with F- actin via its N-terminal domain (By similarity). Interacts with EMD and LMNA in vitro. {ECO:0000250, ECO:0000269|PubMed:12163176, ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:22518138}.
Tissue SpecificityExpressed in HeLa, A431, A172 and HaCaT cells (at protein level). Widely expressed. Highly expressed in skeletal and smooth muscles, heart, spleen, peripheral blood leukocytes, pancreas, cerebellum, stomach, kidney and placenta. {ECO:0000269|PubMed:11792814, ECO:0000269|PubMed:11801724, ECO:0000269|PubMed:15093733, ECO:0000269|PubMed:22518138}.
Web ResourceName=Wikipedia; Note=Enaptin entry; URL="http://en.wikipedia.org/wiki/Enaptin";
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