Database for Annotation, Visualization and Integrated Discovery 2.1
National Institute of Allergy and Infectious Disease
The Database for Annotation, Visualization and Integrated Discovery
0
DAVID Functional Annotation Table
Gene Report
Help and Manual

Right-click and select 'Save Target As' to download results Download File
filamin C(FLNC) filamin C(FLNC) Related Genes Homo sapiens
CHROMOSOME 7,
CYTOBAND 7q32-q35,
ENSEMBL_GENE_ID ENSG00000128591,
GENERIF_SUMMARY Accumulation is a strong but nonspecific immunohistochemical marker of core formation in muscle myopathies., calpain 3 can cleave filamin C (FLNC); FLNC may be substrate for calpain 3, regulating protein-protein interactions with sarcoglycans, gamma filamin has one molecule, with predominantly beta secondary-structure elements, per asymmetric unit, results identify the muscle-specific isoform FLNc as a new physiological substrate for PKB, a mutation in the dimerization domain of filamin c causes a novel type of autosomal dominant myofibrillar myopathy, These observations start to define the basis for PI3K regulation of filamin through LL5beta., The crystal structure of domain 23 of filamin C showed that the protein adopts the expected immunoglobulin (Ig)-like fold. A dimer is formed by domain 24; domain 23 has little interactions with itself or with domain 24., The mutant dimerization domain of filamin C is less stable and more susceptible to proteolysis. As a consequence, it does not dimerize properly and forms aggregates in vitro., Taken together, our data suggest that p73alpha is sequestered in the cytoplasm by filamin A, thereby inhibiting its transcriptional activity., filamin-C, a known component of striated muscle Z-lines, interacts with nebulette modules, Results suggest that the novel p.Val930_Thr933del mutation in filamin C is the cause of MFM but also indicate that filamin C mutations are a comparatively rare cause of MFM., Data show that in myofibrillar myopathies filamin C exhibites significant alterations in their localization., A large number of variations were found in many of the genes (myozenin 1, gamma-filamin, kinectin-1) in patients with limb-girdle muscular dystrophies and controls., We present a Chinese family with filaminopathy with progressive muscle weakness in all limbs with a deletion-insertion mutation in exon 18 of the filamin C, filamin C ABD mutations cause a recognizable distal myopathy, most likely through increased actin affinity, similar to the pathological mechanism of filamin A and filamin B ABD mutations., We conclude that filamin C is a dosage-sensitive gene and that FLNC haploinsufficiency can cause a specific type of myopathy in humans., study indicates that filamins are important regulators of polycystin-2 channel function, and further links actin cytoskeletal dynamics to the regulation of this channel protein, FLNC/filamin C mutations cause protein degradation in myofibrillar myopathy, Increased methylation levels of FLNC is associated with highly active Helicobacter pylori-related gastritis., these studies extend previous findings to show that functional rescue of alpha2C-ARs is mediated through Rap1-filamin signaling. Perturbation of this signaling pathway may lead to alterations in alpha2C-AR trafficking and physiological function., By integrating our WES and CN data we identified three mutated putative candidate genes targeted by 7q deletions (CUL1, EZH2 and FLNC), with FLNC positioned within the well-characterized 7q minimally deleted region., Crystal Structures of FLNa Domains 3-5 and FLNc Domains 4-5 Show a Novel Domain-Domain Organization., Aciculin interacts with filamin C and Xin and is essential for myofibril assembly., alpha2C-adrenoreceptor interaction with filamin-2, Mutations in the gene encoding the sarcomeric protein filamin C cause a new form of familial hypertrophic cardiomyopathy., Findings indicate a functional role of filamin C in cancers.,
OFFICIAL_GENE_SYMBOL FLNC,
OMIM_DISEASE Myopathy, myofibrillar, 5, Myopathy, distal, 4,
SP_COMMENT developmental stage:Expressed in both differentiating and adult muscles., disease:Defects in FLNC are the cause of autosomal dominant filaminopathy [MIM:609524, 601419]. Myofibrillar myopathy (MFM) is a neuromuscular disorder, usually with an adult onset, characterized by focal myofibrillar destruction and pathological cytoplasmic protein aggregations. Autosomal dominant filaminopathy is a form of MFM characterized by morphological features of MFM and clinical features of a limb-girdle myopathy. A heterozygous nonsense mutation which segregates with the disease, has been identified in the FLNC gene., domain:Comprised of a NH2-terminal actin-binding domain, 24 internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation., domain:The filamin 20 repeat mediates interaction with XIRP1., domain:The intradomain insert is specific to FLNC and mediates the targeting to developing and mature Z-disks., function:Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z-disks in muscle cells., miscellaneous:Silenced in MKN28 and MKN74 gastric cancer cell lines due to aberrant methylation of the gene., similarity:Belongs to the filamin family., similarity:Contains 1 actin-binding domain., similarity:Contains 2 CH (calponin-homology) domains., similarity:Contains 24 filamin repeats., subcellular location:A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z-disks, while a minor fraction localizes with subsarcolemme., subunit:Homodimer. Interacts with KY (By similarity). Interacts with FLNB, KCND2, ITGB1A, INPPL1, MYOT, MYOZ1 and MYOZ3. Interacts with sarcoglycans SGCD and SGCG., tissue specificity:Highly expressed in striated muscles. Weakly expressed in thyroid, fetal brain, fetal lung, retina, spinal cord and bone marrow. Not expressed in testis, pancreas, adrenal gland, placenta, liver and kidney.,