MGP Database

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MGP001090

UniProt Annotations

Entry Information
Gene Namefilamin B, beta
Protein EntryFLNB_HUMAN
UniProt IDO75369
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=9; Name=1; Synonyms=ABP-278; IsoId=O75369-1; Sequence=Displayed; Name=2; Synonyms=ABP-276; IsoId=O75369-2; Sequence=VSP_008773; Note=May be due to exon skipping.; Name=3; Synonyms=Var-1; IsoId=O75369-3; Sequence=VSP_008774; Note=May be due to exon skipping.; Name=7; IsoId=O75369-7; Sequence=VSP_024113, VSP_024114, VSP_024115; Name=4; Synonyms=Var-3; IsoId=O75369-4; Sequence=VSP_008775, VSP_008776; Name=5; Synonyms=Var-2; IsoId=O75369-5; Sequence=VSP_008777, VSP_008778; Note=May be due to competing donor splice sites.; Name=6; Synonyms=Var-1-DeltaH1; IsoId=O75369-6; Sequence=VSP_008773, VSP_008774; Note=May be due to exon skipping.; Name=8; IsoId=O75369-8; Sequence=VSP_043446; Name=9; IsoId=O75369-9; Sequence=VSP_024115; Note=No experimental confirmation available.;
DiseaseAtelosteogenesis 1 (AO1) [MIM:108720]: A lethal chondrodysplasia characterized by distal hypoplasia of the humeri and femurs, hypoplasia of the mid-thoracic spine, occasionally complete lack of ossification of single hand bones, and the finding in cartilage of multiple degenerated chondrocytes which are encapsulated in fibrous tissue. {ECO:0000269|PubMed:14991055}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseAtelosteogenesis 3 (AO3) [MIM:108721]: A short-limb lethal skeletal dysplasia with vertebral abnormalities, disharmonious skeletal maturation, poorly modeled long bones and joint dislocations. Recurrent respiratory insufficiency and/or infections usually result in early death. {ECO:0000269|PubMed:14991055}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseBoomerang dysplasia (BOOMD) [MIM:112310]: A perinatal lethal osteochondrodysplasia characterized by absence or underossification of the limb bones and vertebrae. Patients manifest dwarfism with short, bowed, rigid limbs and characteristic facies. Boomerang dysplasia is distinguished from atelosteogenesis on the basis of a more severe defect in mineralization, with complete absence of ossification in some limb elements and vertebral segments. {ECO:0000269|PubMed:15994868}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseLarsen syndrome (LRS) [MIM:150250]: An osteochondrodysplasia characterized by large-joint dislocations and characteristic craniofacial abnormalities. The cardinal features of the condition are dislocations of the hip, knee and elbow joints, with equinovarus or equinovalgus foot deformities. Spatula-shaped fingers, most marked in the thumb, are also present. Craniofacial anomalies include hypertelorism, prominence of the forehead, a depressed nasal bridge, and a flattened midface. Cleft palate and short stature are often associated features. Spinal anomalies include scoliosis and cervical kyphosis. Hearing loss is a well-recognized complication. {ECO:0000269|PubMed:14991055, ECO:0000269|PubMed:16801345}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseNote=Interaction with FLNA may compensate for dysfunctional FLNA homodimer in the periventricular nodular heterotopia (PVNH) disorder.
DiseaseSpondylocarpotarsal synostosis syndrome (SCT) [MIM:272460]: Disorder characterized by short stature and vertebral, carpal and tarsal fusions. {ECO:0000269|PubMed:14991055}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DomainComprised 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. The first hinge region prevents binding to ITGA and ITGB subunits.
FunctionConnects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro.
InteractionSelf; NbExp=4; IntAct=EBI-352089, EBI-352089; P21333:FLNA; NbExp=5; IntAct=EBI-352089, EBI-350432; P62993:GRB2; NbExp=2; IntAct=EBI-352089, EBI-401755; P05161:ISG15; NbExp=4; IntAct=EBI-352089, EBI-746466; Q13233:MAP3K1; NbExp=2; IntAct=EBI-352089, EBI-49776; Q9Y6R4:MAP3K4; NbExp=2; IntAct=EBI-352089, EBI-448104; P16333:NCK1; NbExp=3; IntAct=EBI-352089, EBI-389883; P63000:RAC1; NbExp=2; IntAct=EBI-352089, EBI-413628;
PtmISGylation prevents ability to interact with the upstream activators of the JNK cascade and inhibits IFNA-induced JNK signaling. {ECO:0000269|PubMed:19270716}.
PtmUbiquitination by a SCF-like complex containing ASB2 isoform 2 leads to proteasomal degradation which promotes muscle differentiation. {ECO:0000269|PubMed:19300455}.
Sequence CautionSequence=AAA35505.1; Type=Frameshift; Positions=2432, 2589; Evidence={ECO:0000305};
SimilarityBelongs to the filamin family. {ECO:0000305}.
SimilarityContains 1 actin-binding domain. {ECO:0000305}.
SimilarityContains 24 filamin repeats. {ECO:0000255|PROSITE- ProRule:PRU00087}.
SimilarityContains 2 CH (calponin-homology) domains. {ECO:0000255|PROSITE-ProRule:PRU00044}.
Subcellular LocationIsoform 1: Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. Note=In differentiating myotubes, isoform 1, isoform 2 and isoform 3 are localized diffusely throughout the cytoplasm with regions of enrichment at the longitudinal actin stress fiber. In differentiated tubes, isoform 1 is also detected within the Z- lines.
Subcellular LocationIsoform 2: Cytoplasm, cytoskeleton. Note=Predominantly localized at actin stress fibers.
Subcellular LocationIsoform 3: Cytoplasm, cytoskeleton. Note=Predominantly localized at actin stress fibers.
Subcellular LocationIsoform 6: Cytoplasm, cytoskeleton. Note=Polarized at the periphery of myotubes.
SubunitHomodimer. Interacts with MICALL2 (By similarity). Interacts with FAM101A and FAM101B (By similarity). Isoform 1 interacts with FBLP1, FLNA, FLNC, GP1BA, INPPL1, ITGB1A, PSEN1 and PSEN2. Isoform 3 interacts with ITGB1A, ITGB1D, ITGB3 and ITGB6. Interacts with MYOT and MYOZ1. Interacts with HBV capsid protein. {ECO:0000250, ECO:0000250|UniProtKB:Q80X90, ECO:0000269|PubMed:10754391, ECO:0000269|PubMed:11739414, ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:12393796, ECO:0000269|PubMed:12496242, ECO:0000269|PubMed:12525170, ECO:0000269|PubMed:16076904, ECO:0000269|PubMed:9437013, ECO:0000269|PubMed:9651345, ECO:0000269|PubMed:9694715}.
Tissue SpecificityUbiquitous. Isoform 1 and isoform 2 are expressed in placenta, bone marrow, brain, umbilical vein endothelial cells (HUVEC), retina and skeletal muscle. Isoform 1 is predominantly expressed in prostate, uterus, liver, thyroid, stomach, lymph node, small intestine, spleen, skeletal muscle, kidney, placenta, pancreas, heart, lung, platelets, endothelial cells, megakaryocytic and erythroleukemic cell lines. Isoform 2 is predominantly expressed in spinal cord, platelet and Daudi cells. Also expressed in thyroid adenoma, neurofibrillary tangles (NFT), senile plaques in the hippocampus and cerebral cortex in Alzheimer disease (AD). Isoform 3 and isoform 6 are expressed predominantly in lung, heart, skeletal muscle, testis, spleen, thymus and leukocytes. Isoform 4 and isoform 5 are expressed in heart. {ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:8327473, ECO:0000269|PubMed:9651345, ECO:0000269|PubMed:9694715}.
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