{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O75369","secondaryAccessions":["B2ZZ83","B2ZZ84","B2ZZ85","C9JKE6","C9JMC4","Q13706","Q59EC2","Q60FE7","Q6MZJ1","Q8WXS9","Q8WXT0","Q8WXT1","Q8WXT2","Q8WXT3","Q9NRB5","Q9NT26","Q9UEV9"],"uniProtkbId":"FLNB_HUMAN","entryAudit":{"firstPublicDate":"2003-11-07","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2010-05-18","entryVersion":250,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Filamin-B"},"shortNames":[{"value":"FLN-B"}]},"alternativeNames":[{"fullName":{"value":"ABP-278"}},{"fullName":{"value":"ABP-280 homolog"}},{"fullName":{"value":"Actin-binding-like protein"}},{"fullName":{"value":"Beta-filamin"}},{"fullName":{"value":"Filamin homolog 1"},"shortNames":[{"value":"Fh1"}]},{"fullName":{"value":"Filamin-3"}},{"fullName":{"value":"Thyroid autoantigen"}},{"fullName":{"value":"Truncated actin-binding protein"},"shortNames":[{"value":"Truncated ABP"}]}]},"genes":[{"geneName":{"value":"FLNB"},"synonyms":[{"value":"FLN1L"},{"value":"FLN3"},{"value":"TABP"},{"value":"TAP"}]}],"comments":[{"texts":[{"value":"Connects 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"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q80X90"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10754391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11739414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11807098"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12393796"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12496242"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12525170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16076904"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9437013"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9651345"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9694715"}],"value":"Homodimer. Interacts with MICALL2 (By similarity). Interacts with RFLNA and RFLNB (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. Interacts with ASB2 isoform 1; the interaction targets FLNB for proteasomal degradation (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"O75369","intActId":"EBI-352089"},"interactantTwo":{"uniProtKBAccession":"P21333","geneName":"FLNA","intActId":"EBI-350432"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75369","intActId":"EBI-352089"},"interactantTwo":{"uniProtKBAccession":"O75369","geneName":"FLNB","intActId":"EBI-352089"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75369","intActId":"EBI-352089"},"interactantTwo":{"uniProtKBAccession":"P62993","geneName":"GRB2","intActId":"EBI-401755"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75369","intActId":"EBI-352089"},"interactantTwo":{"uniProtKBAccession":"P05161","geneName":"ISG15","intActId":"EBI-746466"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75369","intActId":"EBI-352089"},"interactantTwo":{"uniProtKBAccession":"Q13233","geneName":"MAP3K1","intActId":"EBI-49776"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75369","intActId":"EBI-352089"},"interactantTwo":{"uniProtKBAccession":"Q9Y6R4","geneName":"MAP3K4","intActId":"EBI-448104"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75369","intActId":"EBI-352089"},"interactantTwo":{"uniProtKBAccession":"P16333","geneName":"NCK1","intActId":"EBI-389883"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O75369","intActId":"EBI-352089"},"interactantTwo":{"uniProtKBAccession":"P63000","geneName":"RAC1","intActId":"EBI-413628"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Isoform 1","note":{"texts":[{"value":"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. 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Repeat 24 and the second hinge domain are important for dimer formation. The first hinge region prevents binding to ITGA and ITGB subunits"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19270716"}],"value":"ISGylation prevents ability to interact with the upstream activators of the JNK cascade and inhibits IFNA-induced JNK signaling"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19300455"}],"value":"Ubiquitination by a SCF-like complex containing ASB2 isoform 1 leads to proteasomal degradation which promotes muscle differentiation"}],"commentType":"PTM"},{"commentType":"DISEASE","note":{"texts":[{"value":"Interaction with FLNA may compensate for dysfunctional FLNA homodimer in the periventricular nodular heterotopia (PVNH) disorder"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Atelosteogenesis 1","diseaseAccession":"DI-00142","acronym":"AO1","description":"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.","diseaseCrossReference":{"database":"MIM","id":"108720"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14991055"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Atelosteogenesis 3","diseaseAccession":"DI-00144","acronym":"AO3","description":"A short-limb lethal skeletal dysplasia with vertebral abnormalities, disharmonious skeletal maturation, poorly modeled long bones and joint dislocations. 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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. 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