FLNA

Protein-coding gene in humans From Wikipedia, the free encyclopedia

Filamin A, alpha (FLNA) is a protein that in humans is encoded by the FLNA gene.[5][6]

PDBOrtholog search: PDBe RCSB
AliasesFLNA, ABP-280, ABPX, CSBS, CVD1, FLN, FLN-A, FLN1, FMD, MNS, NHBP, OPD, OPD1, OPD2, XLVD, XMVD, filamin A, FGS2
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FLNA
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesFLNA, ABP-280, ABPX, CSBS, CVD1, FLN, FLN-A, FLN1, FMD, MNS, NHBP, OPD, OPD1, OPD2, XLVD, XMVD, filamin A, FGS2
External IDsOMIM: 300017; MGI: 95556; HomoloGene: 1119; GeneCards: FLNA; OMA:FLNA - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001110556
NM_001456

NM_001290421
NM_010227

RefSeq (protein)

NP_001104026
NP_001447

NP_001277350
NP_034357
NP_001390993

Location (UCSC)Chr X: 154.35 – 154.37 MbChr X: 73.27 – 73.29 Mb
PubMed search[3][4]
Wikidata
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Structure

The structure of filamin A, alpha includes an actin binding N terminal domain, 24 internal repeats and 2 hinge regions.[7][8]

Function

Actin-binding protein, or filamin, is a 280-kD protein that crosslinks actin filaments into orthogonal networks in cortical cytoplasm and participates in the anchoring of membrane proteins for the actin cytoskeleton. Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. Filamin A, encoded by the FLNA gene, is a widely expressed filamin that regulates the reorganization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes, and secondary messengers.[9] At least 31 disease-causing mutations in this gene have been discovered.[10]

DNA repair

Interaction of FLNA with the BRCA1 protein is required for efficient regulation of early stages of DNA repair processes.[11] FLNA is implicated in the control of the DNA repair process of homologous recombination and non-homologous end joining.[11]

Interactions

Filamin has been shown to interact with:

References

Further reading

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