Protein detail

FLNA

Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin)

Entry name
FLNA
UniProt ID
EVMP confidence score
0.53
Supporting publications (n)
5
Transmembrane count
Protein classification
Disease related genesHuman disease related genesPlasma proteinsPotential drug targetsPredicted intracellular proteinsTransporters
Basic Information
Protein Names
Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin)
Protein Class (6)
Disease related genesHuman disease related genesPlasma proteinsPotential drug targetsPredicted intracellular proteinsTransporters
Protein Function (9)
  • Predicted intracellular proteins
  • Human disease related genes:Congenital malformations:Congenital malformations of the musculoskeletal system
  • Human disease related genes:Digestive system diseases:Gastrointestinal diseases
  • Potential drug targets
  • Human disease related genes:Congenital malformations:Congenital malformations of the circulatory system
  • Human disease related genes:Congenital malformations:Congenital malformations of the nervous system
  • Transporters:Accessory Factors Involved in Transport
  • Disease related genes
  • Human disease related genes:Congenital malformations:Other congenital malformations
Entrez Gene Symbol
Gene Synonym (5)
ABP-280FLNFLN1OPD1OPD2
Gene Description
Filamin A
Chromosome
X
Position
154348524-154374634
Supporting publications (n)
5
EVMP confidence score
0.53
Fluorescence & Localization
FLNA fluorescence
Cell SpecificEnterocytes
Function & Pathway
Protein Function (9)
  • Predicted intracellular proteins
  • Human disease related genes:Congenital malformations:Congenital malformations of the musculoskeletal system
  • Human disease related genes:Digestive system diseases:Gastrointestinal diseases
  • Potential drug targets
  • Human disease related genes:Congenital malformations:Congenital malformations of the circulatory system
  • Human disease related genes:Congenital malformations:Congenital malformations of the nervous system
  • Transporters:Accessory Factors Involved in Transport
  • Disease related genes
  • Human disease related genes:Congenital malformations:Other congenital malformations
Mediation Categories (6)
Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence90

Enzyme-Mediated Modification (45)

45 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
FLNARPS6P62753S2,152phosphorylationSparser_ProtMapperProtMapperProtMapper:18598695
FLNAPRKCAP17252S2,152phosphorylationSparser_ProtMapperProtMapperProtMapper:24309511ProtMapper:21807941
FLNAIGF1P05019S2,152phosphorylationSparser_ProtMapperProtMapperProtMapper:18598695
FLNACAMK2BQ13554S2,523phosphorylationKEAKEA:11290523
FLNACAMK2DQ13557S2,523phosphorylationKEAKEA:11290523
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Ligand-Receptor Signaling (18)

18 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
cell_adhesioncell_adhesionOmniPathYesYes
actin_regulation_adhesomeintracellular_intercellular_relatedAdhesomeYes
intracellular_intercellular_relatedintracellular_intercellular_relatedOmniPathYes
transmembranetransmembraneRamilowski_location
transmembranetransmembraneOmniPath
plasma_membraneplasma_membraneCellinker
plasma_membraneplasma_membraneOmniPath
transmembranetransmembrane_predictedPhobius
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Regulatory Interaction Network (19)

19 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
PAK1Q13153FLNAP21333YesYesHPRD_MIMPSIGNORProtMapperPhosphoSite_KEAphosphoELM_KEAPhosphoNetworksHPRDWangPhosphoSite_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPPhosphoSite_norefiPTMnetKEAphosphoELMSIGNOR_ProtMapperREACH_ProtMapperPhosphoSiteSparser_ProtMapperAdhesomeSPIKE_LCSPIKEProtMapper:24278701SPIKE_LC:12198493HPRD:12198493SIGNOR:12198493ProtMapper:18598695ProtMapper:30568657SPIKE:12198493phosphoELM:12198493PhosphoSite:12198493Adhesome:15024089KEA:12198493KEA:18088087ProtMapper:23246867Adhesome:12198493ProtMapper:18201775ProtMapper:12198493ProtMapper:25472536KEA:15024089ProtMapper:26009991
ROR2Q01974FLNAP21333YesYesSPIKESPIKE_LCSIGNORSPIKE_LC:20359892SIGNOR:18667433SPIKE:20359892
FLNAP21333MP2K4P45985YesYesHPRDWangSIGNORSignaLink3SIGNOR:9006895HPRD:9006895SignaLink3:23331499SignaLink3:9006895SIGNOR:20156194
KAPCAP17612FLNAP21333YesYesWangphosphoELM_MIMPAdhesomeMIMPPhosphoSite_MIMPHPRD_MIMPiPTMnetSIGNORProtMapperCui2007KEACA1Kinexus_KEASIGNOR_ProtMapperPhosphoSite_ProtMapperKEA:17564427CA1:207708Adhesome:15228085SIGNOR:15228085CA1:15228085ProtMapper:15228085Adhesome:207708KEA:15024089
COMPLEX:P07359_P13224_P14770_P40197FLNAP21333YesYesSIGNORSIGNOR:16293600
PP2BCP48454FLNAP21333YesYesSIGNOR_ProtMapperSIGNORProtMapperDEPODDEPOD:16442073SIGNOR:16442073ProtMapper:16442073
ST38LQ9Y2H1FLNAP21333YesYesREACH_ProtMapperSIGNORSparser_ProtMapperProtMapperProtMapper:33330471ProtMapper:34207234SIGNOR:30568657ProtMapper:30568657
ASB2Q96Q27FLNAP21333YesYesHINTSIGNORBioGRIDBioGRID:21750192HINT:24052262SIGNOR:18799729HINT:21750192HINT:18799729BioGRID:24052262
KCC2GQ13555FLNAP21333YesphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperHPRDPhosphoSite_KEAKEAHPRD_KEASIGNOR_ProtMapperHPRD-phosKEA:11290523ProtMapper:11290523HPRD-phos:11290523HPRD:11290523SIGNOR:11290523
MASP04201FLNAP21333YesYesSIGNORSIGNOR:26460884
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Protein Complex Composition (8)

8 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
Filamin A homodimerFLNAP213332ComplexPortalPDBPDB:2wfnPDB:3rghPDB:2j3sintact:EBI-10758568PDB:3horPDB:9lwxPDB:3hopPDB:3cnkPDB:3hoc14755292
FLNALMNAMYCSUMO2P01106P02545P21333P619561:1:1:1CompleatCFinderCompleat:HC9125
ALDOAFLNALGALS1TTC41PP04075P09382P21333Q6P2S70:0:0:0Havugimana2012Havugimana2012:C_186
FLNAGP1BAP07359P213332:2PDBPDB:2bp3
ACTG1CLTACLTBCLTCFLNAP09496P09497P21333P63261Q006100:0:0:0:0hu.MAP2
CLTACLTCFLNAP09496P21333Q006100:0:0hu.MAP2
FLNAPRR5RPS9P21333P46781P852991:1:1CompleatCFinderCompleat:HC7427
FBLIM1FLNAP21333Q8WUP22:1PDBPDB:4p3wPDB:2w0p
Sequence, Structure & Domains

Sequences

Length
2,647
Mass
280,739
Sequence
MSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLFAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSPFSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKVEPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQCYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKVPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTALAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHCDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPRLVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGSPYRVVVP
Alternative Products
Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P21333-1; Sequence=Displayed; Name=2; IsoId=P21333-2; Sequence=VSP_035454; Name=3; Synonyms=VAR-1; IsoId=P21333-3; Sequence=VSP_062479
Alternative Sequence
1649..1656; Missing (in isoform 2); 2127..2167; Missing (in isoform 3)

3D Structural Models

Turn
67..73; 1785..1787; 1891..1893; 2264..2266; 2316..2318; 2429..2431; 2455..2457
Helix
40..43; 44..57; 58..60; 75..85; 100..116; 126..130; 134..149; 168..179; 190..192; 196..205; 213..215; 221..236; 244..247; 254..261; 263..266; 480..482; 488..490; 584..586; 672..674; 680..682; 1160..1162; 1168..1170; 1873..1875; 2041..2043; 2047..2049; 2055..2057; 2171..2173; 2238..2240; 2246..2248; 2437..2439; 2565..2567
Beta Strand
157..159; 181..183; 193..195; 484..487; 501..506; 515..521; 529..534; 537..542; 548..556; 565..571; 579..583; 588..590; 595..604; 609..617; 620..625; 627..636; 639..649; 658..664; 676..679; 683..685; 693..698; 707..712; 714..716; 721..725; 727..735; 739..749; 758..762; 1164..1167; 1172..1174; 1179..1184; 1193..1198; 1206..1211; 1213..1222; 1225..1235; 1244..1250; 1791..1796; 1804..1809; 1819..1822; 1824..1832; 1838..1846; 1855..1860; 1865..1867; 1869..1872; 1877..1879; 1884..1889; 1895..1906; 1909..1914; 1916..1925; 1930..1938; 1947..1953; 1959..1967; 1980..1988; 1998..2001; 2007..2010; 2014..2025; 2034..2039; 2051..2054; 2059..2061; 2066..2071; 2075..2077; 2080..2088; 2091..2096; 2100..2107; 2112..2120; 2129..2136; 2139..2148; 2161..2165; 2174..2179; 2185..2187; 2189..2192; 2194..2201; 2208..2216; 2225..2229; 2234..2236; 2242..2245; 2251..2253; 2257..2262; 2268..2279; 2282..2287; 2289..2298; 2303..2311; 2320..2326; 2433..2436; 2441..2443; 2448..2453; 2462..2470; 2472..2479; 2482..2489; 2491..2506; 2511..2518; 2561..2564; 2576..2581; 2590..2595; 2597..2599; 2602..2610; 2613..2619; 2624..2632; 2641..2646
3D Structure
Electron microscopy (1); NMR spectroscopy (7); X-ray crystallography (18)

Domain & Motif Annotations

Compositional Bias
1..15; Low complexity; 22..39; Basic and acidic residues
Repeat
276..374; Filamin 1; 376..474; Filamin 2; 475..570; Filamin 3; 571..663; Filamin 4; 667..763; Filamin 5; 764..866; Filamin 6; 867..965; Filamin 7; 966..1061; Filamin 8; 1062..1154; Filamin 9; 1155..1249; Filamin 10; 1250..1349; Filamin 11; 1350..1442; Filamin 12; 1443..1539; Filamin 13; 1540..1636; Filamin 14; 1649..1740; Filamin 15; 1779..1860; Filamin 16; 1861..1950; Filamin 17; 1951..2039; Filamin 18; 2042..2131; Filamin 19; 2132..2230; Filamin 20; 2233..2325; Filamin 21; 2327..2420; Filamin 22; 2424..2516; Filamin 23; 2552..2646; Filamin 24
Domain (CC)
Comprised of a NH2-terminal actin-binding domain, 24 immunoglobulin-like internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. Filamin repeat 20 interacts with filamin repeat 21 masking the ligand binding site on filamin repeat 21, resulting in an autoinhibited conformation (PubMed:17690686). The autoinhibition can be relieved by ligands like ITGB7 or FBLIM1 (PubMed:21524097). Filamin repeats 19 and 21 can simultaneously engage ligands (PubMed:21524097).
Domain (FT)
43..149; Calponin-homology (CH) 1; 166..269; Calponin-homology (CH) 2
Region
1..39; Disordered; 2..274; Actin-binding; 271..294; Disordered; 1361..1382; Disordered; 1490..1607; Interaction with furin; 1741..1778; Hinge 1; 2517..2647; Self-association site, tail; 2517..2551; Hinge 2
Protein Families
Filamin family
Sequence Similarities
Belongs to the filamin family.
Clinical Relevance
Disease Involvement (2)
DeafnessDisease variant
Related Diseases (2)
Biomarker
Phase 2
Interaction Protein (7)
ENSG00000077549ENSG00000085733ENSG00000114416ENSG00000134640ENSG00000136068ENSG00000150093ENSG00000164104
Interaction Count
7
Interaction Dataset (2)
biogrid_opencellintact_biogrid
Supporting Publications5
PMIDTitleRelated sentences
28986585Quantitation of putative colorectal cancer biomarker candidates in serum extracellular vesicles by targeted proteomics.No related sentences available
32089743Human umbilical cord mesenchymal stromal cells-derived extracellular vesicles exert potent bone protective effects by CLEC11A-mediated regulation of bone metabolism.No related sentences available
33709510Unbiased proteomic profiling of host cell extracellular vesicle composition and dynamics upon HIV-1 infection.No related sentences available
35611462Extracellular vesicles expressing CEACAM proteins in the urine of bladder cancer patients.No related sentences available
38321535Identification of specific markers for human pluripotent stem cell-derived small extracellular vesicles.No related sentences available