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 score
0.38
Frequency
5
Transmembrane count
Protein classification
Disease related genesHuman disease related genesPlasma proteinsPotential drug targetsPredicted intracellular proteinsTransporters
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
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
Disease related genesHuman disease related genesPlasma proteinsPotential drug targetsPredicted intracellular proteinsTransporters
Protein Function
  • 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
ABP-280FLNFLN1OPD1OPD2
Gene Description
Filamin A
Chromosome
X
Position
154348524-154374634
Frequency
5
EVMP Score
0.38
Fluorescence & Localization
FLNA fluorescence
Cell SpecificEnterocytes
Function & Pathway
Protein Function
  • 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
Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

45 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
FLNAPPP3CCP48454S2,152phosphorylationSIGNOR_ProtMapperProtMapperProtMapper:16442073
FLNAPPP3CAQ08209S2,152dephosphorylationSIGNORDEPODDEPOD:16442073SIGNOR:16442073
FLNAPPP3CAQ08209S2,152phosphorylationSIGNOR_ProtMapperKEAProtMapperProtMapper:16442073KEA:15024089
FLNAPPP3R1P63098S2,152dephosphorylationSIGNORSIGNOR:16442073
FLNAPPP3R1P63098S2,152phosphorylationSIGNOR_ProtMapperProtMapperProtMapper:16442073
FLNAPRKACAP17612S2,152phosphorylationphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperSIGNOR:15228085ProtMapper:15228085KEA:15024089
FLNAPRKACAP17612S2,615phosphorylationKEAKEA:17564427
FLNAPRKACAP17612S343phosphorylationKEAKEA:17564427
FLNAPRKACAP17612T2,336phosphorylationKEAKEA:17564427
FLNARPS6KA1Q15418S2,152phosphorylationphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:15024089KEA:15024089SIGNOR:15024089KEA:12198493
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Ligand-Receptor Signaling

18 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
ecmecmMatrixDBYesNoNoNoNo
ecmecmOmniPathYesNoNoNoNo
extracellularextracellularOmniPathNoNoNoNoNo
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
cell_adhesioncell_adhesionCellinkerYesYesNoNoNo
adhesionadhesionOmniPathYesYesNoNoNo
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Regulatory Interaction Network

19 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
PP2BBP16298FLNAP21333YesNoYesSIGNOR_ProtMapperSIGNORProtMapperDEPODDEPOD:16442073SIGNOR:16442073ProtMapper:16442073
COMPLEX:P63098_Q08209FLNAP21333YesNoYesSIGNORSIGNOR:16442073
FLNAP21333MP2K7O14733YesYesNoSIGNORSIGNOR:20156194
FBLI1Q8WUP2FLNAP21333YesYesNoAdhesomeSIGNORHPRDHINTBioGRIDWangLit-BM-17HINT:18829455Lit-BM-17:12679033Adhesome:12679033HINT:12679033BioGRID:24165133SIGNOR:24165133HPRD:12679033HINT:33961781
PP2BAQ08209FLNAP21333YesNoYesSIGNORProtMapperDEPODELMKinexus_KEAKEASIGNOR_ProtMapperDEPOD:16442073ProtMapper:16442073SIGNOR:16442073KEA:15024089ELM:32645368
KS6A1Q15418FLNAP21333YesYesNophosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperPhosphoSite_KEAKEAKinexus_KEASIGNOR_ProtMapperPhosphoSite_ProtMapperProtMapper:15024089KEA:15024089SIGNOR:15024089KEA:12198493
FLNAP21333KCND2Q9NZV8YesYesNoSIGNORSIGNOR:11102480
CDK1P06493FLNAP21333YesNoNoSparser_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPPhosphoSite_ProtMapperHPRD_MIMPPhosphoSite_norefiPTMnetProtMapperRLIMS-P_ProtMapperKEAKinexus_KEAPhosphoSiteNetworKIN_KEAPhosphoSite:17408621KEA:17570479PhosphoSite:25445790ProtMapper:17408621KEA:18669648KEA:17408621ProtMapper:25445790
KCC2AQ9UQM7FLNAP21333YesNoNophosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointProtMapperPhosphoSite_KEAKEAKinexus_KEAPhosphoSitePhosphoSite_ProtMapperPhosphoSite:11290523KEA:11290523
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Protein Complex Composition

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

Isolation & Detection Technology

0 records.

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
DeafnessDisease variant
Related Diseases
Biomarker
Phase 2
Interaction Protein
ENSG00000077549ENSG00000085733ENSG00000114416ENSG00000134640ENSG00000136068ENSG00000150093ENSG00000164104
Interaction Count
7
Interaction Dataset
biogrid_opencellintact_biogrid