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 |
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.70High >= 0.60Medium >= 0.40Low >= 0.30Basic 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
Ensembl
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
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
Cellular Component (27)
- GO:0002102 podosome
- GO:0005576 extracellular region
- GO:0005634 nucleus
- GO:0005730 nucleolus
- GO:0005737 cytoplasm
- GO:0005802 trans-Golgi network
- GO:0005829 cytosol
- GO:0005884 actin filament
- GO:0005886 plasma membrane
- GO:0005903 brush border
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Molecular Function (15)
- GO:0001664 G protein-coupled receptor binding
- GO:0003723 RNA binding
- GO:0005080 protein kinase C binding
- GO:0005515 protein binding
- GO:0015459 potassium channel regulator activity
- GO:0019900 kinase binding
- GO:0031267 small GTPase binding
- GO:0034988 Fc-gamma receptor I complex binding
- GO:0042803 protein homodimerization activity
- GO:0044325 transmembrane transporter binding
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Biological Process (3)
KEGG (5)
Reactome (14)
- R-hsa-1169410 antimicrobial mechanism of ifn stimulated genes
- R-hsa-1500931 cell cell communication
- R-hsa-446353 cell extracellular matrix interactions
- R-hsa-446728 cell junction organization
- R-hsa-1280215 cytokine signaling in immune system
- R-hsa-430116 gp1b ix v activation signalling
- R-hsa-109582 hemostasis
- R-hsa-913531 interferon signaling
- R-hsa-8983711 oas antiviral response
- R-hsa-76002 platelet activation signaling and aggregation
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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 Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| FLNA | PAK1 | Q13153 | S | 2,152 | phosphorylation | Sparser_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEAphosphoELMSIGNOR_ProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapper | phosphoELM:12198493KEA:12198493ProtMapper:24278701ProtMapper:25472536ProtMapper:12198493KEA:18088087SIGNOR:12198493KEA:15024089ProtMapper:23246867ProtMapper:18598695ProtMapper:26009991 |
| FLNA | PAK1 | Q13153 | S | 2,292 | phosphorylation | PhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper | |
| FLNA | PAK1 | Q13153 | S | 2,370 | phosphorylation | PhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper | |
| FLNA | PAK1 | Q13153 | T | 1,089 | phosphorylation | PhosphoNetworks | |
| FLNA | PAK1 | Q13153 | S | 2,045 | phosphorylation | PhosphoNetworks | |
| FLNA | PAK1 | Q13153 | T | 2,328 | phosphorylation | PhosphoNetworks | |
| FLNA | PAK1 | Q13153 | T | 2,478 | phosphorylation | PhosphoNetworks | |
| FLNA | PPP3CB | P16298 | S | 2,152 | dephosphorylation | SIGNORDEPOD | DEPOD:16442073SIGNOR:16442073 |
| FLNA | PPP3CB | P16298 | S | 2,152 | phosphorylation | SIGNOR_ProtMapperProtMapper | ProtMapper:16442073 |
| FLNA | PPP3CC | P48454 | S | 2,152 | dephosphorylation | SIGNORDEPOD | DEPOD:16442073SIGNOR:16442073 |
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Ligand-Receptor Signaling (18)
18 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| ecm | ecm | MatrixDB | Yes | ||||
| ecm | ecm | OmniPath | Yes | ||||
| extracellular | extracellular | OmniPath | |||||
| intracellular | intracellular | LOCATE | |||||
| intracellular | intracellular | ComPPI | |||||
| intracellular | intracellular | GO_Intercell | |||||
| intracellular | intracellular | UniProt_location | |||||
| intracellular | intracellular | OmniPath | |||||
| cell_adhesion | cell_adhesion | Cellinker | Yes | Yes | |||
| adhesion | adhesion | OmniPath | Yes | Yes |
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Regulatory Interaction Network (19)
19 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| PP2BB | P16298 | FLNA | P21333 | Yes | Yes | SIGNOR_ProtMapperSIGNORProtMapperDEPOD | DEPOD:16442073SIGNOR:16442073ProtMapper:16442073 | |
| COMPLEX:P63098_Q08209 | FLNA | P21333 | Yes | Yes | SIGNOR | SIGNOR:16442073 | ||
| FLNA | P21333 | MP2K7 | O14733 | Yes | Yes | SIGNOR | SIGNOR:20156194 | |
| FBLI1 | Q8WUP2 | FLNA | P21333 | Yes | Yes | AdhesomeSIGNORHPRDHINTBioGRIDWangLit-BM-17 | HINT:18829455Lit-BM-17:12679033Adhesome:12679033HINT:12679033BioGRID:24165133SIGNOR:24165133HPRD:12679033HINT:33961781 | |
| PP2BA | Q08209 | FLNA | P21333 | Yes | Yes | SIGNORProtMapperDEPODELMKinexus_KEAKEASIGNOR_ProtMapper | DEPOD:16442073ProtMapper:16442073SIGNOR:16442073KEA:15024089ELM:32645368 | |
| KS6A1 | Q15418 | FLNA | P21333 | Yes | Yes | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperPhosphoSite_KEAKEAKinexus_KEASIGNOR_ProtMapperPhosphoSite_ProtMapper | ProtMapper:15024089KEA:15024089SIGNOR:15024089KEA:12198493 | |
| FLNA | P21333 | KCND2 | Q9NZV8 | Yes | Yes | SIGNOR | SIGNOR:11102480 | |
| CDK1 | P06493 | FLNA | P21333 | Yes | Sparser_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPPhosphoSite_ProtMapperHPRD_MIMPPhosphoSite_norefiPTMnetProtMapperRLIMS-P_ProtMapperKEAKinexus_KEAPhosphoSiteNetworKIN_KEA | PhosphoSite:17408621KEA:17570479PhosphoSite:25445790ProtMapper:17408621KEA:18669648KEA:17408621ProtMapper:25445790 | ||
| KCC2A | Q9UQM7 | FLNA | P21333 | Yes | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointProtMapperPhosphoSite_KEAKEAKinexus_KEAPhosphoSitePhosphoSite_ProtMapper | PhosphoSite:11290523KEA:11290523 |
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Protein Complex Composition (8)
8 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| Filamin A homodimer | FLNA | P21333 | 2 | ComplexPortalPDB | PDB:2wfnPDB:3rghPDB:2j3sintact:EBI-10758568PDB:3horPDB:9lwxPDB:3hopPDB:3cnkPDB:3hoc | 14755292 |
| FLNALMNAMYCSUMO2 | P01106P02545P21333P61956 | 1:1:1:1 | CompleatCFinder | Compleat:HC9125 | ||
| ALDOAFLNALGALS1TTC41P | P04075P09382P21333Q6P2S7 | 0:0:0:0 | Havugimana2012 | Havugimana2012:C_186 | ||
| FLNAGP1BA | P07359P21333 | 2:2 | PDB | PDB:2bp3 | ||
| ACTG1CLTACLTBCLTCFLNA | P09496P09497P21333P63261Q00610 | 0:0:0:0:0 | hu.MAP2 | |||
| CLTACLTCFLNA | P09496P21333Q00610 | 0:0:0 | hu.MAP2 | |||
| FLNAPRR5RPS9 | P21333P46781P85299 | 1:1:1 | CompleatCFinder | Compleat:HC7427 | ||
| FBLIM1FLNA | P21333Q8WUP2 | 2:1 | PDB | PDB: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
Drugs
Interaction Protein (7)
ENSG00000077549ENSG00000085733ENSG00000114416ENSG00000134640ENSG00000136068ENSG00000150093ENSG00000164104
Interaction Count
7
Interaction Dataset (2)
biogrid_opencellintact_biogrid
Supporting Publications5
| PMID | Title | Related sentences |
|---|---|---|
| 28986585 | Quantitation of putative colorectal cancer biomarker candidates in serum extracellular vesicles by targeted proteomics. | No related sentences available |
| 32089743 | Human umbilical cord mesenchymal stromal cells-derived extracellular vesicles exert potent bone protective effects by CLEC11A-mediated regulation of bone metabolism. | No related sentences available |
| 33709510 | Unbiased proteomic profiling of host cell extracellular vesicle composition and dynamics upon HIV-1 infection. | No related sentences available |
| 35611462 | Extracellular vesicles expressing CEACAM proteins in the urine of bladder cancer patients. | No related sentences available |
| 38321535 | Identification of specific markers for human pluripotent stem cell-derived small extracellular vesicles. | No related sentences available |