Protein detail

FLNB

Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP)

Protein symbol
FLNB
UniProt ID
EVMP score
0.38
Frequency
1
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-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP)
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
  • Potential drug targets
  • Transporters:Accessory Factors Involved in Transport
  • Disease related genes
  • Human disease related genes:Congenital malformations:Other congenital malformations
Entrez Gene Symbol
Gene Synonym
ABP-278FH1FLN1LLRS1TABPTAP
Gene Description
Filamin B
Chromosome
3
Position
58008398-58172251
Frequency
1
EVMP Score
0.38
Fluorescence & Localization
Tissue SpecificbrainCell SpecificAstrocytesSingle-Nuclei Brain Specificastrocyte
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

2 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
FLNBLCKP06239Y2,502phosphorylationKEAKEA:17570479
FLNBPRKCBP05771S1,937phosphorylationKEAKEA:17570479

Ligand-Receptor Signaling

4 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Regulatory Interaction Network

3 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
FBLI1Q8WUP2FLNBO75369YesYesNoHPRDHINTLit-BM-17SIGNORHPRD:12496242HINT:12496242SIGNOR:24165133Lit-BM-17:12496242HINT:33961781
COMPLEX:Q15369_Q15370_Q93034_Q9UBF6FLNBO75369YesNoYesSIGNORSIGNOR:19300455
ASB2Q96Q27FLNBO75369YesNoYesSIGNORSIGNOR:19300455

Protein Complex Composition

4 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
FLNBNASPPRMT3VCPO60678O75369P49321P550720:0:0:0Havugimana2012Havugimana2012:C_375
FLNBO753694PDBPDB:3ferPDB:5dcpPDB:4b7l
CACYBPFLNBHNRNPA0NUP210O75369Q13151Q8TEM1Q9HB710:0:0:0Havugimana2012Havugimana2012:C_236
APOHRFLNBZCCHC17P02749Q8N5W9Q9NP640:0:0hu.MAP2

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMass spectrometry137886648
Sequence, Structure & Domains

Sequences

Length
2,602
Mass
278,164
Sequence
MPVTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPVWEDEGDDDAKKQTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPQKPVDNAREAMQQADDWLGVPQVITPEEIIHPDVDEHSVMTYLSQFPKAKLKPGAPLKPKLNPKKARAYGRGIEPTGNMVKQPAKFTVDTISAGQGDVMVFVEDPEGNKEEAQVTPDSDKNKTYSVEYLPKVTGLHKVTVLFAGQHISKSPFEVSVDKAQGDASKVTAKGPGLEAVGNIANKPTYFDIYTAGAGVGDIGVEVEDPQGKNTVELLVEDKGNQVYRCVYKPMQPGPHVVKIFFAGDTIPKSPFVVQVGEACNPNACRASGRGLQPKGVRIRETTDFKVDTKAAGSGELGVTMKGPKGLEELVKQKDFLDGVYAFEYYPSTPGRYSIAITWGGHHIPKSPFEVQVGPEAGMQKVRAWGPGLHGGIVGRSADFVVESIGSEVGSLGFAIEGPSQAKIEYNDQNDGSCDVKYWPKEPGEYAVHIMCDDEDIKDSPYMAFIHPATGGYNPDLVRAYGPGLEKSGCIVNNLAEFTVDPKDAGKAPLKIFAQDGEGQRIDIQMKNRMDGTYACSYTPVKAIKHTIAVVWGGVNIPHSPYRVNIGQGSHPQKVKVFGPGVERSGLKANEPTHFTVDCTEAGEGDVSVGIKCDARVLSEDEEDVDFDIIHNANDTFTVKYVPPAAGRYTIKVLFASQEIPASPFRVKVDPSHDASKVKAEGPGLSKAGVENGKPTHFTVYTKGAGKAPLNVQFNSPLPGDAVKDLDIIDNYDYSHTVKYTPTQQGNMQVLVTYGGDPIPKSPFTVGVAAPLDLSKIKLNGLENRVEVGKDQEFTVDTRGAGGQGKLDVTILSPSRKVVPCLVTPVTGRENSTAKFIPREEGLYAVDVTYDGHPVPGSPYTVEASLPPDPSKVKAHGPGLEGGLVGKPAEFTIDTKGAGTGGLGLTVEGPCEAKIECSDNGDGTCSVSYLPTKPGEYFVNILFEEVHIPGSPFKADIEMPFDPSKVVASGPGLEHGKVGEAGLLSVDCSEAGPGALGLEAVSDSGTKAEVSIQNNKDGTYAVTYVPLTAGMYTLTMKYGGELVPHFPARVKVEPAVDTSRIKVFGPGIEGKDVFREATTDFTVDSRPLTQVGGDHIKAHIANPSGASTECFVTDNADGTYQVEYTPFEKGLHVVEVTYDDVPIPNSPFKVAVTEGCQPSRVQAQGPGLKEAFTNKPNVFTVVTRGAGIGGLGITVEGPSESKINCRDNKDGSCSAEYIPFAPGDYDVNITYGGAHIPGSPFRVPVKDVVDPSKVKIAGPGLGSGVRARVLQSFTVDSSKAGLAPLEVRVLGPRGLVEPVNVVDNGDGTHTVTYTPSQEGPYMVSVKYADEEIPRSPFKVKVLPTYDASKVTASGPGLSSYGVPASLPVDFAIDARDAGEGLLAVQITDQEGKPKRAIVHDNKDGTYAVTYIPDKTGRYMIGVTYGGDDIPLSPYRIRATQTGDASKCLATGPGIASTVKTGEEVGFVVDAKTAGKGKVTCTVLTPDGTEAEADVIENEDGTYDIFYTAAKPGTYVIYVRFGGVDIPNSPFTVMATDGEVTAVEEAPVNACPPGFRPWVTEEAYVPVSDMNGLGFKPFDLVIPFAVRKGEITGEVHMPSGKTATPEIVDNKDGTVTVRYAPTEVGLHEMHIKYMGSHIPESPLQFYVNYPNSGSVSAYGPGLVYGVANKTATFTIVTEDAGEGGLDLAIEGPSKAEISCIDNKDGTCTVTYLPTLPGDYSILVKYNDKHIPGSPFTAKITDDSRRCSQVKLGSAADFLLDISETDLSSLTASIKAPSGRDEPCLLKRLPNNHIGISFIPREVGEHLVSIKKNGNHVANSPVSIMVVQSEIGDARRAKVYGRGLSEGRTFEMSDFIVDTRDAGYGGISLAVEGPSKVDIQTEDLEDGTCKVSYFPTVPGVYIVSTKFADEHVPGSPFTVKISGEGRVKESITRTSRAPSVATVGSICDLNLKIPEINSSDMSAHVTSPSGRVTEAEIVPMGKNSHCVRFVPQEMGVHTVSVKYRGQHVTGSPFQFTVGPLGEGGAHKVRAGGPGLERGEAGVPAEFSIWTREAGAGGLSIAVEGPSKAEITFDDHKNGSCGVSYIAQEPGNYEVSIKFNDEHIPESPYLVPVIAPSDDARRLTVMSLQESGLKVNQPASFAIRLNGAKGKIDAKVHSPSGAVEECHVSELEPDKYAVRFIPHENGVHTIDVKFNGSHVVGSPFKVRVGEPGQAGNPALVSAYGTGLEGGTTGIQSEFFINTTRAGPGTLSVTIEGPSKVKMDCQETPEGYKVMYTPMAPGNYLISVKYGGPNHIVGSPFKAKVTGQRLVSPGSANETSSILVESVTRSSTETCYSAIPKASSDASKVTSKGAGLSKAFVGQKSSFLVDCSKAGSNMLLIGVHGPTTPCEEVSMKHVGNQQYNVTYVVKERGDYVLAVKWGEEHIPGSPFHVTVP
Alternative Products
Event=Alternative splicing; Named isoforms=9; Name=1; Synonyms=ABP-278; IsoId=O75369-1; Sequence=Displayed; Name=2; Synonyms=ABP-276; IsoId=O75369-2; Sequence=VSP_008773; Name=3; Synonyms=Var-1; IsoId=O75369-3; Sequence=VSP_008774; Name=7; IsoId=O75369-7; Sequence=VSP_024113, VSP_024114, VSP_024115; Name=4; Synonyms=Var-3; IsoId=O75369-4; Sequence=VSP_008775, VSP_008776; Name=5; Synonyms=Var-2; IsoId=O75369-5; Sequence=VSP_008777, VSP_008778; Name=6; Synonyms=Var-1-DeltaH1; IsoId=O75369-6; Sequence=VSP_008773, VSP_008774; Name=8; IsoId=O75369-8; Sequence=VSP_043446; Name=9; IsoId=O75369-9; Sequence=VSP_024115
Alternative Sequence
1..169; Missing (in isoform 7); 170..181; ALGALVDSCAPG -> MQEHSTRRRSLS (in isoform 7); 1463; R -> RADDTDSQSWRSPLKALSEFFKGDPKGDFNKT (in isoform 8); 1704..1727; Missing (in isoform 2 and isoform 6); 1717..1727; Missing (in isoform 7 and isoform 9); 2081..2121; Missing (in isoform 3 and isoform 6); 2123..2150; EINSSDMSAHVTSPSGRVTEAEIVPMGK -> GVRVMNCSAQILWGWRVQFHTGSRNQQQ (in isoform 4); 2123..2146; EINSSDMSAHVTSPSGRVTEAEIV -> GVRVMNCSAQILWGWRVQFHTGSR (in isoform 5); 2147..2602; Missing (in isoform 5); 2151..2602; Missing (in isoform 4)

3D Structural Models

Turn
40..46; 282..284; 1066..1068; 1173..1175; 1354..1356; 1429..1431; 1448..1450; 1780..1782; 1958..1960; 2011..2013; 2028..2030; 2201..2203; 2384..2386; 2393..2395; 2410..2412; 2512..2514; 2538..2540
Helix
5..10; 13..16; 17..30; 31..33; 48..58; 73..89; 99..103; 107..122; 141..152; 163..165; 169..178; 186..188; 194..208; 217..220; 227..234; 236..239; 254..256; 262..264; 1040..1042; 1048..1051; 1133..1135; 1141..1143; 1236..1239; 1336..1339; 1517..1519; 1525..1527; 1622..1624; 1829..1831; 2002..2004; 2126..2128; 2193..2195; 2520..2523
Beta Strand
258..261; 265..267; 275..280; 289..294; 300..302; 304..309; 313..319; 323..333; 342..347; 1044..1047; 1052..1054; 1059..1064; 1073..1077; 1079..1081; 1084..1089; 1091..1100; 1102..1115; 1122..1128; 1136..1140; 1154..1160; 1166..1172; 1179..1184; 1188..1195; 1200..1208; 1217..1223; 1232..1235; 1249..1254; 1256..1258; 1273..1275; 1281..1284; 1286..1294; 1300..1310; 1317..1321; 1332..1335; 1347..1352; 1361..1369; 1374..1377; 1379..1381; 1383..1387; 1393..1401; 1410..1416; 1425..1428; 1441..1446; 1455..1460; 1462..1464; 1475..1483; 1489..1501; 1506..1512; 1520..1524; 1538..1546; 1566..1570; 1573..1580; 1586..1590; 1593..1596; 1603..1609; 1618..1621; 1625..1639; 1641..1643; 1648..1653; 1663..1666; 1672..1677; 1682..1692; 1699..1705; 1747..1751; 1760..1765; 1775..1779; 1783..1788; 1794..1802; 1811..1816; 1825..1828; 1833..1835; 1840..1845; 1855..1863; 1868..1870; 1872..1880; 1886..1898; 1903..1909; 1924..1927; 1941..1943; 1952..1957; 1961..1966; 1972..1977; 1979..1984; 1989..1994; 1997..1999; 2006..2010; 2014..2016; 2021..2026; 2035..2043; 2057..2061; 2067..2077; 2084..2090; 2111..2113; 2118..2120; 2130..2134; 2140..2142; 2144..2147; 2149..2157; 2164..2175; 2180..2185; 2206..2208; 2210..2214; 2219..2221; 2226..2234; 2236..2240; 2250..2256; 2258..2266; 2275..2281; 2288..2294; 2306..2314; 2320..2324; 2330..2332; 2334..2337; 2340..2347; 2352..2365; 2370..2375; 2388..2392; 2403..2408; 2417..2425; 2430..2433; 2435..2442; 2448..2459; 2466..2473; 2516..2519; 2531..2536; 2545..2547; 2557..2565; 2568..2574; 2579..2583; 2585..2591; 2596..2601
3D Structure
NMR spectroscopy (17); X-ray crystallography (6)

Domain & Motif Annotations

Repeat
249..347; Filamin 1; 349..446; Filamin 2; 447..543; Filamin 3; 544..636; Filamin 4; 640..736; Filamin 5; 737..839; Filamin 6; 840..938; Filamin 7; 939..1034; Filamin 8; 1035..1127; Filamin 9; 1128..1222; Filamin 10; 1223..1322; Filamin 11; 1323..1415; Filamin 12; 1416..1511; Filamin 13; 1512..1608; Filamin 14; 1609..1704; Filamin 15; 1729..1813; Filamin 16; 1816..1908; Filamin 17; 1919..1994; Filamin 18; 1997..2089; Filamin 19; 2091..2185; Filamin 20; 2188..2280; Filamin 21; 2282..2375; Filamin 22; 2379..2471; Filamin 23; 2507..2601; Filamin 24
Domain (CC)
Comprised of a NH2-terminal actin-binding domain, 24 internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. The first hinge region prevents binding to ITGA and ITGB subunits.
Domain (FT)
16..122; Calponin-homology (CH) 1; 139..242; Calponin-homology (CH) 2
Region
1..239; Actin-binding; 244..267; Disordered; 1128..1511; Interaction with FBLP1; 1705..1728; Hinge 1; 1862..2148; Interaction with the cytoplasmic tail of GP1BA; 2060..2225; Interaction with FLNA 1; 2130..2602; Interaction with INPPL1; 2472..2602; Self-association site, tail; 2472..2506; Hinge 2; 2507..2602; Interaction with FLNA 2
Protein Families
Filamin family
Sequence Similarities
Belongs to the filamin family.
Clinical Relevance
Disease Involvement
Disease variantDwarfism
Interaction Protein
ENSG00000080815ENSG00000085733ENSG00000143801ENSG00000187608ENSG00000196924
Interaction Count
5
Interaction Dataset
intact_biogridbiogrid_opencell