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Protein

Filamin-A

Gene

Flna

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Actin binding protein that promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins (By similarity). Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking. Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs (PubMed:17172441). Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintainance (PubMed:20713593).By similarity4 Publications

GO - Molecular functioni

GO - Biological processi

  • actin crosslink formation Source: UniProtKB
  • actin cytoskeleton organization Source: MGI
  • actin cytoskeleton reorganization Source: UniProtKB
  • adenylate cyclase-inhibiting dopamine receptor signaling pathway Source: UniProtKB
  • angiogenesis Source: UniProtKB
  • blood vessel remodeling Source: UniProtKB
  • cell-cell junction organization Source: UniProtKB
  • cilium assembly Source: MGI
  • cytoplasmic sequestering of protein Source: UniProtKB
  • early endosome to late endosome transport Source: MGI
  • epithelial to mesenchymal transition Source: MGI
  • establishment of protein localization Source: UniProtKB
  • heart morphogenesis Source: UniProtKB
  • mitotic spindle assembly Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of neuron projection development Source: WormBase
  • negative regulation of protein catabolic process Source: UniProtKB
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • negative regulation of transcription from RNA polymerase I promoter Source: MGI
  • platelet aggregation Source: MGI
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of integrin-mediated signaling pathway Source: MGI
  • positive regulation of substrate adhesion-dependent cell spreading Source: MGI
  • positive regulation of transcription factor import into nucleus Source: UniProtKB
  • protein localization to cell surface Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • receptor clustering Source: UniProtKB
  • regulation of actin filament bundle assembly Source: UniProtKB
  • semaphorin-plexin signaling pathway Source: WormBase
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-430116. GP1b-IX-V activation signalling.
R-MMU-446353. Cell-extracellular matrix interactions.
R-MMU-5627123. RHO GTPases activate PAKs.

Names & Taxonomyi

Protein namesi
Recommended name:
Filamin-A
Short name:
FLN-A
Alternative name(s):
Actin-binding protein 280
Short name:
ABP-280
Alpha-filamin
Endothelial actin-binding protein
Filamin-1
Non-muscle filamin
Gene namesi
Name:Flna
Synonyms:Fln, Fln1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:95556. Flna.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • actin filament bundle Source: MGI
  • brush border Source: UniProtKB
  • cell cortex Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: GOC
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • growth cone Source: WormBase
  • membrane Source: MGI
  • Myb complex Source: MGI
  • nucleolus Source: MGI
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

Female heterozygous knockout mice show normal development, but 20% die in the first 3-4 months with many anomalies, including lung edema and emphysema, liver thrombi and necrosis, leukocytosis, and heart dilation. Some females die after birth; only about 50% of expected female heterozygous mice are observed at weaning. Male hemizygous knockout mice die by embryonic day E14.5 with vascular defects; their blood vessels are coarse and dilated and extend aberrant branches and sprouts into somitic tissues. Male hemizygous knockout mice display severe cardiac structural defects involving ventricles, atria, and outflow tracts. Conditional Flna knockout males, in the neural crest, survive until birth but die on the first postnatal day with cyanosis; all males show abnormal cardiac outflow tracts (PubMed:17172441). Female heterozygous knockout mice present a mild thrombocytopenia and conditional Flna knockout males, in platelets display a macrothrombocytopenia (PubMed:20713593).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 26472646Filamin-APRO_0000087297Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei20 – 201PhosphoserineCombined sources
Cross-linki42 – 42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki43 – 43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki135 – 135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki299 – 299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei376 – 3761N6-acetyllysineCombined sources
Modified residuei508 – 5081N6-acetyllysineBy similarity
Modified residuei700 – 7001N6-acetyllysineCombined sources
Modified residuei781 – 7811N6-acetyllysineBy similarity
Modified residuei837 – 8371N6-acetyllysineBy similarity
Modified residuei865 – 8651N6-acetyllysineCombined sources
Modified residuei906 – 9061N6-acetyllysineCombined sources
Modified residuei968 – 9681PhosphoserineCombined sources
Modified residuei1055 – 10551PhosphoserineBy similarity
Modified residuei1071 – 10711N6-acetyllysine; alternateCombined sources
Modified residuei1071 – 10711N6-succinyllysine; alternateCombined sources
Modified residuei1084 – 10841PhosphoserineBy similarity
Modified residuei1089 – 10891PhosphothreonineBy similarity
Modified residuei1338 – 13381PhosphoserineBy similarity
Modified residuei1372 – 13721N6-acetyllysineCombined sources
Modified residuei1459 – 14591PhosphoserineCombined sources
Modified residuei1533 – 15331PhosphoserineBy similarity
Modified residuei1538 – 15381N6-acetyllysineCombined sources
Modified residuei1630 – 16301PhosphoserineBy similarity
Modified residuei1734 – 17341PhosphoserineBy similarity
Modified residuei1750 – 17501PhosphothreonineCombined sources
Modified residuei1967 – 19671PhosphoserineBy similarity
Modified residuei2053 – 20531PhosphoserineBy similarity
Modified residuei2152 – 21521PhosphoserineCombined sources
Modified residuei2158 – 21581PhosphoserineBy similarity
Modified residuei2163 – 21631PhosphoserineBy similarity
Modified residuei2180 – 21801PhosphoserineCombined sources
Modified residuei2284 – 22841PhosphoserineBy similarity
Modified residuei2327 – 23271PhosphoserineBy similarity
Modified residuei2329 – 23291PhosphoserineCombined sources
Modified residuei2336 – 23361PhosphothreonineCombined sources
Modified residuei2370 – 23701PhosphoserineCombined sources
Modified residuei2414 – 24141PhosphoserineBy similarity
Modified residuei2510 – 25101PhosphoserineBy similarity
Modified residuei2523 – 25231PhosphoserineCombined sources
Modified residuei2526 – 25261PhosphoserineCombined sources
Modified residuei2569 – 25691N6-acetyllysine; alternateCombined sources
Modified residuei2569 – 25691N6-succinyllysine; alternateCombined sources
Modified residuei2575 – 25751N6-acetyllysineCombined sources
Modified residuei2599 – 25991PhosphothreonineCombined sources
Modified residuei2607 – 26071N6-acetyllysineBy similarity
Modified residuei2621 – 26211N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylation at Ser-2152 is negatively regulated by the autoinhibited conformation of filamin repeats 19-21. Ligand binding induces a conformational switch triggering phosphorylation at Ser-2152 by PKA.By similarity
Polyubiquitination in the CH1 domain by a SCF-like complex containing ASB2 leads to proteasomal degradation. Prior dissociation from actin may be required to expose the target lysines. Ubiquitinated in endothelial cells by RNF213 downstream of the non-canonical Wnt signaling pathway, leading to its degradation by the proteasome.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8BTM8.
MaxQBiQ8BTM8.
PaxDbiQ8BTM8.
PRIDEiQ8BTM8.

PTM databases

iPTMnetiQ8BTM8.
PhosphoSiteiQ8BTM8.
SwissPalmiQ8BTM8.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in Purkinje cells.

Developmental stagei

Widely distributed. Expressed at 12.5 dpc in the ventricular and subventricular zones. Highly expressed at 16 dpc in blood vessels, renal cortices, respiratory and alimentary tracts, olfactory epithelium, presumed isles of hematopoiesis within the liver; lower expression in the cerbral cortex and choroid plexus.1 Publication

Gene expression databases

BgeeiQ8BTM8.
CleanExiMM_FLNA.
ExpressionAtlasiQ8BTM8. baseline and differential.
GenevisibleiQ8BTM8. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with FCGR1A, FLNB, FURIN, HSPB7, KCND2, INPPL1, MYOT, MYOZ1, PDLIM2, ARHGAP24, PSEN1, PSEN2 and ECSCR. Interacts also with various other binding partners in addition to filamentous actin. Interacts (via N-terminus) with TAF1B. Interacts (via N-terminus) with MIS18BP1 (via N-terminus) (By similarity). Interacts with TMEM67 (via C-terminus) and MKS1 (By similarity). Interacts (via actin-binding domain) with MICALL2 (via CH domain). Interacts with FAM101A and FAM101B (PubMed:24436304, PubMed:21709252). Interacts (via filamin repeat 5) with SYK; docks SYK to the plasma membrane. Interacts (via filamin repeats 19 and 21) with DRD3; increased PKA-mediated phosphorylation at Ser-2152. Interacts (via filamin repeat 21) with MAS1, AGTR1 and ADRA1D; increases PKA-mediated phosphorylation of FLNA at Ser-2152. Interacts (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) with GP1BA (high affinity), ITGB7, ITGB2 and FBLIM1 (By similarity).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Plcg2Q8CIH53EBI-641991,EBI-617954

GO - Molecular functioni

Protein-protein interaction databases

BioGridi228662. 13 interactions.
IntActiQ8BTM8. 11 interactions.
MINTiMINT-1867095.
STRINGi10090.ENSMUSP00000098997.

Structurei

3D structure databases

ProteinModelPortaliQ8BTM8.
SMRiQ8BTM8. Positions 39-374, 478-766, 1044-1643, 1773-2328, 2331-2522, 2559-2647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 274273Actin-bindingAdd
BLAST
Domaini43 – 149107CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini166 – 266101CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati276 – 37499Filamin 1Add
BLAST
Repeati376 – 47499Filamin 2Add
BLAST
Repeati475 – 57096Filamin 3Add
BLAST
Repeati571 – 66393Filamin 4Add
BLAST
Repeati667 – 76397Filamin 5Add
BLAST
Repeati764 – 866103Filamin 6Add
BLAST
Repeati867 – 96599Filamin 7Add
BLAST
Repeati966 – 106196Filamin 8Add
BLAST
Repeati1062 – 115493Filamin 9Add
BLAST
Repeati1155 – 124995Filamin 10Add
BLAST
Repeati1250 – 1349100Filamin 11Add
BLAST
Repeati1350 – 144293Filamin 12Add
BLAST
Repeati1443 – 153997Filamin 13Add
BLAST
Repeati1540 – 163697Filamin 14Add
BLAST
Repeati1641 – 1740100Filamin 15Add
BLAST
Repeati1765 – 186096Filamin 16Add
BLAST
Repeati1861 – 195292Filamin 17Add
BLAST
Repeati1953 – 203987Filamin 18Add
BLAST
Repeati2042 – 213493Filamin 19Add
BLAST
Repeati2135 – 223096Filamin 20Add
BLAST
Repeati2233 – 232593Filamin 21Add
BLAST
Repeati2327 – 242094Filamin 22Add
BLAST
Repeati2424 – 251693Filamin 23Add
BLAST
Repeati2552 – 264695Filamin 24Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1490 – 1607118Interaction with furinAdd
BLAST
Regioni1741 – 177838Hinge 1By similarityAdd
BLAST
Regioni2517 – 2647131Self-association site, tailBy similarityAdd
BLAST
Regioni2517 – 255337Hinge 2By similarityAdd
BLAST

Domaini

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. The autoinhibition can be relieved by ligands like ITGB7 or FBLIM1. Filamin repeats 19 and 21 can simultaneously engage ligands.By similarity

Sequence similaritiesi

Belongs to the filamin family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 24 filamin repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0518. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00660000095431.
HOVERGENiHBG004163.
InParanoidiQ8BTM8.
OMAiVQDNEGC.
OrthoDBiEOG76T9QC.
TreeFamiTF313685.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR028559. FLN_A.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11915:SF173. PTHR11915:SF173. 1 hit.
PfamiPF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 24 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BTM8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSSHSRCGQ SAAVASPGGS IDSRDAEMPA TEKDLAEDAP WKKIQQNTFT
60 70 80 90 100
RWCNEHLKCV SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR
110 120 130 140 150
QMQLENVSVA LEFLDRESIK LVSIDSKAIV DGNLKLILGL IWTLILHYSI
160 170 180 190 200
SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL PQLPITNFSR DWQSGRALGA
210 220 230 240 250
LVDSCAPGLC PDWDSWDASK PVNNAREAMQ QADDWLGIPQ VITPEEIVDP
260 270 280 290 300
NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK
310 320 330 340 350
RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV
360 370 380 390 400
TGTHKVTVLF AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK
410 420 430 440 450
TTYFEIFTAG AGMGEVEVVI QDPTGQKGTV EPQLEARGDS TYRCSYQPTM
460 470 480 490 500
EGVHTVHVTF AGVPIPRSPY TVTVGQACNP AACRAIGRGL QPKGVRVKET
510 520 530 540 550
ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF EYYPTIPGTY
560 570 580 590 600
TVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGI VGKSADFVVE
610 620 630 640 650
AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN
660 670 680 690 700
SEDIRLSPFM ADIREAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK
710 720 730 740 750
HAGKAPLRVQ VQDNEGCSVE ATVKDNGNGT YSCSYVPRKP VKHTAMVSWG
760 770 780 790 800
GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA KTGLKAHEPT YFTVDCTEAG
810 820 830 840 850
QGDVSIGIKC APGVVGPTEA DIDFDIIRND NDTFTVKYTP CGAGSYTIMV
860 870 880 890 900
LFADQATPTS PIRVKVEPSH DASKVKAEGP GLNRTGVELG KPTHFTVNAK
910 920 930 940 950
TAGKGKLDVQ FSGLAKGDAV RDVDIIDHHD NTYTVKYIPV QQGPVGVNVT
960 970 980 990 1000
YGGDHIPKSP FSVGVSPSLD LSKIKVSGLG DKVDVGKDQE FTVKSKGAGG
1010 1020 1030 1040 1050
QGKVASKIVS PSGAAVPCKV EPGLGADNSV VRFVPREEGP YEVEVTYDGV
1060 1070 1080 1090 1100
PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG NAGSPARFTI DTKGAGTGGL
1110 1120 1130 1140 1150
GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF ADTHIPGSPF
1160 1170 1180 1190 1200
KAHVAPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE
1210 1220 1230 1240 1250
AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE
1260 1270 1280 1290 1300
PAVDTSGVQC YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP
1310 1320 1330 1340 1350
SGNLTDTYVQ DCGDGTYKVE YTPYEEGVHS VDVTYDGSPV PSSPFQVPVT
1360 1370 1380 1390 1400
EGCDPSRVRV HGPGIQSGTT NKPNKFTVET RGAGTGGLGL AVEGPSEAKM
1410 1420 1430 1440 1450
SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV PVHDVTDASK
1460 1470 1480 1490 1500
VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV
1510 1520 1530 1540 1550
DNADGTQTVN YVPSREGSYS ISVLYGEEEV PRSPFKVKVL PTHDASKVKA
1560 1570 1580 1590 1600
SGPGLNTTGV PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH
1610 1620 1630 1640 1650
DGTYTVAYVP DVPGRYTILI KYGGDEIPFS PYRVRAVPTG DASKCTVTVS
1660 1670 1680 1690 1700
IGGHGLGAGI GPTIQIGEET VITVDTKAAG KGKVTCTVCT PDGSEVDVDV
1710 1720 1730 1740 1750
VENEDGTFDI FYTAPQPGKY VICVRFGGEH VPNSPFQVTA LAGDQPTVQT
1760 1770 1780 1790 1800
PLRSQQLAPQ YNYPQGSQQT WIPERPMVGV NGLDVTSLRP FDLVIPFTIK
1810 1820 1830 1840 1850
KGEITGEVRM PSGKVAQPSI TDNKDGTVTV RYSPSEAGLH EMDIRYDNMH
1860 1870 1880 1890 1900
IPGSPLQFYV DYVNCGHITA YGPGLTHGVV NKPATFTVNT KDAGEGGLSL
1910 1920 1930 1940 1950
AIEGPSKAEI SCTDNQDGTC SVSYLPVLPG DYSILVKYND QHIPGSPFTA
1960 1970 1980 1990 2000
RVTGDDSMRM SHLKVGSAAD IPINISETDL SLLTATVVPP SGREEPCLLK
2010 2020 2030 2040 2050
RLRNGHVGIS FVPKETGEHL VHVKKNGQHV ASSPIPVVIS QSEIGDASRV
2060 2070 2080 2090 2100
RVSGQGLHEG HTFEPAEFII DTRDAGYGGL SLSIEGPSKV DINTEDLEDG
2110 2120 2130 2140 2150
TCRVTYCPTE PGNYIINIKF ADQHVPGSPF SVKVTGEGRV KESITRRRRA
2160 2170 2180 2190 2200
PSVANIGSHC DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI
2210 2220 2230 2240 2250
RFVPAEMGMH TVSVKYKGQH VPGSPFQFTV GPLGEGGAHK VRAGGPGLER
2260 2270 2280 2290 2300
AEVGVPAEFG IWTREAGAGG LAIAVEGPSK AEISFEDRKD GSCGVAYVVQ
2310 2320 2330 2340 2350
EPGDYEVSVK FNEEHIPDSP FVVPVASPSG DARRLTVSSL QESGLKVNQP
2360 2370 2380 2390 2400
ASFAVSLNGA KGAIDAKVHS PSGALEECYV TEIDQDKYAV RFIPRENGIY
2410 2420 2430 2440 2450
LIDVKFNGTH IPGSPFKIRV GEPGHGGDPG LVSAYGAGLE GGVTGSPAEF
2460 2470 2480 2490 2500
IVNTSNAGAG ALSVTIDGPS KVKMDCQECP EGYRVTYTPM APGSYLISIK
2510 2520 2530 2540 2550
YGGPYHIGGS PFKAKVTGPR LVSNHSLHET SSVFVDSLTK VATVPQHATS
2560 2570 2580 2590 2600
GPGPADVSKV VAKGLGLSKA YVGQKSNFTV DCSKAGNNML LVGVHGPRTP
2610 2620 2630 2640
CEEILVKHMG SRLYSVSYLL KDKGEYTLVV KWGDEHIPGS PYRIMVP
Length:2,647
Mass (Da):281,222
Last modified:July 27, 2011 - v5
Checksum:i217E3275F8468FEB
GO
Isoform 2 (identifier: Q8BTM8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     125-249: DSKAIVDGNL...QVITPEEIVD → GEGTGYTGAL...DTHAFHLQQF
     250-2647: Missing.

Note: May be due to an intron retention.
Show »
Length:249
Mass (Da):27,426
Checksum:i5856E9AC74C92E4F
GO

Sequence cautioni

The sequence BAC40787.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC40837.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BC038478 differs from that shown. Reason: Frameshift at position 496. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti661 – 6611A → T in BAC40837 (PubMed:16141072).Curated
Sequence conflicti2127 – 21271G → D in AAL68447 (PubMed:11807098).Curated
Sequence conflicti2253 – 22531V → A in AAH04061 (PubMed:15489334).Curated
Sequence conflicti2253 – 22531V → A in BC038478 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei125 – 249125DSKAI…EEIVD → GEGTGYTGALSGCGRGRNKF FLSSPLESLLVVFPSCCTQP RLPLGPLAALFFEVLENKRL AWRACEPLRAPARSALLACS QAELTSSVGRAPNAAPEVGQ AQTRLLPLRAAPHPWDTHAF HLQQF in isoform 2. 1 PublicationVSP_008779Add
BLAST
Alternative sequencei250 – 26472398Missing in isoform 2. 1 PublicationVSP_008780Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044856 mRNA. Translation: BAC32121.1.
AK089195 mRNA. Translation: BAC40787.1. Different initiation.
AK089311 mRNA. Translation: BAC40837.2. Different initiation.
AL807376 Genomic DNA. Translation: CAT00728.1.
BC004061 mRNA. Translation: AAH04061.1.
BC038478 mRNA. No translation available.
BC054432 mRNA. Translation: AAH54432.1.
AF034129 mRNA. Translation: AAC02062.1.
AF353668 mRNA. Translation: AAL68444.1.
AF353671 mRNA. Translation: AAL68447.1.
RefSeqiXP_006527974.1. XM_006527911.2. [Q8BTM8-1]
UniGeneiMm.295533.

Genome annotation databases

EnsembliENSMUST00000033699; ENSMUSP00000033699; ENSMUSG00000031328. [Q8BTM8-1]
GeneIDi192176.
UCSCiuc009tnz.1. mouse. [Q8BTM8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044856 mRNA. Translation: BAC32121.1.
AK089195 mRNA. Translation: BAC40787.1. Different initiation.
AK089311 mRNA. Translation: BAC40837.2. Different initiation.
AL807376 Genomic DNA. Translation: CAT00728.1.
BC004061 mRNA. Translation: AAH04061.1.
BC038478 mRNA. No translation available.
BC054432 mRNA. Translation: AAH54432.1.
AF034129 mRNA. Translation: AAC02062.1.
AF353668 mRNA. Translation: AAL68444.1.
AF353671 mRNA. Translation: AAL68447.1.
RefSeqiXP_006527974.1. XM_006527911.2. [Q8BTM8-1]
UniGeneiMm.295533.

3D structure databases

ProteinModelPortaliQ8BTM8.
SMRiQ8BTM8. Positions 39-374, 478-766, 1044-1643, 1773-2328, 2331-2522, 2559-2647.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228662. 13 interactions.
IntActiQ8BTM8. 11 interactions.
MINTiMINT-1867095.
STRINGi10090.ENSMUSP00000098997.

PTM databases

iPTMnetiQ8BTM8.
PhosphoSiteiQ8BTM8.
SwissPalmiQ8BTM8.

Proteomic databases

EPDiQ8BTM8.
MaxQBiQ8BTM8.
PaxDbiQ8BTM8.
PRIDEiQ8BTM8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033699; ENSMUSP00000033699; ENSMUSG00000031328. [Q8BTM8-1]
GeneIDi192176.
UCSCiuc009tnz.1. mouse. [Q8BTM8-1]

Organism-specific databases

CTDi2316.
MGIiMGI:95556. Flna.

Phylogenomic databases

eggNOGiKOG0518. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00660000095431.
HOVERGENiHBG004163.
InParanoidiQ8BTM8.
OMAiVQDNEGC.
OrthoDBiEOG76T9QC.
TreeFamiTF313685.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-430116. GP1b-IX-V activation signalling.
R-MMU-446353. Cell-extracellular matrix interactions.
R-MMU-5627123. RHO GTPases activate PAKs.

Miscellaneous databases

ChiTaRSiFlna. mouse.
PROiQ8BTM8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BTM8.
CleanExiMM_FLNA.
ExpressionAtlasiQ8BTM8. baseline and differential.
GenevisibleiQ8BTM8. MM.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
2.60.40.10. 24 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR017868. Filamin/ABP280_repeat-like.
IPR001298. Filamin/ABP280_rpt.
IPR028559. FLN_A.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11915:SF173. PTHR11915:SF173. 1 hit.
PfamiPF00307. CH. 2 hits.
PF00630. Filamin. 23 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00557. IG_FLMN. 24 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF81296. SSF81296. 24 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50194. FILAMIN_REPEAT. 24 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-1253 (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Embryo.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-2647 (ISOFORM 1).
    Tissue: Eye and Mammary tumor.
  4. "Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway."
    Liu G., Thomas L., Warren R.A., Enns C.A., Cunningham C.C., Hartwig J.H., Thomas G.
    J. Cell Biol. 139:1719-1733(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1490-1607 (ISOFORM 1), FUNCTION, INTERACTION WITH FURIN.
  5. "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits."
    van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A.
    J. Cell Biol. 156:361-376(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1691-1805 AND 2076-2226 (ISOFORM 1), DEVELOPMENTAL STAGE.
    Strain: C3H/HeJ.
  6. "Filamin A (FLNA) is required for cell-cell contact in vascular development and cardiac morphogenesis."
    Feng Y., Chen M.H., Moskowitz I.P., Mendonza A.M., Vidali L., Nakamura F., Kwiatkowski D.J., Walsh C.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:19836-19841(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459 AND THR-1750, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-20; SER-968; SER-1459; THR-1750; SER-2152; SER-2180; SER-2329; THR-2336; SER-2370; SER-2523; SER-2526 AND THR-2599, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "A novel interaction between FlnA and Syk regulates platelet ITAM-mediated receptor signaling and function."
    Falet H., Pollitt A.Y., Begonja A.J., Weber S.E., Duerschmied D., Wagner D.D., Watson S.P., Hartwig J.H.
    J. Exp. Med. 207:1967-1979(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  12. "RefilinB (FAM101B) targets filamin A to organize perinuclear actin networks and regulates nuclear shape."
    Gay O., Gilquin B., Nakamura F., Jenkins Z.A., McCartney R., Krakow D., Deshiere A., Assard N., Hartwig J.H., Robertson S.P., Baudier J.
    Proc. Natl. Acad. Sci. U.S.A. 108:11464-11469(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM101A AND FAM101B.
  13. Cited for: FUNCTION IN CILIOGENESIS.
  14. "Junctional Rab13-binding protein (JRAB) regulates cell spreading via filamins."
    Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T., Imoto I., Matsushita N., Sasaki T.
    Genes Cells 18:810-822(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICALL2.
  15. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-376; LYS-700; LYS-865; LYS-906; LYS-1071; LYS-1372; LYS-1538; LYS-2569 AND LYS-2575, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-1071 AND LYS-2569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  16. "Filamin-interacting proteins, Cfm1 and Cfm2, are essential for the formation of cartilaginous skeletal elements."
    Mizuhashi K., Kanamoto T., Moriishi T., Muranishi Y., Miyazaki T., Terada K., Omori Y., Ito M., Komori T., Furukawa T.
    Hum. Mol. Genet. 23:2953-2967(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM101A AND FAM101B.

Entry informationi

Entry nameiFLNA_MOUSE
AccessioniPrimary (citable) accession number: Q8BTM8
Secondary accession number(s): B7FAV0
, O54934, Q7TQI1, Q8BLK1, Q8BTN7, Q8VHX5, Q8VHX8, Q99KQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 144 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.