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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

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-cell adherens junction Source: MGI
  • cell-cell junction Source: UniProtKB
  • cell cortex Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: GOC
  • extracellular exosome Source: MGI
  • extracellular matrix 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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000872972 – 2647Filamin-AAdd BLAST2646

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei11PhosphoserineBy similarity1
Modified residuei16PhosphoserineCombined sources1
Modified residuei20PhosphoserineCombined sources1
Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei376N6-acetyllysineCombined sources1
Modified residuei508N6-acetyllysineBy similarity1
Modified residuei700N6-acetyllysineCombined sources1
Modified residuei781N6-acetyllysineBy similarity1
Modified residuei837N6-acetyllysineBy similarity1
Modified residuei865N6-acetyllysineCombined sources1
Modified residuei906N6-acetyllysineCombined sources1
Modified residuei968PhosphoserineCombined sources1
Modified residuei1055PhosphoserineBy similarity1
Modified residuei1071N6-acetyllysine; alternateCombined sources1
Modified residuei1071N6-succinyllysine; alternateCombined sources1
Modified residuei1084PhosphoserineBy similarity1
Modified residuei1089PhosphothreonineBy similarity1
Modified residuei1301PhosphoserineBy similarity1
Modified residuei1338PhosphoserineBy similarity1
Modified residuei1372N6-acetyllysineCombined sources1
Modified residuei1459PhosphoserineCombined sources1
Modified residuei1533PhosphoserineBy similarity1
Modified residuei1538N6-acetyllysineCombined sources1
Modified residuei1630PhosphoserineBy similarity1
Modified residuei1734PhosphoserineBy similarity1
Modified residuei1750PhosphothreonineCombined sources1
Modified residuei1835PhosphoserineBy similarity1
Modified residuei1967PhosphoserineBy similarity1
Modified residuei2053PhosphoserineBy similarity1
Modified residuei2128PhosphoserineBy similarity1
Modified residuei2152PhosphoserineCombined sources1
Modified residuei2158PhosphoserineBy similarity1
Modified residuei2163PhosphoserineBy similarity1
Modified residuei2180PhosphoserineCombined sources1
Modified residuei2284PhosphoserineBy similarity1
Modified residuei2327PhosphoserineBy similarity1
Modified residuei2329PhosphoserineCombined sources1
Modified residuei2336PhosphothreonineCombined sources1
Modified residuei2338PhosphoserineBy similarity1
Modified residuei2370PhosphoserineCombined sources1
Modified residuei2414PhosphoserineBy similarity1
Modified residuei2510PhosphoserineBy similarity1
Modified residuei2523PhosphoserineCombined sources1
Modified residuei2526PhosphoserineCombined sources1
Modified residuei2569N6-acetyllysine; alternateCombined sources1
Modified residuei2569N6-succinyllysine; alternateCombined sources1
Modified residuei2575N6-acetyllysineCombined sources1
Modified residuei2599PhosphothreonineCombined sources1
Modified residuei2607N6-acetyllysineBy similarity1
Modified residuei2621N6-acetyllysineBy similarity1

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.
PaxDbiQ8BTM8.
PeptideAtlasiQ8BTM8.
PRIDEiQ8BTM8.

PTM databases

iPTMnetiQ8BTM8.
PhosphoSitePlusiQ8BTM8.
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

BgeeiENSMUSG00000031328.
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). Interacts with CEACAM1 (via cytoplasmic domain); inhibits cell migration and cell scattering by interfering with the interaction between FLNA and RALA (By similarity).By similarity4 Publications

Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi228662. 13 interactors.
IntActiQ8BTM8. 12 interactors.
MINTiMINT-1867095.
STRINGi10090.ENSMUSP00000098997.

Structurei

3D structure databases

ProteinModelPortaliQ8BTM8.
SMRiQ8BTM8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 274Actin-bindingAdd BLAST273
Domaini43 – 149CH 1PROSITE-ProRule annotationAdd BLAST107
Domaini166 – 266CH 2PROSITE-ProRule annotationAdd BLAST101
Repeati276 – 374Filamin 1Add BLAST99
Repeati376 – 474Filamin 2Add BLAST99
Repeati475 – 570Filamin 3Add BLAST96
Repeati571 – 663Filamin 4Add BLAST93
Repeati667 – 763Filamin 5Add BLAST97
Repeati764 – 866Filamin 6Add BLAST103
Repeati867 – 965Filamin 7Add BLAST99
Repeati966 – 1061Filamin 8Add BLAST96
Repeati1062 – 1154Filamin 9Add BLAST93
Repeati1155 – 1249Filamin 10Add BLAST95
Repeati1250 – 1349Filamin 11Add BLAST100
Repeati1350 – 1442Filamin 12Add BLAST93
Repeati1443 – 1539Filamin 13Add BLAST97
Repeati1540 – 1636Filamin 14Add BLAST97
Repeati1641 – 1740Filamin 15Add BLAST100
Repeati1765 – 1860Filamin 16Add BLAST96
Repeati1861 – 1952Filamin 17Add BLAST92
Repeati1953 – 2039Filamin 18Add BLAST87
Repeati2042 – 2134Filamin 19Add BLAST93
Repeati2135 – 2230Filamin 20Add BLAST96
Repeati2233 – 2325Filamin 21Add BLAST93
Repeati2327 – 2420Filamin 22Add BLAST94
Repeati2424 – 2516Filamin 23Add BLAST93
Repeati2552 – 2646Filamin 24Add BLAST95

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1490 – 1607Interaction with furinAdd BLAST118
Regioni1741 – 1778Hinge 1By similarityAdd BLAST38
Regioni2517 – 2647Self-association site, tailBy similarityAdd BLAST131
Regioni2517 – 2553Hinge 2By similarityAdd BLAST37

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.
OrthoDBiEOG091G00U5.
TreeFamiTF313685.

Family and domain databases

CDDicd00014. CH. 2 hits.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC40837 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)DescriptionActionsGraphical viewLength
Sequence conflicti661A → T in BAC40837 (PubMed:16141072).Curated1
Sequence conflicti2127G → D in AAL68447 (PubMed:11807098).Curated1
Sequence conflicti2253V → A in AAH04061 (PubMed:15489334).Curated1
Sequence conflicti2253V → A in BC038478 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_008779125 – 249DSKAI…EEIVD → GEGTGYTGALSGCGRGRNKF FLSSPLESLLVVFPSCCTQP RLPLGPLAALFFEVLENKRL AWRACEPLRAPARSALLACS QAELTSSVGRAPNAAPEVGQ AQTRLLPLRAAPHPWDTHAF HLQQF in isoform 2. 1 PublicationAdd BLAST125
Alternative sequenceiVSP_008780250 – 2647Missing in isoform 2. 1 PublicationAdd BLAST2398

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_006527911.3. [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_006527911.3. [Q8BTM8-1]
UniGeneiMm.295533.

3D structure databases

ProteinModelPortaliQ8BTM8.
SMRiQ8BTM8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228662. 13 interactors.
IntActiQ8BTM8. 12 interactors.
MINTiMINT-1867095.
STRINGi10090.ENSMUSP00000098997.

PTM databases

iPTMnetiQ8BTM8.
PhosphoSitePlusiQ8BTM8.
SwissPalmiQ8BTM8.

Proteomic databases

EPDiQ8BTM8.
PaxDbiQ8BTM8.
PeptideAtlasiQ8BTM8.
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.
OrthoDBiEOG091G00U5.
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

BgeeiENSMUSG00000031328.
CleanExiMM_FLNA.
ExpressionAtlasiQ8BTM8. baseline and differential.
GenevisibleiQ8BTM8. MM.

Family and domain databases

CDDicd00014. CH. 2 hits.
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...

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: November 30, 2016
This is version 149 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.