Q8BTM8 (FLNA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Flna
Synonyms:	Fln, Fln1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2647 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4 Ref.10
Subunit structure	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. Ref.4
Subcellular location	Cytoplasm › cell cortex By similarity. Cytoplasm › cytoskeleton By similarity.
Tissue specificity	Widely expressed. Highly expressed in Purkinje cells.
Developmental stage	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. Ref.5
Domain	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 By similarity.
Sequence similarities	Belongs to the filamin family. Contains 1 actin-binding domain. Contains 2 CH (calponin-homology) domains. Contains 24 filamin repeats.
Sequence caution	The sequence BAC40787.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC40837.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BC038478 differs from that shown. Reason: Frameshift at position 496.

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin crosslink formation Inferred from sequence or structural similarity. Source: UniProtKB actin cytoskeleton reorganization Inferred from sequence or structural similarity. Source: UniProtKB adenylate cyclase-inhibiting dopamine receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB cell projection organization Inferred from electronic annotation. Source: UniProtKB-KW cytoplasmic sequestering of protein Inferred from sequence or structural similarity. Source: UniProtKB early endosome to late endosome transport Inferred from direct assay Ref.4. Source: MGI epithelial to mesenchymal transition Inferred from genetic interaction PubMed 21709252. Source: MGI establishment of protein localization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription factor import into nucleus Inferred from sequence or structural similarity. Source: UniProtKB protein localization to cell surface Inferred from sequence or structural similarity. Source: UniProtKB protein stabilization Inferred from sequence or structural similarity. Source: UniProtKB receptor clustering Inferred from sequence or structural similarity. Source: UniProtKB spindle assembly involved in mitosis Inferred from sequence orthology PubMed 18548008. Source: MGI
Cellular_component	Myb complex Inferred from sequence orthology PubMed 18548008. Source: MGI cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB trans-Golgi network Inferred from direct assay Ref.4. Source: MGI
Molecular_function	Fc-gamma receptor I complex binding Inferred from sequence or structural similarity. Source: UniProtKB Rac GTPase binding Inferred from sequence or structural similarity. Source: UniProtKB actin filament binding Inferred from sequence or structural similarity. Source: UniProtKB glycoprotein binding Inferred from sequence or structural similarity. Source: UniProtKB protein kinase C binding Inferred from direct assay PubMed 12704190. Source: MGI signal transducer activity Inferred from sequence or structural similarity. Source: UniProtKB transcription factor binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Plcg2	Q8CIH5	3	EBI-641991,EBI-617954

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8BTM8-1)

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.

Isoform 2 (identifier: Q8BTM8-2)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 2647	2646	Filamin-A		PRO_0000087297
Regions
	Domain	2 – 274	273	Actin-binding
	Domain	43 – 149	107	CH 1
	Domain	166 – 266	101	CH 2
	Repeat	276 – 374	99	Filamin 1
	Repeat	376 – 474	99	Filamin 2
	Repeat	475 – 570	96	Filamin 3
	Repeat	571 – 663	93	Filamin 4
	Repeat	667 – 763	97	Filamin 5
	Repeat	764 – 866	103	Filamin 6
	Repeat	867 – 965	99	Filamin 7
	Repeat	966 – 1061	96	Filamin 8
	Repeat	1062 – 1154	93	Filamin 9
	Repeat	1155 – 1249	95	Filamin 10
	Repeat	1250 – 1349	100	Filamin 11
	Repeat	1350 – 1442	93	Filamin 12
	Repeat	1443 – 1539	97	Filamin 13
	Repeat	1540 – 1636	97	Filamin 14
	Repeat	1641 – 1740	100	Filamin 15
	Repeat	1765 – 1860	96	Filamin 16
	Repeat	1861 – 1952	92	Filamin 17
	Repeat	1953 – 2039	87	Filamin 18
	Repeat	2042 – 2134	93	Filamin 19
	Repeat	2135 – 2230	96	Filamin 20
	Repeat	2233 – 2325	93	Filamin 21
	Repeat	2327 – 2420	94	Filamin 22
	Repeat	2424 – 2516	93	Filamin 23
	Repeat	2552 – 2646	95	Filamin 24
	Region	1490 – 1607	118	Interaction with furin
	Region	1741 – 1778	38	Hinge 1 By similarity
	Region	2517 – 2647	131	Self-association site, tail By similarity
	Region	2517 – 2553	37	Hinge 2 By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	11	1	Phosphoserine By similarity
	Modified residue	508	1	N6-acetyllysine By similarity
	Modified residue	700	1	N6-acetyllysine By similarity
	Modified residue	781	1	N6-acetyllysine By similarity
	Modified residue	837	1	N6-acetyllysine By similarity
	Modified residue	1084	1	Phosphoserine By similarity
	Modified residue	1089	1	Phosphothreonine By similarity
	Modified residue	1286	1	Phosphothreonine Ref.6
	Modified residue	1338	1	Phosphoserine By similarity
	Modified residue	1459	1	Phosphoserine Ref.9
	Modified residue	1533	1	Phosphoserine By similarity
	Modified residue	1630	1	Phosphoserine By similarity
	Modified residue	1734	1	Phosphoserine By similarity
	Modified residue	1750	1	Phosphothreonine Ref.9
	Modified residue	2053	1	Phosphoserine By similarity
	Modified residue	2152	1	Phosphoserine Ref.7 Ref.8
	Modified residue	2158	1	Phosphoserine By similarity
	Modified residue	2284	1	Phosphoserine By similarity
	Modified residue	2327	1	Phosphoserine By similarity
	Modified residue	2336	1	Phosphothreonine By similarity
	Modified residue	2414	1	Phosphoserine By similarity
	Modified residue	2510	1	Phosphoserine By similarity
	Modified residue	2607	1	N6-acetyllysine By similarity
	Modified residue	2621	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	125 – 249	125	DSKAI…EEIVD → GEGTGYTGALSGCGRGRNKF FLSSPLESLLVVFPSCCTQP RLPLGPLAALFFEVLENKRL AWRACEPLRAPARSALLACS QAELTSSVGRAPNAAPEVGQ AQTRLLPLRAAPHPWDTHAF HLQQF in isoform 2.		VSP_008779
	Alternative sequence	250 – 2647	2398	Missing in isoform 2.		VSP_008780
Experimental info
	Sequence conflict	661	1	A → T in BAC40837. Ref.1
	Sequence conflict	2127	1	G → D in AAL68447. Ref.5
	Sequence conflict	2253	1	V → A in AAH04061. Ref.3
	Sequence conflict	2253	1	V → A in BC038478. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 5. Checksum: 217E3275F8468FEB	FASTA	2,647	281,222
	10 20 30 40 50 60 MSSSHSRCGQ SAAVASPGGS IDSRDAEMPA TEKDLAEDAP WKKIQQNTFT RWCNEHLKCV 70 80 90 100 110 120 SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR QMQLENVSVA LEFLDRESIK 130 140 150 160 170 180 LVSIDSKAIV DGNLKLILGL IWTLILHYSI SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL 190 200 210 220 230 240 PQLPITNFSR DWQSGRALGA LVDSCAPGLC PDWDSWDASK PVNNAREAMQ QADDWLGIPQ 250 260 270 280 290 300 VITPEEIVDP NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK 310 320 330 340 350 360 RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV TGTHKVTVLF 370 380 390 400 410 420 AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK TTYFEIFTAG AGMGEVEVVI 430 440 450 460 470 480 QDPTGQKGTV EPQLEARGDS TYRCSYQPTM EGVHTVHVTF AGVPIPRSPY TVTVGQACNP 490 500 510 520 530 540 AACRAIGRGL QPKGVRVKET ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF 550 560 570 580 590 600 EYYPTIPGTY TVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGI VGKSADFVVE 610 620 630 640 650 660 AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN SEDIRLSPFM 670 680 690 700 710 720 ADIREAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK HAGKAPLRVQ VQDNEGCSVE 730 740 750 760 770 780 ATVKDNGNGT YSCSYVPRKP VKHTAMVSWG GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA 790 800 810 820 830 840 KTGLKAHEPT YFTVDCTEAG QGDVSIGIKC APGVVGPTEA DIDFDIIRND NDTFTVKYTP 850 860 870 880 890 900 CGAGSYTIMV LFADQATPTS PIRVKVEPSH DASKVKAEGP GLNRTGVELG KPTHFTVNAK 910 920 930 940 950 960 TAGKGKLDVQ FSGLAKGDAV RDVDIIDHHD NTYTVKYIPV QQGPVGVNVT YGGDHIPKSP 970 980 990 1000 1010 1020 FSVGVSPSLD LSKIKVSGLG DKVDVGKDQE FTVKSKGAGG QGKVASKIVS PSGAAVPCKV 1030 1040 1050 1060 1070 1080 EPGLGADNSV VRFVPREEGP YEVEVTYDGV PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG 1090 1100 1110 1120 1130 1140 NAGSPARFTI DTKGAGTGGL GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF 1150 1160 1170 1180 1190 1200 ADTHIPGSPF KAHVAPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE 1210 1220 1230 1240 1250 1260 AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE PAVDTSGVQC 1270 1280 1290 1300 1310 1320 YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP SGNLTDTYVQ DCGDGTYKVE 1330 1340 1350 1360 1370 1380 YTPYEEGVHS VDVTYDGSPV PSSPFQVPVT EGCDPSRVRV HGPGIQSGTT NKPNKFTVET 1390 1400 1410 1420 1430 1440 RGAGTGGLGL AVEGPSEAKM SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV 1450 1460 1470 1480 1490 1500 PVHDVTDASK VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV 1510 1520 1530 1540 1550 1560 DNADGTQTVN YVPSREGSYS ISVLYGEEEV PRSPFKVKVL PTHDASKVKA SGPGLNTTGV 1570 1580 1590 1600 1610 1620 PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH DGTYTVAYVP DVPGRYTILI 1630 1640 1650 1660 1670 1680 KYGGDEIPFS PYRVRAVPTG DASKCTVTVS IGGHGLGAGI GPTIQIGEET VITVDTKAAG 1690 1700 1710 1720 1730 1740 KGKVTCTVCT PDGSEVDVDV VENEDGTFDI FYTAPQPGKY VICVRFGGEH VPNSPFQVTA 1750 1760 1770 1780 1790 1800 LAGDQPTVQT PLRSQQLAPQ YNYPQGSQQT WIPERPMVGV NGLDVTSLRP FDLVIPFTIK 1810 1820 1830 1840 1850 1860 KGEITGEVRM PSGKVAQPSI TDNKDGTVTV RYSPSEAGLH EMDIRYDNMH IPGSPLQFYV 1870 1880 1890 1900 1910 1920 DYVNCGHITA YGPGLTHGVV NKPATFTVNT KDAGEGGLSL AIEGPSKAEI SCTDNQDGTC 1930 1940 1950 1960 1970 1980 SVSYLPVLPG DYSILVKYND QHIPGSPFTA RVTGDDSMRM SHLKVGSAAD IPINISETDL 1990 2000 2010 2020 2030 2040 SLLTATVVPP SGREEPCLLK RLRNGHVGIS FVPKETGEHL VHVKKNGQHV ASSPIPVVIS 2050 2060 2070 2080 2090 2100 QSEIGDASRV RVSGQGLHEG HTFEPAEFII DTRDAGYGGL SLSIEGPSKV DINTEDLEDG 2110 2120 2130 2140 2150 2160 TCRVTYCPTE PGNYIINIKF ADQHVPGSPF SVKVTGEGRV KESITRRRRA PSVANIGSHC 2170 2180 2190 2200 2210 2220 DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI RFVPAEMGMH TVSVKYKGQH 2230 2240 2250 2260 2270 2280 VPGSPFQFTV GPLGEGGAHK VRAGGPGLER AEVGVPAEFG IWTREAGAGG LAIAVEGPSK 2290 2300 2310 2320 2330 2340 AEISFEDRKD GSCGVAYVVQ EPGDYEVSVK FNEEHIPDSP FVVPVASPSG DARRLTVSSL 2350 2360 2370 2380 2390 2400 QESGLKVNQP ASFAVSLNGA KGAIDAKVHS PSGALEECYV TEIDQDKYAV RFIPRENGIY 2410 2420 2430 2440 2450 2460 LIDVKFNGTH IPGSPFKIRV GEPGHGGDPG LVSAYGAGLE GGVTGSPAEF IVNTSNAGAG 2470 2480 2490 2500 2510 2520 ALSVTIDGPS KVKMDCQECP EGYRVTYTPM APGSYLISIK YGGPYHIGGS PFKAKVTGPR 2530 2540 2550 2560 2570 2580 LVSNHSLHET SSVFVDSLTK VATVPQHATS GPGPADVSKV VAKGLGLSKA YVGQKSNFTV 2590 2600 2610 2620 2630 2640 DCSKAGNNML LVGVHGPRTP CEEILVKHMG SRLYSVSYLL KDKGEYTLVV KWGDEHIPGS PYRIMVP
	Isoform 2 [UniParc]. Checksum: 5856E9AC74C92E4F	FASTA	249	27,426
	10 20 30 40 50 60 MSSSHSRCGQ SAAVASPGGS IDSRDAEMPA TEKDLAEDAP WKKIQQNTFT RWCNEHLKCV 70 80 90 100 110 120 SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR QMQLENVSVA LEFLDRESIK 130 140 150 160 170 180 LVSIGEGTGY TGALSGCGRG RNKFFLSSPL ESLLVVFPSC CTQPRLPLGP LAALFFEVLE 190 200 210 220 230 240 NKRLAWRACE PLRAPARSAL LACSQAELTS SVGRAPNAAP EVGQAQTRLL PLRAAPHPWD THAFHLQQF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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.
[6]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1286, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2152, MASS SPECTROMETRY. Tissue: Melanoma.
[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, MASS SPECTROMETRY. Tissue: Macrophage.
[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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[10]	"A meckelin-filamin A interaction mediates ciliogenesis." Adams M., Simms R.J., Abdelhamed Z., Dawe H.R., Szymanska K., Logan C.V., Wheway G., Pitt E., Gull K., Knowles M.A., Blair E., Cross S.H., Sayer J.A., Johnson C.A. Hum. Mol. Genet. 21:1272-1286(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CILIOGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00131138. IPI00387373.
RefSeq	NP_034357.2. NM_010227.2.
UniGene	Mm.295533.
3D structure databases
ProteinModelPortal	Q8BTM8.
SMR	Q8BTM8. Positions 39-374, 1044-1643, 1773-2329, 2331-2522, 2559-2647.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8BTM8. 3 interactions.
MINT	MINT-1867095.
PTM databases
PhosphoSite	Q8BTM8.
Proteomic databases
PaxDb	Q8BTM8.
PRIDE	Q8BTM8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000033699; ENSMUSP00000033699; ENSMUSG00000031328.
GeneID	192176.
KEGG	mmu:192176.
Organism-specific databases
CTD	2316.
MGI	MGI:95556. Flna.
Phylogenomic databases
eggNOG	COG5069.
GeneTree	ENSGT00660000095431.
HOVERGEN	HBG004163.
InParanoid	Q8BTM8.
KO	K04437.
Gene expression databases
ArrayExpress	Q8BTM8.
Bgee	Q8BTM8.
CleanEx	MM_FLNA.
Genevestigator	Q8BTM8.
GermOnline	ENSMUSG00000031328. Mus musculus.
Family and domain databases
Gene3D	1.10.418.10. 2 hits. 2.60.40.10. 24 hits.
InterPro	IPR001589. Actinin_actin-bd_CS. IPR001715. CH-domain. IPR001298. Filamin. IPR017868. Filamin/ABP280_repeat-like. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. [Graphical view]
Pfam	PF00307. CH. 2 hits. PF00630. Filamin. 23 hits. [Graphical view]
SMART	SM00033. CH. 2 hits. SM00557. IG_FLMN. 24 hits. [Graphical view]
SUPFAM	SSF47576. Calponin-homology. 1 hit. SSF81296. Ig_E-set. 24 hits.
PROSITE	PS00019. ACTININ_1. 1 hit. PS00020. ACTININ_2. 1 hit. PS50021. CH. 2 hits. PS50194. FILAMIN_REPEAT. 24 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FLNA. mouse.
NextBio	371188.
SOURCE	Search...

Entry information

Entry name

FLNA_MOUSE

Accession

Primary (citable) accession number: Q8BTM8
Secondary accession number(s): B7FAV0 , O54934, Q7TQI1, Q8BLK1, Q8BTN7, Q8VHX5, Q8VHX8, Q99KQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 114 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program