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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)

 FLNB_HUMAN              Reviewed;        2602 AA.
O75369; B2ZZ83; B2ZZ84; B2ZZ85; C9JKE6; C9JMC4; Q13706; Q59EC2;
Q60FE7; Q6MZJ1; Q8WXS9; Q8WXT0; Q8WXT1; Q8WXT2; Q8WXT3; Q9NRB5;
Q9NT26; Q9UEV9;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
30-AUG-2017, entry version 193.
RecName: Full=Filamin-B;
Short=FLN-B;
AltName: Full=ABP-278;
AltName: Full=ABP-280 homolog;
AltName: Full=Actin-binding-like protein;
AltName: Full=Beta-filamin;
AltName: Full=Filamin homolog 1;
Short=Fh1;
AltName: Full=Filamin-3;
AltName: Full=Thyroid autoantigen;
AltName: Full=Truncated actin-binding protein;
Short=Truncated ABP;
Name=FLNB; Synonyms=FLN1L, FLN3, TABP, TAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, INTERACTION WITH GP1BA, AND VARIANTS ASN-1157
AND MET-1471.
TISSUE=Endothelial cell, and Placenta;
PubMed=9651345; DOI=10.1074/jbc.273.28.17531;
Takafuta T., Wu G., Murphy G.F., Shapiro S.S.;
"Human beta-filamin is a new protein that interacts with the
cytoplasmic tail of glycoprotein Ibalpha.";
J. Biol. Chem. 273:17531-17538(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE
SPECIFICITY, AND INTERACTION WITH GP1BA.
TISSUE=Placenta;
PubMed=9694715;
Xu W.-F., Xie Z.-W., Chung D.W., Davie E.W.;
"A novel human actin-binding protein homologue that binds to platelet
glycoprotein Ibalpha.";
Blood 92:1268-1276(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4 AND 5), TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH ISOFORMS OF
ITGB1.
TISSUE=Keratinocyte, and Skeletal muscle;
PubMed=11807098; DOI=10.1083/jcb.200103037;
van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M.,
Takafuta T., Shapiro S.S., Sonnenberg A.;
"Different splice variants of filamin-B affect myogenesis, subcellular
distribution, and determine binding to integrin (beta) subunits.";
J. Cell Biol. 156:361-376(2002).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), GENE
ORGANIZATION, SIMILARITY TO OTHER MEMBERS OF THE FAMILY, AND VARIANTS
ASN-1157 AND MET-1471.
PubMed=11153914; DOI=10.1007/s004390000414;
Chakarova C., Wehnert M.S., Uhl K., Sakthivel S., Vosberg H.-P.,
van der Ven P.F.M., Fuerst D.O.;
"Genomic structure and fine mapping of the two human filamin gene
paralogues FLNB and FLNC and comparative analysis of the filamin gene
family.";
Hum. Genet. 107:597-611(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 8 AND 9), AND VARIANTS
ASN-1157 AND MET-1471.
PubMed=18487259; DOI=10.1093/dnares/dsn010;
Oshikawa M., Sugai Y., Usami R., Ohtoko K., Toyama S., Kato S.;
"Fine expression profiling of full-length transcripts using a size-
unbiased cDNA library prepared with the vector-capping method.";
DNA Res. 15:123-136(2008).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 8 AND 9).
PubMed=16106752; DOI=10.1093/dnares/12.1.53;
Kato S., Ohtoko K., Ohtake H., Kimura T.;
"Vector-capping: a simple method for preparing a high-quality full-
length cDNA library.";
DNA Res. 12:53-62(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Endometrial tumor, and Fetal brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 990-2602.
TISSUE=Aortic endothelium;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 2130-2602, AND INTERACTION WITH INPPL1.
TISSUE=Skeletal muscle;
PubMed=11739414; DOI=10.1083/jcb.200104005;
Dyson J.M., O'Malley C.J., Becanovic J., Munday A.D., Berndt M.C.,
Coghill I.D., Nandurkar H.H., Ooms L.M., Mitchell C.A.;
"The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2,
binds filamin and regulates submembraneous actin.";
J. Cell Biol. 155:1065-1079(2001).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1874-2602.
TISSUE=Fetal brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 2311-2602, AND INTERACTION WITH PSEN1
AND PSEN2.
TISSUE=Fetal brain;
PubMed=9437013;
Zhang W., Han S.W., McKeel D.W., Goate A., Wu J.Y.;
"Interaction of presenilins with the filamin family of actin-binding
proteins.";
J. Neurosci. 18:914-922(1998).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 2404-2602, AND TISSUE SPECIFICITY.
TISSUE=Thyroid;
PubMed=8327473; DOI=10.1073/pnas.90.13.5994;
Leedman P.J., Faulkner-Jones B., Cram D.C., Harrison P.J., West J.,
O'Brien E.J., Simpson R., Coppel R.L., Harrison L.C.;
"Cloning from the thyroid of a protein related to actin binding
protein that is recognized by Graves disease immunoglobulins.";
Proc. Natl. Acad. Sci. U.S.A. 90:5994-5998(1993).
[14]
INTERACTION WITH HBV CAPSID PROTEIN.
PubMed=10754391; DOI=10.1007/BF02256623;
Huang C.J., Chen Y.H., Ting L.P.;
"Hepatitis B virus core protein interacts with the C-terminal region
of actin-binding protein.";
J. Biomed. Sci. 7:160-168(2000).
[15]
INTERACTION WITH FLNA.
PubMed=12393796; DOI=10.1093/hmg/11.23.2845;
Sheen V.L., Feng Y., Graham D., Takafuta T., Shapiro S.S., Walsh C.A.;
"Filamin A and filamin B are co-expressed within neurons during
periods of neuronal migration and can physically interact.";
Hum. Mol. Genet. 11:2845-2854(2002).
[16]
INTERACTION WITH FBLP1.
TISSUE=Placenta;
PubMed=12496242; DOI=10.1074/jbc.M209339200;
Takafuta T., Saeki M., Fujimoto T.-T., Fujimura K., Shapiro S.S.;
"A new member of the LIM protein family binds to filamin B and
localizes at stress fibers.";
J. Biol. Chem. 278:12175-12181(2003).
[17]
DIMERIZATION, AND INTERACTION WITH FLNC.
PubMed=12525170; DOI=10.1021/bi026501+;
Himmel M., van der Ven P.F.M., Stoecklein W., Fuerst D.O.;
"The limits of promiscuity: isoform-specific dimerization of
filamins.";
Biochemistry 42:430-439(2003).
[18]
INTERACTION WITH ITGB1; MYOT AND MYOZ1.
PubMed=16076904; DOI=10.1242/jcs.02484;
Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A.,
Carpen O., Faulkner G., Borradori L.;
"The Z-disc proteins myotilin and FATZ-1 interact with each other and
are connected to the sarcolemma via muscle-specific filamins.";
J. Cell Sci. 118:3739-3749(2005).
[19]
REVIEW.
PubMed=11336782; DOI=10.1016/S0167-4889(01)00072-6;
van der Flier A., Sonnenberg A.;
"Structural and functional aspects of filamins.";
Biochim. Biophys. Acta 1538:99-117(2001).
[20]
REVIEW.
PubMed=11252955; DOI=10.1038/35052082;
Stossel T.P., Condeelis J., Cooley L., Hartwig J.H., Noegel A.,
Schleicher M., Shapiro S.S.;
"Filamins as integrators of cell mechanics and signalling.";
Nat. Rev. Mol. Cell Biol. 2:138-145(2001).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519; SER-983; SER-1028;
SER-1316; SER-1505; SER-1602; SER-2083; SER-2107; SER-2478 AND
SER-2481, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
UBIQUITINATION.
PubMed=19300455; DOI=10.1038/cdd.2009.27;
Bello N.F., Lamsoul I., Heuze M.L., Metais A., Moreaux G.,
Calderwood D.A., Duprez D., Moog-Lutz C., Lutz P.G.;
"The E3 ubiquitin ligase specificity subunit ASB2beta is a novel
regulator of muscle differentiation that targets filamin B to
proteasomal degradation.";
Cell Death Differ. 16:921-932(2009).
[25]
ISGYLATION AT LYS-2468, AND MUTAGENESIS OF LYS-2468.
PubMed=19270716; DOI=10.1038/embor.2009.23;
Jeon Y.J., Choi J.S., Lee J.Y., Yu K.R., Kim S.M., Ka S.H., Oh K.H.,
Kim K.I., Zhang D.E., Bang O.S., Chung C.H.;
"ISG15 modification of filamin B negatively regulates the type I
interferon-induced JNK signalling pathway.";
EMBO Rep. 10:374-380(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 AND SER-2478, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-681 AND LYS-2576, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519; SER-730; SER-886;
SER-932; SER-983; SER-1316; SER-1433; SER-2369; SER-2465 AND SER-2478,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983; SER-1433; SER-1505;
SER-2083; SER-2107; SER-2465; SER-2478 AND SER-2481, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216; THR-1307; SER-1316;
SER-2107; SER-2113 AND SER-2492, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-1474 (ISOFORM 8), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[34]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-242.
PubMed=19505475; DOI=10.1016/j.jmb.2009.06.009;
Sawyer G.M., Clark A.R., Robertson S.P., Sutherland-Smith A.J.;
"Disease-associated substitutions in the filamin B actin binding
domain confer enhanced actin binding affinity in the absence of major
structural disturbance: Insights from the crystal structures of
filamin B actin binding domains.";
J. Mol. Biol. 390:1030-1047(2009).
[35]
STRUCTURE BY NMR OF 1017-1721; 1736-2488 AND 2509-2602.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the 9th through 24th filamin domains from human
filamin-B.";
Submitted (FEB-2009) to the PDB data bank.
[36]
INVOLVEMENT IN SCT, VARIANTS LRS CYS-161; LYS-227; ASN-1571 DEL;
ARG-1586 AND SER-1691, VARIANTS AO1 VAL-173 AND PRO-188, VARIANT AO3
ARG-751, AND VARIANT AO1/AO3 VAL-202.
PubMed=14991055; DOI=10.1038/ng1319;
Krakow D., Robertson S.P., King L.M., Morgan T., Sebald E.T.,
Bertolotto C., Wachsmann-Hogiu S., Acuna D., Shapiro S.S.,
Takafuta T., Aftimos S., Kim C.A., Firth H., Steiner C.E.,
Cormier-Daire V., Superti-Furga A., Bonafe L., Graham J.M. Jr.,
Grix A., Bacino C.A., Allanson J., Bialer M.G., Lachman R.S.,
Rimoin D.L., Cohn D.H.;
"Mutations in the gene encoding filamin B disrupt vertebral
segmentation, joint formation and skeletogenesis.";
Nat. Genet. 36:405-410(2004).
[37]
STRUCTURE BY NMR OF 1017-2602.
RIKEN structural genomics initiative (RSGI);
"Solution structure of filamin domains from human filamin-B.";
Submitted (AUG-2007) to the PDB data bank.
[38]
VARIANTS BOOMD ARG-171 AND PRO-235.
PubMed=15994868; DOI=10.1136/jmg.2004.029967;
Bicknell L.S., Morgan T., Bonafe L., Wessels M.W., Bialer M.G.,
Willems P.J., Cohn D.H., Krakow D., Robertson S.P.;
"Mutations in FLNB cause boomerang dysplasia.";
J. Med. Genet. 42:E43-E43(2005).
[39]
VARIANTS [LARGE SCALE ANALYSIS] GLN-566; LYS-663; LYS-703 AND
GLY-1534.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[40]
VARIANTS LRS CYS-161; SER-168; LYS-227; VAL-234; SER-361; GLU-363;
ARG-1431; ASN-1571 DEL; ARG-1586; ASP-1592; LEU-1603; SER-1691 AND
ARG-1834.
PubMed=16801345; DOI=10.1136/jmg.2006.043687;
Bicknell L.S., Farrington-Rock C., Shafeghati Y., Rump P., Alanay Y.,
Alembik Y., Al-Madani N., Firth H., Karimi-Nejad M.H., Kim C.A.,
Leask K., Maisenbacher M., Moran E., Pappas J.G., Prontera P.,
de Ravel T., Fryns J.-P., Sweeney E., Fryer A., Unger S., Wilson L.C.,
Lachman R.S., Rimoin D.L., Cohn D.H., Krakow D., Robertson S.P.;
"A molecular and clinical study of Larsen syndrome caused by mutations
in FLNB.";
J. Med. Genet. 44:89-98(2007).
-!- FUNCTION: Connects cell membrane constituents to the actin
cytoskeleton. May promote orthogonal branching of actin filaments
and links actin filaments to membrane glycoproteins. Anchors
various transmembrane proteins to the actin cytoskeleton.
Interaction with FLNA may allow neuroblast migration from the
ventricular zone into the cortical plate. Various interactions and
localizations of isoforms affect myotube morphology and
myogenesis. Isoform 6 accelerates muscle differentiation in vitro.
-!- SUBUNIT: Homodimer. Interacts with MICALL2 (By similarity).
Interacts with RFLNA and RFLNB (By similarity). Isoform 1
interacts with FBLP1, FLNA, FLNC, GP1BA, INPPL1, ITGB1A, PSEN1 and
PSEN2. Isoform 3 interacts with ITGB1A, ITGB1D, ITGB3 and ITGB6.
Interacts with MYOT and MYOZ1. Interacts with HBV capsid protein.
{ECO:0000250, ECO:0000250|UniProtKB:Q80X90,
ECO:0000269|PubMed:10754391, ECO:0000269|PubMed:11739414,
ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:12393796,
ECO:0000269|PubMed:12496242, ECO:0000269|PubMed:12525170,
ECO:0000269|PubMed:16076904, ECO:0000269|PubMed:9437013,
ECO:0000269|PubMed:9651345, ECO:0000269|PubMed:9694715}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-352089, EBI-352089;
P21333:FLNA; NbExp=5; IntAct=EBI-352089, EBI-350432;
P62993:GRB2; NbExp=2; IntAct=EBI-352089, EBI-401755;
P05161:ISG15; NbExp=4; IntAct=EBI-352089, EBI-746466;
Q13233:MAP3K1; NbExp=2; IntAct=EBI-352089, EBI-49776;
Q9Y6R4:MAP3K4; NbExp=2; IntAct=EBI-352089, EBI-448104;
P16333:NCK1; NbExp=3; IntAct=EBI-352089, EBI-389883;
P63000:RAC1; NbExp=2; IntAct=EBI-352089, EBI-413628;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cell cortex.
Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line.
Note=In differentiating myotubes, isoform 1, isoform 2 and isoform
3 are localized diffusely throughout the cytoplasm with regions of
enrichment at the longitudinal actin stress fiber. In
differentiated tubes, isoform 1 is also detected within the Z-
lines.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton.
Note=Predominantly localized at actin stress fibers.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm, cytoskeleton.
Note=Predominantly localized at actin stress fibers.
-!- SUBCELLULAR LOCATION: Isoform 6: Cytoplasm, cytoskeleton.
Note=Polarized at the periphery of myotubes.
-!- 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;
Note=May be due to exon skipping.;
Name=3; Synonyms=Var-1;
IsoId=O75369-3; Sequence=VSP_008774;
Note=May be due to exon skipping.;
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;
Note=May be due to competing donor splice sites.;
Name=6; Synonyms=Var-1-DeltaH1;
IsoId=O75369-6; Sequence=VSP_008773, VSP_008774;
Note=May be due to exon skipping.;
Name=8;
IsoId=O75369-8; Sequence=VSP_043446;
Note=Contains a phosphoserine at position 1474.
{ECO:0000244|PubMed:24275569};
Name=9;
IsoId=O75369-9; Sequence=VSP_024115;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Isoform 1 and isoform 2 are
expressed in placenta, bone marrow, brain, umbilical vein
endothelial cells (HUVEC), retina and skeletal muscle. Isoform 1
is predominantly expressed in prostate, uterus, liver, thyroid,
stomach, lymph node, small intestine, spleen, skeletal muscle,
kidney, placenta, pancreas, heart, lung, platelets, endothelial
cells, megakaryocytic and erythroleukemic cell lines. Isoform 2 is
predominantly expressed in spinal cord, platelet and Daudi cells.
Also expressed in thyroid adenoma, neurofibrillary tangles (NFT),
senile plaques in the hippocampus and cerebral cortex in Alzheimer
disease (AD). Isoform 3 and isoform 6 are expressed predominantly
in lung, heart, skeletal muscle, testis, spleen, thymus and
leukocytes. Isoform 4 and isoform 5 are expressed in heart.
{ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:8327473,
ECO:0000269|PubMed:9651345, ECO:0000269|PubMed:9694715}.
-!- DOMAIN: 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.
-!- PTM: ISGylation prevents ability to interact with the upstream
activators of the JNK cascade and inhibits IFNA-induced JNK
signaling. {ECO:0000269|PubMed:19270716}.
-!- PTM: Ubiquitination by a SCF-like complex containing ASB2 isoform
2 leads to proteasomal degradation which promotes muscle
differentiation. {ECO:0000269|PubMed:19300455}.
-!- DISEASE: Note=Interaction with FLNA may compensate for
dysfunctional FLNA homodimer in the periventricular nodular
heterotopia (PVNH) disorder.
-!- DISEASE: Atelosteogenesis 1 (AO1) [MIM:108720]: A lethal
chondrodysplasia characterized by distal hypoplasia of the humeri
and femurs, hypoplasia of the mid-thoracic spine, occasionally
complete lack of ossification of single hand bones, and the
finding in cartilage of multiple degenerated chondrocytes which
are encapsulated in fibrous tissue. {ECO:0000269|PubMed:14991055}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Atelosteogenesis 3 (AO3) [MIM:108721]: A short-limb
lethal skeletal dysplasia with vertebral abnormalities,
disharmonious skeletal maturation, poorly modeled long bones and
joint dislocations. Recurrent respiratory insufficiency and/or
infections usually result in early death.
{ECO:0000269|PubMed:14991055}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Boomerang dysplasia (BOOMD) [MIM:112310]: A perinatal
lethal osteochondrodysplasia characterized by absence or
underossification of the limb bones and vertebrae. Patients
manifest dwarfism with short, bowed, rigid limbs and
characteristic facies. Boomerang dysplasia is distinguished from
atelosteogenesis on the basis of a more severe defect in
mineralization, with complete absence of ossification in some limb
elements and vertebral segments. {ECO:0000269|PubMed:15994868}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Larsen syndrome (LRS) [MIM:150250]: An
osteochondrodysplasia characterized by large-joint dislocations
and characteristic craniofacial abnormalities. The cardinal
features of the condition are dislocations of the hip, knee and
elbow joints, with equinovarus or equinovalgus foot deformities.
Spatula-shaped fingers, most marked in the thumb, are also
present. Craniofacial anomalies include hypertelorism, prominence
of the forehead, a depressed nasal bridge, and a flattened
midface. Cleft palate and short stature are often associated
features. Spinal anomalies include scoliosis and cervical
kyphosis. Hearing loss is a well-recognized complication.
{ECO:0000269|PubMed:14991055, ECO:0000269|PubMed:16801345}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Spondylocarpotarsal synostosis syndrome (SCT)
[MIM:272460]: Disorder characterized by short stature and
vertebral, carpal and tarsal fusions.
{ECO:0000269|PubMed:14991055}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA35505.1; Type=Frameshift; Positions=2432, 2589; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF042166; AAC39842.1; -; mRNA.
EMBL; AF043045; AAC33845.1; -; mRNA.
EMBL; AF353666; AAL68439.1; -; mRNA.
EMBL; AF353667; AAL68440.1; -; Genomic_DNA.
EMBL; AF353667; AAL68441.1; -; Genomic_DNA.
EMBL; AF353667; AAL68442.1; -; Genomic_DNA.
EMBL; AF353667; AAL68443.1; -; Genomic_DNA.
EMBL; AF191633; AAF72339.1; -; Genomic_DNA.
EMBL; AF191594; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191595; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191596; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191597; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191598; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191599; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191600; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191601; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191602; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191603; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191604; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191605; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191606; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191607; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191608; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191609; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191611; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191610; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191613; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191612; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191614; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191615; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191617; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191616; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191618; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191619; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191620; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191621; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191622; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191623; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191624; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191625; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191627; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191626; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191628; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191629; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191630; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191631; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF191632; AAF72339.1; JOINED; Genomic_DNA.
EMBL; AF238609; AAF97046.1; -; mRNA.
EMBL; AB371580; BAG48309.1; -; mRNA.
EMBL; AB371581; BAG48310.1; -; mRNA.
EMBL; AB371582; BAG48311.1; -; mRNA.
EMBL; AB191258; BAD52434.1; -; mRNA.
EMBL; BX641085; CAE46040.1; -; mRNA.
EMBL; AC114399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC137936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL137574; CAB70818.1; -; mRNA.
EMBL; AB209889; BAD93126.1; -; mRNA.
EMBL; M62994; AAA35505.1; ALT_FRAME; mRNA.
CCDS; CCDS2885.1; -. [O75369-1]
CCDS; CCDS54599.1; -. [O75369-8]
CCDS; CCDS54600.1; -. [O75369-9]
CCDS; CCDS54601.1; -. [O75369-2]
PIR; T46270; T46270.
RefSeq; NP_001157789.1; NM_001164317.1. [O75369-8]
RefSeq; NP_001157790.1; NM_001164318.1. [O75369-9]
RefSeq; NP_001157791.1; NM_001164319.1. [O75369-2]
RefSeq; NP_001448.2; NM_001457.3. [O75369-1]
UniGene; Hs.476448; -.
PDB; 2DI8; NMR; -; A=1999-2096.
PDB; 2DI9; NMR; -; A=1017-1134.
PDB; 2DIA; NMR; -; A=1130-1229.
PDB; 2DIB; NMR; -; A=1215-1329.
PDB; 2DIC; NMR; -; A=1325-1422.
PDB; 2DJ4; NMR; -; A=1418-1518.
PDB; 2DLG; NMR; -; A=2104-2192.
PDB; 2DMB; NMR; -; A=1611-1721.
PDB; 2DMC; NMR; -; A=1899-2001.
PDB; 2E9I; NMR; -; A=2094-2192.
PDB; 2E9J; NMR; -; A=1504-1615.
PDB; 2EE6; NMR; -; A=2190-2287.
PDB; 2EE9; NMR; -; A=1736-1823.
PDB; 2EEA; NMR; -; A=1808-1915.
PDB; 2EEB; NMR; -; A=2284-2382.
PDB; 2EEC; NMR; -; A=2371-2488.
PDB; 2EED; NMR; -; A=2509-2602.
PDB; 2WA5; X-ray; 1.90 A; A=2-242.
PDB; 2WA6; X-ray; 1.95 A; A=2-242.
PDB; 2WA7; X-ray; 1.85 A; A=2-242.
PDB; 3FER; X-ray; 2.40 A; A/B/C/D=1-252.
PDB; 4B7L; X-ray; 2.05 A; A/B=1-347.
PDB; 5DCP; X-ray; 2.49 A; A/B=1737-1911.
PDBsum; 2DI8; -.
PDBsum; 2DI9; -.
PDBsum; 2DIA; -.
PDBsum; 2DIB; -.
PDBsum; 2DIC; -.
PDBsum; 2DJ4; -.
PDBsum; 2DLG; -.
PDBsum; 2DMB; -.
PDBsum; 2DMC; -.
PDBsum; 2E9I; -.
PDBsum; 2E9J; -.
PDBsum; 2EE6; -.
PDBsum; 2EE9; -.
PDBsum; 2EEA; -.
PDBsum; 2EEB; -.
PDBsum; 2EEC; -.
PDBsum; 2EED; -.
PDBsum; 2WA5; -.
PDBsum; 2WA6; -.
PDBsum; 2WA7; -.
PDBsum; 3FER; -.
PDBsum; 4B7L; -.
PDBsum; 5DCP; -.
ProteinModelPortal; O75369; -.
SMR; O75369; -.
BioGrid; 108606; 105.
IntAct; O75369; 54.
MINT; MINT-4998813; -.
STRING; 9606.ENSP00000420213; -.
TCDB; 8.A.66.1.5; the dystrophin (dystrophin) family.
iPTMnet; O75369; -.
PhosphoSitePlus; O75369; -.
SwissPalm; O75369; -.
BioMuta; FLNB; -.
EPD; O75369; -.
MaxQB; O75369; -.
PaxDb; O75369; -.
PeptideAtlas; O75369; -.
PRIDE; O75369; -.
DNASU; 2317; -.
Ensembl; ENST00000295956; ENSP00000295956; ENSG00000136068. [O75369-1]
Ensembl; ENST00000358537; ENSP00000351339; ENSG00000136068. [O75369-2]
Ensembl; ENST00000429972; ENSP00000415599; ENSG00000136068. [O75369-9]
Ensembl; ENST00000490882; ENSP00000420213; ENSG00000136068. [O75369-8]
GeneID; 2317; -.
KEGG; hsa:2317; -.
UCSC; uc003djj.3; human. [O75369-1]
CTD; 2317; -.
DisGeNET; 2317; -.
GeneCards; FLNB; -.
GeneReviews; FLNB; -.
H-InvDB; HIX0003397; -.
HGNC; HGNC:3755; FLNB.
HPA; CAB019322; -.
HPA; HPA004747; -.
HPA; HPA004886; -.
MalaCards; FLNB; -.
MIM; 108720; phenotype.
MIM; 108721; phenotype.
MIM; 112310; phenotype.
MIM; 150250; phenotype.
MIM; 272460; phenotype.
MIM; 603381; gene.
neXtProt; NX_O75369; -.
OpenTargets; ENSG00000136068; -.
Orphanet; 1190; Atelosteogenesis type I.
Orphanet; 56305; Atelosteogenesis type III.
Orphanet; 503; Autosomal dominant Larsen syndrome.
Orphanet; 1263; Boomerang dysplasia.
Orphanet; 3275; Spondylocarpotarsal synostosis.
PharmGKB; PA28173; -.
eggNOG; KOG0518; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00660000095431; -.
HOGENOM; HOG000044235; -.
HOVERGEN; HBG004163; -.
InParanoid; O75369; -.
KO; K04437; -.
OMA; GTYDIFY; -.
OrthoDB; EOG091G00U5; -.
PhylomeDB; O75369; -.
TreeFam; TF313685; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
SignaLink; O75369; -.
ChiTaRS; FLNB; human.
EvolutionaryTrace; O75369; -.
GeneWiki; FLNB; -.
GenomeRNAi; 2317; -.
PRO; PR:O75369; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000136068; -.
ExpressionAtlas; O75369; baseline and differential.
Genevisible; O75369; HS.
GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
GO; GO:0005903; C:brush border; IEA:Ensembl.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; NAS:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; TAS:ProtInc.
GO; GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl.
GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
CDD; cd00014; CH; 2.
Gene3D; 1.10.418.10; -; 2.
Gene3D; 2.60.40.10; -; 24.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR001715; CH-domain.
InterPro; IPR017868; Filamin/ABP280_repeat-like.
InterPro; IPR001298; Filamin/ABP280_rpt.
InterPro; IPR029874; FLNB.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
PANTHER; PTHR11915:SF419; PTHR11915:SF419; 1.
Pfam; PF00307; CH; 2.
Pfam; PF00630; Filamin; 23.
SMART; SM00033; CH; 2.
SMART; SM00557; IG_FLMN; 24.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF81296; SSF81296; 24.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS50194; FILAMIN_REPEAT; 24.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alternative splicing;
Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
Differentiation; Disease mutation; Dwarfism; Isopeptide bond;
Myogenesis; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Ubl conjugation.
CHAIN 1 2602 Filamin-B.
/FTId=PRO_0000087298.
DOMAIN 1 239 Actin-binding.
DOMAIN 16 122 Calponin-homology 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 139 239 Calponin-homology 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REPEAT 249 347 Filamin 1.
REPEAT 349 446 Filamin 2.
REPEAT 447 543 Filamin 3.
REPEAT 544 636 Filamin 4.
REPEAT 640 736 Filamin 5.
REPEAT 737 839 Filamin 6.
REPEAT 840 938 Filamin 7.
REPEAT 939 1034 Filamin 8.
REPEAT 1035 1127 Filamin 9.
REPEAT 1128 1222 Filamin 10.
REPEAT 1223 1322 Filamin 11.
REPEAT 1323 1415 Filamin 12.
REPEAT 1416 1511 Filamin 13.
REPEAT 1512 1608 Filamin 14.
REPEAT 1609 1704 Filamin 15.
REPEAT 1729 1813 Filamin 16.
REPEAT 1816 1908 Filamin 17.
REPEAT 1919 1994 Filamin 18.
REPEAT 1997 2089 Filamin 19.
REPEAT 2091 2185 Filamin 20.
REPEAT 2188 2280 Filamin 21.
REPEAT 2282 2375 Filamin 22.
REPEAT 2379 2471 Filamin 23.
REPEAT 2507 2601 Filamin 24.
REGION 1128 1511 Interaction with FBLP1.
{ECO:0000269|PubMed:12496242}.
REGION 1705 1728 Hinge 1. {ECO:0000250}.
REGION 1862 2148 Interaction with the cytoplasmic tail of
GP1BA.
REGION 2060 2225 Interaction with FLNA 1.
REGION 2130 2602 Interaction with INPPL1.
{ECO:0000269|PubMed:11739414}.
REGION 2472 2602 Self-association site, tail.
{ECO:0000250}.
REGION 2472 2506 Hinge 2. {ECO:0000250}.
REGION 2507 2602 Interaction with FLNA 2.
MOD_RES 216 216 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 519 519 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 681 681 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 730 730 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 932 932 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 983 983 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1307 1307 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1316 1316 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 1433 1433 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1505 1505 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1602 1602 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1780 1780 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q80X90}.
MOD_RES 2083 2083 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2107 2107 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2113 2113 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2369 2369 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2465 2465 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2478 2478 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2481 2481 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2492 2492 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2518 2518 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q80X90}.
MOD_RES 2524 2524 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q80X90}.
MOD_RES 2576 2576 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 2468 2468 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
{ECO:0000269|PubMed:19270716}.
VAR_SEQ 1 169 Missing (in isoform 7).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_024113.
VAR_SEQ 170 181 ALGALVDSCAPG -> MQEHSTRRRSLS (in isoform
7). {ECO:0000303|PubMed:17974005}.
/FTId=VSP_024114.
VAR_SEQ 1463 1463 R -> RADDTDSQSWRSPLKALSEFFKGDPKGDFNKT (in
isoform 8). {ECO:0000303|PubMed:16106752,
ECO:0000303|PubMed:18487259}.
/FTId=VSP_043446.
VAR_SEQ 1704 1727 Missing (in isoform 2 and isoform 6).
{ECO:0000303|PubMed:16106752,
ECO:0000303|PubMed:18487259,
ECO:0000303|PubMed:9694715}.
/FTId=VSP_008773.
VAR_SEQ 1717 1727 Missing (in isoform 7 and isoform 9).
{ECO:0000303|PubMed:16106752,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:18487259}.
/FTId=VSP_024115.
VAR_SEQ 2081 2121 Missing (in isoform 3 and isoform 6).
{ECO:0000305}.
/FTId=VSP_008774.
VAR_SEQ 2123 2150 EINSSDMSAHVTSPSGRVTEAEIVPMGK -> GVRVMNCSA
QILWGWRVQFHTGSRNQQQ (in isoform 4).
{ECO:0000305}.
/FTId=VSP_008775.
VAR_SEQ 2123 2146 EINSSDMSAHVTSPSGRVTEAEIV -> GVRVMNCSAQILW
GWRVQFHTGSR (in isoform 5).
{ECO:0000305}.
/FTId=VSP_008777.
VAR_SEQ 2147 2602 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_008778.
VAR_SEQ 2151 2602 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_008776.
VARIANT 161 161 F -> C (in LRS; dbSNP:rs80356506).
{ECO:0000269|PubMed:14991055,
ECO:0000269|PubMed:16801345}.
/FTId=VAR_033069.
VARIANT 168 168 G -> S (in LRS; dbSNP:rs80356504).
{ECO:0000269|PubMed:16801345}.
/FTId=VAR_033070.
VARIANT 171 171 L -> R (in BOOMD; dbSNP:rs80356494).
{ECO:0000269|PubMed:15994868}.
/FTId=VAR_033071.
VARIANT 173 173 A -> V (in AO1; dbSNP:rs121908894).
{ECO:0000269|PubMed:14991055}.
/FTId=VAR_033072.
VARIANT 188 188 S -> P (in AO1).
{ECO:0000269|PubMed:14991055}.
/FTId=VAR_033073.
VARIANT 202 202 M -> V (in AO1 and AO3;
dbSNP:rs121908895).
{ECO:0000269|PubMed:14991055}.
/FTId=VAR_033074.
VARIANT 227 227 E -> K (in LRS; dbSNP:rs80356508).
{ECO:0000269|PubMed:14991055,
ECO:0000269|PubMed:16801345}.
/FTId=VAR_033075.
VARIANT 234 234 L -> V (in LRS; dbSNP:rs80356507).
{ECO:0000269|PubMed:16801345}.
/FTId=VAR_033076.
VARIANT 235 235 S -> P (in BOOMD; dbSNP:rs121908896).
{ECO:0000269|PubMed:15994868}.
/FTId=VAR_033077.
VARIANT 361 361 G -> S (in LRS; dbSNP:rs80356509).
{ECO:0000269|PubMed:16801345}.
/FTId=VAR_033078.
VARIANT 363 363 G -> E (in LRS; dbSNP:rs80356510).
{ECO:0000269|PubMed:16801345}.
/FTId=VAR_033079.
VARIANT 566 566 R -> Q (in a breast cancer sample;
somatic mutation; dbSNP:rs150747960).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035917.
VARIANT 663 663 N -> K (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035918.
VARIANT 703 703 T -> K (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035919.
VARIANT 751 751 G -> R (in AO3; dbSNP:rs28937587).
{ECO:0000269|PubMed:14991055}.
/FTId=VAR_033080.
VARIANT 1018 1018 V -> M (in dbSNP:rs2276742).
/FTId=VAR_017182.
VARIANT 1157 1157 D -> N (in dbSNP:rs1131356).
{ECO:0000269|PubMed:11153914,
ECO:0000269|PubMed:18487259,
ECO:0000269|PubMed:9651345}.
/FTId=VAR_017183.
VARIANT 1179 1179 E -> K (in dbSNP:rs17058845).
/FTId=VAR_031392.
VARIANT 1431 1431 L -> R (in LRS; dbSNP:rs80356511).
{ECO:0000269|PubMed:16801345}.
/FTId=VAR_033081.
VARIANT 1471 1471 V -> M (in dbSNP:rs12632456).
{ECO:0000269|PubMed:11153914,
ECO:0000269|PubMed:18487259,
ECO:0000269|PubMed:9651345}.
/FTId=VAR_031393.
VARIANT 1534 1534 A -> G (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035920.
VARIANT 1571 1571 Missing (in LRS).
{ECO:0000269|PubMed:14991055,
ECO:0000269|PubMed:16801345}.
/FTId=VAR_033082.
VARIANT 1586 1586 G -> R (in LRS; dbSNP:rs28939706).
{ECO:0000269|PubMed:14991055,
ECO:0000269|PubMed:16801345}.
/FTId=VAR_033083.
VARIANT 1592 1592 V -> D (in LRS; dbSNP:rs80356514).
{ECO:0000269|PubMed:16801345}.
/FTId=VAR_033084.
VARIANT 1603 1603 P -> L (in LRS; dbSNP:rs80356515).
{ECO:0000269|PubMed:16801345}.
/FTId=VAR_033085.
VARIANT 1691 1691 G -> S (in LRS; dbSNP:rs80356503).
{ECO:0000269|PubMed:14991055,
ECO:0000269|PubMed:16801345}.
/FTId=VAR_033086.
VARIANT 1834 1834 G -> R (in LRS; dbSNP:rs80356516).
{ECO:0000269|PubMed:16801345}.
/FTId=VAR_033087.
MUTAGEN 2468 2468 K->R: Cytoplasmic localization.
{ECO:0000269|PubMed:19270716}.
CONFLICT 816 816 A -> T (in Ref. 7; CAE46040).
{ECO:0000305}.
CONFLICT 924 924 Y -> H (in Ref. 7; CAE46040).
{ECO:0000305}.
CONFLICT 1411 1411 F -> L (in Ref. 7; CAE46040).
{ECO:0000305}.
CONFLICT 1560 1560 E -> G (in Ref. 7; CAE46040).
{ECO:0000305}.
CONFLICT 1953 1953 L -> F (in Ref. 4; AAF97046).
{ECO:0000305}.
CONFLICT 2006 2006 K -> R (in Ref. 2; AAC33845).
{ECO:0000305}.
CONFLICT 2099 2099 I -> S (in Ref. 7; CAE46040).
{ECO:0000305}.
CONFLICT 2170 2170 K -> N (in Ref. 4; AAF97046).
{ECO:0000305}.
CONFLICT 2293 2293 M -> V (in Ref. 4; AAF97046 and 7;
CAE46040). {ECO:0000305}.
CONFLICT 2354 2354 V -> A (in Ref. 11; CAB70818).
{ECO:0000305}.
CONFLICT 2487 2487 S -> C (in Ref. 13; AAA35505).
{ECO:0000305}.
CONFLICT 2571 2571 V -> A (in Ref. 11; CAB70818).
{ECO:0000305}.
HELIX 5 10 {ECO:0000244|PDB:2WA5}.
HELIX 13 16 {ECO:0000244|PDB:2WA7}.
HELIX 17 30 {ECO:0000244|PDB:2WA7}.
HELIX 31 33 {ECO:0000244|PDB:2WA7}.
TURN 40 46 {ECO:0000244|PDB:2WA7}.
HELIX 48 58 {ECO:0000244|PDB:2WA7}.
HELIX 73 89 {ECO:0000244|PDB:2WA7}.
HELIX 99 103 {ECO:0000244|PDB:2WA7}.
HELIX 107 122 {ECO:0000244|PDB:2WA7}.
HELIX 141 152 {ECO:0000244|PDB:2WA7}.
HELIX 163 165 {ECO:0000244|PDB:2WA7}.
HELIX 169 178 {ECO:0000244|PDB:2WA7}.
HELIX 186 188 {ECO:0000244|PDB:2WA7}.
HELIX 194 208 {ECO:0000244|PDB:2WA7}.
HELIX 217 220 {ECO:0000244|PDB:2WA7}.
HELIX 227 234 {ECO:0000244|PDB:2WA7}.
HELIX 236 239 {ECO:0000244|PDB:2WA7}.
HELIX 254 256 {ECO:0000244|PDB:4B7L}.
STRAND 258 261 {ECO:0000244|PDB:4B7L}.
HELIX 262 264 {ECO:0000244|PDB:4B7L}.
STRAND 265 267 {ECO:0000244|PDB:4B7L}.
STRAND 275 280 {ECO:0000244|PDB:4B7L}.
TURN 282 284 {ECO:0000244|PDB:4B7L}.
STRAND 289 294 {ECO:0000244|PDB:4B7L}.
STRAND 300 302 {ECO:0000244|PDB:4B7L}.
STRAND 304 309 {ECO:0000244|PDB:4B7L}.
STRAND 313 319 {ECO:0000244|PDB:4B7L}.
STRAND 323 333 {ECO:0000244|PDB:4B7L}.
STRAND 342 347 {ECO:0000244|PDB:4B7L}.
HELIX 1040 1042 {ECO:0000244|PDB:2DI9}.
STRAND 1044 1047 {ECO:0000244|PDB:2DI9}.
HELIX 1048 1051 {ECO:0000244|PDB:2DI9}.
STRAND 1052 1054 {ECO:0000244|PDB:2DI9}.
STRAND 1059 1064 {ECO:0000244|PDB:2DI9}.
TURN 1066 1068 {ECO:0000244|PDB:2DI9}.
STRAND 1073 1077 {ECO:0000244|PDB:2DI9}.
STRAND 1079 1081 {ECO:0000244|PDB:2DI9}.
STRAND 1084 1089 {ECO:0000244|PDB:2DI9}.
STRAND 1091 1100 {ECO:0000244|PDB:2DI9}.
STRAND 1102 1115 {ECO:0000244|PDB:2DI9}.
STRAND 1122 1128 {ECO:0000244|PDB:2DI9}.
HELIX 1133 1135 {ECO:0000244|PDB:2DIA}.
STRAND 1136 1140 {ECO:0000244|PDB:2DIA}.
HELIX 1141 1143 {ECO:0000244|PDB:2DIA}.
STRAND 1154 1160 {ECO:0000244|PDB:2DIA}.
STRAND 1166 1172 {ECO:0000244|PDB:2DIA}.
TURN 1173 1175 {ECO:0000244|PDB:2DIA}.
STRAND 1179 1184 {ECO:0000244|PDB:2DIA}.
STRAND 1188 1195 {ECO:0000244|PDB:2DIA}.
STRAND 1200 1208 {ECO:0000244|PDB:2DIA}.
STRAND 1217 1223 {ECO:0000244|PDB:2DIA}.
STRAND 1232 1235 {ECO:0000244|PDB:2DIB}.
HELIX 1236 1239 {ECO:0000244|PDB:2DIB}.
STRAND 1249 1254 {ECO:0000244|PDB:2DIB}.
STRAND 1256 1258 {ECO:0000244|PDB:2DIB}.
STRAND 1273 1275 {ECO:0000244|PDB:2DIB}.
STRAND 1281 1284 {ECO:0000244|PDB:2DIB}.
STRAND 1286 1294 {ECO:0000244|PDB:2DIB}.
STRAND 1300 1310 {ECO:0000244|PDB:2DIB}.
STRAND 1317 1321 {ECO:0000244|PDB:2DIB}.
STRAND 1332 1335 {ECO:0000244|PDB:2DIC}.
HELIX 1336 1339 {ECO:0000244|PDB:2DIC}.
STRAND 1347 1352 {ECO:0000244|PDB:2DIC}.
TURN 1354 1356 {ECO:0000244|PDB:2DIC}.
STRAND 1361 1369 {ECO:0000244|PDB:2DIC}.
STRAND 1374 1377 {ECO:0000244|PDB:2DIC}.
STRAND 1379 1381 {ECO:0000244|PDB:2DIC}.
STRAND 1383 1387 {ECO:0000244|PDB:2DIC}.
STRAND 1393 1401 {ECO:0000244|PDB:2DIC}.
STRAND 1410 1416 {ECO:0000244|PDB:2DIC}.
STRAND 1425 1428 {ECO:0000244|PDB:2DJ4}.
TURN 1429 1431 {ECO:0000244|PDB:2DJ4}.
STRAND 1441 1446 {ECO:0000244|PDB:2DJ4}.
TURN 1448 1450 {ECO:0000244|PDB:2DJ4}.
STRAND 1455 1460 {ECO:0000244|PDB:2DJ4}.
STRAND 1462 1464 {ECO:0000244|PDB:2DJ4}.
STRAND 1475 1483 {ECO:0000244|PDB:2DJ4}.
STRAND 1489 1501 {ECO:0000244|PDB:2DJ4}.
STRAND 1506 1512 {ECO:0000244|PDB:2DJ4}.
HELIX 1517 1519 {ECO:0000244|PDB:2E9J}.
STRAND 1520 1524 {ECO:0000244|PDB:2E9J}.
HELIX 1525 1527 {ECO:0000244|PDB:2E9J}.
STRAND 1538 1546 {ECO:0000244|PDB:2E9J}.
STRAND 1566 1570 {ECO:0000244|PDB:2E9J}.
STRAND 1573 1580 {ECO:0000244|PDB:2E9J}.
STRAND 1586 1590 {ECO:0000244|PDB:2E9J}.
STRAND 1593 1596 {ECO:0000244|PDB:2E9J}.
STRAND 1603 1609 {ECO:0000244|PDB:2E9J}.
STRAND 1618 1621 {ECO:0000244|PDB:2DMB}.
HELIX 1622 1624 {ECO:0000244|PDB:2DMB}.
STRAND 1625 1639 {ECO:0000244|PDB:2DMB}.
STRAND 1641 1643 {ECO:0000244|PDB:2DMB}.
STRAND 1648 1653 {ECO:0000244|PDB:2DMB}.
STRAND 1663 1666 {ECO:0000244|PDB:2DMB}.
STRAND 1672 1677 {ECO:0000244|PDB:2DMB}.
STRAND 1682 1692 {ECO:0000244|PDB:2DMB}.
STRAND 1699 1705 {ECO:0000244|PDB:2DMB}.
STRAND 1747 1751 {ECO:0000244|PDB:5DCP}.
STRAND 1760 1765 {ECO:0000244|PDB:5DCP}.
STRAND 1775 1779 {ECO:0000244|PDB:5DCP}.
TURN 1780 1782 {ECO:0000244|PDB:5DCP}.
STRAND 1783 1788 {ECO:0000244|PDB:5DCP}.
STRAND 1794 1802 {ECO:0000244|PDB:5DCP}.
STRAND 1811 1816 {ECO:0000244|PDB:5DCP}.
STRAND 1825 1828 {ECO:0000244|PDB:5DCP}.
HELIX 1829 1831 {ECO:0000244|PDB:5DCP}.
STRAND 1833 1835 {ECO:0000244|PDB:5DCP}.
STRAND 1840 1845 {ECO:0000244|PDB:5DCP}.
STRAND 1855 1863 {ECO:0000244|PDB:5DCP}.
STRAND 1868 1870 {ECO:0000244|PDB:5DCP}.
STRAND 1872 1880 {ECO:0000244|PDB:5DCP}.
STRAND 1886 1898 {ECO:0000244|PDB:5DCP}.
STRAND 1903 1909 {ECO:0000244|PDB:5DCP}.
STRAND 1924 1927 {ECO:0000244|PDB:2DMC}.
STRAND 1941 1943 {ECO:0000244|PDB:2DMC}.
STRAND 1952 1957 {ECO:0000244|PDB:2DMC}.
TURN 1958 1960 {ECO:0000244|PDB:2DMC}.
STRAND 1961 1966 {ECO:0000244|PDB:2DMC}.
STRAND 1972 1977 {ECO:0000244|PDB:2DMC}.
STRAND 1979 1984 {ECO:0000244|PDB:2DMC}.
STRAND 1989 1994 {ECO:0000244|PDB:2DMC}.
STRAND 1997 1999 {ECO:0000244|PDB:2DMC}.
HELIX 2002 2004 {ECO:0000244|PDB:2DI8}.
STRAND 2006 2010 {ECO:0000244|PDB:2DI8}.
TURN 2011 2013 {ECO:0000244|PDB:2DI8}.
STRAND 2014 2016 {ECO:0000244|PDB:2DI8}.
STRAND 2021 2026 {ECO:0000244|PDB:2DI8}.
TURN 2028 2030 {ECO:0000244|PDB:2DI8}.
STRAND 2035 2043 {ECO:0000244|PDB:2DI8}.
STRAND 2057 2061 {ECO:0000244|PDB:2DI8}.
STRAND 2067 2077 {ECO:0000244|PDB:2DI8}.
STRAND 2084 2090 {ECO:0000244|PDB:2DI8}.
STRAND 2111 2113 {ECO:0000244|PDB:2DLG}.
STRAND 2118 2120 {ECO:0000244|PDB:2DLG}.
HELIX 2126 2128 {ECO:0000244|PDB:2DLG}.
STRAND 2130 2134 {ECO:0000244|PDB:2DLG}.
STRAND 2140 2142 {ECO:0000244|PDB:2DLG}.
STRAND 2144 2147 {ECO:0000244|PDB:2DLG}.
STRAND 2149 2157 {ECO:0000244|PDB:2DLG}.
STRAND 2164 2175 {ECO:0000244|PDB:2DLG}.
STRAND 2180 2185 {ECO:0000244|PDB:2DLG}.
HELIX 2193 2195 {ECO:0000244|PDB:2EE6}.
TURN 2201 2203 {ECO:0000244|PDB:2EE6}.
STRAND 2206 2208 {ECO:0000244|PDB:2EE6}.
STRAND 2210 2214 {ECO:0000244|PDB:2EE6}.
STRAND 2219 2221 {ECO:0000244|PDB:2EE6}.
STRAND 2226 2234 {ECO:0000244|PDB:2EE6}.
STRAND 2236 2240 {ECO:0000244|PDB:2EE6}.
STRAND 2250 2256 {ECO:0000244|PDB:2EE6}.
STRAND 2258 2266 {ECO:0000244|PDB:2EE6}.
STRAND 2275 2281 {ECO:0000244|PDB:2EE6}.
STRAND 2288 2294 {ECO:0000244|PDB:2EEB}.
STRAND 2306 2314 {ECO:0000244|PDB:2EEB}.
STRAND 2320 2324 {ECO:0000244|PDB:2EEB}.
STRAND 2330 2332 {ECO:0000244|PDB:2EEB}.
STRAND 2334 2337 {ECO:0000244|PDB:2EEB}.
STRAND 2340 2347 {ECO:0000244|PDB:2EEB}.
STRAND 2352 2365 {ECO:0000244|PDB:2EEB}.
STRAND 2370 2375 {ECO:0000244|PDB:2EEB}.
TURN 2384 2386 {ECO:0000244|PDB:2EEC}.
STRAND 2388 2392 {ECO:0000244|PDB:2EEC}.
TURN 2393 2395 {ECO:0000244|PDB:2EEC}.
STRAND 2403 2408 {ECO:0000244|PDB:2EEC}.
TURN 2410 2412 {ECO:0000244|PDB:2EEC}.
STRAND 2417 2425 {ECO:0000244|PDB:2EEC}.
STRAND 2430 2433 {ECO:0000244|PDB:2EEC}.
STRAND 2435 2442 {ECO:0000244|PDB:2EEC}.
STRAND 2448 2459 {ECO:0000244|PDB:2EEC}.
STRAND 2466 2473 {ECO:0000244|PDB:2EEC}.
TURN 2512 2514 {ECO:0000244|PDB:2EED}.
STRAND 2516 2519 {ECO:0000244|PDB:2EED}.
HELIX 2520 2523 {ECO:0000244|PDB:2EED}.
STRAND 2531 2536 {ECO:0000244|PDB:2EED}.
TURN 2538 2540 {ECO:0000244|PDB:2EED}.
STRAND 2545 2547 {ECO:0000244|PDB:2EED}.
STRAND 2557 2565 {ECO:0000244|PDB:2EED}.
STRAND 2568 2574 {ECO:0000244|PDB:2EED}.
STRAND 2579 2583 {ECO:0000244|PDB:2EED}.
STRAND 2585 2591 {ECO:0000244|PDB:2EED}.
STRAND 2596 2601 {ECO:0000244|PDB:2EED}.
SEQUENCE 2602 AA; 278164 MW; 1BF5C64C86360C6A CRC64;
MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL IALLEVLSQK
RMYRKYHQRP TFRQMQLENV SVALEFLDRE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH
YSISMPVWED EGDDDAKKQT PKQRLLGWIQ NKIPYLPITN FNQNWQDGKA LGALVDSCAP
GLCPDWESWD PQKPVDNARE AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA
KLKPGAPLKP KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK
EEAQVTPDSD KNKTYSVEYL PKVTGLHKVT VLFAGQHISK SPFEVSVDKA QGDASKVTAK
GPGLEAVGNI ANKPTYFDIY TAGAGVGDIG VEVEDPQGKN TVELLVEDKG NQVYRCVYKP
MQPGPHVVKI FFAGDTIPKS PFVVQVGEAC NPNACRASGR GLQPKGVRIR ETTDFKVDTK
AAGSGELGVT MKGPKGLEEL VKQKDFLDGV YAFEYYPSTP GRYSIAITWG GHHIPKSPFE
VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG SLGFAIEGPS QAKIEYNDQN
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GGYNPDLVRA YGPGLEKSGC
IVNNLAEFTV DPKDAGKAPL KIFAQDGEGQ RIDIQMKNRM DGTYACSYTP VKAIKHTIAV
VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP GVERSGLKAN EPTHFTVDCT EAGEGDVSVG
IKCDARVLSE DEEDVDFDII HNANDTFTVK YVPPAAGRYT IKVLFASQEI PASPFRVKVD
PSHDASKVKA EGPGLSKAGV ENGKPTHFTV YTKGAGKAPL NVQFNSPLPG DAVKDLDIID
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKLN GLENRVEVGK
DQEFTVDTRG AGGQGKLDVT ILSPSRKVVP CLVTPVTGRE NSTAKFIPRE EGLYAVDVTY
DGHPVPGSPY TVEASLPPDP SKVKAHGPGL EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP
CEAKIECSDN GDGTCSVSYL PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG
PGLEHGKVGE AGLLSVDCSE AGPGALGLEA VSDSGTKAEV SIQNNKDGTY AVTYVPLTAG
MYTLTMKYGG ELVPHFPARV KVEPAVDTSR IKVFGPGIEG KDVFREATTD FTVDSRPLTQ
VGGDHIKAHI ANPSGASTEC FVTDNADGTY QVEYTPFEKG LHVVEVTYDD VPIPNSPFKV
AVTEGCQPSR VQAQGPGLKE AFTNKPNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD
GSCSAEYIPF APGDYDVNIT YGGAHIPGSP FRVPVKDVVD PSKVKIAGPG LGSGVRARVL
QSFTVDSSKA GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YMVSVKYADE
EIPRSPFKVK VLPTYDASKV TASGPGLSSY GVPASLPVDF AIDARDAGEG LLAVQITDQE
GKPKRAIVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDDIP LSPYRIRATQ TGDASKCLAT
GPGIASTVKT GEEVGFVVDA KTAGKGKVTC TVLTPDGTEA EADVIENEDG TYDIFYTAAK
PGTYVIYVRF GGVDIPNSPF TVMATDGEVT AVEEAPVNAC PPGFRPWVTE EAYVPVSDMN
GLGFKPFDLV IPFAVRKGEI TGEVHMPSGK TATPEIVDNK DGTVTVRYAP TEVGLHEMHI
KYMGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG EGGLDLAIEG
PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP GSPFTAKITD DSRRCSQVKL
GSAADFLLDI SETDLSSLTA SIKAPSGRDE PCLLKRLPNN HIGISFIPRE VGEHLVSIKK
NGNHVANSPV SIMVVQSEIG DARRAKVYGR GLSEGRTFEM SDFIVDTRDA GYGGISLAVE
GPSKVDIQTE DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVKESIT
RTSRAPSVAT VGSICDLNLK IPEINSSDMS AHVTSPSGRV TEAEIVPMGK NSHCVRFVPQ
EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG PGLERGEAGV PAEFSIWTRE
AGAGGLSIAV EGPSKAEITF DDHKNGSCGV SYIAQEPGNY EVSIKFNDEH IPESPYLVPV
IAPSDDARRL TVMSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP
DKYAVRFIPH ENGVHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GTGLEGGTTG
IQSEFFINTT RAGPGTLSVT IEGPSKVKMD CQETPEGYKV MYTPMAPGNY LISVKYGGPN
HIVGSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKASS DASKVTSKGA
GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH GPTTPCEEVS MKHVGNQQYN VTYVVKERGD
YVLAVKWGEE HIPGSPFHVT VP


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CSB-EL008725RB Rabbit filamin B, beta (actin binding protein 278) (FLNB) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
CSB-EL008725HU Human filamin B, beta (actin binding protein 278) (FLNB) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL008725MO Mouse filamin B, beta (actin binding protein 278) (FLNB) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
orb81123 Filamin protein Ultra Pure Filamin having a molecular mass of 250 kDa. For research use only. 10
CSB-PA008725GA01HU Rabbit anti-human filamin B, beta (actin binding protein 278) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA008725GA01HU Rabbit anti-human filamin B, beta (actin binding protein 278) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-EL008724HU Human filamin A, alpha (actin binding protein 280) (FLNA) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL008724MO Mouse filamin A, alpha (actin binding protein 280) (FLNA) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL008726HU Human filamin C, gamma (actin binding protein 280) (FLNC) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL008726MO Mouse filamin C, gamma (actin binding protein 280) (FLNC) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
1107NF-V10256 Monoclonal Antibodies: Filamin; reactive species: Human, Mouse, Rat, Chicken; Clone: FLMN01 (same as PM6_317); Isotype: IgG1; Specificity: Filamin 0.5 ml
LF-MA10110 anti-Filamin A (4E10-1B2), Mouse monoclonal to Filamin A, Isotype IgG1, Host Mouse 100 ug
LF-MA41411 anti-Filamin , Mouse monoclonal to Filamin , Isotype IgG1, Host Mouse 50 ug
RPR-473 Recombinant Human Filamin Binding LIM Protein 1 2
pro-1473 Recombinant Human Filamin Binding LIM Protein 1 10
pro-1473 Recombinant Human Filamin Binding LIM Protein 1 100
E80514Ra ELISA Kit for Filamin Binding LIM Protein 1 (FBLIM1) 96T/Kit
201-11-1343 Rat Filamin Binding LIM Protein 1(FBLIM1)ELISA kit 96T
201-20-1992 FBLIM1{filamin binding LIM protein 1}rabbit.pAb 0.2ml
FBLN2 FBLIM1 Gene filamin binding LIM protein 1
201-11-1343 Rat Filamin Binding LIM Protein 1 (FBLIM1)ELISA kit 96T
FBLI1_MOUSE Mouse ELISA Kit FOR Filamin-binding LIM protein 1 96T
pro-1473 Recombinant Human Filamin Binding LIM Protein 1 2
UB-E10302 Rat Filamin Binding LIM Protein 1(FBLIM1)ELISA kit 96T


 

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