FLNB_HUMAN
ID FLNB_HUMAN Reviewed; 2602 AA.
AC O75369; B2ZZ83; B2ZZ84; B2ZZ85; C9JKE6; C9JMC4; Q13706; Q59EC2; Q60FE7;
AC Q6MZJ1; Q8WXS9; Q8WXT0; Q8WXT1; Q8WXT2; Q8WXT3; Q9NRB5; Q9NT26; Q9UEV9;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=Filamin-B;
DE Short=FLN-B;
DE AltName: Full=ABP-278;
DE AltName: Full=ABP-280 homolog;
DE AltName: Full=Actin-binding-like protein;
DE AltName: Full=Beta-filamin;
DE AltName: Full=Filamin homolog 1;
DE Short=Fh1;
DE AltName: Full=Filamin-3;
DE AltName: Full=Thyroid autoantigen;
DE AltName: Full=Truncated actin-binding protein;
DE Short=Truncated ABP;
GN Name=FLNB; Synonyms=FLN1L, FLN3, TABP, TAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INTERACTION WITH GP1BA, AND VARIANTS ASN-1157 AND MET-1471.
RC TISSUE=Endothelial cell, and Placenta;
RX PubMed=9651345; DOI=10.1074/jbc.273.28.17531;
RA Takafuta T., Wu G., Murphy G.F., Shapiro S.S.;
RT "Human beta-filamin is a new protein that interacts with the cytoplasmic
RT tail of glycoprotein Ibalpha.";
RL J. Biol. Chem. 273:17531-17538(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND INTERACTION WITH GP1BA.
RC TISSUE=Placenta;
RX PubMed=9694715;
RA Xu W.-F., Xie Z.-W., Chung D.W., Davie E.W.;
RT "A novel human actin-binding protein homologue that binds to platelet
RT glycoprotein Ibalpha.";
RL Blood 92:1268-1276(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4 AND 5), TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH ISOFORMS OF ITGB1.
RC TISSUE=Keratinocyte, and Skeletal muscle;
RX PubMed=11807098; DOI=10.1083/jcb.200103037;
RA van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T.,
RA Shapiro S.S., Sonnenberg A.;
RT "Different splice variants of filamin-B affect myogenesis, subcellular
RT distribution, and determine binding to integrin (beta) subunits.";
RL J. Cell Biol. 156:361-376(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), GENE ORGANIZATION,
RP SIMILARITY TO OTHER MEMBERS OF THE FAMILY, AND VARIANTS ASN-1157 AND
RP MET-1471.
RX PubMed=11153914; DOI=10.1007/s004390000414;
RA Chakarova C., Wehnert M.S., Uhl K., Sakthivel S., Vosberg H.-P.,
RA van der Ven P.F.M., Fuerst D.O.;
RT "Genomic structure and fine mapping of the two human filamin gene
RT paralogues FLNB and FLNC and comparative analysis of the filamin gene
RT family.";
RL Hum. Genet. 107:597-611(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 8 AND 9), AND VARIANTS ASN-1157
RP AND MET-1471.
RX PubMed=18487259; DOI=10.1093/dnares/dsn010;
RA Oshikawa M., Sugai Y., Usami R., Ohtoko K., Toyama S., Kato S.;
RT "Fine expression profiling of full-length transcripts using a size-unbiased
RT cDNA library prepared with the vector-capping method.";
RL DNA Res. 15:123-136(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 8 AND 9).
RX PubMed=16106752; DOI=10.1093/dnares/12.1.53;
RA Kato S., Ohtoko K., Ohtake H., Kimura T.;
RT "Vector-capping: a simple method for preparing a high-quality full-length
RT cDNA library.";
RL DNA Res. 12:53-62(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Endometrial tumor, and Fetal brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 990-2602.
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2130-2602, AND INTERACTION WITH INPPL1.
RC TISSUE=Skeletal muscle;
RX PubMed=11739414; DOI=10.1083/jcb.200104005;
RA Dyson J.M., O'Malley C.J., Becanovic J., Munday A.D., Berndt M.C.,
RA Coghill I.D., Nandurkar H.H., Ooms L.M., Mitchell C.A.;
RT "The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds
RT filamin and regulates submembraneous actin.";
RL J. Cell Biol. 155:1065-1079(2001).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1874-2602.
RC TISSUE=Fetal brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2311-2602, AND INTERACTION WITH PSEN1 AND
RP PSEN2.
RC TISSUE=Fetal brain;
RX PubMed=9437013; DOI=10.1523/jneurosci.18-03-00914.1998;
RA Zhang W., Han S.W., McKeel D.W., Goate A., Wu J.Y.;
RT "Interaction of presenilins with the filamin family of actin-binding
RT proteins.";
RL J. Neurosci. 18:914-922(1998).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2404-2602, AND TISSUE SPECIFICITY.
RC TISSUE=Thyroid;
RX PubMed=8327473; DOI=10.1073/pnas.90.13.5994;
RA Leedman P.J., Faulkner-Jones B., Cram D.C., Harrison P.J., West J.,
RA O'Brien E.J., Simpson R., Coppel R.L., Harrison L.C.;
RT "Cloning from the thyroid of a protein related to actin binding protein
RT that is recognized by Graves disease immunoglobulins.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5994-5998(1993).
RN [14]
RP INTERACTION WITH HBV CAPSID PROTEIN.
RX PubMed=10754391; DOI=10.1159/000025442;
RA Huang C.J., Chen Y.H., Ting L.P.;
RT "Hepatitis B virus core protein interacts with the C-terminal region of
RT actin-binding protein.";
RL J. Biomed. Sci. 7:160-168(2000).
RN [15]
RP INTERACTION WITH FLNA.
RX PubMed=12393796; DOI=10.1093/hmg/11.23.2845;
RA Sheen V.L., Feng Y., Graham D., Takafuta T., Shapiro S.S., Walsh C.A.;
RT "Filamin A and filamin B are co-expressed within neurons during periods of
RT neuronal migration and can physically interact.";
RL Hum. Mol. Genet. 11:2845-2854(2002).
RN [16]
RP INTERACTION WITH FBLP1.
RC TISSUE=Placenta;
RX PubMed=12496242; DOI=10.1074/jbc.m209339200;
RA Takafuta T., Saeki M., Fujimoto T.-T., Fujimura K., Shapiro S.S.;
RT "A new member of the LIM protein family binds to filamin B and localizes at
RT stress fibers.";
RL J. Biol. Chem. 278:12175-12181(2003).
RN [17]
RP DIMERIZATION, AND INTERACTION WITH FLNC.
RX PubMed=12525170; DOI=10.1021/bi026501+;
RA Himmel M., van der Ven P.F.M., Stoecklein W., Fuerst D.O.;
RT "The limits of promiscuity: isoform-specific dimerization of filamins.";
RL Biochemistry 42:430-439(2003).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [19]
RP INTERACTION WITH ITGB1; MYOT AND MYOZ1.
RX PubMed=16076904; DOI=10.1242/jcs.02484;
RA Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A.,
RA Carpen O., Faulkner G., Borradori L.;
RT "The Z-disc proteins myotilin and FATZ-1 interact with each other and are
RT connected to the sarcolemma via muscle-specific filamins.";
RL J. Cell Sci. 118:3739-3749(2005).
RN [20]
RP REVIEW.
RX PubMed=11336782; DOI=10.1016/s0167-4889(01)00072-6;
RA van der Flier A., Sonnenberg A.;
RT "Structural and functional aspects of filamins.";
RL Biochim. Biophys. Acta 1538:99-117(2001).
RN [21]
RP REVIEW.
RX PubMed=11252955; DOI=10.1038/35052082;
RA Stossel T.P., Condeelis J., Cooley L., Hartwig J.H., Noegel A.,
RA Schleicher M., Shapiro S.S.;
RT "Filamins as integrators of cell mechanics and signalling.";
RL Nat. Rev. Mol. Cell Biol. 2:138-145(2001).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519; SER-983; SER-1028;
RP SER-1316; SER-1505; SER-1602; SER-2083; SER-2107; SER-2478 AND SER-2481,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
RP UBIQUITINATION.
RX PubMed=19300455; DOI=10.1038/cdd.2009.27;
RA Bello N.F., Lamsoul I., Heuze M.L., Metais A., Moreaux G., Calderwood D.A.,
RA Duprez D., Moog-Lutz C., Lutz P.G.;
RT "The E3 ubiquitin ligase specificity subunit ASB2beta is a novel regulator
RT of muscle differentiation that targets filamin B to proteasomal
RT degradation.";
RL Cell Death Differ. 16:921-932(2009).
RN [26]
RP ISGYLATION AT LYS-2468, AND MUTAGENESIS OF LYS-2468.
RX PubMed=19270716; DOI=10.1038/embor.2009.23;
RA Jeon Y.J., Choi J.S., Lee J.Y., Yu K.R., Kim S.M., Ka S.H., Oh K.H.,
RA Kim K.I., Zhang D.E., Bang O.S., Chung C.H.;
RT "ISG15 modification of filamin B negatively regulates the type I
RT interferon-induced JNK signalling pathway.";
RL EMBO Rep. 10:374-380(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 AND SER-2478, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-681 AND LYS-2576, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519; SER-730; SER-886;
RP SER-932; SER-983; SER-1316; SER-1433; SER-2369; SER-2465 AND SER-2478, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983; SER-1433; SER-1505;
RP SER-2083; SER-2107; SER-2465; SER-2478 AND SER-2481, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216; THR-1307; SER-1316;
RP SER-2107; SER-2113 AND SER-2492, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-1474 (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-242.
RX PubMed=19505475; DOI=10.1016/j.jmb.2009.06.009;
RA Sawyer G.M., Clark A.R., Robertson S.P., Sutherland-Smith A.J.;
RT "Disease-associated substitutions in the filamin B actin binding domain
RT confer enhanced actin binding affinity in the absence of major structural
RT disturbance: Insights from the crystal structures of filamin B actin
RT binding domains.";
RL J. Mol. Biol. 390:1030-1047(2009).
RN [36]
RP STRUCTURE BY NMR OF 1017-1721; 1736-2488 AND 2509-2602.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 9th through 24th filamin domains from human
RT filamin-B.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [37]
RP INVOLVEMENT IN SCT, VARIANTS LRS CYS-161; LYS-227; ASN-1571 DEL; ARG-1586
RP AND SER-1691, VARIANTS AO1 VAL-173 AND PRO-188, VARIANT AO3 ARG-751, AND
RP VARIANT AO1/AO3 VAL-202.
RX PubMed=14991055; DOI=10.1038/ng1319;
RA Krakow D., Robertson S.P., King L.M., Morgan T., Sebald E.T.,
RA Bertolotto C., Wachsmann-Hogiu S., Acuna D., Shapiro S.S., Takafuta T.,
RA Aftimos S., Kim C.A., Firth H., Steiner C.E., Cormier-Daire V.,
RA Superti-Furga A., Bonafe L., Graham J.M. Jr., Grix A., Bacino C.A.,
RA Allanson J., Bialer M.G., Lachman R.S., Rimoin D.L., Cohn D.H.;
RT "Mutations in the gene encoding filamin B disrupt vertebral segmentation,
RT joint formation and skeletogenesis.";
RL Nat. Genet. 36:405-410(2004).
RN [38]
RP STRUCTURE BY NMR OF 1017-2602.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of filamin domains from human filamin-B.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [39]
RP VARIANTS BOOMD ARG-171 AND PRO-235.
RX PubMed=15994868; DOI=10.1136/jmg.2004.029967;
RA Bicknell L.S., Morgan T., Bonafe L., Wessels M.W., Bialer M.G.,
RA Willems P.J., Cohn D.H., Krakow D., Robertson S.P.;
RT "Mutations in FLNB cause boomerang dysplasia.";
RL J. Med. Genet. 42:E43-E43(2005).
RN [40]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-566; LYS-663; LYS-703 AND GLY-1534.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [41]
RP VARIANTS LRS CYS-161; SER-168; LYS-227; VAL-234; SER-361; GLU-363;
RP ARG-1431; ASN-1571 DEL; ARG-1586; ASP-1592; LEU-1603; SER-1691 AND
RP ARG-1834.
RX PubMed=16801345; DOI=10.1136/jmg.2006.043687;
RA Bicknell L.S., Farrington-Rock C., Shafeghati Y., Rump P., Alanay Y.,
RA Alembik Y., Al-Madani N., Firth H., Karimi-Nejad M.H., Kim C.A., Leask K.,
RA Maisenbacher M., Moran E., Pappas J.G., Prontera P., de Ravel T.,
RA Fryns J.-P., Sweeney E., Fryer A., Unger S., Wilson L.C., Lachman R.S.,
RA Rimoin D.L., Cohn D.H., Krakow D., Robertson S.P.;
RT "A molecular and clinical study of Larsen syndrome caused by mutations in
RT FLNB.";
RL J. Med. Genet. 44:89-98(2007).
CC -!- FUNCTION: Connects cell membrane constituents to the actin
CC cytoskeleton. May promote orthogonal branching of actin filaments and
CC links actin filaments to membrane glycoproteins. Anchors various
CC transmembrane proteins to the actin cytoskeleton. Interaction with FLNA
CC may allow neuroblast migration from the ventricular zone into the
CC cortical plate. Various interactions and localizations of isoforms
CC affect myotube morphology and myogenesis. Isoform 6 accelerates muscle
CC differentiation in vitro.
CC -!- SUBUNIT: Homodimer. Interacts with MICALL2 (By similarity). Interacts
CC with RFLNA and RFLNB (By similarity). Isoform 1 interacts with FBLP1,
CC FLNA, FLNC, GP1BA, INPPL1, ITGB1A, PSEN1 and PSEN2. Isoform 3 interacts
CC with ITGB1A, ITGB1D, ITGB3 and ITGB6. Interacts with MYOT and MYOZ1.
CC Interacts with HBV capsid protein. Interacts with ASB2 isoform 1; the
CC interaction targets FLNB for proteasomal degradation (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q80X90,
CC ECO:0000269|PubMed:10754391, ECO:0000269|PubMed:11739414,
CC ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:12393796,
CC ECO:0000269|PubMed:12496242, ECO:0000269|PubMed:12525170,
CC ECO:0000269|PubMed:16076904, ECO:0000269|PubMed:9437013,
CC ECO:0000269|PubMed:9651345, ECO:0000269|PubMed:9694715}.
CC -!- INTERACTION:
CC O75369; P21333: FLNA; NbExp=5; IntAct=EBI-352089, EBI-350432;
CC O75369; O75369: FLNB; NbExp=4; IntAct=EBI-352089, EBI-352089;
CC O75369; P62993: GRB2; NbExp=2; IntAct=EBI-352089, EBI-401755;
CC O75369; P05161: ISG15; NbExp=4; IntAct=EBI-352089, EBI-746466;
CC O75369; Q13233: MAP3K1; NbExp=2; IntAct=EBI-352089, EBI-49776;
CC O75369; Q9Y6R4: MAP3K4; NbExp=2; IntAct=EBI-352089, EBI-448104;
CC O75369; P16333: NCK1; NbExp=3; IntAct=EBI-352089, EBI-389883;
CC O75369; P63000: RAC1; NbExp=2; IntAct=EBI-352089, EBI-413628;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cell cortex. Cytoplasm,
CC cytoskeleton. Cytoplasm, cytoskeleton, stress fiber. Cytoplasm,
CC myofibril, sarcomere, Z line. Note=In differentiating myotubes, isoform
CC 1, isoform 2 and isoform 3 are localized diffusely throughout the
CC cytoplasm with regions of enrichment at the longitudinal actin stress
CC fiber. In differentiated tubes, isoform 1 is also detected within the
CC Z-lines.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton, stress
CC fiber.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytoskeleton, stress
CC fiber.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytoskeleton.
CC Note=Polarized at the periphery of myotubes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=ABP-278;
CC IsoId=O75369-1; Sequence=Displayed;
CC Name=2; Synonyms=ABP-276;
CC IsoId=O75369-2; Sequence=VSP_008773;
CC Name=3; Synonyms=Var-1;
CC IsoId=O75369-3; Sequence=VSP_008774;
CC Name=7;
CC IsoId=O75369-7; Sequence=VSP_024113, VSP_024114, VSP_024115;
CC Name=4; Synonyms=Var-3;
CC IsoId=O75369-4; Sequence=VSP_008775, VSP_008776;
CC Name=5; Synonyms=Var-2;
CC IsoId=O75369-5; Sequence=VSP_008777, VSP_008778;
CC Name=6; Synonyms=Var-1-DeltaH1;
CC IsoId=O75369-6; Sequence=VSP_008773, VSP_008774;
CC Name=8;
CC IsoId=O75369-8; Sequence=VSP_043446;
CC Name=9;
CC IsoId=O75369-9; Sequence=VSP_024115;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Isoform 1 and isoform 2 are expressed
CC in placenta, bone marrow, brain, umbilical vein endothelial cells
CC (HUVEC), retina and skeletal muscle. Isoform 1 is predominantly
CC expressed in prostate, uterus, liver, thyroid, stomach, lymph node,
CC small intestine, spleen, skeletal muscle, kidney, placenta, pancreas,
CC heart, lung, platelets, endothelial cells, megakaryocytic and
CC erythroleukemic cell lines. Isoform 2 is predominantly expressed in
CC spinal cord, platelet and Daudi cells. Also expressed in thyroid
CC adenoma, neurofibrillary tangles (NFT), senile plaques in the
CC hippocampus and cerebral cortex in Alzheimer disease (AD). Isoform 3
CC and isoform 6 are expressed predominantly in lung, heart, skeletal
CC muscle, testis, spleen, thymus and leukocytes. Isoform 4 and isoform 5
CC are expressed in heart. {ECO:0000269|PubMed:11807098,
CC ECO:0000269|PubMed:8327473, ECO:0000269|PubMed:9651345,
CC ECO:0000269|PubMed:9694715}.
CC -!- DOMAIN: Comprised of a NH2-terminal actin-binding domain, 24 internally
CC homologous repeats and two hinge regions. Repeat 24 and the second
CC hinge domain are important for dimer formation. The first hinge region
CC prevents binding to ITGA and ITGB subunits.
CC -!- PTM: ISGylation prevents ability to interact with the upstream
CC activators of the JNK cascade and inhibits IFNA-induced JNK signaling.
CC {ECO:0000269|PubMed:19270716}.
CC -!- PTM: Ubiquitination by a SCF-like complex containing ASB2 isoform 1
CC leads to proteasomal degradation which promotes muscle differentiation.
CC {ECO:0000269|PubMed:19300455}.
CC -!- DISEASE: Note=Interaction with FLNA may compensate for dysfunctional
CC FLNA homodimer in the periventricular nodular heterotopia (PVNH)
CC disorder.
CC -!- DISEASE: Atelosteogenesis 1 (AO1) [MIM:108720]: A lethal
CC chondrodysplasia characterized by distal hypoplasia of the humeri and
CC femurs, hypoplasia of the mid-thoracic spine, occasionally complete
CC lack of ossification of single hand bones, and the finding in cartilage
CC of multiple degenerated chondrocytes which are encapsulated in fibrous
CC tissue. {ECO:0000269|PubMed:14991055}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Atelosteogenesis 3 (AO3) [MIM:108721]: A short-limb lethal
CC skeletal dysplasia with vertebral abnormalities, disharmonious skeletal
CC maturation, poorly modeled long bones and joint dislocations. Recurrent
CC respiratory insufficiency and/or infections usually result in early
CC death. {ECO:0000269|PubMed:14991055}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Boomerang dysplasia (BOOMD) [MIM:112310]: A perinatal lethal
CC osteochondrodysplasia characterized by absence or underossification of
CC the limb bones and vertebrae. Patients manifest dwarfism with short,
CC bowed, rigid limbs and characteristic facies. Boomerang dysplasia is
CC distinguished from atelosteogenesis on the basis of a more severe
CC defect in mineralization, with complete absence of ossification in some
CC limb elements and vertebral segments. {ECO:0000269|PubMed:15994868}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Larsen syndrome (LRS) [MIM:150250]: An osteochondrodysplasia
CC characterized by large-joint dislocations and characteristic
CC craniofacial abnormalities. The cardinal features of the condition are
CC dislocations of the hip, knee and elbow joints, with equinovarus or
CC equinovalgus foot deformities. Spatula-shaped fingers, most marked in
CC the thumb, are also present. Craniofacial anomalies include
CC hypertelorism, prominence of the forehead, a depressed nasal bridge,
CC and a flattened midface. Cleft palate and short stature are often
CC associated features. Spinal anomalies include scoliosis and cervical
CC kyphosis. Hearing loss is a well-recognized complication.
CC {ECO:0000269|PubMed:14991055, ECO:0000269|PubMed:16801345}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Spondylocarpotarsal synostosis syndrome (SCT) [MIM:272460]:
CC Disorder characterized by short stature and vertebral, carpal and
CC tarsal fusions. {ECO:0000269|PubMed:14991055}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to exon skipping. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to exon skipping. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to competing donor splice sites.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: May be due to exon skipping. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35505.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; AF042166; AAC39842.1; -; mRNA.
DR EMBL; AF043045; AAC33845.1; -; mRNA.
DR EMBL; AF353666; AAL68439.1; -; mRNA.
DR EMBL; AF353667; AAL68440.1; -; Genomic_DNA.
DR EMBL; AF353667; AAL68441.1; -; Genomic_DNA.
DR EMBL; AF353667; AAL68442.1; -; Genomic_DNA.
DR EMBL; AF353667; AAL68443.1; -; Genomic_DNA.
DR EMBL; AF191633; AAF72339.1; -; Genomic_DNA.
DR EMBL; AF191594; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191595; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191596; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191597; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191598; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191599; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191600; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191601; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191602; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191603; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191604; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191605; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191606; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191607; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191608; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191609; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191611; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191610; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191613; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191612; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191614; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191615; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191617; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191616; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191618; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191619; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191620; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191621; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191622; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191623; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191624; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191625; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191627; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191626; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191628; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191629; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191630; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191631; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF191632; AAF72339.1; JOINED; Genomic_DNA.
DR EMBL; AF238609; AAF97046.1; -; mRNA.
DR EMBL; AB371580; BAG48309.1; -; mRNA.
DR EMBL; AB371581; BAG48310.1; -; mRNA.
DR EMBL; AB371582; BAG48311.1; -; mRNA.
DR EMBL; AB191258; BAD52434.1; -; mRNA.
DR EMBL; BX641085; CAE46040.1; -; mRNA.
DR EMBL; AC114399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137574; CAB70818.1; -; mRNA.
DR EMBL; AB209889; BAD93126.1; -; mRNA.
DR EMBL; M62994; AAA35505.1; ALT_FRAME; mRNA.
DR CCDS; CCDS2885.1; -. [O75369-1]
DR CCDS; CCDS54599.1; -. [O75369-8]
DR CCDS; CCDS54600.1; -. [O75369-9]
DR CCDS; CCDS54601.1; -. [O75369-2]
DR PIR; T46270; T46270.
DR RefSeq; NP_001157789.1; NM_001164317.1. [O75369-8]
DR RefSeq; NP_001157790.1; NM_001164318.1. [O75369-9]
DR RefSeq; NP_001157791.1; NM_001164319.1. [O75369-2]
DR RefSeq; NP_001448.2; NM_001457.3. [O75369-1]
DR PDB; 2DI8; NMR; -; A=1999-2096.
DR PDB; 2DI9; NMR; -; A=1017-1134.
DR PDB; 2DIA; NMR; -; A=1130-1229.
DR PDB; 2DIB; NMR; -; A=1215-1329.
DR PDB; 2DIC; NMR; -; A=1325-1422.
DR PDB; 2DJ4; NMR; -; A=1418-1518.
DR PDB; 2DLG; NMR; -; A=2104-2192.
DR PDB; 2DMB; NMR; -; A=1611-1721.
DR PDB; 2DMC; NMR; -; A=1899-2001.
DR PDB; 2E9I; NMR; -; A=2094-2192.
DR PDB; 2E9J; NMR; -; A=1504-1615.
DR PDB; 2EE6; NMR; -; A=2190-2287.
DR PDB; 2EE9; NMR; -; A=1736-1823.
DR PDB; 2EEA; NMR; -; A=1808-1915.
DR PDB; 2EEB; NMR; -; A=2284-2382.
DR PDB; 2EEC; NMR; -; A=2371-2488.
DR PDB; 2EED; NMR; -; A=2509-2602.
DR PDB; 2WA5; X-ray; 1.90 A; A=2-242.
DR PDB; 2WA6; X-ray; 1.95 A; A=2-242.
DR PDB; 2WA7; X-ray; 1.85 A; A=2-242.
DR PDB; 3FER; X-ray; 2.40 A; A/B/C/D=1-252.
DR PDB; 4B7L; X-ray; 2.05 A; A/B=1-347.
DR PDB; 5DCP; X-ray; 2.49 A; A/B=1737-1911.
DR PDBsum; 2DI8; -.
DR PDBsum; 2DI9; -.
DR PDBsum; 2DIA; -.
DR PDBsum; 2DIB; -.
DR PDBsum; 2DIC; -.
DR PDBsum; 2DJ4; -.
DR PDBsum; 2DLG; -.
DR PDBsum; 2DMB; -.
DR PDBsum; 2DMC; -.
DR PDBsum; 2E9I; -.
DR PDBsum; 2E9J; -.
DR PDBsum; 2EE6; -.
DR PDBsum; 2EE9; -.
DR PDBsum; 2EEA; -.
DR PDBsum; 2EEB; -.
DR PDBsum; 2EEC; -.
DR PDBsum; 2EED; -.
DR PDBsum; 2WA5; -.
DR PDBsum; 2WA6; -.
DR PDBsum; 2WA7; -.
DR PDBsum; 3FER; -.
DR PDBsum; 4B7L; -.
DR PDBsum; 5DCP; -.
DR AlphaFoldDB; O75369; -.
DR SMR; O75369; -.
DR BioGRID; 108606; 180.
DR IntAct; O75369; 73.
DR MINT; O75369; -.
DR STRING; 9606.ENSP00000420213; -.
DR ChEMBL; CHEMBL4295677; -.
DR TCDB; 8.A.66.1.5; the dystrophin (dystrophin) family.
DR CarbonylDB; O75369; -.
DR GlyConnect; 2041; 2 N-Linked glycans (1 site).
DR GlyGen; O75369; 5 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (4 sites).
DR iPTMnet; O75369; -.
DR MetOSite; O75369; -.
DR PhosphoSitePlus; O75369; -.
DR SwissPalm; O75369; -.
DR BioMuta; FLNB; -.
DR CPTAC; CPTAC-511; -.
DR EPD; O75369; -.
DR jPOST; O75369; -.
DR MassIVE; O75369; -.
DR MaxQB; O75369; -.
DR PaxDb; O75369; -.
DR PeptideAtlas; O75369; -.
DR PRIDE; O75369; -.
DR ProteomicsDB; 49938; -. [O75369-1]
DR ProteomicsDB; 49939; -. [O75369-2]
DR ProteomicsDB; 49940; -. [O75369-3]
DR ProteomicsDB; 49941; -. [O75369-4]
DR ProteomicsDB; 49942; -. [O75369-5]
DR ProteomicsDB; 49943; -. [O75369-6]
DR ProteomicsDB; 49944; -. [O75369-7]
DR ProteomicsDB; 49945; -. [O75369-8]
DR ProteomicsDB; 49946; -. [O75369-9]
DR ProteomicsDB; 75100; -.
DR ABCD; O75369; 2 sequenced antibodies.
DR Antibodypedia; 1496; 291 antibodies from 32 providers.
DR DNASU; 2317; -.
DR Ensembl; ENST00000295956.9; ENSP00000295956.5; ENSG00000136068.16. [O75369-1]
DR Ensembl; ENST00000358537.7; ENSP00000351339.3; ENSG00000136068.16. [O75369-2]
DR Ensembl; ENST00000429972.6; ENSP00000415599.2; ENSG00000136068.16. [O75369-9]
DR Ensembl; ENST00000490882.5; ENSP00000420213.1; ENSG00000136068.16. [O75369-8]
DR GeneID; 2317; -.
DR KEGG; hsa:2317; -.
DR MANE-Select; ENST00000295956.9; ENSP00000295956.5; NM_001457.4; NP_001448.2.
DR UCSC; uc003djj.3; human. [O75369-1]
DR CTD; 2317; -.
DR DisGeNET; 2317; -.
DR GeneCards; FLNB; -.
DR GeneReviews; FLNB; -.
DR HGNC; HGNC:3755; FLNB.
DR HPA; ENSG00000136068; Low tissue specificity.
DR MalaCards; FLNB; -.
DR MIM; 108720; phenotype.
DR MIM; 108721; phenotype.
DR MIM; 112310; phenotype.
DR MIM; 150250; phenotype.
DR MIM; 272460; phenotype.
DR MIM; 603381; gene.
DR neXtProt; NX_O75369; -.
DR OpenTargets; ENSG00000136068; -.
DR Orphanet; 1190; Atelosteogenesis type I.
DR Orphanet; 56305; Atelosteogenesis type III.
DR Orphanet; 1263; Boomerang dysplasia.
DR Orphanet; 503; Larsen syndrome.
DR Orphanet; 3275; Spondylocarpotarsal synostosis.
DR PharmGKB; PA28173; -.
DR VEuPathDB; HostDB:ENSG00000136068; -.
DR eggNOG; KOG0518; Eukaryota.
DR GeneTree; ENSGT00940000156286; -.
DR HOGENOM; CLU_000783_0_0_1; -.
DR InParanoid; O75369; -.
DR OMA; ITYGGVH; -.
DR OrthoDB; 35998at2759; -.
DR PhylomeDB; O75369; -.
DR TreeFam; TF313685; -.
DR PathwayCommons; O75369; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR SignaLink; O75369; -.
DR SIGNOR; O75369; -.
DR BioGRID-ORCS; 2317; 13 hits in 1074 CRISPR screens.
DR ChiTaRS; FLNB; human.
DR EvolutionaryTrace; O75369; -.
DR GeneWiki; FLNB; -.
DR GenomeRNAi; 2317; -.
DR Pharos; O75369; Tbio.
DR PRO; PR:O75369; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O75369; protein.
DR Bgee; ENSG00000136068; Expressed in mucosa of transverse colon and 199 other tissues.
DR ExpressionAtlas; O75369; baseline and differential.
DR Genevisible; O75369; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl.
DR GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR CDD; cd00014; CH; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.60.40.10; -; 24.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR044801; Filamin.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR029874; FLNB.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR38537; PTHR38537; 3.
DR PANTHER; PTHR38537:SF7; PTHR38537:SF7; 3.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00630; Filamin; 23.
DR SMART; SM00033; CH; 2.
DR SMART; SM00557; IG_FLMN; 24.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF81296; SSF81296; 24.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 24.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Disease variant;
KW Dwarfism; Isopeptide bond; Myogenesis; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN 1..2602
FT /note="Filamin-B"
FT /id="PRO_0000087298"
FT DOMAIN 16..122
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 139..242
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 249..347
FT /note="Filamin 1"
FT REPEAT 349..446
FT /note="Filamin 2"
FT REPEAT 447..543
FT /note="Filamin 3"
FT REPEAT 544..636
FT /note="Filamin 4"
FT REPEAT 640..736
FT /note="Filamin 5"
FT REPEAT 737..839
FT /note="Filamin 6"
FT REPEAT 840..938
FT /note="Filamin 7"
FT REPEAT 939..1034
FT /note="Filamin 8"
FT REPEAT 1035..1127
FT /note="Filamin 9"
FT REPEAT 1128..1222
FT /note="Filamin 10"
FT REPEAT 1223..1322
FT /note="Filamin 11"
FT REPEAT 1323..1415
FT /note="Filamin 12"
FT REPEAT 1416..1511
FT /note="Filamin 13"
FT REPEAT 1512..1608
FT /note="Filamin 14"
FT REPEAT 1609..1704
FT /note="Filamin 15"
FT REPEAT 1729..1813
FT /note="Filamin 16"
FT REPEAT 1816..1908
FT /note="Filamin 17"
FT REPEAT 1919..1994
FT /note="Filamin 18"
FT REPEAT 1997..2089
FT /note="Filamin 19"
FT REPEAT 2091..2185
FT /note="Filamin 20"
FT REPEAT 2188..2280
FT /note="Filamin 21"
FT REPEAT 2282..2375
FT /note="Filamin 22"
FT REPEAT 2379..2471
FT /note="Filamin 23"
FT REPEAT 2507..2601
FT /note="Filamin 24"
FT REGION 1..239
FT /note="Actin-binding"
FT REGION 244..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1511
FT /note="Interaction with FBLP1"
FT /evidence="ECO:0000269|PubMed:12496242"
FT REGION 1705..1728
FT /note="Hinge 1"
FT /evidence="ECO:0000250"
FT REGION 1862..2148
FT /note="Interaction with the cytoplasmic tail of GP1BA"
FT REGION 2060..2225
FT /note="Interaction with FLNA 1"
FT REGION 2130..2602
FT /note="Interaction with INPPL1"
FT /evidence="ECO:0000269|PubMed:11739414"
FT REGION 2472..2602
FT /note="Self-association site, tail"
FT /evidence="ECO:0000250"
FT REGION 2472..2506
FT /note="Hinge 2"
FT /evidence="ECO:0000250"
FT REGION 2507..2602
FT /note="Interaction with FLNA 2"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 519
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 681
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1307
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 1433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1780
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80X90"
FT MOD_RES 2083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2518
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80X90"
FT MOD_RES 2524
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80X90"
FT MOD_RES 2576
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 2468
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000269|PubMed:19270716"
FT VAR_SEQ 1..169
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_024113"
FT VAR_SEQ 170..181
FT /note="ALGALVDSCAPG -> MQEHSTRRRSLS (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_024114"
FT VAR_SEQ 1463
FT /note="R -> RADDTDSQSWRSPLKALSEFFKGDPKGDFNKT (in isoform
FT 8)"
FT /evidence="ECO:0000303|PubMed:16106752,
FT ECO:0000303|PubMed:18487259"
FT /id="VSP_043446"
FT VAR_SEQ 1704..1727
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16106752,
FT ECO:0000303|PubMed:18487259, ECO:0000303|PubMed:9694715"
FT /id="VSP_008773"
FT VAR_SEQ 1717..1727
FT /note="Missing (in isoform 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:16106752,
FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:18487259"
FT /id="VSP_024115"
FT VAR_SEQ 2081..2121
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_008774"
FT VAR_SEQ 2123..2150
FT /note="EINSSDMSAHVTSPSGRVTEAEIVPMGK -> GVRVMNCSAQILWGWRVQFH
FT TGSRNQQQ (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_008775"
FT VAR_SEQ 2123..2146
FT /note="EINSSDMSAHVTSPSGRVTEAEIV -> GVRVMNCSAQILWGWRVQFHTGSR
FT (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_008777"
FT VAR_SEQ 2147..2602
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_008778"
FT VAR_SEQ 2151..2602
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_008776"
FT VARIANT 161
FT /note="F -> C (in LRS; dbSNP:rs80356506)"
FT /evidence="ECO:0000269|PubMed:14991055,
FT ECO:0000269|PubMed:16801345"
FT /id="VAR_033069"
FT VARIANT 168
FT /note="G -> S (in LRS; dbSNP:rs80356504)"
FT /evidence="ECO:0000269|PubMed:16801345"
FT /id="VAR_033070"
FT VARIANT 171
FT /note="L -> R (in BOOMD; dbSNP:rs80356494)"
FT /evidence="ECO:0000269|PubMed:15994868"
FT /id="VAR_033071"
FT VARIANT 173
FT /note="A -> V (in AO1; dbSNP:rs121908894)"
FT /evidence="ECO:0000269|PubMed:14991055"
FT /id="VAR_033072"
FT VARIANT 188
FT /note="S -> P (in AO1)"
FT /evidence="ECO:0000269|PubMed:14991055"
FT /id="VAR_033073"
FT VARIANT 202
FT /note="M -> V (in AO1 and AO3; dbSNP:rs121908895)"
FT /evidence="ECO:0000269|PubMed:14991055"
FT /id="VAR_033074"
FT VARIANT 227
FT /note="E -> K (in LRS; dbSNP:rs80356508)"
FT /evidence="ECO:0000269|PubMed:14991055,
FT ECO:0000269|PubMed:16801345"
FT /id="VAR_033075"
FT VARIANT 234
FT /note="L -> V (in LRS; dbSNP:rs80356507)"
FT /evidence="ECO:0000269|PubMed:16801345"
FT /id="VAR_033076"
FT VARIANT 235
FT /note="S -> P (in BOOMD; dbSNP:rs121908896)"
FT /evidence="ECO:0000269|PubMed:15994868"
FT /id="VAR_033077"
FT VARIANT 361
FT /note="G -> S (in LRS; dbSNP:rs80356509)"
FT /evidence="ECO:0000269|PubMed:16801345"
FT /id="VAR_033078"
FT VARIANT 363
FT /note="G -> E (in LRS; dbSNP:rs80356510)"
FT /evidence="ECO:0000269|PubMed:16801345"
FT /id="VAR_033079"
FT VARIANT 566
FT /note="R -> Q (in a breast cancer sample; somatic mutation;
FT dbSNP:rs150747960)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035917"
FT VARIANT 663
FT /note="N -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035918"
FT VARIANT 703
FT /note="T -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035919"
FT VARIANT 751
FT /note="G -> R (in AO3; dbSNP:rs28937587)"
FT /evidence="ECO:0000269|PubMed:14991055"
FT /id="VAR_033080"
FT VARIANT 1018
FT /note="V -> M (in dbSNP:rs2276742)"
FT /id="VAR_017182"
FT VARIANT 1157
FT /note="D -> N (in dbSNP:rs1131356)"
FT /evidence="ECO:0000269|PubMed:11153914,
FT ECO:0000269|PubMed:18487259, ECO:0000269|PubMed:9651345"
FT /id="VAR_017183"
FT VARIANT 1179
FT /note="E -> K (in dbSNP:rs17058845)"
FT /id="VAR_031392"
FT VARIANT 1431
FT /note="L -> R (in LRS; dbSNP:rs80356511)"
FT /evidence="ECO:0000269|PubMed:16801345"
FT /id="VAR_033081"
FT VARIANT 1471
FT /note="V -> M (in dbSNP:rs12632456)"
FT /evidence="ECO:0000269|PubMed:11153914,
FT ECO:0000269|PubMed:18487259, ECO:0000269|PubMed:9651345"
FT /id="VAR_031393"
FT VARIANT 1534
FT /note="A -> G (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035920"
FT VARIANT 1571
FT /note="Missing (in LRS; dbSNP:rs80356512)"
FT /evidence="ECO:0000269|PubMed:14991055,
FT ECO:0000269|PubMed:16801345"
FT /id="VAR_033082"
FT VARIANT 1586
FT /note="G -> R (in LRS; dbSNP:rs80356513)"
FT /evidence="ECO:0000269|PubMed:14991055,
FT ECO:0000269|PubMed:16801345"
FT /id="VAR_033083"
FT VARIANT 1592
FT /note="V -> D (in LRS; dbSNP:rs80356514)"
FT /evidence="ECO:0000269|PubMed:16801345"
FT /id="VAR_033084"
FT VARIANT 1603
FT /note="P -> L (in LRS; dbSNP:rs80356515)"
FT /evidence="ECO:0000269|PubMed:16801345"
FT /id="VAR_033085"
FT VARIANT 1691
FT /note="G -> S (in LRS; dbSNP:rs80356503)"
FT /evidence="ECO:0000269|PubMed:14991055,
FT ECO:0000269|PubMed:16801345"
FT /id="VAR_033086"
FT VARIANT 1834
FT /note="G -> R (in LRS; dbSNP:rs80356516)"
FT /evidence="ECO:0000269|PubMed:16801345"
FT /id="VAR_033087"
FT MUTAGEN 2468
FT /note="K->R: Cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:19270716"
FT CONFLICT 816
FT /note="A -> T (in Ref. 7; CAE46040)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="Y -> H (in Ref. 7; CAE46040)"
FT /evidence="ECO:0000305"
FT CONFLICT 1411
FT /note="F -> L (in Ref. 7; CAE46040)"
FT /evidence="ECO:0000305"
FT CONFLICT 1560
FT /note="E -> G (in Ref. 7; CAE46040)"
FT /evidence="ECO:0000305"
FT CONFLICT 1953
FT /note="L -> F (in Ref. 4; AAF97046)"
FT /evidence="ECO:0000305"
FT CONFLICT 2006
FT /note="K -> R (in Ref. 2; AAC33845)"
FT /evidence="ECO:0000305"
FT CONFLICT 2099
FT /note="I -> S (in Ref. 7; CAE46040)"
FT /evidence="ECO:0000305"
FT CONFLICT 2170
FT /note="K -> N (in Ref. 4; AAF97046)"
FT /evidence="ECO:0000305"
FT CONFLICT 2293
FT /note="M -> V (in Ref. 4; AAF97046 and 7; CAE46040)"
FT /evidence="ECO:0000305"
FT CONFLICT 2354
FT /note="V -> A (in Ref. 11; CAB70818)"
FT /evidence="ECO:0000305"
FT CONFLICT 2487
FT /note="S -> C (in Ref. 13; AAA35505)"
FT /evidence="ECO:0000305"
FT CONFLICT 2571
FT /note="V -> A (in Ref. 11; CAB70818)"
FT /evidence="ECO:0000305"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:2WA5"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2WA7"
FT TURN 40..46
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:2WA7"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:4B7L"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:4B7L"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4B7L"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:4B7L"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:4B7L"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:4B7L"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:4B7L"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4B7L"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:4B7L"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:4B7L"
FT STRAND 323..333
FT /evidence="ECO:0007829|PDB:4B7L"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:4B7L"
FT HELIX 1040..1042
FT /evidence="ECO:0007829|PDB:2DI9"
FT STRAND 1044..1047
FT /evidence="ECO:0007829|PDB:2DI9"
FT HELIX 1048..1051
FT /evidence="ECO:0007829|PDB:2DI9"
FT STRAND 1052..1054
FT /evidence="ECO:0007829|PDB:2DI9"
FT STRAND 1059..1064
FT /evidence="ECO:0007829|PDB:2DI9"
FT TURN 1066..1068
FT /evidence="ECO:0007829|PDB:2DI9"
FT STRAND 1073..1077
FT /evidence="ECO:0007829|PDB:2DI9"
FT STRAND 1079..1081
FT /evidence="ECO:0007829|PDB:2DI9"
FT STRAND 1084..1089
FT /evidence="ECO:0007829|PDB:2DI9"
FT STRAND 1091..1100
FT /evidence="ECO:0007829|PDB:2DI9"
FT STRAND 1102..1115
FT /evidence="ECO:0007829|PDB:2DI9"
FT STRAND 1122..1128
FT /evidence="ECO:0007829|PDB:2DI9"
FT HELIX 1133..1135
FT /evidence="ECO:0007829|PDB:2DIA"
FT STRAND 1136..1140
FT /evidence="ECO:0007829|PDB:2DIA"
FT HELIX 1141..1143
FT /evidence="ECO:0007829|PDB:2DIA"
FT STRAND 1154..1160
FT /evidence="ECO:0007829|PDB:2DIA"
FT STRAND 1166..1172
FT /evidence="ECO:0007829|PDB:2DIA"
FT TURN 1173..1175
FT /evidence="ECO:0007829|PDB:2DIA"
FT STRAND 1179..1184
FT /evidence="ECO:0007829|PDB:2DIA"
FT STRAND 1188..1195
FT /evidence="ECO:0007829|PDB:2DIA"
FT STRAND 1200..1208
FT /evidence="ECO:0007829|PDB:2DIA"
FT STRAND 1217..1223
FT /evidence="ECO:0007829|PDB:2DIA"
FT STRAND 1232..1235
FT /evidence="ECO:0007829|PDB:2DIB"
FT HELIX 1236..1239
FT /evidence="ECO:0007829|PDB:2DIB"
FT STRAND 1249..1254
FT /evidence="ECO:0007829|PDB:2DIB"
FT STRAND 1256..1258
FT /evidence="ECO:0007829|PDB:2DIB"
FT STRAND 1273..1275
FT /evidence="ECO:0007829|PDB:2DIB"
FT STRAND 1281..1284
FT /evidence="ECO:0007829|PDB:2DIB"
FT STRAND 1286..1294
FT /evidence="ECO:0007829|PDB:2DIB"
FT STRAND 1300..1310
FT /evidence="ECO:0007829|PDB:2DIB"
FT STRAND 1317..1321
FT /evidence="ECO:0007829|PDB:2DIB"
FT STRAND 1332..1335
FT /evidence="ECO:0007829|PDB:2DIC"
FT HELIX 1336..1339
FT /evidence="ECO:0007829|PDB:2DIC"
FT STRAND 1347..1352
FT /evidence="ECO:0007829|PDB:2DIC"
FT TURN 1354..1356
FT /evidence="ECO:0007829|PDB:2DIC"
FT STRAND 1361..1369
FT /evidence="ECO:0007829|PDB:2DIC"
FT STRAND 1374..1377
FT /evidence="ECO:0007829|PDB:2DIC"
FT STRAND 1379..1381
FT /evidence="ECO:0007829|PDB:2DIC"
FT STRAND 1383..1387
FT /evidence="ECO:0007829|PDB:2DIC"
FT STRAND 1393..1401
FT /evidence="ECO:0007829|PDB:2DIC"
FT STRAND 1410..1416
FT /evidence="ECO:0007829|PDB:2DIC"
FT STRAND 1425..1428
FT /evidence="ECO:0007829|PDB:2DJ4"
FT TURN 1429..1431
FT /evidence="ECO:0007829|PDB:2DJ4"
FT STRAND 1441..1446
FT /evidence="ECO:0007829|PDB:2DJ4"
FT TURN 1448..1450
FT /evidence="ECO:0007829|PDB:2DJ4"
FT STRAND 1455..1460
FT /evidence="ECO:0007829|PDB:2DJ4"
FT STRAND 1462..1464
FT /evidence="ECO:0007829|PDB:2DJ4"
FT STRAND 1475..1483
FT /evidence="ECO:0007829|PDB:2DJ4"
FT STRAND 1489..1501
FT /evidence="ECO:0007829|PDB:2DJ4"
FT STRAND 1506..1512
FT /evidence="ECO:0007829|PDB:2DJ4"
FT HELIX 1517..1519
FT /evidence="ECO:0007829|PDB:2E9J"
FT STRAND 1520..1524
FT /evidence="ECO:0007829|PDB:2E9J"
FT HELIX 1525..1527
FT /evidence="ECO:0007829|PDB:2E9J"
FT STRAND 1538..1546
FT /evidence="ECO:0007829|PDB:2E9J"
FT STRAND 1566..1570
FT /evidence="ECO:0007829|PDB:2E9J"
FT STRAND 1573..1580
FT /evidence="ECO:0007829|PDB:2E9J"
FT STRAND 1586..1590
FT /evidence="ECO:0007829|PDB:2E9J"
FT STRAND 1593..1596
FT /evidence="ECO:0007829|PDB:2E9J"
FT STRAND 1603..1609
FT /evidence="ECO:0007829|PDB:2E9J"
FT STRAND 1618..1621
FT /evidence="ECO:0007829|PDB:2DMB"
FT HELIX 1622..1624
FT /evidence="ECO:0007829|PDB:2DMB"
FT STRAND 1625..1639
FT /evidence="ECO:0007829|PDB:2DMB"
FT STRAND 1641..1643
FT /evidence="ECO:0007829|PDB:2DMB"
FT STRAND 1648..1653
FT /evidence="ECO:0007829|PDB:2DMB"
FT STRAND 1663..1666
FT /evidence="ECO:0007829|PDB:2DMB"
FT STRAND 1672..1677
FT /evidence="ECO:0007829|PDB:2DMB"
FT STRAND 1682..1692
FT /evidence="ECO:0007829|PDB:2DMB"
FT STRAND 1699..1705
FT /evidence="ECO:0007829|PDB:2DMB"
FT STRAND 1747..1751
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1760..1765
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1775..1779
FT /evidence="ECO:0007829|PDB:5DCP"
FT TURN 1780..1782
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1783..1788
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1794..1802
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1811..1816
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1825..1828
FT /evidence="ECO:0007829|PDB:5DCP"
FT HELIX 1829..1831
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1833..1835
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1840..1845
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1855..1863
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1868..1870
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1872..1880
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1886..1898
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1903..1909
FT /evidence="ECO:0007829|PDB:5DCP"
FT STRAND 1924..1927
FT /evidence="ECO:0007829|PDB:2DMC"
FT STRAND 1941..1943
FT /evidence="ECO:0007829|PDB:2DMC"
FT STRAND 1952..1957
FT /evidence="ECO:0007829|PDB:2DMC"
FT TURN 1958..1960
FT /evidence="ECO:0007829|PDB:2DMC"
FT STRAND 1961..1966
FT /evidence="ECO:0007829|PDB:2DMC"
FT STRAND 1972..1977
FT /evidence="ECO:0007829|PDB:2DMC"
FT STRAND 1979..1984
FT /evidence="ECO:0007829|PDB:2DMC"
FT STRAND 1989..1994
FT /evidence="ECO:0007829|PDB:2DMC"
FT STRAND 1997..1999
FT /evidence="ECO:0007829|PDB:2DMC"
FT HELIX 2002..2004
FT /evidence="ECO:0007829|PDB:2DI8"
FT STRAND 2006..2010
FT /evidence="ECO:0007829|PDB:2DI8"
FT TURN 2011..2013
FT /evidence="ECO:0007829|PDB:2DI8"
FT STRAND 2014..2016
FT /evidence="ECO:0007829|PDB:2DI8"
FT STRAND 2021..2026
FT /evidence="ECO:0007829|PDB:2DI8"
FT TURN 2028..2030
FT /evidence="ECO:0007829|PDB:2DI8"
FT STRAND 2035..2043
FT /evidence="ECO:0007829|PDB:2DI8"
FT STRAND 2057..2061
FT /evidence="ECO:0007829|PDB:2DI8"
FT STRAND 2067..2077
FT /evidence="ECO:0007829|PDB:2DI8"
FT STRAND 2084..2090
FT /evidence="ECO:0007829|PDB:2DI8"
FT STRAND 2111..2113
FT /evidence="ECO:0007829|PDB:2DLG"
FT STRAND 2118..2120
FT /evidence="ECO:0007829|PDB:2DLG"
FT HELIX 2126..2128
FT /evidence="ECO:0007829|PDB:2DLG"
FT STRAND 2130..2134
FT /evidence="ECO:0007829|PDB:2DLG"
FT STRAND 2140..2142
FT /evidence="ECO:0007829|PDB:2DLG"
FT STRAND 2144..2147
FT /evidence="ECO:0007829|PDB:2DLG"
FT STRAND 2149..2157
FT /evidence="ECO:0007829|PDB:2DLG"
FT STRAND 2164..2175
FT /evidence="ECO:0007829|PDB:2DLG"
FT STRAND 2180..2185
FT /evidence="ECO:0007829|PDB:2DLG"
FT HELIX 2193..2195
FT /evidence="ECO:0007829|PDB:2EE6"
FT TURN 2201..2203
FT /evidence="ECO:0007829|PDB:2EE6"
FT STRAND 2206..2208
FT /evidence="ECO:0007829|PDB:2EE6"
FT STRAND 2210..2214
FT /evidence="ECO:0007829|PDB:2EE6"
FT STRAND 2219..2221
FT /evidence="ECO:0007829|PDB:2EE6"
FT STRAND 2226..2234
FT /evidence="ECO:0007829|PDB:2EE6"
FT STRAND 2236..2240
FT /evidence="ECO:0007829|PDB:2EE6"
FT STRAND 2250..2256
FT /evidence="ECO:0007829|PDB:2EE6"
FT STRAND 2258..2266
FT /evidence="ECO:0007829|PDB:2EE6"
FT STRAND 2275..2281
FT /evidence="ECO:0007829|PDB:2EE6"
FT STRAND 2288..2294
FT /evidence="ECO:0007829|PDB:2EEB"
FT STRAND 2306..2314
FT /evidence="ECO:0007829|PDB:2EEB"
FT STRAND 2320..2324
FT /evidence="ECO:0007829|PDB:2EEB"
FT STRAND 2330..2332
FT /evidence="ECO:0007829|PDB:2EEB"
FT STRAND 2334..2337
FT /evidence="ECO:0007829|PDB:2EEB"
FT STRAND 2340..2347
FT /evidence="ECO:0007829|PDB:2EEB"
FT STRAND 2352..2365
FT /evidence="ECO:0007829|PDB:2EEB"
FT STRAND 2370..2375
FT /evidence="ECO:0007829|PDB:2EEB"
FT TURN 2384..2386
FT /evidence="ECO:0007829|PDB:2EEC"
FT STRAND 2388..2392
FT /evidence="ECO:0007829|PDB:2EEC"
FT TURN 2393..2395
FT /evidence="ECO:0007829|PDB:2EEC"
FT STRAND 2403..2408
FT /evidence="ECO:0007829|PDB:2EEC"
FT TURN 2410..2412
FT /evidence="ECO:0007829|PDB:2EEC"
FT STRAND 2417..2425
FT /evidence="ECO:0007829|PDB:2EEC"
FT STRAND 2430..2433
FT /evidence="ECO:0007829|PDB:2EEC"
FT STRAND 2435..2442
FT /evidence="ECO:0007829|PDB:2EEC"
FT STRAND 2448..2459
FT /evidence="ECO:0007829|PDB:2EEC"
FT STRAND 2466..2473
FT /evidence="ECO:0007829|PDB:2EEC"
FT TURN 2512..2514
FT /evidence="ECO:0007829|PDB:2EED"
FT STRAND 2516..2519
FT /evidence="ECO:0007829|PDB:2EED"
FT HELIX 2520..2523
FT /evidence="ECO:0007829|PDB:2EED"
FT STRAND 2531..2536
FT /evidence="ECO:0007829|PDB:2EED"
FT TURN 2538..2540
FT /evidence="ECO:0007829|PDB:2EED"
FT STRAND 2545..2547
FT /evidence="ECO:0007829|PDB:2EED"
FT STRAND 2557..2565
FT /evidence="ECO:0007829|PDB:2EED"
FT STRAND 2568..2574
FT /evidence="ECO:0007829|PDB:2EED"
FT STRAND 2579..2583
FT /evidence="ECO:0007829|PDB:2EED"
FT STRAND 2585..2591
FT /evidence="ECO:0007829|PDB:2EED"
FT STRAND 2596..2601
FT /evidence="ECO:0007829|PDB:2EED"
FT MOD_RES O75369-8:1474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ 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
