ID FLNA_HUMAN Reviewed; 2647 AA. AC P21333; E9KL45; Q5HY53; Q5HY55; Q8NF52; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 270. DE RecName: Full=Filamin-A; DE Short=FLN-A; DE AltName: Full=Actin-binding protein 280; DE Short=ABP-280; DE AltName: Full=Alpha-filamin; DE AltName: Full=Endothelial actin-binding protein; DE AltName: Full=Filamin-1; DE AltName: Full=Non-muscle filamin; GN Name=FLNA; Synonyms=FLN, FLN1; 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), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=2391361; DOI=10.1083/jcb.111.3.1089; RA Gorlin J.B., Yamin R., Egan S., Stewart M., Stossel T.P., Kwiatkowski D.J., RA Hartwig J.H.; RT "Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a RT molecular leaf spring."; RL J. Cell Biol. 111:1089-1105(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8088819; DOI=10.1006/geno.1994.1226; RA Patrosso M.C., Repetto M., Villa A., Milanesi L., Frattini A., Faranda S., RA Mancini M., Maestrini E., Toniolo D., Vezzoni P.; RT "The exon-intron organization of the human X-linked gene (FLN1) encoding RT actin-binding protein 280."; RL Genomics 21:71-76(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8733135; DOI=10.1093/hmg/5.5.659; RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., RA Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.; RT "Long-range sequence analysis in Xq28: thirteen known and six candidate RT genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."; RL Hum. Mol. Genet. 5:659-668(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=20736409; DOI=10.1074/mcp.m110.001719; RA Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., RA Jin S., Liu J., Zhu P., Liu Y.; RT "Systematic mapping and functional analysis of a family of human epididymal RT secretory sperm-located proteins."; RL Mol. Cell. Proteomics 9:2517-2528(2010). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=21697133; DOI=10.1167/iovs.11-7479; RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., RA Usami R., Ohtoko K., Kato S.; RT "Full-length transcriptome analysis of human retina-derived cell lines RT ARPE-19 and Y79 using the vector-capping method."; RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP PROTEIN SEQUENCE OF 2-24; 44-51; 64-87; 101-127; 172-190; 300-376; 384-400; RP 428-437; 497-504; 581-593; 656-664; 685-700; 761-771; 774-781; 829-837; RP 842-900; 907-916; 959-973; 983-994; 1020-1032; 1165-1172; 1235-1294; RP 1297-1312; 1360-1399; 1440-1450; 1465-1486; 1492-1532; 1539-1547; RP 1550-1592; 1622-1633; 1636-1644; 1726-1753; 1801-1809; 1815-1831; RP 1892-1907; 1965-1993; 2015-2024; 2026-2049; 2202-2215; 2243-2250; RP 2265-2289; 2311-2333; 2335-2361; 2396-2405; 2521-2540; 2585-2598 AND RP 2613-2631, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Platelet; RA Bienvenut W.V., Claeys D.; RL Submitted (NOV-2005) to UniProtKB. RN [10] RP PROTEIN SEQUENCE OF 25-54; 917-940; 1037-1050; 1754-1783 AND 2148-2168. RX PubMed=2248958; DOI=10.1021/bi00492a019; RA Hock R.S., Davis G., Speicher D.W.; RT "Purification of human smooth muscle filamin and characterization of RT structural domains and functional sites."; RL Biochemistry 29:9441-9451(1990). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1658-1772. RX PubMed=7689010; DOI=10.1093/hmg/2.6.761; RA Maestrini E., Patrosso C., Mancini M., Rivella S., Rocchi M., Repetto M., RA Villa A., Frattini A., Zoppe M., Vezzoni P., Toniolo D.; RT "Mapping of two genes encoding isoforms of the actin binding protein ABP- RT 280, a dystrophin like protein, to Xq28 and to chromosome 7."; RL Hum. Mol. Genet. 2:761-766(1993). RN [12] RP SIMILARITY TO OTHER MEMBERS OF THE FAMILY. 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 [13] RP INTERACTION WITH PSEN1 AND PSEN2. 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 [14] RP INTERACTION WITH KCND2. RX PubMed=11102480; DOI=10.1523/jneurosci.20-23-08736.2000; RA Petrecca K., Miller D.M., Shrier A.; RT "Localization and enhanced current density of the Kv4.2 potassium channel RT by interaction with the actin-binding protein filamin."; RL J. Neurosci. 20:8736-8744(2000). RN [15] RP INTERACTION WITH INPPL1. 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 [16] RP INTERACTION WITH FLNB. 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 [17] RP INTERACTION WITH 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 [18] 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 [19] 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 [20] RP INTERACTION WITH CEACAM1, AND SUBCELLULAR LOCATION. RX PubMed=16291724; DOI=10.1242/jcs.02660; RA Klaile E., Mueller M.M., Kannicht C., Singer B.B., Lucka L.; RT "CEACAM1 functionally interacts with filamin A and exerts a dual role in RT the regulation of cell migration."; RL J. Cell Sci. 118:5513-5524(2005). RN [21] RP INTERACTION WITH FOXC1. RX PubMed=15684392; DOI=10.1128/mcb.25.4.1415-1424.2005; RA Berry F.B., O'Neill M.A., Coca-Prados M., Walter M.A.; RT "FOXC1 transcriptional regulatory activity is impaired by PBX1 in a filamin RT A-mediated manner."; RL Mol. Cell. Biol. 25:1415-1424(2005). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1089; SER-1459; SER-2152 AND RP SER-2284, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [23] RP INVOLVEMENT IN PVNH1. RX PubMed=16299064; DOI=10.1136/jmg.2005.038505; RA Hehr U., Hehr A., Uyanik G., Phelan E., Winkler J., Reardon W.; RT "A filamin A splice mutation resulting in a syndrome of facial dysmorphism, RT periventricular nodular heterotopia, and severe constipation reminiscent of RT cerebro-fronto-facial syndrome."; RL J. Med. Genet. 43:541-544(2006). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084 AND SER-1459, AND RP IDENTIFICATION BY 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 [25] RP INTERACTION WITH ARHGAP24. RX PubMed=16862148; DOI=10.1038/ncb1437; RA Ohta Y., Hartwig J.H., Stossel T.P.; RT "FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control RT actin remodelling."; RL Nat. Cell Biol. 8:803-814(2006). RN [26] RP INVOLVEMENT IN IPOX. RX PubMed=17357080; DOI=10.1086/513321; RA Gargiulo A., Auricchio R., Barone M.V., Cotugno G., Reardon W., Milla P.J., RA Ballabio A., Ciccodicola A., Auricchio A.; RT "Filamin A is mutated in X-linked chronic idiopathic intestinal pseudo- RT obstruction with central nervous system involvement."; RL Am. J. Hum. Genet. 80:751-758(2007). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [28] RP INTERACTION WITH ECSCR. RX PubMed=18556573; DOI=10.1161/atvbaha.108.162511; RA Armstrong L.-J., Heath V.L., Sanderson S., Kaur S., Beesley J.F.J., RA Herbert J.M.J., Legg J.A., Poulsom R., Bicknell R.; RT "ECSM2, an endothelial specific filamin a binding protein that mediates RT chemotaxis."; RL Arterioscler. Thromb. Vasc. Biol. 28:1640-1646(2008). RN [29] RP INTERACTION WITH FCGR1A. RX PubMed=18322202; DOI=10.4049/jimmunol.180.6.3938; RA Beekman J.M., van der Poel C.E., van der Linden J.A., van den Berg D.L.C., RA van den Berghe P.V.E., van de Winkel J.G.J., Leusen J.H.W.; RT "Filamin A stabilizes FcgammaRI surface expression and prevents its RT lysosomal routing."; RL J. Immunol. 180:3938-3945(2008). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1459; SER-2152 AND RP SER-2158, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081, AND IDENTIFICATION BY RP 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 [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084; SER-1338; SER-1459; RP SER-1533; SER-1630; SER-2053; SER-2152; SER-2327; SER-2414 AND SER-2510, 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 [35] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [36] RP INTERACTION WITH GP1BA; ITGB7; ITGB2 AND FBLIM1. RX PubMed=19828450; DOI=10.1074/jbc.m109.060954; RA Ithychanda S.S., Hsu D., Li H., Yan L., Liu D.D., Liu D., Das M., RA Plow E.F., Qin J.; RT "Identification and characterization of multiple similar ligand-binding RT repeats in filamin: implication on filamin-mediated receptor clustering and RT cross-talk."; RL J. Biol. Chem. 284:35113-35121(2009). RN [37] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1084, AND IDENTIFICATION BY RP 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 [38] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-508; LYS-700; LYS-781; LYS-837; RP LYS-2607 AND LYS-2621, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [39] RP INTERACTION WITH SYK. RX PubMed=20713593; DOI=10.1084/jem.20100222; RA Falet H., Pollitt A.Y., Begonja A.J., Weber S.E., Duerschmied D., RA Wagner D.D., Watson S.P., Hartwig J.H.; RT "A novel interaction between FlnA and Syk regulates platelet ITAM-mediated RT receptor signaling and function."; RL J. Exp. Med. 207:1967-1979(2010). RN [40] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081; SER-1084; SER-1459; RP SER-1533; SER-1734; SER-2053; SER-2152; SER-2284; SER-2327; THR-2336 AND RP SER-2414, AND 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 [41] 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 [42] RP INTERACTION WITH ITGB7 AND FBLIM1, AND DOMAIN. RX PubMed=21524097; DOI=10.1021/bi2003229; RA Ithychanda S.S., Qin J.; RT "Evidence for multisite ligand binding and stretching of filamin by RT integrin and migfilin."; RL Biochemistry 50:4229-4231(2011). RN [43] RP INTERACTION WITH TAF1B AND MIS18BP1, AND CHARACTERIZATION OF VARIANTS RP ALA-1159; THR-1188 AND LEU-1199. RX PubMed=21228480; DOI=10.1271/bbb.100567; RA Qiu H., Nomiyama R., Moriguchi K., Fukada T., Sugimoto K.; RT "Identification of novel nuclear protein interactions with the N-terminal RT part of filamin A."; RL Biosci. Biotechnol. Biochem. 75:145-147(2011). RN [44] RP INVOLVEMENT IN MACROTHROMBOCYTOPENIA, AND VARIANT LYS-1803. RX PubMed=21960593; DOI=10.1182/blood-2011-07-365601; RA Nurden P., Debili N., Coupry I., Bryckaert M., Youlyouz-Marfak I., Sole G., RA Pons A.C., Berrou E., Adam F., Kauskot A., Lamaziere J.M., Rameau P., RA Fergelot P., Rooryck C., Cailley D., Arveiler B., Lacombe D., RA Vainchenker W., Nurden A., Goizet C.; RT "Thrombocytopenia resulting from mutations in filamin A can be expressed as RT an isolated syndrome."; RL Blood 118:5928-5937(2011). RN [45] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-1081; SER-1084; RP SER-1459; SER-2152 AND SER-2327, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [46] RP FUNCTION IN CILIOGENESIS, AND INTERACTION WITH TMEM67 AND MKS1. RX PubMed=22121117; DOI=10.1093/hmg/ddr557; RA Adams M., Simms R.J., Abdelhamed Z., Dawe H.R., Szymanska K., Logan C.V., RA Wheway G., Pitt E., Gull K., Knowles M.A., Blair E., Cross S.H., RA Sayer J.A., Johnson C.A.; RT "A meckelin-filamin A interaction mediates ciliogenesis."; RL Hum. Mol. Genet. 21:1272-1286(2012). RN [47] RP INTERACTION WITH MICALL2. RX PubMed=23890175; DOI=10.1111/gtc.12078; RA Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T., RA Imoto I., Matsushita N., Sasaki T.; RT "Junctional Rab13-binding protein (JRAB) regulates cell spreading via RT filamins."; RL Genes Cells 18:810-822(2013). RN [48] RP INVOLVEMENT IN CSBSX. RX PubMed=23037936; DOI=10.1038/gim.2012.123; RA van der Werf C.S., Sribudiani Y., Verheij J.B., Carroll M., O'Loughlin E., RA Chen C.H., Brooks A.S., Liszewski M.K., Atkinson J.P., Hofstra R.M.; RT "Congenital short bowel syndrome as the presenting symptom in male patients RT with FLNA mutations."; RL Genet. Med. 15:310-313(2013). RN [49] RP UBIQUITINATION AT LYS-42; LYS-43 AND LYS-135, AND MUTAGENESIS OF LYS-42; RP LYS-43 AND LYS-135. RX PubMed=24052262; DOI=10.1074/jbc.m113.496604; RA Razinia Z., Baldassarre M., Cantelli G., Calderwood D.A.; RT "ASB2alpha, an E3 ubiquitin ligase specificity subunit, regulates cell RT spreading and triggers proteasomal degradation of filamins by targeting the RT filamin calponin homology 1 domain."; RL J. Biol. Chem. 288:32093-32105(2013). RN [50] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081; SER-1084; SER-1301; RP SER-1459; SER-1533; SER-1630; SER-1835; SER-2128; SER-2152; SER-2158; RP SER-2284; SER-2327; THR-2336; SER-2338 AND SER-2510, 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 [51] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1055; SER-1081; SER-1459; RP SER-1734; SER-1967; SER-2152; SER-2158 AND SER-2163, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE 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 [52] RP FUNCTION, AND INTERACTION WITH CRMP1; DPYSL3 AND DPYSL4. RX PubMed=25358863; DOI=10.1038/ncomms6325; RA Nakamura F., Kumeta K., Hida T., Isono T., Nakayama Y., RA Kuramata-Matsuoka E., Yamashita N., Uchida Y., Ogura K., Gengyo-Ando K., RA Mitani S., Ogino T., Goshima Y.; RT "Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to RT mediate Sema3A signalling."; RL Nat. Commun. 5:5325-5325(2014). RN [53] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [54] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [55] RP INTERACTION WITH DRD3; MAS1; AGTR1 AND ADRA1D, AND PHOSPHORYLATION AT RP SER-2152. RX PubMed=26460884; DOI=10.1021/acs.biochem.5b00975; RA Tirupula K.C., Ithychanda S.S., Mohan M.L., Naga Prasad S.V., Qin J., RA Karnik S.S.; RT "G Protein-Coupled Receptors Directly Bind Filamin A with High Affinity and RT Promote Filamin Phosphorylation."; RL Biochemistry 54:6673-6683(2015). RN [56] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [57] RP PHOSPHORYLATION AT SER-2152 AND THR-2336, REGULATION OF PHOSPHORYLATION AT RP SER-2152, INTERACTION WITH GP1BA, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25666618; DOI=10.1074/jbc.m114.633446; RA Ithychanda S.S., Fang X., Mohan M.L., Zhu L., Tirupula K.C., RA Naga Prasad S.V., Wang Y.X., Karnik S.S., Qin J.; RT "A mechanism of global shape-dependent recognition and phosphorylation of RT filamin by protein kinase A."; RL J. Biol. Chem. 290:8527-8538(2015). RN [58] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [59] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [60] RP UBIQUITINATION. RX PubMed=26766444; DOI=10.1016/j.devcel.2015.12.015; RA Scholz B., Korn C., Wojtarowicz J., Mogler C., Augustin I., Boutros M., RA Niehrs C., Augustin H.G.; RT "Endothelial RSPO3 controls vascular stability and pruning through non- RT canonical WNT/Ca(2+)/NFAT signaling."; RL Dev. Cell 36:79-93(2016). RN [61] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [62] RP VARIANT LEU-606. RX PubMed=30500825; DOI=10.1371/journal.pgen.1007671; RA Hiatt S.M., Neu M.B., Ramaker R.C., Hardigan A.A., Prokop J.W., RA Hancarova M., Prchalova D., Havlovicova M., Prchal J., Stranecky V., RA Yim D.K.C., Powis Z., Keren B., Nava C., Mignot C., Rio M., RA Revah-Politi A., Hemati P., Stong N., Iglesias A.D., Suchy S.F., RA Willaert R., Wentzensen I.M., Wheeler P.G., Brick L., Kozenko M., RA Hurst A.C.E., Wheless J.W., Lacassie Y., Myers R.M., Barsh G.S., RA Sedlacek Z., Cooper G.M.; RT "De novo mutations in the GTP/GDP-binding region of RALA, a RAS-like small RT GTPase, cause intellectual disability and developmental delay."; RL PLoS Genet. 14:e1007671-e1007671(2018). RN [63] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2045-2329, AND DOMAIN. RX PubMed=17690686; DOI=10.1038/sj.emboj.7601827; RA Lad Y., Kiema T., Jiang P., Pentikainen O.T., Coles C.H., Campbell I.D., RA Calderwood D.A., Ylanne J.; RT "Structure of three tandem filamin domains reveals auto-inhibition of RT ligand binding."; RL EMBO J. 26:3993-4004(2007). RN [64] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-278, ACTIN-BINDING REGION, AND RP SUBUNIT. RX PubMed=19923718; DOI=10.1107/s0907444909037330; RA Ruskamo S., Ylanne J.; RT "Structure of the human filamin A actin-binding domain."; RL Acta Crystallogr. D 65:1217-1221(2009). RN [65] RP STRUCTURE BY NMR OF 1772-1956 AND 1954-2141. RX PubMed=19622754; DOI=10.1074/jbc.m109.019661; RA Heikkinen O.K., Ruskamo S., Konarev P.V., Svergun D.I., Iivanainen T., RA Heikkinen S.M., Permi P., Koskela H., Kilpelainen I., Ylanne J.; RT "Atomic structures of two novel immunoglobulin-like domain pairs in the RT actin cross-linking protein filamin."; RL J. Biol. Chem. 284:25450-25458(2009). RN [66] RP VARIANT PVNH1 PHE-656, AND VARIANT THR-1764. RX PubMed=11532987; DOI=10.1093/hmg/10.17.1775; RA Sheen V.L., Dixon P.H., Fox J.W., Hong S.E., Kinton L., Sisodiya S.M., RA Duncan J.S., Dubeau F., Scheffer I.E., Schachter S.C., Wilner A., RA Henchy R., Crino P., Kamuro K., DiMario F., Berg M., Kuzniecky R., RA Cole A.J., Bromfield E., Biber M., Schomer D., Wheless J., Silver K., RA Mochida G.H., Berkovic S.F., Andermann F., Andermann E., Dobyns W.B., RA Wood N.W., Walsh C.A.; RT "Mutations in the X-linked filamin 1 gene cause periventricular nodular RT heterotopia in males as well as in females."; RL Hum. Mol. Genet. 10:1775-1783(2001). RN [67] RP VARIANT MET-528. RX PubMed=12410386; DOI=10.1007/s00401-002-0594-9; RA Kakita A., Hayashi S., Moro F., Guerrini R., Ozawa T., Ono K., Kameyama S., RA Walsh C.A., Takahashi H.; RT "Bilateral periventricular nodular heterotopia due to filamin 1 gene RT mutation: widespread glomeruloid microvascular anomaly and dysplastic RT cytoarchitecture in the cerebral cortex."; RL Acta Neuropathol. 104:649-657(2002). RN [68] RP VARIANT PVNH1 VAL-82. RX PubMed=11914408; DOI=10.1212/wnl.58.6.916; RA Moro F., Carrozzo R., Veggiotti P., Tortorella G., Toniolo D., Volzone A., RA Guerrini R.; RT "Familial periventricular heterotopia: missense and distal truncating RT mutations of the FLN1 gene."; RL Neurology 58:916-921(2002). RN [69] RP VARIANTS OPD1 PHE-172; TRP-196 AND LEU-207, VARIANTS OPD2 PRO-170; GLY-196; RP SER-200; LYS-254; PRO-273; LYS-555 AND PHE-1645, VARIANTS FMD1 ALA-1159; RP LEU-1186 AND ILE-1620 DEL, VARIANTS MNS GLU-1184; THR-1188 AND LEU-1199, RP AND VARIANTS MET-429 AND THR-1764. RX PubMed=12612583; DOI=10.1038/ng1119; RA Robertson S.P., Twigg S.R.F., Sutherland-Smith A.J., Biancalana V., RA Gorlin R.J., Horn D., Kenwrick S.J., Kim C.A., Morava E., Newbury-Ecob R., RA Oerstavik K.H., Quarrell O.W.J., Schwartz C.E., Shears D.J., Suri M., RA Kendrick-Jones J., Wilkie A.O.M.; RT "Localized mutations in the gene encoding the cytoskeletal protein filamin RT A cause diverse malformations in humans."; RL Nat. Genet. 33:487-491(2003). RN [70] RP VARIANTS PVNH1 VAL-102 AND PHE-149. RX PubMed=15249610; DOI=10.1212/01.wnl.0000132818.84827.4d; RA Guerrini R., Mei D., Sisodiya S.M., Sicca F., Harding B., Takahashi Y., RA Dorn T., Yoshida A., Campistol J., Kraemer G., Moro F., Dobyns W.B., RA Parrini E.; RT "Germline and mosaic mutations of FLN1 in men with periventricular RT heterotopia."; RL Neurology 63:51-56(2004). RN [71] RP VARIANT OTOPALATODIGITAL SPECTRUM DISORDER 1635-ARG--VAL-1637 DEL. RX PubMed=15654694; DOI=10.1002/ajmg.a.30484; RA Stefanova M., Meinecke P., Gal A., Bolz H.; RT "A novel 9 bp deletion in the filamin A gene causes an otopalatodigital- RT spectrum disorder with a variable, intermediate phenotype."; RL Am. J. Med. Genet. A 132:386-390(2005). RN [72] RP VARIANT OPD1 TYR-203. RX PubMed=15940695; DOI=10.1002/ajmg.a.30792; RA Hidalgo-Bravo A., Pompa-Mera E.N., Kofman-Alfaro S., Gonzalez-Bonilla C.R., RA Zenteno J.C.; RT "A novel filamin A D203Y mutation in a female patient with otopalatodigital RT type 1 syndrome and extremely skewed X chromosome inactivation."; RL Am. J. Med. Genet. A 136:190-193(2005). RN [73] RP VARIANT PVNH1 GLY-39. RX PubMed=15668422; DOI=10.1212/01.wnl.0000149512.79621.df; RA Sheen V.L., Jansen A., Chen M.H., Parrini E., Morgan T., Ravenscroft R., RA Ganesh V., Underwood T., Wiley J., Leventer R., Vaid R.R., Ruiz D.E., RA Hutchins G.M., Menasha J., Willner J., Geng Y., Gripp K.W., Nicholson L., RA Berry-Kravis E., Bodell A., Apse K., Hill R.S., Dubeau F., Andermann F., RA Barkovich J., Andermann E., Shugart Y.Y., Thomas P., Viri M., Veggiotti P., RA Robertson S., Guerrini R., Walsh C.A.; RT "Filamin A mutations cause periventricular heterotopia with Ehlers-Danlos RT syndrome."; RL Neurology 64:254-262(2005). RN [74] RP VARIANTS FMD1 LEU-1186 AND CYS-1728. RX PubMed=16596676; DOI=10.1002/ajmg.a.31213; RA Zenker M., Naehrlich L., Sticht H., Reis A., Horn D.; RT "Genotype-epigenotype-phenotype correlations in females with RT frontometaphyseal dysplasia."; RL Am. J. Med. Genet. A 140:1069-1073(2006). RN [75] RP VARIANT PVNH1 VAL-128. RX PubMed=15994863; DOI=10.1136/jmg.2004.029173; RA Gomez-Garre P., Seijo M., Gutierrez-Delicado E., Castro del Rio M., RA de la Torre C., Gomez-Abad C., Morales-Corraliza J., Puig M., RA Serratosa J.M.; RT "Ehlers-Danlos syndrome and periventricular nodular heterotopia in a RT Spanish family with a single FLNA mutation."; RL J. Med. Genet. 43:232-237(2006). RN [76] RP VARIANT OPD2 PHE-210. RX PubMed=17431908; DOI=10.1002/ajmg.a.31696; RA Marino-Enriquez A., Lapunzina P., Robertson S.P., Rodriguez J.I.; RT "Otopalatodigital syndrome type 2 in two siblings with a novel filamin A RT 629G>T mutation: clinical, pathological, and molecular findings."; RL Am. J. Med. Genet. A 143:1120-1125(2007). RN [77] RP VARIANT FGS2 LEU-1291. RX PubMed=17632775; DOI=10.1002/ajmg.a.31751; RA Unger S., Mainberger A., Spitz C., Baehr A., Zeschnigk C., Zabel B., RA Superti-Furga A., Morris-Rosendahl D.J.; RT "Filamin A mutation is one cause of FG syndrome."; RL Am. J. Med. Genet. A 143:1876-1879(2007). RN [78] RP VARIANTS CVDPX ARG-288; GLN-637 AND ASP-711. RX PubMed=17190868; DOI=10.1161/circulationaha.106.622621; RA Kyndt F., Gueffet J.P., Probst V., Jaafar P., Legendre A., Le Bouffant F., RA Toquet C., Roy E., McGregor L., Lynch S.A., Newbury-Ecob R., Tran V., RA Young I., Trochu J.N., Le Marec H., Schott J.J.; RT "Mutations in the gene encoding filamin A as a cause for familial cardiac RT valvular dystrophy."; RL Circulation 115:40-49(2007). RN [79] RP VARIANT TOD 1724-VAL--THR-1739 DEL. RX PubMed=20598277; DOI=10.1016/j.ajhg.2010.06.008; RA Sun Y., Almomani R., Aten E., Celli J., van der Heijden J., Venselaar H., RA Robertson S.P., Baroncini A., Franco B., Basel-Vanagaite L., Horii E., RA Drut R., Ariyurek Y., den Dunnen J.T., Breuning M.H.; RT "Terminal osseous dysplasia is caused by a single recurrent mutation in the RT FLNA gene."; RL Am. J. Hum. Genet. 87:146-153(2010). RN [80] RP VARIANT MET-528. RX PubMed=20844545; DOI=10.1038/jhg.2010.114; RA Kunishima S., Ito-Yamamura Y., Hayakawa A., Yamamoto T., Saito H.; RT "FLNA p.V528M substitution is neither associated with bilateral RT periventricular nodular heterotopia nor with macrothrombocytopenia."; RL J. Hum. Genet. 55:844-846(2010). RN [81] RP VARIANTS OPD2 SER-187 AND GLY-196, VARIANTS OPD1 LEU-207; THR-267; ASP-804 RP AND HIS-2391, VARIANTS FMD1 VAL-1142; LEU-1186 AND ARG-1840, AND VARIANTS RP MNS LEU-1163 AND THR-1188. RX PubMed=27193221; DOI=10.1038/jhg.2016.37; RA Moutton S., Fergelot P., Naudion S., Cordier M.P., Sole G., Guerineau E., RA Hubert C., Rooryck C., Vuillaume M.L., Houcinat N., Deforges J., Bouron J., RA Deves S., Le Merrer M., David A., Genevieve D., Giuliano F., Journel H., RA Megarbane A., Faivre L., Chassaing N., Francannet C., Sarrazin E., RA Stattin E.L., Vigneron J., Leclair D., Abadie C., Sarda P., Baumann C., RA Delrue M.A., Arveiler B., Lacombe D., Goizet C., Coupry I.; RT "Otopalatodigital spectrum disorders: refinement of the phenotypic and RT mutational spectrum."; RL J. Hum. Genet. 61:693-699(2016). CC -!- FUNCTION: Promotes orthogonal branching of actin filaments and links CC actin filaments to membrane glycoproteins. Anchors various CC transmembrane proteins to the actin cytoskeleton and serves as a CC scaffold for a wide range of cytoplasmic signaling proteins. CC Interaction with FLNB may allow neuroblast migration from the CC ventricular zone into the cortical plate. Tethers cell surface- CC localized furin, modulates its rate of internalization and directs its CC intracellular trafficking (By similarity). Involved in ciliogenesis. CC Plays a role in cell-cell contacts and adherens junctions during the CC development of blood vessels, heart and brain organs. Plays a role in CC platelets morphology through interaction with SYK that regulates CC ITAM- and ITAM-like-containing receptor signaling, resulting in by CC platelet cytoskeleton organization maintenance (By similarity). During CC the axon guidance process, required for growth cone collapse induced by CC SEMA3A-mediated stimulation of neurons (PubMed:25358863). {ECO:0000250, CC ECO:0000250|UniProtKB:Q8BTM8, ECO:0000269|PubMed:22121117, CC ECO:0000269|PubMed:25358863}. CC -!- SUBUNIT: Homodimer. Interacts with PDLIM2 (By similarity). Interacts CC with RFLNA and RFLNB (By similarity). Interacts with FCGR1A, FLNB, CC FURIN, HSPB7, INPPL1, KCND2, MYOT, MYOZ1, ARHGAP24, PSEN1, PSEN2 and CC ECSCR. Interacts also with various other binding partners in addition CC to filamentous actin. Interacts (via N-terminus) with MIS18BP1 (via N- CC terminus). Interacts (via N-terminus) with TAF1B. Interacts with TMEM67 CC (via C-terminus) and MKS1. Interacts (via actin-binding domain) with CC MICALL2 (via CH domain). Interacts (via filamin repeat 5) with SYK; CC docks SYK to the plasma membrane (PubMed:20713593). Interacts (via CC filamin repeats 19 and 21) with DRD3; increased PKA-mediated CC phosphorylation at Ser-2152. Interacts (via filamin repeat 21) with CC MAS1, AGTR1 and ADRA1D; increases PKA-mediated phosphorylation of FLNA CC at Ser-2152 (PubMed:26460884). Interacts (via filamin repeats 4, 9, 12, CC 17, 19, 21, and 23) with GP1BA (high affinity), ITGB7, ITGB2 and FBLIM1 CC (PubMed:19828450, PubMed:21524097, PubMed:25666618). Interacts with CC CEACAM1 (via cytoplasmic domain); inhibits cell migration and cell CC scattering by interfering with the interaction between FLNA and RALA CC (PubMed:16291724). Interacts with FOXC1 (PubMed:15684392). Interacts CC (via calponin-homology (CH) domain 1 and filamin repeat 24) with CRMP1; CC the interaction alters FLNA ternary structure and thus promotes FLNA CC dissociation from F-actin (PubMed:25358863). Interacts with CC DPYSL3/CRMP3 and DPYSL4/CRMP4 (PubMed:25358863). {ECO:0000250, CC ECO:0000250|UniProtKB:Q8BTM8, ECO:0000269|PubMed:11102480, CC ECO:0000269|PubMed:11739414, ECO:0000269|PubMed:12393796, CC ECO:0000269|PubMed:15684392, ECO:0000269|PubMed:16076904, CC ECO:0000269|PubMed:16291724, ECO:0000269|PubMed:16862148, CC ECO:0000269|PubMed:18322202, ECO:0000269|PubMed:18556573, CC ECO:0000269|PubMed:19828450, ECO:0000269|PubMed:19923718, CC ECO:0000269|PubMed:20713593, ECO:0000269|PubMed:21228480, CC ECO:0000269|PubMed:21524097, ECO:0000269|PubMed:22121117, CC ECO:0000269|PubMed:23890175, ECO:0000269|PubMed:25358863, CC ECO:0000269|PubMed:25666618, ECO:0000269|PubMed:26460884, CC ECO:0000269|PubMed:9437013}. CC -!- INTERACTION: CC P21333; Q8N264: ARHGAP24; NbExp=6; IntAct=EBI-350432, EBI-988764; CC P21333; O95067: CCNB2; NbExp=8; IntAct=EBI-350432, EBI-375024; CC P21333; P46108: CRK; NbExp=3; IntAct=EBI-350432, EBI-886; CC P21333; O75369: FLNB; NbExp=5; IntAct=EBI-350432, EBI-352089; CC P21333; Q12948: FOXC1; NbExp=8; IntAct=EBI-350432, EBI-1175253; CC P21333; P51114: FXR1; NbExp=2; IntAct=EBI-350432, EBI-713291; CC P21333; P62993: GRB2; NbExp=2; IntAct=EBI-350432, EBI-401755; CC P21333; P08514-1: ITGA2B; NbExp=3; IntAct=EBI-350432, EBI-15805658; CC P21333; P05556: ITGB1; NbExp=5; IntAct=EBI-350432, EBI-703066; CC P21333; P05556-1: ITGB1; NbExp=2; IntAct=EBI-350432, EBI-6082935; CC P21333; P05106: ITGB3; NbExp=3; IntAct=EBI-350432, EBI-702847; CC P21333; P26010: ITGB7; NbExp=6; IntAct=EBI-350432, EBI-702932; CC P21333; P26010-1: ITGB7; NbExp=2; IntAct=EBI-350432, EBI-15944630; CC P21333; O14786: NRP1; NbExp=2; IntAct=EBI-350432, EBI-1187100; CC P21333; P35372: OPRM1; NbExp=5; IntAct=EBI-350432, EBI-2624570; CC P21333; Q86SQ0: PHLDB2; NbExp=3; IntAct=EBI-350432, EBI-2798483; CC P21333; Q9BYB0: SHANK3; NbExp=2; IntAct=EBI-350432, EBI-1752330; CC P21333; P07228: ITGB1; Xeno; NbExp=2; IntAct=EBI-350432, EBI-5606437; CC P21333; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=6; IntAct=EBI-350432, EBI-6863741; CC P21333; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=6; IntAct=EBI-350432, EBI-6863748; CC P21333-2; Q6UY14-3: ADAMTSL4; NbExp=6; IntAct=EBI-9641086, EBI-10173507; CC P21333-2; Q9XRX5-2: ANKRD13C-DT; NbExp=3; IntAct=EBI-9641086, EBI-12051311; CC P21333-2; P05067: APP; NbExp=3; IntAct=EBI-9641086, EBI-77613; CC P21333-2; Q14457: BECN1; NbExp=3; IntAct=EBI-9641086, EBI-949378; CC P21333-2; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-9641086, EBI-18924329; CC P21333-2; Q9BSJ5: C17orf80; NbExp=3; IntAct=EBI-9641086, EBI-2872520; CC P21333-2; Q96NX5: CAMK1G; NbExp=3; IntAct=EBI-9641086, EBI-3920838; CC P21333-2; Q8N5S9-2: CAMKK1; NbExp=3; IntAct=EBI-9641086, EBI-25850646; CC P21333-2; Q6ZP82: CCDC141; NbExp=3; IntAct=EBI-9641086, EBI-928795; CC P21333-2; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-9641086, EBI-2872414; CC P21333-2; P53672: CRYBA2; NbExp=3; IntAct=EBI-9641086, EBI-750444; CC P21333-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-9641086, EBI-3867333; CC P21333-2; Q96D03: DDIT4L; NbExp=5; IntAct=EBI-9641086, EBI-742054; CC P21333-2; O00472: ELL2; NbExp=3; IntAct=EBI-9641086, EBI-395274; CC P21333-2; P07148: FABP1; NbExp=3; IntAct=EBI-9641086, EBI-2115989; CC P21333-2; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-9641086, EBI-3893327; CC P21333-2; Q8TAK5: GABPB2; NbExp=3; IntAct=EBI-9641086, EBI-8468945; CC P21333-2; F2Z2M7: GALNT10; NbExp=3; IntAct=EBI-9641086, EBI-23893155; CC P21333-2; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-9641086, EBI-347538; CC P21333-2; P17066: HSPA6; NbExp=3; IntAct=EBI-9641086, EBI-355106; CC P21333-2; Q9UBY9: HSPB7; NbExp=10; IntAct=EBI-9641086, EBI-739361; CC P21333-2; P80217-2: IFI35; NbExp=3; IntAct=EBI-9641086, EBI-12823003; CC P21333-2; Q9UKP3-2: ITGB1BP2; NbExp=3; IntAct=EBI-9641086, EBI-25856470; CC P21333-2; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-9641086, EBI-742916; CC P21333-2; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-9641086, EBI-743960; CC P21333-2; Q53G59: KLHL12; NbExp=6; IntAct=EBI-9641086, EBI-740929; CC P21333-2; Q8TCE9: LGALS14; NbExp=6; IntAct=EBI-9641086, EBI-10274069; CC P21333-2; Q14693: LPIN1; NbExp=3; IntAct=EBI-9641086, EBI-5278370; CC P21333-2; Q8TD91-2: MAGEC3; NbExp=3; IntAct=EBI-9641086, EBI-10694180; CC P21333-2; P02795: MT2A; NbExp=3; IntAct=EBI-9641086, EBI-996616; CC P21333-2; Q9NP98: MYOZ1; NbExp=6; IntAct=EBI-9641086, EBI-744402; CC P21333-2; Q9NQS3: NECTIN3; NbExp=3; IntAct=EBI-9641086, EBI-2826725; CC P21333-2; Q9BRX2: PELO; NbExp=6; IntAct=EBI-9641086, EBI-1043580; CC P21333-2; Q8TCD6: PHOSPHO2; NbExp=3; IntAct=EBI-9641086, EBI-2861380; CC P21333-2; Q9H8W4: PLEKHF2; NbExp=5; IntAct=EBI-9641086, EBI-742388; CC P21333-2; O43741: PRKAB2; NbExp=3; IntAct=EBI-9641086, EBI-1053424; CC P21333-2; Q09028: RBBP4; NbExp=3; IntAct=EBI-9641086, EBI-620823; CC P21333-2; P57052: RBM11; NbExp=3; IntAct=EBI-9641086, EBI-741332; CC P21333-2; Q04864: REL; NbExp=3; IntAct=EBI-9641086, EBI-307352; CC P21333-2; Q6ZTI6: RFLNA; NbExp=3; IntAct=EBI-9641086, EBI-10200920; CC P21333-2; Q6ZTI6-2: RFLNA; NbExp=3; IntAct=EBI-9641086, EBI-12362431; CC P21333-2; Q8N488: RYBP; NbExp=3; IntAct=EBI-9641086, EBI-752324; CC P21333-2; O15127: SCAMP2; NbExp=3; IntAct=EBI-9641086, EBI-712703; CC P21333-2; P08195-4: SLC3A2; NbExp=3; IntAct=EBI-9641086, EBI-12832276; CC P21333-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-9641086, EBI-358489; CC P21333-2; Q13573: SNW1; NbExp=3; IntAct=EBI-9641086, EBI-632715; CC P21333-2; Q9BXN6: SPANXD; NbExp=3; IntAct=EBI-9641086, EBI-10301202; CC P21333-2; P15884: TCF4; NbExp=3; IntAct=EBI-9641086, EBI-533224; CC P21333-2; P04637: TP53; NbExp=3; IntAct=EBI-9641086, EBI-366083; CC P21333-2; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-9641086, EBI-10316321; CC P21333-2; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-9641086, EBI-7705033; CC P21333-2; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-9641086, EBI-12949277; CC P21333-2; Q96E88; NbExp=3; IntAct=EBI-9641086, EBI-10976904; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex CC {ECO:0000269|PubMed:16291724}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:Q8BTM8}. Perikaryon CC {ECO:0000250|UniProtKB:Q8BTM8}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:Q8BTM8}. Note=Colocalizes with CPMR1 in the CC central region of DRG neuron growth cone (By similarity). Following CC SEMA3A stimulation of DRG neurons, colocalizes with F-actin (By CC similarity). {ECO:0000250|UniProtKB:Q8BTM8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P21333-1; Sequence=Displayed; CC Name=2; CC IsoId=P21333-2; Sequence=VSP_035454; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DOMAIN: Comprised of a NH2-terminal actin-binding domain, 24 CC immunoglobulin-like internally homologous repeats and two hinge CC regions. Repeat 24 and the second hinge domain are important for dimer CC formation. Filamin repeat 20 interacts with filamin repeat 21 masking CC the ligand binding site on filamin repeat 21, resulting in an CC autoinhibited conformation (PubMed:17690686). The autoinhibition can be CC relieved by ligands like ITGB7 or FBLIM1 (PubMed:21524097). Filamin CC repeats 19 and 21 can simultaneously engage ligands (PubMed:21524097). CC {ECO:0000269|PubMed:17690686, ECO:0000269|PubMed:21524097}. CC -!- PTM: Phosphorylation at Ser-2152 is negatively regulated by the CC autoinhibited conformation of filamin repeats 19-21. Ligand binding CC induces a conformational switch triggering phosphorylation at Ser-2152 CC by PKA. {ECO:0000269|PubMed:25666618}. CC -!- PTM: Phosphorylation extent changes in response to cell activation. CC -!- PTM: Polyubiquitination in the CH1 domain by a SCF-like complex CC containing ASB2 leads to proteasomal degradation. Prior dissociation CC from actin may be required to expose the target lysines CC (PubMed:24052262). Ubiquitinated in endothelial cells by RNF213 CC downstream of the non-canonical Wnt signaling pathway, leading to its CC degradation by the proteasome (PubMed:26766444). CC {ECO:0000269|PubMed:24052262, ECO:0000269|PubMed:26766444}. CC -!- DISEASE: Periventricular nodular heterotopia 1 (PVNH1) [MIM:300049]: A CC developmental disorder characterized by the presence of periventricular CC nodules of cerebral gray matter, resulting from a failure of neurons to CC migrate normally from the lateral ventricular proliferative zone, where CC they are formed, to the cerebral cortex. PVNH1 is an X-linked dominant CC form. Heterozygous females have normal intelligence but suffer from CC seizures and various manifestations outside the central nervous system, CC especially related to the vascular system. Hemizygous affected males CC die in the prenatal or perinatal period. {ECO:0000269|PubMed:11532987, CC ECO:0000269|PubMed:11914408, ECO:0000269|PubMed:15249610, CC ECO:0000269|PubMed:15668422, ECO:0000269|PubMed:15994863, CC ECO:0000269|PubMed:16299064}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Otopalatodigital syndrome 1 (OPD1) [MIM:311300]: X-linked CC dominant multiple congenital anomalies disease mainly characterized by CC a generalized skeletal dysplasia, mild intellectual disability, hearing CC loss, cleft palate, and typical facial anomalies. OPD1 belongs to a CC group of X-linked skeletal dysplasias known as oto-palato-digital CC syndrome spectrum disorders that also include OPD2, Melnick-Needles CC syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of CC the cytoskeleton is central to the modulation of cell shape and CC migration. FLNA is a widely expressed protein that regulates re- CC organization of the actin cytoskeleton by interacting with integrins, CC transmembrane receptor complexes and second messengers. Males with OPD1 CC have cleft palate, malformations of the ossicles causing deafness and CC milder bone and limb defects than those associated with OPD2. Obligate CC female carriers of mutations causing both OPD1 and OPD2 have variable CC (often milder) expression of a similar phenotypic spectrum. CC {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:15940695, CC ECO:0000269|PubMed:27193221}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Otopalatodigital syndrome 2 (OPD2) [MIM:304120]: Congenital CC bone disorder that is characterized by abnormally modeled, bowed bones, CC small or absent first digits and, more variably, cleft palate, CC posterior fossa brain anomalies, omphalocele and cardiac defects. CC {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:17431908, CC ECO:0000269|PubMed:27193221}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Frontometaphyseal dysplasia 1 (FMD1) [MIM:305620]: An X-linked CC disease characterized by generalized skeletal dysplasia, deafness, and CC urogenital defects. {ECO:0000269|PubMed:12612583, CC ECO:0000269|PubMed:16596676, ECO:0000269|PubMed:27193221}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Melnick-Needles syndrome (MNS) [MIM:309350]: Severe congenital CC bone disorder characterized by typical facies (exophthalmos, full CC cheeks, micrognathia and malalignment of teeth), flaring of the CC metaphyses of long bones, s-like curvature of bones of legs, irregular CC constrictions in the ribs, and sclerosis of base of skull. CC {ECO:0000269|PubMed:12612583, ECO:0000269|PubMed:27193221}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Intestinal pseudoobstruction, neuronal, chronic idiopathic, X- CC linked (IPOX) [MIM:300048]: A disease characterized by a severe CC abnormality of gastrointestinal motility due to primary qualitative CC defects of enteric ganglia and nerve fibers. Affected individuals CC manifest recurrent signs of intestinal obstruction in the absence of CC any mechanical lesion. {ECO:0000269|PubMed:17357080}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- DISEASE: FG syndrome 2 (FGS2) [MIM:300321]: FG syndrome (FGS) is an X- CC linked disorder characterized by intellectual disability, relative CC macrocephaly, hypotonia and constipation. CC {ECO:0000269|PubMed:17632775}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Terminal osseous dysplasia (TOD) [MIM:300244]: A rare X-linked CC dominant male-lethal disease characterized by skeletal dysplasia of the CC limbs, pigmentary defects of the skin and recurrent digital fibroma CC during infancy. A significant phenotypic variability is observed in CC affected females. {ECO:0000269|PubMed:20598277}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Cardiac valvular dysplasia, X-linked (CVDPX) [MIM:314400]: A CC rare X-linked heart disease characterized by mitral and/or aortic valve CC regurgitation. The histologic features include fragmentation of CC collagenous bundles within the valve fibrosa and accumulation of CC proteoglycans, which produces excessive valve tissue leading to CC billowing of the valve leaflets. {ECO:0000269|PubMed:17190868}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Note=Defects in FLNA may be a cause of macrothrombocytopenia, CC a disorder characterized by subnormal levels of blood platelets. Blood CC platelets are abnormally enlarged (PubMed:21960593). CC {ECO:0000269|PubMed:21960593}. CC -!- DISEASE: Congenital short bowel syndrome, X-linked (CSBSX) CC [MIM:300048]: A disease characterized by a shortened small intestine, CC and malabsorption. The mean length of the small intestine in affected CC individuals is approximately 50 cm, compared with a normal length at CC birth of 190-280 cm. It is associated with significant mortality and CC morbidity. Infants usually present with failure to thrive, recurrent CC vomiting, and diarrhea. {ECO:0000269|PubMed:23037936}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC03408.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X53416; CAA37495.1; -; mRNA. DR EMBL; L44140; AAA92644.1; -; Genomic_DNA. DR EMBL; X70082; CAA49687.1; -; Genomic_DNA. DR EMBL; X70085; CAA49690.1; -; Genomic_DNA. DR EMBL; GU727643; ADU87644.1; -; mRNA. DR EMBL; AK090427; BAC03408.2; ALT_INIT; mRNA. DR EMBL; AB593010; BAJ83965.1; -; mRNA. DR EMBL; BX664723; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX936346; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471172; EAW72745.1; -; Genomic_DNA. DR EMBL; CH471172; EAW72746.1; -; Genomic_DNA. DR CCDS; CCDS44021.1; -. [P21333-2] DR CCDS; CCDS48194.1; -. [P21333-1] DR PIR; A37098; A37098. DR RefSeq; NP_001104026.1; NM_001110556.1. [P21333-1] DR RefSeq; NP_001447.2; NM_001456.3. [P21333-2] DR PDB; 2AAV; NMR; -; A=1863-1956. DR PDB; 2BP3; X-ray; 2.32 A; A/B=1863-1956. DR PDB; 2BRQ; X-ray; 2.10 A; A/B=2236-2329. DR PDB; 2J3S; X-ray; 2.50 A; A/B=2045-2329. DR PDB; 2JF1; X-ray; 2.20 A; A=2236-2329. DR PDB; 2K3T; NMR; -; A=2427-2522. DR PDB; 2K7P; NMR; -; A=1772-1956. DR PDB; 2K7Q; NMR; -; A=1954-2141. DR PDB; 2MTP; NMR; -; A=2236-2330. DR PDB; 2W0P; X-ray; 1.90 A; A/B=2236-2329. DR PDB; 2WFN; X-ray; 3.20 A; A/B=1-278. DR PDB; 3CNK; X-ray; 1.65 A; A/B=2559-2647. DR PDB; 3HOC; X-ray; 2.30 A; A/B=2-269. DR PDB; 3HOP; X-ray; 2.30 A; A/B=2-269. DR PDB; 3HOR; X-ray; 2.70 A; A/B=2-269. DR PDB; 3ISW; X-ray; 2.80 A; A/B=2236-2329. DR PDB; 3RGH; X-ray; 2.44 A; A/B=1158-1252. DR PDB; 4M9P; X-ray; 1.72 A; A=478-766. DR PDB; 4P3W; X-ray; 2.00 A; A/B/C/D/E/F=2152-2329. DR PDB; 5XR1; NMR; -; A=2236-2329. DR PDB; 6D8C; EM; 3.54 A; A/B/C/D/E=1-278. DR PDB; 6EW1; X-ray; 2.31 A; A=478-766. DR PDB; 7SC4; X-ray; 1.85 A; A/B=2236-2329. DR PDB; 7SFT; NMR; -; A=2236-2330. DR PDBsum; 2AAV; -. DR PDBsum; 2BP3; -. DR PDBsum; 2BRQ; -. DR PDBsum; 2J3S; -. DR PDBsum; 2JF1; -. DR PDBsum; 2K3T; -. DR PDBsum; 2K7P; -. DR PDBsum; 2K7Q; -. DR PDBsum; 2MTP; -. DR PDBsum; 2W0P; -. DR PDBsum; 2WFN; -. DR PDBsum; 3CNK; -. DR PDBsum; 3HOC; -. DR PDBsum; 3HOP; -. DR PDBsum; 3HOR; -. DR PDBsum; 3ISW; -. DR PDBsum; 3RGH; -. DR PDBsum; 4M9P; -. DR PDBsum; 4P3W; -. DR PDBsum; 5XR1; -. DR PDBsum; 6D8C; -. DR PDBsum; 6EW1; -. DR PDBsum; 7SC4; -. DR PDBsum; 7SFT; -. DR AlphaFoldDB; P21333; -. DR EMDB; EMD-7831; -. DR EMDB; EMD-7832; -. DR EMDB; EMD-7833; -. DR SASBDB; P21333; -. DR SMR; P21333; -. DR BioGRID; 108605; 587. DR ComplexPortal; CPX-117; Glycoprotein Ib-IX-V-Filamin-A complex. DR ComplexPortal; CPX-122; Filamin A homodimer. DR CORUM; P21333; -. DR DIP; DIP-1136N; -. DR IntAct; P21333; 323. DR MINT; P21333; -. DR STRING; 9606.ENSP00000358866; -. DR ChEMBL; CHEMBL4804243; -. DR DrugBank; DB11638; Artenimol. DR MoonDB; P21333; Predicted. DR TCDB; 8.A.66.1.4; the dystrophin (dystrophin) family. DR CarbonylDB; P21333; -. DR GlyCosmos; P21333; 4 sites, 2 glycans. DR GlyGen; P21333; 7 sites, 2 O-linked glycans (7 sites). DR iPTMnet; P21333; -. DR MetOSite; P21333; -. DR PhosphoSitePlus; P21333; -. DR SwissPalm; P21333; -. DR BioMuta; FLNA; -. DR DMDM; 116241365; -. DR OGP; P21333; -. DR CPTAC; CPTAC-508; -. DR CPTAC; CPTAC-509; -. DR EPD; P21333; -. DR jPOST; P21333; -. DR MassIVE; P21333; -. DR MaxQB; P21333; -. DR PaxDb; 9606-ENSP00000358866; -. DR PeptideAtlas; P21333; -. DR PRIDE; P21333; -. DR ProteomicsDB; 53859; -. [P21333-1] DR ProteomicsDB; 53860; -. [P21333-2] DR Pumba; P21333; -. DR ABCD; P21333; 3 sequenced antibodies. DR Antibodypedia; 341; 822 antibodies from 39 providers. DR DNASU; 2316; -. DR Ensembl; ENST00000360319.9; ENSP00000353467.4; ENSG00000196924.19. [P21333-2] DR Ensembl; ENST00000369850.10; ENSP00000358866.3; ENSG00000196924.19. [P21333-1] DR GeneID; 2316; -. DR KEGG; hsa:2316; -. DR MANE-Select; ENST00000369850.10; ENSP00000358866.3; NM_001110556.2; NP_001104026.1. DR UCSC; uc004fkk.3; human. [P21333-1] DR AGR; HGNC:3754; -. DR CTD; 2316; -. DR DisGeNET; 2316; -. DR GeneCards; FLNA; -. DR GeneReviews; FLNA; -. DR HGNC; HGNC:3754; FLNA. DR HPA; ENSG00000196924; Tissue enhanced (endometrium, intestine). DR MalaCards; FLNA; -. DR MIM; 300017; gene. DR MIM; 300048; phenotype. DR MIM; 300049; phenotype. DR MIM; 300244; phenotype. DR MIM; 300321; phenotype. DR MIM; 304120; phenotype. DR MIM; 305620; phenotype. DR MIM; 309350; phenotype. DR MIM; 311300; phenotype. DR MIM; 314400; phenotype. DR neXtProt; NX_P21333; -. DR OpenTargets; ENSG00000196924; -. DR Orphanet; 2301; Congenital short bowel syndrome. DR Orphanet; 555877; FLNA-related X-linked myxomatous valvular dysplasia. DR Orphanet; 1826; Frontometaphyseal dysplasia. DR Orphanet; 2484; Melnick-Needles syndrome. DR Orphanet; 99811; Neuronal intestinal pseudoobstruction. DR Orphanet; 323; NON RARE IN EUROPE: FG syndrome phenotypic spectrum. DR Orphanet; 90650; Otopalatodigital syndrome type 1. DR Orphanet; 90652; Otopalatodigital syndrome type 2. DR Orphanet; 98892; Periventricular nodular heterotopia. DR Orphanet; 88630; Terminal osseous dysplasia-pigmentary defects syndrome. DR Orphanet; 75497; X-linked Ehlers-Danlos syndrome. DR Orphanet; 482606; X-linked keloid scarring-reduced joint mobility-increased optic cup-to-disc ratio syndrome. DR PharmGKB; PA28172; -. DR VEuPathDB; HostDB:ENSG00000196924; -. DR eggNOG; KOG0518; Eukaryota. DR GeneTree; ENSGT00940000153588; -. DR InParanoid; P21333; -. DR OMA; KWADEHI; -. DR OrthoDB; 298396at2759; -. DR PhylomeDB; P21333; -. DR TreeFam; TF313685; -. DR PathwayCommons; P21333; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-430116; GP1b-IX-V activation signalling. DR Reactome; R-HSA-446353; Cell-extracellular matrix interactions. DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs. DR Reactome; R-HSA-8983711; OAS antiviral response. DR SignaLink; P21333; -. DR SIGNOR; P21333; -. DR BioGRID-ORCS; 2316; 14 hits in 785 CRISPR screens. DR ChiTaRS; FLNA; human. DR EvolutionaryTrace; P21333; -. DR GeneWiki; FLNA; -. DR GenomeRNAi; 2316; -. DR Pharos; P21333; Tbio. DR PRO; PR:P21333; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P21333; Protein. DR Bgee; ENSG00000196924; Expressed in right coronary artery and 200 other cell types or tissues. DR ExpressionAtlas; P21333; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:WormBase. DR GO; GO:0005884; C:actin filament; IEA:Ensembl. DR GO; GO:0032432; C:actin filament bundle; IEA:Ensembl. DR GO; GO:0097440; C:apical dendrite; IEA:Ensembl. DR GO; GO:0044295; C:axonal growth cone; IEA:Ensembl. DR GO; GO:0005903; C:brush border; IEA:Ensembl. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; NAS:ComplexPortal. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0031523; C:Myb complex; IDA:MGI. DR GO; GO:0005730; C:nucleolus; IMP:CACAO. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0098794; C:postsynapse; IEA:Ensembl. DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl. DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL. DR GO; GO:0051015; F:actin filament binding; IDA:BHF-UCL. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0034988; F:Fc-gamma receptor I complex binding; IDA:BHF-UCL. DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:UniProtKB. DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB. DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB. DR GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl. DR GO; GO:0031267; F:small GTPase binding; IDA:BHF-UCL. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL. DR GO; GO:0051764; P:actin crosslink formation; IDA:BHF-UCL. DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:BHF-UCL. DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl. DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; NAS:ComplexPortal. DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl. DR GO; GO:0045216; P:cell-cell junction organization; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:BHF-UCL. DR GO; GO:0045022; P:early endosome to late endosome transport; IEA:Ensembl. DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl. DR GO; GO:0045184; P:establishment of protein localization; IDA:BHF-UCL. DR GO; GO:0097368; P:establishment of Sertoli cell barrier; IEA:Ensembl. DR GO; GO:0021943; P:formation of radial glial scaffolds; IEA:Ensembl. DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl. DR GO; GO:0035855; P:megakaryocyte development; NAS:ComplexPortal. DR GO; GO:0090307; P:mitotic spindle assembly; IDA:MGI. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO. DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:BHF-UCL. DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IDA:CACAO. DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB. DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IEA:Ensembl. DR GO; GO:0048680; P:positive regulation of axon regeneration; IEA:Ensembl. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB. DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IMP:CACAO. DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IEA:Ensembl. DR GO; GO:2001224; P:positive regulation of neuron migration; IEA:Ensembl. DR GO; GO:0010572; P:positive regulation of platelet activation; NAS:ComplexPortal. DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:BHF-UCL. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB. DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:CACAO. DR GO; GO:1902396; P:protein localization to bicellular tight junction; IEA:Ensembl. DR GO; GO:0034394; P:protein localization to cell surface; IDA:BHF-UCL. DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL. DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL. DR GO; GO:0043113; P:receptor clustering; IDA:BHF-UCL. DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB. DR GO; GO:1905000; P:regulation of membrane repolarization during atrial cardiac muscle cell action potential; IC:BHF-UCL. DR GO; GO:1905031; P:regulation of membrane repolarization during cardiac muscle cell action potential; ISS:BHF-UCL. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; NAS:ComplexPortal. DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IGI:WormBase. DR GO; GO:0050808; P:synapse organization; IEA:Ensembl. DR GO; GO:0090042; P:tubulin deacetylation; IMP:CACAO. DR GO; GO:0044319; P:wound healing, spreading of cells; IDA:UniProtKB. DR CDD; cd21308; CH_FLNA_rpt1; 1. DR CDD; cd21312; CH_FLNA_rpt2; 1. DR DisProt; DP01950; -. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 2.60.40.10; Immunoglobulins; 24. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. 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; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR PANTHER; PTHR38537; JITTERBUG, ISOFORM N; 1. DR PANTHER; PTHR38537:SF17; JITTERBUG, ISOFORM N; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF00630; Filamin; 24. DR SMART; SM00033; CH; 2. DR SMART; SM00557; IG_FLMN; 24. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF81296; E set domains; 24. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS50194; FILAMIN_REPEAT; 24. DR Genevisible; P21333; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; KW Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; KW Deafness; Direct protein sequencing; Disease variant; Isopeptide bond; KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:25944712" FT CHAIN 2..2647 FT /note="Filamin-A" FT /id="PRO_0000087296" FT DOMAIN 43..149 FT /note="Calponin-homology (CH) 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 166..269 FT /note="Calponin-homology (CH) 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REPEAT 276..374 FT /note="Filamin 1" FT REPEAT 376..474 FT /note="Filamin 2" FT REPEAT 475..570 FT /note="Filamin 3" FT REPEAT 571..663 FT /note="Filamin 4" FT REPEAT 667..763 FT /note="Filamin 5" FT REPEAT 764..866 FT /note="Filamin 6" FT REPEAT 867..965 FT /note="Filamin 7" FT REPEAT 966..1061 FT /note="Filamin 8" FT REPEAT 1062..1154 FT /note="Filamin 9" FT REPEAT 1155..1249 FT /note="Filamin 10" FT REPEAT 1250..1349 FT /note="Filamin 11" FT REPEAT 1350..1442 FT /note="Filamin 12" FT REPEAT 1443..1539 FT /note="Filamin 13" FT REPEAT 1540..1636 FT /note="Filamin 14" FT REPEAT 1649..1740 FT /note="Filamin 15" FT REPEAT 1779..1860 FT /note="Filamin 16" FT REPEAT 1861..1950 FT /note="Filamin 17" FT REPEAT 1951..2039 FT /note="Filamin 18" FT REPEAT 2042..2131 FT /note="Filamin 19" FT REPEAT 2132..2230 FT /note="Filamin 20" FT REPEAT 2233..2325 FT /note="Filamin 21" FT REPEAT 2327..2420 FT /note="Filamin 22" FT REPEAT 2424..2516 FT /note="Filamin 23" FT REPEAT 2552..2646 FT /note="Filamin 24" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..274 FT /note="Actin-binding" FT REGION 271..294 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1361..1382 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1490..1607 FT /note="Interaction with furin" FT /evidence="ECO:0000250" FT REGION 1741..1778 FT /note="Hinge 1" FT REGION 2517..2647 FT /note="Self-association site, tail" FT REGION 2517..2551 FT /note="Hinge 2" FT COMPBIAS 1363..1378 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 1761..1762 FT /note="Cleavage; by calpain" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:25944712" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 376 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 508 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 700 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 781 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 837 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 865 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 906 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 968 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 1055 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1071 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 1071 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 1081 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1084 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1089 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 1301 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1338 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1372 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 1459 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1533 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 1538 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 1630 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1734 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1835 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1967 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 2053 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 2128 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2152 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:25666618, FT ECO:0000269|PubMed:26460884, ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 2158 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 2163 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 2180 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 2284 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 2327 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2329 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 2336 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:25666618, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 2338 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2370 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 2414 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 2510 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2523 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 2526 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 2569 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 2569 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 2575 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 2599 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8BTM8" FT MOD_RES 2607 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 2621 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 42 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:24052262" FT CROSSLNK 43 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:24052262" FT CROSSLNK 135 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:24052262" FT CROSSLNK 299 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 299 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT VAR_SEQ 1649..1656 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_035454" FT VARIANT 39 FT /note="A -> G (in PVNH1; dbSNP:rs137853313)" FT /evidence="ECO:0000269|PubMed:15668422" FT /id="VAR_022734" FT VARIANT 82 FT /note="E -> V (in PVNH1; dbSNP:rs28935169)" FT /evidence="ECO:0000269|PubMed:11914408" FT /id="VAR_015699" FT VARIANT 102 FT /note="M -> V (in PVNH1)" FT /evidence="ECO:0000269|PubMed:15249610" FT /id="VAR_031305" FT VARIANT 128 FT /note="A -> V (in PVNH1; dbSNP:rs137853315)" FT /evidence="ECO:0000269|PubMed:15994863" FT /id="VAR_031306" FT VARIANT 149 FT /note="S -> F (in PVNH1)" FT /evidence="ECO:0000269|PubMed:15249610" FT /id="VAR_031307" FT VARIANT 170 FT /note="Q -> P (in OPD2; dbSNP:rs863223628)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_015713" FT VARIANT 172 FT /note="L -> F (in OPD1)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_015714" FT VARIANT 187 FT /note="N -> S (in OPD2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27193221" FT /id="VAR_076500" FT VARIANT 196 FT /note="R -> G (in OPD2)" FT /evidence="ECO:0000269|PubMed:12612583, FT ECO:0000269|PubMed:27193221" FT /id="VAR_015715" FT VARIANT 196 FT /note="R -> W (in OPD1; dbSNP:rs137853317)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_015716" FT VARIANT 200 FT /note="A -> S (in OPD2)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_015717" FT VARIANT 203 FT /note="D -> Y (in OPD1; dbSNP:rs137853314)" FT /evidence="ECO:0000269|PubMed:15940695" FT /id="VAR_031308" FT VARIANT 207 FT /note="P -> L (in OPD1; dbSNP:rs28935469)" FT /evidence="ECO:0000269|PubMed:12612583, FT ECO:0000269|PubMed:27193221" FT /id="VAR_015700" FT VARIANT 210 FT /note="C -> F (in OPD2; dbSNP:rs137853318)" FT /evidence="ECO:0000269|PubMed:17431908" FT /id="VAR_058720" FT VARIANT 254 FT /note="E -> K (in OPD2; dbSNP:rs28935470)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_015701" FT VARIANT 267 FT /note="A -> T (in OPD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27193221" FT /id="VAR_076501" FT VARIANT 273 FT /note="A -> P (in OPD2)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_015718" FT VARIANT 288 FT /note="G -> R (in CVDPX; dbSNP:rs267606816)" FT /evidence="ECO:0000269|PubMed:17190868" FT /id="VAR_064156" FT VARIANT 320 FT /note="V -> A (in dbSNP:rs1064816)" FT /id="VAR_012831" FT VARIANT 370 FT /note="F -> L (in dbSNP:rs1064817)" FT /id="VAR_012832" FT VARIANT 429 FT /note="T -> M (in dbSNP:rs36051194)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_069803" FT VARIANT 528 FT /note="V -> M (in dbSNP:rs143873938)" FT /evidence="ECO:0000269|PubMed:12410386, FT ECO:0000269|PubMed:20844545" FT /id="VAR_031309" FT VARIANT 552 FT /note="V -> A (in dbSNP:rs730319)" FT /id="VAR_012833" FT VARIANT 555 FT /note="T -> K (in OPD2; dbSNP:rs782611953)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_015719" FT VARIANT 606 FT /note="V -> L (found in a child with developmental FT disabilities; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30500825" FT /id="VAR_085766" FT VARIANT 637 FT /note="P -> Q (in CVDPX; dbSNP:rs267606815)" FT /evidence="ECO:0000269|PubMed:17190868" FT /id="VAR_064157" FT VARIANT 656 FT /note="L -> F (in PVNH1; dbSNP:rs137853311)" FT /evidence="ECO:0000269|PubMed:11532987" FT /id="VAR_012834" FT VARIANT 711 FT /note="V -> D (in CVDPX; dbSNP:rs267606817)" FT /evidence="ECO:0000269|PubMed:17190868" FT /id="VAR_064158" FT VARIANT 804 FT /note="V -> D (in OPD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27193221" FT /id="VAR_076502" FT VARIANT 1012 FT /note="S -> L (in dbSNP:rs17091204)" FT /id="VAR_031310" FT VARIANT 1142 FT /note="D -> V (in FMD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27193221" FT /id="VAR_076503" FT VARIANT 1159 FT /note="D -> A (in FMD1; does not inhibit interaction with FT MIS18BP1; dbSNP:rs28935471)" FT /evidence="ECO:0000269|PubMed:12612583, FT ECO:0000269|PubMed:21228480" FT /id="VAR_015702" FT VARIANT 1163 FT /note="V -> L (in MNS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27193221" FT /id="VAR_076504" FT VARIANT 1184 FT /note="D -> E (in MNS; dbSNP:rs80338837)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_015720" FT VARIANT 1186 FT /note="S -> L (in FMD1; dbSNP:rs137853312)" FT /evidence="ECO:0000269|PubMed:12612583, FT ECO:0000269|PubMed:16596676, ECO:0000269|PubMed:27193221" FT /id="VAR_015721" FT VARIANT 1188 FT /note="A -> T (in MNS; does not inhibit interaction with FT MIS18BP1; dbSNP:rs28935472)" FT /evidence="ECO:0000269|PubMed:12612583, FT ECO:0000269|PubMed:21228480, ECO:0000269|PubMed:27193221" FT /id="VAR_015703" FT VARIANT 1199 FT /note="S -> L (in MNS; does not inhibit interaction with FT MIS18BP1; dbSNP:rs28935473)" FT /evidence="ECO:0000269|PubMed:12612583, FT ECO:0000269|PubMed:21228480" FT /id="VAR_015704" FT VARIANT 1291 FT /note="P -> L (in FGS2; dbSNP:rs137853319)" FT /evidence="ECO:0000269|PubMed:17632775" FT /id="VAR_058721" FT VARIANT 1419 FT /note="A -> G (in dbSNP:rs35504556)" FT /id="VAR_032083" FT VARIANT 1620 FT /note="Missing (in FMD1)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_015722" FT VARIANT 1635..1637 FT /note="Missing (in otopalatodigital spectrum disorder)" FT /evidence="ECO:0000269|PubMed:15654694" FT /id="VAR_031311" FT VARIANT 1645 FT /note="C -> F (in OPD2)" FT /evidence="ECO:0000269|PubMed:12612583" FT /id="VAR_015723" FT VARIANT 1724..1739 FT /note="Missing (in TOD)" FT /evidence="ECO:0000269|PubMed:20598277" FT /id="VAR_064159" FT VARIANT 1728 FT /note="G -> C (in FMD1; dbSNP:rs137853316)" FT /evidence="ECO:0000269|PubMed:16596676" FT /id="VAR_031312" FT VARIANT 1764 FT /note="A -> T (in dbSNP:rs57108893)" FT /evidence="ECO:0000269|PubMed:11532987, FT ECO:0000269|PubMed:12612583" FT /id="VAR_012835" FT VARIANT 1803 FT /note="E -> K (found in a patient with FT macrothrombocytopenia; likely pathogenic; FT dbSNP:rs368750879)" FT /evidence="ECO:0000269|PubMed:21960593" FT /id="VAR_067251" FT VARIANT 1840 FT /note="H -> R (in FMD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27193221" FT /id="VAR_076505" FT VARIANT 2391 FT /note="R -> H (in OPD1; uncertain significance; FT dbSNP:rs727503930)" FT /evidence="ECO:0000269|PubMed:27193221" FT /id="VAR_076506" FT MUTAGEN 42 FT /note="K->R: Abrogates ASB2alpha-mediated degradation FT without altering ASB2alpha binding; when associated with FT R-43 and R-135." FT /evidence="ECO:0000269|PubMed:24052262" FT MUTAGEN 43 FT /note="K->R: Abrogates ASB2alpha-mediated degradation FT without altering ASB2alpha binding; when associated with FT R-42 and R-135." FT /evidence="ECO:0000269|PubMed:24052262" FT MUTAGEN 135 FT /note="K->R: Abrogates ASB2alpha-mediated degradation FT without altering ASB2alpha binding; when associated with FT R-42 and R-43." FT /evidence="ECO:0000269|PubMed:24052262" FT CONFLICT 44 FT /note="I -> T (in Ref. 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1772 FT /note="A -> G (in Ref. 11; CAA49687)" FT /evidence="ECO:0000305" FT CONFLICT 2341 FT /note="Q -> R (in Ref. 5; BAC03408)" FT /evidence="ECO:0000305" FT CONFLICT 2634 FT /note="D -> H (in Ref. 2; CAA37495)" FT /evidence="ECO:0000305" FT HELIX 40..43 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 44..57 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:3HOC" FT TURN 67..73 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 75..85 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 100..116 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 126..130 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 134..149 FT /evidence="ECO:0007829|PDB:3HOC" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:3HOP" FT HELIX 168..179 FT /evidence="ECO:0007829|PDB:3HOC" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:3HOR" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:3HOC" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:3HOR" FT HELIX 196..205 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 221..236 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 244..247 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 254..261 FT /evidence="ECO:0007829|PDB:3HOC" FT HELIX 263..266 FT /evidence="ECO:0007829|PDB:3HOP" FT HELIX 480..482 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 484..487 FT /evidence="ECO:0007829|PDB:4M9P" FT HELIX 488..490 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 501..506 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 515..521 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 529..534 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 537..542 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 548..556 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 565..571 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 579..583 FT /evidence="ECO:0007829|PDB:4M9P" FT HELIX 584..586 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 588..590 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 595..604 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 609..617 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 620..625 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 627..636 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 639..649 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 658..664 FT /evidence="ECO:0007829|PDB:4M9P" FT HELIX 672..674 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 676..679 FT /evidence="ECO:0007829|PDB:4M9P" FT HELIX 680..682 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 683..685 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 693..698 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 707..712 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 714..716 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 721..725 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 727..735 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 739..749 FT /evidence="ECO:0007829|PDB:4M9P" FT STRAND 758..762 FT /evidence="ECO:0007829|PDB:4M9P" FT HELIX 1160..1162 FT /evidence="ECO:0007829|PDB:3RGH" FT STRAND 1164..1167 FT /evidence="ECO:0007829|PDB:3RGH" FT HELIX 1168..1170 FT /evidence="ECO:0007829|PDB:3RGH" FT STRAND 1172..1174 FT /evidence="ECO:0007829|PDB:3RGH" FT STRAND 1179..1184 FT /evidence="ECO:0007829|PDB:3RGH" FT STRAND 1193..1198 FT /evidence="ECO:0007829|PDB:3RGH" FT STRAND 1206..1211 FT /evidence="ECO:0007829|PDB:3RGH" FT STRAND 1213..1222 FT /evidence="ECO:0007829|PDB:3RGH" FT STRAND 1225..1235 FT /evidence="ECO:0007829|PDB:3RGH" FT STRAND 1244..1250 FT /evidence="ECO:0007829|PDB:3RGH" FT TURN 1785..1787 FT /evidence="ECO:0007829|PDB:2K7P" FT STRAND 1791..1796 FT /evidence="ECO:0007829|PDB:2K7P" FT STRAND 1804..1809 FT /evidence="ECO:0007829|PDB:2K7P" FT STRAND 1819..1822 FT /evidence="ECO:0007829|PDB:2K7P" FT STRAND 1824..1832 FT /evidence="ECO:0007829|PDB:2K7P" FT STRAND 1838..1846 FT /evidence="ECO:0007829|PDB:2K7P" FT STRAND 1855..1860 FT /evidence="ECO:0007829|PDB:2K7P" FT STRAND 1865..1867 FT /evidence="ECO:0007829|PDB:2K7P" FT STRAND 1869..1872 FT /evidence="ECO:0007829|PDB:2BP3" FT HELIX 1873..1875 FT /evidence="ECO:0007829|PDB:2BP3" FT STRAND 1877..1879 FT /evidence="ECO:0007829|PDB:2BP3" FT STRAND 1884..1889 FT /evidence="ECO:0007829|PDB:2BP3" FT TURN 1891..1893 FT /evidence="ECO:0007829|PDB:2AAV" FT STRAND 1895..1906 FT /evidence="ECO:0007829|PDB:2BP3" FT STRAND 1909..1914 FT /evidence="ECO:0007829|PDB:2BP3" FT STRAND 1916..1925 FT /evidence="ECO:0007829|PDB:2BP3" FT STRAND 1930..1938 FT /evidence="ECO:0007829|PDB:2BP3" FT STRAND 1947..1953 FT /evidence="ECO:0007829|PDB:2BP3" FT STRAND 1959..1967 FT /evidence="ECO:0007829|PDB:2K7Q" FT STRAND 1980..1988 FT /evidence="ECO:0007829|PDB:2K7Q" FT STRAND 1998..2001 FT /evidence="ECO:0007829|PDB:2K7Q" FT STRAND 2007..2010 FT /evidence="ECO:0007829|PDB:2K7Q" FT STRAND 2014..2025 FT /evidence="ECO:0007829|PDB:2K7Q" FT STRAND 2034..2039 FT /evidence="ECO:0007829|PDB:2K7Q" FT HELIX 2041..2043 FT /evidence="ECO:0007829|PDB:2K7Q" FT HELIX 2047..2049 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2051..2054 FT /evidence="ECO:0007829|PDB:2J3S" FT HELIX 2055..2057 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2059..2061 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2066..2071 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2075..2077 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2080..2088 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2091..2096 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2100..2107 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2112..2120 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2129..2136 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2139..2148 FT /evidence="ECO:0007829|PDB:2J3S" FT STRAND 2161..2165 FT /evidence="ECO:0007829|PDB:4P3W" FT HELIX 2171..2173 FT /evidence="ECO:0007829|PDB:4P3W" FT STRAND 2174..2179 FT /evidence="ECO:0007829|PDB:4P3W" FT STRAND 2185..2187 FT /evidence="ECO:0007829|PDB:4P3W" FT STRAND 2189..2192 FT /evidence="ECO:0007829|PDB:4P3W" FT STRAND 2194..2201 FT /evidence="ECO:0007829|PDB:4P3W" FT STRAND 2208..2216 FT /evidence="ECO:0007829|PDB:4P3W" FT STRAND 2225..2229 FT /evidence="ECO:0007829|PDB:4P3W" FT STRAND 2234..2236 FT /evidence="ECO:0007829|PDB:4P3W" FT HELIX 2238..2240 FT /evidence="ECO:0007829|PDB:7SC4" FT STRAND 2242..2245 FT /evidence="ECO:0007829|PDB:7SC4" FT HELIX 2246..2248 FT /evidence="ECO:0007829|PDB:7SC4" FT STRAND 2251..2253 FT /evidence="ECO:0007829|PDB:5XR1" FT STRAND 2257..2262 FT /evidence="ECO:0007829|PDB:7SC4" FT TURN 2264..2266 FT /evidence="ECO:0007829|PDB:7SC4" FT STRAND 2268..2279 FT /evidence="ECO:0007829|PDB:7SC4" FT STRAND 2282..2287 FT /evidence="ECO:0007829|PDB:7SC4" FT STRAND 2289..2298 FT /evidence="ECO:0007829|PDB:7SC4" FT STRAND 2303..2311 FT /evidence="ECO:0007829|PDB:7SC4" FT TURN 2316..2318 FT /evidence="ECO:0007829|PDB:5XR1" FT STRAND 2320..2326 FT /evidence="ECO:0007829|PDB:7SC4" FT TURN 2429..2431 FT /evidence="ECO:0007829|PDB:2K3T" FT STRAND 2433..2436 FT /evidence="ECO:0007829|PDB:2K3T" FT HELIX 2437..2439 FT /evidence="ECO:0007829|PDB:2K3T" FT STRAND 2441..2443 FT /evidence="ECO:0007829|PDB:2K3T" FT STRAND 2448..2453 FT /evidence="ECO:0007829|PDB:2K3T" FT TURN 2455..2457 FT /evidence="ECO:0007829|PDB:2K3T" FT STRAND 2462..2470 FT /evidence="ECO:0007829|PDB:2K3T" FT STRAND 2472..2479 FT /evidence="ECO:0007829|PDB:2K3T" FT STRAND 2482..2489 FT /evidence="ECO:0007829|PDB:2K3T" FT STRAND 2491..2506 FT /evidence="ECO:0007829|PDB:2K3T" FT STRAND 2511..2518 FT /evidence="ECO:0007829|PDB:2K3T" FT STRAND 2561..2564 FT /evidence="ECO:0007829|PDB:3CNK" FT HELIX 2565..2567 FT /evidence="ECO:0007829|PDB:3CNK" FT STRAND 2576..2581 FT /evidence="ECO:0007829|PDB:3CNK" FT STRAND 2590..2595 FT /evidence="ECO:0007829|PDB:3CNK" FT STRAND 2597..2599 FT /evidence="ECO:0007829|PDB:3CNK" FT STRAND 2602..2610 FT /evidence="ECO:0007829|PDB:3CNK" FT STRAND 2613..2619 FT /evidence="ECO:0007829|PDB:3CNK" FT STRAND 2624..2632 FT /evidence="ECO:0007829|PDB:3CNK" FT STRAND 2641..2646 FT /evidence="ECO:0007829|PDB:3CNK" SQ SEQUENCE 2647 AA; 280739 MW; 6C1A07041DF50142 CRC64; MSSSHSRAGQ SAAGAAPGGG VDTRDAEMPA TEKDLAEDAP WKKIQQNTFT RWCNEHLKCV SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR QMQLENVSVA LEFLDRESIK LVSIDSKAIV DGNLKLILGL IWTLILHYSI SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL PQLPITNFSR DWQSGRALGA LVDSCAPGLC PDWDSWDASK PVTNAREAMQ QADDWLGIPQ VITPEEIVDP NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV TGTHKVTVLF AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK TTYFEIFTAG AGTGEVEVVI QDPMGQKGTV EPQLEARGDS TYRCSYQPTM EGVHTVHVTF AGVPIPRSPY TVTVGQACNP SACRAVGRGL QPKGVRVKET ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF EYYPMVPGTY IVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGV VGKSADFVVE AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN SEDIRLSPFM ADIRDAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK HGGKAPLRVQ VQDNEGCPVE ALVKDNGNGT YSCSYVPRKP VKHTAMVSWG GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA KTGLKAHEPT YFTVDCAEAG QGDVSIGIKC APGVVGPAEA DIDFDIIRND NDTFTVKYTP RGAGSYTIMV LFADQATPTS PIRVKVEPSH DASKVKAEGP GLSRTGVELG KPTHFTVNAK AAGKGKLDVQ FSGLTKGDAV RDVDIIDHHD NTYTVKYTPV QQGPVGVNVT YGGDPIPKSP FSVAVSPSLD LSKIKVSGLG EKVDVGKDQE FTVKSKGAGG QGKVASKIVG PSGAAVPCKV EPGLGADNSV VRFLPREEGP YEVEVTYDGV PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG SAGSPARFTI DTKGAGTGGL GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF ADTHIPGSPF KAHVVPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE PAVDTSGVQC YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP SGNLTETYVQ DRGDGMYKVE YTPYEEGLHS VDVTYDGSPV PSSPFQVPVT EGCDPSRVRV HGPGIQSGTT NKPNKFTVET RGAGTGGLGL AVEGPSEAKM SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV PVHDVTDASK VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV DNADGTQTVN YVPSREGPYS ISVLYGDEEV PRSPFKVKVL PTHDASKVKA SGPGLNTTGV PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH DGTYTVAYVP DVTGRYTILI KYGGDEIPFS PYRVRAVPTG DASKCTVTVS IGGHGLGAGI GPTIQIGEET VITVDTKAAG KGKVTCTVCT PDGSEVDVDV VENEDGTFDI FYTAPQPGKY VICVRFGGEH VPNSPFQVTA LAGDQPSVQP PLRSQQLAPQ YTYAQGGQQT WAPERPLVGV NGLDVTSLRP FDLVIPFTIK KGEITGEVRM PSGKVAQPTI TDNKDGTVTV RYAPSEAGLH EMDIRYDNMH IPGSPLQFYV DYVNCGHVTA YGPGLTHGVV NKPATFTVNT KDAGEGGLSL AIEGPSKAEI SCTDNQDGTC SVSYLPVLPG DYSILVKYNE QHVPGSPFTA RVTGDDSMRM SHLKVGSAAD IPINISETDL SLLTATVVPP SGREEPCLLK RLRNGHVGIS FVPKETGEHL VHVKKNGQHV ASSPIPVVIS QSEIGDASRV RVSGQGLHEG HTFEPAEFII DTRDAGYGGL SLSIEGPSKV DINTEDLEDG TCRVTYCPTE PGNYIINIKF ADQHVPGSPF SVKVTGEGRV KESITRRRRA PSVANVGSHC DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI RFVPAEMGTH TVSVKYKGQH VPGSPFQFTV GPLGEGGAHK VRAGGPGLER AEAGVPAEFS IWTREAGAGG LAIAVEGPSK AEISFEDRKD GSCGVAYVVQ EPGDYEVSVK FNEEHIPDSP FVVPVASPSG DARRLTVSSL QESGLKVNQP ASFAVSLNGA KGAIDAKVHS PSGALEECYV TEIDQDKYAV RFIPRENGVY LIDVKFNGTH IPGSPFKIRV GEPGHGGDPG LVSAYGAGLE GGVTGNPAEF VVNTSNAGAG ALSVTIDGPS KVKMDCQECP EGYRVTYTPM APGSYLISIK YGGPYHIGGS PFKAKVTGPR LVSNHSLHET SSVFVDSLTK ATCAPQHGAP GPGPADASKV VAKGLGLSKA YVGQKSSFTV DCSKAGNNML LVGVHGPRTP CEEILVKHVG SRLYSVSYLL KDKGEYTLVV KWGDEHIPGS PYRVVVP //