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Genet.2475-477VARIANT MFS SER-2144Mutation screening of complete fibrillin-1 coding sequence: report of five new mutations, including two in 8-cysteine domains.Tynan K.Comeau K.Pearson M.Wilgenbus P.Levitt D.Gasner C.Berg M.A.Miller D.C.Francke U.doi:10.1093/hmg/2.11.18131993Hum. Mol. Genet.21813-1821VARIANTS MFS ARG-862; TYR-1117; PRO-1137 AND PHE-1589VARIANT ALA-1148A compound-heterozygous Marfan patient: two defective fibrillin alleles result in a lethal phenotype.Karttunen L.Raghunath M.Loennqvist L.Peltonen L.1994Am. J. Hum. Genet.551083-1091VARIANTS MFS GLY-217 AND ARG-2627A novel mutation of the fibrillin gene causing ectopia lentis.Lonnqvist L.Child A.Kainulainen K.Davidson R.Puhakka L.Peltonen L.doi:10.1006/geno.1994.11101994Genomics19573-576VARIANT ECTOL1 LYS-2447Two novel mutations and a neutral polymorphism in EGF-like domains of the fibrillin gene (FBN1): SSCP screening of exons 15-21 in Marfan syndrome patients.Hayward C.Rae A.L.Porteous M.E.M.Logie L.J.Brock L.J.doi:10.1093/hmg/3.2.3731994Hum. Mol. Genet.3373-375VARIANT MFS CYS-627Substitution of a cysteine residue in a non-calcium binding, EGF-like domain of fibrillin segregates with the Marfan syndrome in a large kindred.Piersall L.D.Dietz H.C.Hall B.D.Cadle R.G.Pyeritz R.E.Francomano C.A.McIntosh I.doi:10.1093/hmg/3.6.10131994Hum. Mol. Genet.31013-1014VARIANT MFS GLY-476Identification of a novel nonsense mutation in the fibrillin gene (FBN1) using nonisotopic techniques.Hayward C.Porteous M.E.Brock D.J.doi:10.1002/humu.13800302121994Hum. Mutat.3159-162VARIANT 2776-ARG--LEU-2781 DELAn extra cysteine in one of the non-calcium-binding epidermal growth factor-like motifs of the FBN1 polypeptide is connected to a novel variant of Marfan syndrome.Stahl-Hallengren C.Ukkonen T.Kainulainen K.Kristofersson U.Saxne T.Tornqvist K.Peltonen L.doi:10.1172/jci1173891994J. Clin. Invest.94709-713VARIANT MFS CYS-122A new missense mutation of fibrillin in a patient with Marfan syndrome.Hewett D.R.Lynch J.R.Child A.Sykes B.C.doi:10.1136/jmg.31.4.3381994J. Med. Genet.31338-339VARIANT MFS TYR-1223A novel mutation in the fibrillin gene (FBN1) in familial arachnodactyly.Hayward C.Porteous M.E.M.Brock D.J.H.doi:10.1006/mcpr.1994.10451994Mol. Cell. Probes8325-327VARIANT MFS HIS-1170Mutations in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome.Kainulainen K.Karttunen L.Puhakka L.Sakai L.Peltonen L.doi:10.1038/ng0194-641994Nat. Genet.664-69VARIANTS MFS GLY-217; ASN-1023; ARG-1074; TYR-1242; ARG-1513; GLU-2127; TRP-2151; LYS-2447 AND ARG-2511A Gly1127Ser mutation in an EGF-like domain of the fibrillin-1 gene is a risk factor for ascending aortic aneurysm and dissection.Francke U.Berg M.A.Tynan K.Brenn T.Liu W.Aoyama T.Gasner C.Miller D.C.Furthmayr H.1995Am. J. Hum. Genet.561287-1296VARIANT MFS SER-1127Fifteen novel FBN1 mutations causing Marfan syndrome detected by heteroduplex analysis of genomic amplicons.Nijbroek G.Sood S.McIntosh I.Francomano C.A.Bull E.Pereira L.Ramirez F.Pyeritz R.E.Dietz H.C.1995Am. J. Hum. Genet.578-21VARIANTS MFS TYR-129; PHE-166; CYS-746; ARG-926; ARG-1013; LYS-1073; SER-1382 AND ARG-1928The phenotypic continuum associated with FBN1 mutations includes the Shprintzen-Goldberg syndrome.Dietz H.C.Sood I.McIntosh I.1995Am. J. Hum. Genet.57A211VARIANT MFS TYR-1223A mutation in FBN1 disrupts profibrillin processing and results in isolated skeletal features of the Marfan syndrome.Milewicz D.M.Grossfield J.Cao S.-N.Kielty C.Covitz W.Jewett T.doi:10.1172/jci1179301995J. Clin. Invest.952373-2378VARIANT TRP-2726CHARACTERIZATION OF VARIANT TRP-2726INVOLVEMENT IN MFSDelineation of the Marfan phenotype associated with mutations in exons 23-32 of the FBN1 gene.Putnam E.A.Cho M.Zinn A.B.Towbin J.A.Byers P.H.Milewicz D.M.doi:10.1002/(sici)1096-8628(19960329)62:3<233::aid-ajmg7>3.0.co;2-u1996Am. J. Med. Genet.62233-242VARIANTS MFS ARG-1053; GLY-1072; LYS-1073 AND GLY-1117Characterisation of four novel fibrillin-1 (FBN1) mutations in Marfan syndrome.Ades L.C.Haan E.A.Colley A.F.Richards R.I.doi:10.1136/jmg.33.8.6651996J. Med. Genet.33665-671VARIANTS MFS THR-705; TYR-711; GLY-1055 AND TYR-1153A novel de novo mutation in exon 14 of the fibrillin-1 gene associated with delayed secretion of fibrillin in a patient with a mild Marfan phenotype.Booms P.Withers A.P.Boxer M.Kaufmann U.C.Hagemeier C.Vetter U.Robinson P.N.doi:10.1007/s0043900504891997Hum. Genet.100195-200VARIANT MFS TYR-587The pathogenicity of the Pro1148Ala substitution in the FBN1 gene: causing or predisposing to Marfan syndrome and aortic aneurysm, or clinically innocent?Schrijver I.Liu W.Francke U.doi:10.1007/s0043900504141997Hum. Genet.99607-611VARIANT ALA-1148Mutation screening of all 65 exons of the fibrillin-1 gene in 60 patients with Marfan syndrome: report of 12 novel mutations.Hayward C.Porteous M.E.M.Brock D.J.H.doi:10.1002/(sici)1098-1004(1997)10:4<280::aid-humu3>3.0.co;2-l1997Hum. Mutat.10280-289VARIANTS MFS ARG-111; CYS-545; CYS-627; GLY-750; ARG-1074; HIS-1170; TRP-1171; LYS-1173; TYR-1404; GLY-1610; LYS-1893; TRP-2099; TYR-2111; ARG-2258; TRP-2282 AND ARG-2489P1148A in fibrillin-1 is not a mutation leading to Shprintzen-Goldberg syndrome.Watanabe Y.Yano S.Koga Y.Yukizane S.Nishiyori A.Yoshino M.Kato H.doi:10.1002/(sici)1098-1004(1997)10:4<326::aid-humu10>3.0.co;2-11997Hum. Mutat.10326-327VARIANT ALA-1148Fibrillin-1 mutations in Marfan syndrome and other type-1 fibrillinopathies.Hayward C.Brock D.J.H.doi:10.1002/(sici)1098-1004(1997)10:6<415::aid-humu1>3.0.co;2-c1997Hum. Mutat.10415-423VARIANTS MFS ARG-996; THR-1048; THR-1048 DEL; CYS-1058 INS; TRP-1086; SER-1837 AND CYS-2680P1148A in fibrillin-1 is not a mutation anymore.Wang M.Mathews K.R.Imaizumi K.Beiraghi S.Blumberg B.Scheuner M.Graham J.M. Jr.Godfrey M.doi:10.1038/ng0197-121997Nat. Genet.1512VARIANT ALA-1148Marfan Database (second edition): software and database for the analysis of mutations in the human FBN1 gene.Collod-Beroud G.Beroud C.Ades L.Black C.Boxer M.Brock D.J.Godfrey M.Hayward C.Karttunen L.Milewicz D.Peltonen L.Richards R.I.Wang W.Junien C.Boileau C.doi:10.1093/nar/25.1.1471997Nucleic Acids Res.25147-150VARIANTS MFS ARG-661; ARG-1043 AND ARG-2511Multiple molecular mechanisms underlying subdiagnostic variants of Marfan syndrome.Montgomery R.A.Geraghty M.T.Bull E.Gelb B.D.Johnson M.McIntosh I.Francomano C.A.Dietz H.C.doi:10.1086/3021441998Am. J. Hum. Genet.631703-1711VARIANT MFS ARG-1265Correlation of a recurrent FBN1 mutation (R122C) with an atypical familial Marfan syndrome phenotype.Black C.Withers A.P.Gray J.R.Bridges A.B.Craig A.Baty D.U.Boxer M.doi:10.1002/humu.13801101641998Hum. Mutat. Suppl.1S198-S200VARIANT MFS CYS-122A novel mutation in the neonatal region of the fibrillin (FBN) 1 gene associated with a classical phenotype of Marfan syndrome (MfS).Grau U.Klein H.-G.Detter C.Mair H.Welz A.Seidel D.Reichart B.doi:10.1002/(sici)1098-1004(1998)12:2%3c137::aid-humu14%3e3.0.co;2-p1998Hum. Mutat.12137VARIANT MFS ILE-984Demonstration of the recurrence of Marfan-like skeletal and cardiovascular manifestations due to germline mosaicism for an FBN1 mutation.Collod-Beroud G.Lackmy-Port-Lys M.Jondeau G.Mathieu M.Maingourd Y.Coulon M.Guillotel M.Junien C.Boileau C.doi:10.1086/3025451999Am. J. Hum. Genet.65917-921VARIANT MFS GLU-985Identification of 9 novel FBN1 mutations in German patients with Marfan syndrome.El-Aleem A.A.Karck M.Haverich A.Schmidtke J.Arslan-Kirchner M.doi:10.1002/(sici)1098-1004(1999)14:2<181::aid-humu10>3.0.co;2-61999Hum. Mutat.14181VARIANTS MFS PHE-504; TYR-1129; CYS-1261; SER-1833 AND TYR-2142Genotype and phenotype analysis of 171 patients referred for molecular study of the fibrillin-1 gene FBN1 because of suspected Marfan syndrome.Loeys B.Nuytinck L.Delvaux I.De Bie S.De Paepe A.doi:10.1001/archinte.161.20.24472001Arch. Intern. Med.1612447-2454VARIANTS MFS PHE-89; CYS-122; CYS-240; CYS-366; CYS-545; SER-560; TYR-570; ASP-592; TRP-598; TYR-776; ARG-781; GLY-913; ARG-985; ARG-1013; TRP-1055; TYR-1055; CYS-1101; PRO-1337; TYR-1339; SER-1429; PRO-1790; TYR-1791; TYR-1835; THR-1909; SER-1915; TYR-1971; TYR-1977; HIS-2223; TRP-2282; TYR-2406; PHE-2581; THR-2585; ARG-2618; LYS-2624 AND CYS-2668VARIANTS ECTOL1 CYS-1530 AND ARG-2154VARIANT MITRAL VALVE PROLAPSE ILE-1128TGGE screening of the entire FBN1 coding sequence in 126 individuals with Marfan syndrome and related fibrillinopathies.Katzke S.Booms P.Tiecke F.Palz M.Pletschacher A.Turkmen S.Neumann L.M.Pregla R.Leitner C.Schramm C.Lorenz P.Hagemeier C.Fuchs J.Skovby F.Rosenberg T.Robinson P.N.doi:10.1002/humu.101122002Hum. Mutat.20197-208VARIANTS MFS CYS-62; TYR-587; TYR-596; ASN-654; TYR-681; ARG-683; TRP-685; VAL-723; PHE-734; TYR-748; GLY-776; ARG-781; ARG-908; GLY-921; PRO-1790; SER-1806; VAL-1931 DEL; TYR-1998; GLY-2221; THR-2269 AND TRP-2335VARIANTS ECTOL1 CYS-115; TYR-661 AND TYR-2339VARIANT MET-2101Mutation screening of the fibrillin-1 (FBN1) gene in 76 unrelated patients with Marfan syndrome or Marfanoid features leads to the identification of 11 novel and three previously reported mutations.Rommel K.Karck M.Haverich A.Schmidtke J.Arslan-Kirchner M.doi:10.1002/humu.90752002Hum. Mutat.20406-407VARIANTS MFS 429-ARG--HIS-2871 DEL; ILE-449; SER-880; CYS-1101; TYR-1806; ILE-1908; ASP-1919 AND ARG-2251Sensitivity of conformation sensitive gel electrophoresis in detecting mutations in Marfan syndrome and related conditions.Koerkkoe J.Kaitila I.Loennqvist L.Peltonen L.Ala-Kokko L.doi:10.1136/jmg.39.1.342002J. Med. Genet.3934-41VARIANTS MFS CYS-114; ARG-890; GLY-1200; TYR-1835; ARG-2111; CYS-2474 AND GLY-2652VARIANT ECTOL1 CYS-240Twelve novel FBN1 mutations in Marfan syndrome and Marfan related phenotypes test the feasibility of FBN1 mutation testing in clinical practice.Halliday D.J.Hutchinson S.Lonie L.Hurst J.A.Firth H.Handford P.A.Wordsworth P.doi:10.1136/jmg.39.8.5892002J. Med. Genet.39589-593VARIANTS MFS CYS-627; ASN-654; TYR-748; 1541-ARG--HIS-2871 DEL; TYR-1835; ARG-1977; TYR-2258; 2394-ARG--HIS-2871 DEL; 2466-TYR--HIS-2871 DEL AND 2467-GLN--HIS-2871 DELVARIANT PRO-2780In frame fibrillin-1 gene deletion in autosomal dominant Weill-Marchesani syndrome.Faivre L.Gorlin R.J.Wirtz M.K.Godfrey M.Dagoneau N.Samples J.R.Le Merrer M.Collod-Beroud G.Boileau C.Munnich A.Cormier-Daire V.doi:10.1136/jmg.40.1.342003J. Med. Genet.4034-36VARIANT WMS2 1692-ARG--TYR-1699 DELDetection of thirty novel FBN1 mutations in patients with Marfan syndrome or a related fibrillinopathy.Biggin A.Holman K.Brett M.Bennetts B.Ades L.doi:10.1002/humu.92072004Hum. Mutat.2399VARIANTS MFS SER-154; SER-166; CYS-240; SER-652; THR-705; TYR-711; SER-816; ARG-1013; TYR-1044; GLY-1055; CYS-1101; TYR-1117; TYR-1153; ASN-1155; GLN-1325; LYS-1366; SER-1374; ARG-1389; 1394-GLY--THR-1396 DEL; ALA-1424; CYS-1530; TYR-1564; PHE-1770; TRP-1793; GLU-1796; TRP-2442; THR-2585 AND PRO-2623Consequences of cysteine mutations in calcium-binding epidermal growth factor modules of fibrillin-1.Vollbrandt T.Tiedemann K.El-Hallous E.Lin G.Brinckmann J.John H.Baetge B.Notbohm H.Reinhardt D.P.doi:10.1074/jbc.m4052392002004J. Biol. Chem.27932924-32931CHARACTERIZATION OF VARIANTS MFS CYS-627; GLY-750 AND ARG-926Identification of sixty-two novel and twelve known FBN1 mutations in eighty-one unrelated probands with Marfan syndrome and other fibrillinopathies.Arbustini E.Grasso M.Ansaldi S.Malattia C.Pilotto A.Porcu E.Disabella E.Marziliano N.Pisani A.Lanzarini L.Mannarino S.Larizza D.Mosconi M.Antoniazzi E.Zoia M.C.Meloni G.Magrassi L.Brega A.Bedeschi M.F.Torrente I.Mari F.Tavazzi L.doi:10.1002/humu.93772005Hum. Mutat.26494VARIANTS MFS CYS-20; TYR-123; ARG-177; ARG-224; GLY-439; 629-VAL--GLY-633 DEL; CYS-635; ILE-636; TYR-832; GLY-890; ASP-1058; SER-1153; PHE-1211 DEL; CYS-1219; ASP-1261; SER-1278; SER-1333; ARG-1402; SER-1424; PHE-1564; GLY-1631; TYR-1663; TYR-1876; ILE-1887; ARG-1895; TYR-1900; PRO-2160; PHE-2221; THR-2385; ARG-2500; TYR-2500; TRP-2535; LYS-2570; ARG-2571; SER-2592; LYS-2610 AND CYS-2629Identification of 29 novel and nine recurrent fibrillin-1 (FBN1) mutations and genotype-phenotype correlations in 76 patients with Marfan syndrome.Rommel K.Karck M.Haverich A.von Kodolitsch Y.Rybczynski M.Muller G.Singh K.K.Schmidtke J.Arslan-Kirchner M.doi:10.1002/humu.202392005Hum. Mutat.26529-539VARIANTS MFS ASN-507 DEL; TYR-541; CYS-627; TYR-781; ARG-985; ARG-1013; VAL-1113; GLY-1284; SER-1475; GLU-1475; THR-1576; ARG-1791; GLY-1928; TYR-1928; TYR-2038; ARG-2085; SER-2144; ARG-2536 AND TYR-2605The importance of mutation detection in Marfan syndrome and Marfan-related disorders: report of 193 FBN1 mutations.Comeglio P.Johnson P.Arno G.Brice G.Evans A.Aragon-Martin J.da Silva F.P.Kiotsekoglou A.Child A.doi:10.1002/humu.95052007Hum. Mutat.28928VARIANTS MFS CYS-122; SER-214; 248-ASP--HIS-2871 DEL; 351-GLN--HIS-2871 DEL; ARG-365; 366-TRP--HIS-2871 DEL; TRP-474; CYS-545; TRP-546; 565-ARG--HIS-2871 DEL; TYR-727; CYS-828; TYR-832; 861-ARG--HIS-2871 DEL; VAL-882; CYS-974; HIS-976; 994-GLU--HIS-2871 DEL; TYR-1032; THR-1048; TYR-1074; ILE-1088; 1125-ARG--HIS-2871 DEL; TYR-1138; 1140-CYS--HIS-2871 DEL; GLY-1158; HIS-1170; ARG-1223; ARG-1249; TYR-1307; ARG-1326; LEU-1346; LYS-1366; TYR-1402; ALA-1424; ASP-1427; ARG-1485; TYR-1528; 1541-ARG--HIS-2871 DEL; ARG-1622; TYR-1720; TYR-1793; VAL-1796; SER-1806; LYS-1811; CYS-1830; PHE-1835; TRP-1847; ASP-1879; ARG-1987; 2053-CYS--HIS-2871 DEL; MET-2118; GLU-2127; ASP-2144; PRO-2145; TYR-2153; THR-2185; 2220-ARG--HIS-2871 DEL; THR-2269; TRP-2274; LYS-2447; ARG-2489; MET-2520; ARG-2536; 2542-GLN--HIS-2871 DEL; VAL-2555; 2571-CYS--HIS-2871 DEL; TYR-2577; THR-2585; LYS-2610 AND ARG-2618VARIANTS ECTOL1 CYS-63; SER-68; CYS-240; TRP-365; CYS-545; ARG-596; PRO-634; VAL-882; 1086-CYS--HIS-2871 DEL; ASN-1155; ARG-1692 DEL; GLY-2250; CYS-2272; LYS-2447 AND ARG-2448VARIANTS ASP-127; ARG-160; SER-164; 215-ARG--HIS-2871 DEL; 364-ARG--HIS-2871 DEL; ARG-504; TYR-652; 653-VAL--HIS-2871 DEL; 752-SER--HIS-2871 DEL; CYS-954; 966-GLU--HIS-2871 DEL; 988-TRP--HIS-2871 DEL; GLY-1028; GLY-1406; SER-1633; 1644-ARG--HIS-2871 DEL; PHE-1777; 1796-GLY--HIS-2871 DEL; TYR-1812; SER-1907; HIS-1930; LYS-2105; ASP-2136; 2169-GLU--HIS-2871 DEL; ARG-2195; PRO-2224; 2229-GLU--HIS-2871 DEL; MET-2234; THR-2273; TRP-2289; TYR-2302; TYR-2365; TRP-2470; ILE-2516; SER-2526; PHE-2541; TRP-2554; TRP-2726 AND 2840-LYS--HIS-2871 DELFBN1 mutation screening of patients with Marfan syndrome and related disorders: detection of 46 novel FBN1 mutations.Attanasio M.Lapini I.Evangelisti L.Lucarini L.Giusti B.Porciani M.Fattori R.Anichini C.Abbate R.Gensini G.Pepe G.doi:10.1111/j.1399-0004.2008.01007.x2008Clin. Genet.7439-46VARIANTS MFS TYR-123; SER-136; SER-177; TYR-177; SER-214; 348-GLN--HIS-2871 DEL; 429-ARG--HIS-2871 DEL; ARG-488; TYR-576; ARG-582; PHE-623; CYS-635; TYR-684; CYS-721; ARG-816; SER-880; GLU-884; TYR-1008; SER-1042; 1125-ARG--HIS-2871 DEL; 1136-TYR--HIS-2871 DEL; TRP-1182; TYR-1265; ARG-1320; 1534-CYS--HIS-2871 DEL; 1539-ARG--HIS-2871 DEL; 1541-ARG--HIS-2871 DEL; GLY-1631; ARG-1672; TYR-1672; GLY-1674; 1735-GLN--HIS-2871 DEL; LYS-1811; ARG-1847; TYR-1860; LYS-1894; TYR-1900; GLY-1934; TRP-1977; 2057-ARG--HIS-2871 DEL; 2062-TYR--HIS-2871 DEL; 2064-LYS--HIS-2871 DEL; TYR-2084; LYS-2130; ARG-2221; TYR-2232; THR-2269; THR-2284; TYR-2470; PRO-2561; LYS-2570; ARG-2577 AND 2694-ARG--HIS-2871 DELVARIANTS PRO-39; ARG-937; ALA-1020; TRP-2726 AND 2774-LYS--HIS-2871 DELIdentification of novel FBN1 and TGFBR2 mutations in 65 probands with Marfan syndrome or Marfan-like phenotypes.Chung B.H.Lam S.T.Tong T.M.Li S.Y.Lun K.S.Chan D.H.Fok S.F.Or J.S.Smith D.K.Yang W.Lau Y.L.doi:10.1002/ajmg.a.329182009Am. J. Med. Genet. A149A1452-1459VARIANTS MFS ASP-57; TYR-100; TYR-129; 861-ARG--HIS-2871 DEL; HIS-910; 921-CYS--HIS-2871 DEL; PRO-1130; 1790-ARG--HIS-2871 DEL; ARG-1812; SER-1826; TRP-2084; LYS-2130; SER-2144; 2298-LYS--HIS-2871 DEL; TYR-2522 AND SER-2708Identification of the minimal combination of clinical features in probands for efficient mutation detection in the FBN1 gene.Stheneur C.Collod-Beroud G.Faivre L.Buyck J.F.Gouya L.Le Parc J.M.Moura B.Muti C.Grandchamp B.Sultan G.Claustres M.Aegerter P.Chevallier B.Jondeau G.Boileau C.doi:10.1038/ejhg.2009.362009Eur. J. Hum. Genet.171121-1128VARIANT 2867-GLN--HIS-2871 DELCentral nervous system abnormalities in two cases with neonatal Marfan syndrome with novel mutations in the fibrillin-1 gene.Barnett C.P.Wilson G.J.Chiasson D.A.Gross G.J.Hinek A.Hawkins C.Chitayat D.doi:10.1002/ajmg.a.334062010Am. J. Med. Genet. A1522409-2412VARIANT MFS GLY-1068Identification of a novel lethal fibrillin-1 gene mutation in a Chinese Marfan family and correlation of 3' fibrillin-1 gene mutations with phenotype.Gao L.G.Zhang L.Song L.Wang H.Chang Q.Wu Y.B.Hui R.T.Zhou X.L.2010Chin. Med. J.1232874-2878VARIANT 2849-TYR--HIS-2871 DELPaucity of skeletal manifestations in Hispanic families with FBN1 mutations.Villamizar C.Regalado E.S.Fadulu V.T.Hasham S.N.Gupta P.Willing M.C.Kuang S.Q.Guo D.Muilenburg A.Yee R.W.Fan Y.Towbin J.Coselli J.S.LeMaire S.A.Milewicz D.M.doi:10.1016/j.ejmg.2009.11.0012010Eur. J. Med. Genet.5380-84VARIANTS MFS 515-CYS-ARG-516 DELINS TRP-GLY AND CYS-1530A Japanese-specific allele in the GALNT11 gene.Yuasa I.Umetsu K.Matsusue A.Nishimukai H.Harihara S.Fukumori Y.Saitou N.Jin F.Chattopadhyay P.K.Henke L.Henke J.doi:10.1016/j.legalmed.2010.04.0012010Leg. Med.12208-211VARIANT ALA-1148Mutations in fibrillin-1 cause congenital scleroderma: stiff skin syndrome.Loeys B.L.Gerber E.E.Riegert-Johnson D.Iqbal S.Whiteman P.McConnell V.Chillakuri C.R.Macaya D.Coucke P.J.De Paepe A.Judge D.P.Wigley F.Davis E.C.Mardon H.J.Handford P.Keene D.R.Sakai L.Y.Dietz H.C.doi:10.1126/scitranslmed.30004882010Sci. Transl. Med.223RA20VARIANTS SSKS SER-1564; CYS-1570; GLY-1577 AND ASP-1594Mutations in the TGFbeta binding-protein-like domain 5 of FBN1 are responsible for acromicric and geleophysic dysplasias.Le Goff C.Mahaut C.Wang L.W.Allali S.Abhyankar A.Jensen S.Zylberberg L.Collod-Beroud G.Bonnet D.Alanay Y.Brady A.F.Cordier M.P.Devriendt K.Genevieve D.Kiper P.O.Kitoh H.Krakow D.Lynch S.A.Le Merrer M.Megarbane A.Mortier G.Odent S.Polak M.Rohrbach M.Sillence D.Stolte-Dijkstra I.Superti-Furga A.Rimoin D.L.Topouchian V.Unger S.Zabel B.Bole-Feysot C.Nitschke P.Handford P.Casanova J.L.Boileau C.Apte S.S.Munnich A.Cormier-Daire V.doi:10.1016/j.ajhg.2011.05.0122011Am. J. Hum. Genet.897-14VARIANTS GPHYSD2 CYS-1696; ASP-1699; CYS-1699; TYR-1706; TRP-1719; THR-1728; VAL-1728; TYR-1733 AND SER-1762VARIANTS ACMICD CYS-1699; CYS-1700; ARG-1714; CYS-1722; VAL-1726; THR-1728; GLN-1735 INS; ARG-1750 AND VAL-1758Applying massive parallel sequencing to molecular diagnosis of Marfan and Loeys-Dietz syndromes.Baetens M.Van Laer L.De Leeneer K.Hellemans J.De Schrijver J.Van De Voorde H.Renard M.Dietz H.Lacro R.V.Menten B.Van Criekinge W.De Backer J.De Paepe A.Loeys B.Coucke P.J.doi:10.1002/humu.215252011Hum. Mutat.321053-1062VARIANTS MFS GLY-80; TYR-490; TYR-499; ARG-611; GLY-617; TRP-685; TYR-685; TYR-790; TYR-811; SER-853; TYR-926; SER-1090; ASP-1185; TYR-1284; PHE-1350; ALA-1401; TRP-1431; TYR-1431; ALA-1487; LYS-1489; CYS-1838; TYR-1900; THR-1909; SER-1934; GLY-1976; ARG-1984; ASN-2166; THR-2185; GLY-2247; ARG-2318; TYR-2406; SER-2442; ARG-2511; VAL-2606 DEL; LYS-2610 AND ARG-2646VARIANTS GLY-1481 AND HIS-2793Exon 47 skipping of fibrillin-1 leads preferentially to cardiovascular defects in patients with thoracic aortic aneurysms and dissections.Wang W.J.Han P.Zheng J.Hu F.Y.Zhu Y.Xie J.S.Guo J.Zhang Z.Dong J.Zheng G.Y.Cao H.Liu T.S.Fu Q.Sun L.Yang B.B.Tian X.L.doi:10.1007/s00109-012-0931-y2013J. Mol. Med.9137-47VARIANTS MFS GLU-55; GLN-219; SER-699; SER-880; TYR-908; ARG-1117; ALA-1199; 1539-ARG--HIS-2871 DEL; GLY-1642; ARG-1865; 2081-GLN--HIS-2871 DEL AND 2220-ARG--HIS-2871 DELProtein Spotlight; Two birds, one stone - Issue 248 of June 2022Different initiation.A=2052-2125A=2124-2205A=2124-2205A=1069-11542.25A/B/C=1486-16471.35A=1486-16471.78A=1486-16472.40A=1486-1647A=45-1781.80A=807-951A=113-287283562 N-Linked glycans (12 sites)46 sites, 69 glycans48 sites, 68 N-linked glycans (12 sites), 3 O-linked glycans (30 sites)559 antibodies from 37 providers3 antibodieshumanFBN1Tissue enhanced (adipose tissue, placenta)phenotypephenotypegenephenotypephenotypephenotypephenotypephenotypephenotypeAcromicric dysplasiaFamilial thoracic aortic aneurysm and aortic dissectionGeleophysic dysplasiaGlaucoma-ectopia lentis-microspherophakia-stiff joints-short stature syndromeIsolated ectopia lentisMarfan syndrome type 1Neonatal Marfan syndromeProgeroid and marfanoid aspect-lipodystrophy syndromeShprintzen-Goldberg syndromeStiff skin syndromeWeill-Marchesani syndromeEukaryotaDegradation of the extracellular matrixElastic fibre formationMolecules associated with elastic fibresIntegrin cell surface interactionsTGF-beta receptor signaling activates SMADsRegulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)Post-translational protein phosphorylation8 hits in 1157 CRISPR screenshumanTbioProteinExpressed in synovial joint and 193 other cell types or tissuesbaseline and differentialHSEGF_CALamininTGF-beta binding (TB) domaincEGFEGF-like_Ca-bd_domEGF-like_CSEGF-like_domEGF-type_Asp/Asn_hydroxyl_siteEGF_Ca-bd_CSEGF_domFBN_EGF_NFibrillin_U_NGrowth_fac_rcpt_cys_sfTB_domTB_dom_sfVON WILLEBRAND FACTOR C AND EGF DOMAIN-CONTAINING PROTEINVON WILLEBRAND FACTOR C AND EGF DOMAIN-CONTAINING PROTEINcEGFEGF_3EGF_CAFBN_EGF_st1Fibrillin_U_NFXa_inhibitionhEGFTBFibrillinEGFEGF_CAEGF/LamininGrowth factor receptor domainTB module/8-cys domainASX_HYDROXYLEGF_1EGF_2EGF_3EGF_CATBFibrillin-1AsprosinFBN1FBNStructural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:1860873, PubMed:15062093). Fibrillin-1-containing microfibrils provide long-term force bearing structural support (PubMed:27026396). In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin (PubMed:27026396). In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles (PubMed:27026396). Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11 (PubMed:24039232). This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921).Adipokine secreted by white adipose tissue that plays an important regulatory role in the glucose metabolism of liver, muscle and pancreas (PubMed:27087445, PubMed:30853600). Hormone that targets the liver in response to fasting to increase plasma glucose levels (PubMed:27087445). Binds the olfactory receptor OR4M1 at the surface of hepatocytes and promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation (PubMed:27087445, PubMed:31230984). May act as a regulator of adaptive thermogenesis by inhibiting browning and energy consumption, while increasing lipid deposition in white adipose tissue (By similarity). Also acts as an orexigenic hormone that increases appetite: crosses the blood brain barrier and exerts effects on the hypothalamus (By similarity). In the arcuate nucleus of the hypothalamus, asprosin directly activates orexigenic AgRP neurons and indirectly inhibits anorexigenic POMC neurons, resulting in appetite stimulation (By similarity). Activates orexigenic AgRP neurons via binding to the olfactory receptor OR4M1 (By similarity). May also play a role in sperm motility in testis via interaction with OR4M1 receptor (By similarity).Interacts with COL16A1 (PubMed:15165854). Interacts with integrin alpha-V/beta-3 (PubMed:15062093). Interacts with ADAMTS10; this interaction promotes microfibril assembly (PubMed:21402694). Interacts with THSD4; this interaction promotes fibril formation (By similarity). Interacts (via N-terminal domain) with FBLN2 and FBLN5 (PubMed:15790312, PubMed:17255108). Interacts with ELN (PubMed:15790312). Forms a ternary complex with ELN and FBLN2 or FBLN5 and a significant interaction with ELN seen only in the presence of FBLN2 or FBLN5 (PubMed:17255108). Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner (PubMed:17293099). Interacts (via N-terminal domain) with LTBP1 (via C-terminal domain) (PubMed:17293099). Interacts with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6 (PubMed:17158881, PubMed:12807887). Interacts (via N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5 (PubMed:18339631). Interacts (via N-terminal domain) with MFAP2 and MFAP5 (PubMed:15131124). Interacts with ADAMTSL5 (PubMed:23010571). Interacts with MFAP4 (PubMed:26601954). Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent manner (PubMed:24039232). Interacts (via N-terminal domain) with EFEMP2; this interaction inhibits EFEMP2 binding to LOX and ELN (PubMed:17255108, PubMed:19349279, PubMed:19570982).Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166).Secreted by white adipose tissue and circulates in the plasma.Asprosin levels are elevated in patients with type II diabetes and metabolic syndrome (at protein level).Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils (PubMed:27026396). The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide (PubMed:24982166). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils (PubMed:24982166).Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils.O-glycosylated on serine residues by POGLUT2 and POGLUT3 which is necessary for efficient protein secretion.The disease is caused by variants affecting the gene represented in this entry. The majority of the more than a thousand mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations. Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini.The disease is caused by variants affecting the gene represented in this entry.The disease is caused by variants affecting the gene represented in this entry.The disease is caused by variants affecting the gene represented in this entry.The disease is caused by variants affecting the gene represented in this entry.The disease is caused by variants affecting the gene represented in this entry.The disease is caused by variants affecting the gene represented in this entry.The disease is caused by variants affecting the gene represented in this entry.Attractive therapeutic target for type II diabetes and metabolic syndrome.Was named after the Greek word for white, because of the reduction in subcutaneous white adipose tissue that is displayed by asprosin-deficient patients.Belongs to the fibrillin family.Extended N-terminus.1242544Fibrillin-1291649452731Asprosin1588327322871EGF-like 181112EGF-like 2115146EGF-like 3147178TB 1184236EGF-like 4; calcium-binding246287EGF-like 5; calcium-binding288329TB 2334389EGF-like 6449489EGF-like 7; calcium-binding490529EGF-like 8; calcium-binding530571EGF-like 9; calcium-binding572612EGF-like 10; calcium-binding613653TB 3659711EGF-like 11; calcium-binding723764EGF-like 12; calcium-binding765806EGF-like 13; calcium-binding807846TB 4851902EGF-like 14; calcium-binding910951TB 59561008EGF-like 15; calcium-binding10281069EGF-like 16; calcium-binding10701112EGF-like 17; calcium-binding11131154EGF-like 18; calcium-binding11551196EGF-like 19; calcium-binding11971237EGF-like 20; calcium-binding12381279EGF-like 21; calcium-binding12801321EGF-like 22; calcium-binding13221362EGF-like 23; calcium-binding13631403EGF-like 24; calcium-binding14041445EGF-like 25; calcium-binding14461486EGF-like 26; calcium-binding14871527TB 615321589EGF-like 27; calcium-binding16061647EGF-like 28; calcium-binding16481688TB 716931748EGF-like 29; calcium-binding17661807EGF-like 30; calcium-binding18081848EGF-like 31; calcium-binding18491890EGF-like 32; calcium-binding18911929EGF-like 33; calcium-binding19301972EGF-like 34; calcium-binding19732012EGF-like 35; calcium-binding20132054TB 820592111EGF-like 36; calcium-binding21272165EGF-like 37; calcium-binding21662205EGF-like 38; calcium-binding22062246EGF-like 39; calcium-binding22472290EGF-like 40; calcium-binding22912332TB 923372390EGF-like 41; calcium-binding24022443EGF-like 42; calcium-binding24442484EGF-like 43; calcium-binding24852523EGF-like 44; calcium-binding25242566EGF-like 45; calcium-binding25672606EGF-like 46; calcium-binding26072647EGF-like 47; calcium-binding26482687N-terminal domain450Fibrillin unique N-terminal (FUN) domainInteraction with MFAP4119Hybrid domain 1195221Hybrid domain 2862887C-terminal domain1528Disordered27262746Cell attachment site15411543Cleavage; by furinCleavage; by furinPhosphoserine; by FAM20C2702Phosphoserine2709O-linked (Glc) serine268N-linked (GlcNAc...) asparagine448O-linked (Glc) serine471O-linked (Glc) serine510O-linked (Glc) serine552O-linked (Glc) serine593O-linked (Glc) serine634O-linked (Glc) serine787O-linked (Glc) serine827O-linked (Glc) serine1050N-linked (GlcNAc...) asparagine1067O-linked (Glc) serine1135N-linked (GlcNAc...) asparagine1149O-linked (Glc) serine1218O-linked (Glc) serine1302O-linked (Glc) serine1345N-linked (GlcNAc...) asparagine1369O-linked (Glc) serine1386N-linked (GlcNAc...) asparagine1484O-linked (Glc) serine1508N-linked (GlcNAc...) asparagine1581O-linked (Glc) serine1628N-linked (GlcNAc...) asparagine1669N-linked (GlcNAc...) asparagine1703N-linked (GlcNAc...) asparagine1713O-linked (Glc) serine1830O-linked (Glc) serine1871N-linked (GlcNAc...) asparagine1902O-linked (Glc) serine1911O-linked (Glc) serine1953O-linked (Glc) serine2035N-linked (GlcNAc...) asparagine2077O-linked (Glc) serine2148N-linked (GlcNAc...) asparagine2178O-linked (Glc) serine2227O-linked (Glc) serine2313O-linked (Glc) serine2465O-linked (Glc) serine2547O-linked (Glc) serine2628N-linked (GlcNAc...) asparagine2734N-linked (GlcNAc...) asparagine2750N-linked (GlcNAc...) asparagine27675968678085948910010211112912313413614515016015416616817725026225727127328629230429931331532845346546047447648849450449951351552853454654155555757057658758259659861161762862363763965272773973474875076376978177679079280581182181683083284585387587689089690891492692193593795010321044103910531055106810741086108110951097111111171129112411381140115311591171116611801182119512011212120812211223123612421254124912631265127812841296129113051307132013261339133313481350136113671380137413891391140214081420141514291431144414501461145614701472148514911502149715111513152615341562154915741563157715641610162216171631163316461652166316581672167416871770178217771791179318061812182418181833183518471853186518601874187618891895190519001914191619281934194719421956195819711977198919841998200020112017202920242038204020532061208320702096208420992085213121422137215121532164217021812176219021922204221022212217223022322245225122652258227422762289229523072302231623182331240624182413242724292442244824592455246824702483248925002496250925112522252825412535255025522565257125812577259025922605261126222617263126332646265226632659267226742686In MFS.C20T27Found in a patient with Marfan-like syndrome; likely pathogenic.P39In MFS.E55In MFS.D57In MFS; also in a patient with ectopia lentis and retinal detachment.C62In ECTOL1.C63In ECTOL1.SIn MFS.GIn MFS.FIn MFS.YIn MFS.RIn MFS.C114In ECTOL1.CIn MFS.C122In MFS.YFound in a patient with Marfan-like syndrome; likely pathogenic.D127In MFS; severe neonatal.YQ133In MFS.SIn MFS.SFound in a patient with Marfan-like syndrome; likely pathogenic.RFound in a patient with Marfan-like syndrome; likely pathogenic.S164In MFS.FIn MFS.SIn MFS.RIn MFS.SIn MFS.YIn MFS.S214Found in a patient with Marfan-like syndrome; likely pathogenic.215In MFS.G217In MFS.Q219In MFS.R224In MFS and ECTOL1.C240In MFS.248TIn MFS.348In MFS.351S363Found in a patient with Marfan-like syndrome; likely pathogenic.364In MFS.R365In ECTOL1.WIn MFS.366In MFS.CIn MFS.429In MFS.G439In MFS.IC472In MFS.WIn MFS.GIn MFS.RIn MFS.YIn MFS.YIn MFS.FFound in a patient with Marfan-like syndrome; likely pathogenic.RIn MFS.507In MFS.WG516In MFS.YIn MFS and ECTOL1.C545In MFS.WIn MFS.I548In MFS.S560In MFS.565In MFS.YIn MFS.YIn MFS.RIn MFS.YIn MFS.D592In ECTOL1.RIn MFS.YIn MFS.WIn MFS.RIn MFS.GIn MFS.FIn MFS; enhances proteolytic degradation.C627In MFS.629633In ECTOL1.PIn MFS.C635In MFS.I636In MFS.SFound in a patient with Marfan-like syndrome; likely pathogenic.YFound in a patient with Marfan-like syndrome; likely pathogenic.In MFS.N654In MFS.R661In ECTOL1; patient presenting also mitral valve prolapse.YIn MFS.Y681In MFS.R683In MFS.Y684In MFS.W685In MFS.YIn MFS.S699In MFS.T705In MFS.YIn MFS.C721In MFS.AIn MFS.VIn MFS.YIn MFS.FIn MFS.C746In MFS.YIn MFS; enhances proteolytic degradation.GFound in a patient with Marfan-like syndrome; likely pathogenic.752In MFS.GIn MFS.YIn MFS.RIn MFS.YIn MFS.YIn MFS.YIn MFS.RIn MFS.SIn MFS.C828In MFS.YIn MFS.SIn MFS.861In MFS.RIn MFS.S880In MFS and ECTOL1.V882In MFS.E884In MFS.GIn MFS.RIn MFS.RIn MFS.YIn MFS.HIn MFS.G913In MFS.In MFS.GIn MFS; enhances proteolytic degradation.RIn MFS.YFound in a patient with Marfan-like syndrome; likely pathogenic.RFound in a patient with Marfan-like syndrome; likely pathogenic.C954Found in a patient with Marfan-like syndrome; likely pathogenic.966In MFS.C974In MFS.H976In MFS.I984In MFS; atypical.E985In MFS.RFound in a patient with Marfan-like syndrome; likely pathogenic.988In MFS.994In MFS.R996In MFS.YIn MFS; severe neonatal.R1013Found in a patient with Marfan-like syndrome; likely pathogenic.A1020In MFS; severe neonatal.N1023Found in a patient with Marfan-like syndrome; likely pathogenic.GIn MFS; severe neonatal.YIn MFS.S1042In MFS.R1043In MFS.YIn MFS; severe neonatal.T1048VIn MFS.In MFS.RIn MFS; neonatal.GIn MFS.WIn MFS.YIn MFS.D1058In MFS.GCIn MFS; neonatal form.GIn MFS.G1072In MFS; severe neonatal.K1073In MFS; severe neonatal.RIn MFS; severe neonatal.YIn ECTOL1.In MFS.WIn MFS; severe neonatal.I1088In MFS.S1090In MFS.C1101GIn MFS.VIn MFS.GIn MFS.RIn MFS.YIn MFS.1125In MFS; mild form.S1127In a patient with mitral valve prolapse.I1128In MFS.YIn MFS.P1130Y1131In MFS.1136In MFS.P1137In MFS.YIn MFS.A1148In MFS.SIn MFS; severe.YIn MFS and ECTOL1.NIn MFS.G1158In MFS.H1170In MFS.WIn MFS.K1173In MFS.WIn MFS.D1185In MFS.A1199In MFS.G1200In MFS.1211In MFS.C1219In MFS; severe neonatal.RIn MFS; also found in a patient with Shprintzen-Goldberg craniosynostosis syndrome.YIn MFS.YIn MFS.RIn MFS.SIn MFS.C1261In MFS.DIn MFS.RIn MFS.YIn MFS.SS1282In MFS.GIn MFS.YIn MFS; severe neonatal.YIn MFS.RIn MFS.Q1325In MFS; severe neonatal.RIn MFS.SIn MFS; neonatal.P1337In MFS.YIn MFS.L1346In MFS.FIn MFS.K1366In MFS.SIn MFS.S1382In MFS.RIn MFS.13941396In MFS.A1401In MFS.RIn MFS.YIn MFS.YFound in a patient with Marfan-like syndrome; likely pathogenic.G1406In MFS.A1424In MFS.SIn MFS.D1427In MFS.SIn MFS.WIn MFS.YIn MFS.E1475In MFS.SG1481In MFS.RIn MFS.AIn MFS.K1489In MFS.RIn MFS.YIn MFS and ECTOL1.C1530In MFS.In MFS.1539In MFS.In MFS.FIn SSKS.SIn MFS.YIn SSKS.C1570In MFS.T1576In SSKS.GIn MFS.FIn SSKS.D1594In MFS.GIn MFS.RIn MFS.GFound in a patient with Marfan-like syndrome; likely pathogenic.SIn MFS.G1642Found in a patient with Marfan-like syndrome; likely pathogenic.1644In MFS.RIn MFS.YFIn MFS.RIn MFS.YIn MFS.GIn WMS2.16921699In ECTOL1.In GPHYSD2.C1696In GPHYSD2 and ACMICD.CIn GPHYSD2.DIn ACMICD.C1700In GPHYSD2.Y1706In ACMICD.R1714In GPHYSD2.W1719In MFS.Y1720In ACMICD.C1722In ACMICD.V1726In GPHYSD2 and ACMICD.T1728In GPHYSD2.VIn GPHYSD2.Y1733In MFS.1735In ACMICD.QQIn ACMICD.R1750In ACMICD.V1758In GPHYSD2.S1762In MFS.FFound in a patient with Marfan-like syndrome; likely pathogenic.FIn MFS.1790In MFS.PIn MFS.RIn MFS.YIn MFS.WIn MFS.YFound in a patient with Marfan-like syndrome; likely pathogenic.1796In MFS.EIn MFS.VIn MFS.SIn MFS.YIn MFS.K1811In MFS.RFound in a patient with Marfan-like syndrome; likely pathogenic.YIn MFS.S1826In MFS.CIn MFS.SIn MFS.FIn MFS.YIn MFS.S1837In MFS.C1838In MFS.RIn MFS.WIn MFS.YIn MFS.RIn MFS.YIn MFS.D1879In MFS.I1887In MFS.K1893In MFS.K1894In MFS.RIn MFS.YFound in a patient with Marfan-like syndrome; likely pathogenic.S1907In MFS.I1908In MFS.T1909In MFS.S1915In MFS.D1919In MFS.GIn MFS.RIn MFS.YFound in a patient with Marfan-like syndrome; likely pathogenic.HIn MFS.1931In MFS.GIn MFS.SIn MFS.YIn MFS.G1976In MFS.RIn MFS.WIn MFS.YIn MFS.RIn MFS.R1987In MFS.YI2018In MFS.YIn MFS.FIn MFS.2057In MFS.2062In MFS.2064In MFS.2081In MFS.WIn MFS.YIn MFS.RIn MFS.WM2101Found in a patient with Marfan-like syndrome; likely pathogenic.K2105In MFS.RIn MFS.YF2113In MFS.M2118In MFS.EIn MFS.K2130Found in a patient with Marfan-like syndrome; likely pathogenic.D2136In MFS.YIn MFS.D2144In MFS.SIn MFS.P2145In MFS.WIn MFS.YIn ECTOL1.R2154In MFS.P2160In MFS.NFound in a patient with Marfan-like syndrome; likely pathogenic.2169FIn MFS.T2185Found in a patient with Marfan-like syndrome; likely pathogenic.R2195In MFS.2220In MFS.FIn MFS.GIn MFS.RIn MFS.SIn MFS.H2223Found in a patient with Marfan-like syndrome; likely pathogenic.P2224Found in a patient with Marfan-like syndrome; likely pathogenic.2229In MFS.YFound in a patient with Marfan-like syndrome; likely pathogenic.M2234In MFS.GIn ECTOL1.G2250In MFS.RIn MFS.RIn MFS.YIn MFS.T2269In ECTOL1.C2272Found in a patient with Marfan-like syndrome; likely pathogenic.T2273In MFS.WS2278In MFS.W2282In MFS.T2284Found in a patient with Marfan-like syndrome; likely pathogenic.WIn MFS.2298Found in a patient with Marfan-like syndrome; likely pathogenic.YIn MFS.SIn MFS.RE2329In MFS.W2335In ECTOL1; patient presenting also flat corneas.Y2339Found in a patient with Marfan-like syndrome; likely pathogenic.Y2365In MFS.T2385In MFS.2394In MFS.YIn MFS.SIn MFS.WIn ECTOL1 and MFS.K2447In ECTOL1.RIn MFS.2466In MFS.2467Found in a patient with Marfan-like syndrome; likely pathogenic.WIn MFS.YIn MFS.C2474In MFS.RIn MFS.RIn MFS.YIn MFS.RFound in a patient with Marfan-like syndrome; likely pathogenic.I2516In MFS.M2520In MFS.YFound in a patient with Marfan-like syndrome; likely pathogenic.S2526In MFS.WIn MFS.R2536Found in a patient with Marfan-like syndrome; likely pathogenic.FIn MFS.2542Found in a patient with Marfan-like syndrome; likely pathogenic.W2554In MFS.V2555In MFS.P2561In MFS.K2570In MFS.In MFS.RIn MFS.RIn MFS.YIn MFS.FIn MFS.T2585In MFS.SIn MFS.YIn MFS.In MFS.K2610In MFS; uncertain significance.R2618In MFS.P2623In MFS.K2624In MFS.R2627In MFS.C2629In MFS.RIn MFS.GIn MFS.SIn MFS.C2668In MFS.C2680In MFS.2694In MFS.S2708Found in a patient with Marfan-like syndrome; likely pathogenic; defects in protein processing.WIn MFLS.T2741Found in a patient with Marfan-like syndrome; likely pathogenic.2774Found in a patient with Marfan-like syndrome; likely pathogenic; prevents secretion into the extracellular matrix.27762781Found in a patient with Marfan-like syndrome; likely pathogenic; prevents secretion into the extracellular matrix.P2780Found in a patient with Marfan-like syndrome; likely pathogenic.H2793Found in a patient with Marfan-like syndrome; likely pathogenic.2840Found in a patient with Marfan-like syndrome; likely pathogenic; prevents secretion into the extracellular matrix.2849Found in a patient with Marfan-like syndrome; likely pathogenic; prevents secretion into the extracellular matrix.2867Loss of integrin-mediated cell adhesion.D1542Abolishes furin cleavage site, leading to defects in protein processing at the C-terminus.A2728Abolishes furin cleavage site, leading to defects in protein processing at the C-terminus.KDefects in protein processing at the C-terminus.TQ207T2158T505254565860929699101107110118120128130135142155157159162165167170172174176187191193206211218229231235237239241244249252253255258265272281284810813819824831836838842847858870872877879881883894900904907916929932936107610801083108910921099110311051107110811161119112311261132115014901492149614981500150515121523153715441546155015571559156615681571158315881595159715991601160416091612161416201624162916321641164320562065207320802090209220932110213321382157216321712177217921832193219622002202false3false3false6false2false2false3false3false2false2false3FBN1EFEMP2FBLN5FBN2FN1GET4HGSLOXLTBP1SGTB2019-04-104true312298f8f84ac9dc30f3ff640ad4f691fee2b1MRRGRLLEIALGFTVLLASYTSHGADANLEAGNVKETRASRAKRRGGGGHDALKGPNVCGSRYNAYCCPGWKTLPGGNQCIVPICRHSCGDGFCSRPNMCTCPSGQIAPSCGSRSIQHCNIRCMNGGSCSDDHCLCQKGYIGTHCGQPVCESGCLNGGRCVAPNRCACTYGFTGPQCERDYRTGPCFTVISNQMCQGQLSGIVCTKTLCCATVGRAWGHPCEMCPAQPHPCRRGFIPNIRTGACQDVDECQAIPGLCQGGNCINTVGSFECKCPAGHKLNEVSQKCEDIDECSTIPGICEGGECTNTVSSYFCKCPPGFYTSPDGTRCIDVRPGYCYTALTNGRCSNQLPQSITKMQCCCDAGRCWSPGVTVAPEMCPIRATEDFNKLCSVPMVIPGRPEYPPPPLGPIPPVLPVPPGFPPGPQIPVPRPPVEYLYPSREPPRVLPVNVTDYCQLVRYLCQNGRCIPTPGSYRCECNKGFQLDLRGECIDVDECEKNPCAGGECINNQGSYTCQCRAGYQSTLTRTECRDIDECLQNGRICNNGRCINTDGSFHCVCNAGFHVTRDGKNCEDMDECSIRNMCLNGMCINEDGSFKCICKPGFQLASDGRYCKDINECETPGICMNGRCVNTDGSYRCECFPGLAVGLDGRVCVDTHMRSTCYGGYKRGQCIKPLFGAVTKSECCCASTEYAFGEPCQPCPAQNSAEYQALCSSGPGMTSAGSDINECALDPDICPNGICENLRGTYKCICNSGYEVDSTGKNCVDINECVLNSLLCDNGQCRNTPGSFVCTCPKGFIYKPDLKTCEDIDECESSPCINGVCKNSPGSFICECSSESTLDPTKTICIETIKGTCWQTVIDGRCEININGATLKSQCCSSLGAAWGSPCTLCQVDPICGKGYSRIKGTQCEDIDECEVFPGVCKNGLCVNTRGSFKCQCPSGMTLDATGRICLDIRLETCFLRYEDEECTLPIAGRHRMDACCCSVGAAWGTEECEECPMRNTPEYEELCPRGPGFATKEITNGKPFFKDINECKMIPSLCTHGKCRNTIGSFKCRCDSGFALDSEERNCTDIDECRISPDLCGRGQCVNTPGDFECKCDEGYESGFMMMKNCMDIDECQRDPLLCRGGVCHNTEGSYRCECPPGHQLSPNISACIDINECELSAHLCPNGRCVNLIGKYQCACNPGYHSTPDRLFCVDIDECSIMNGGCETFCTNSEGSYECSCQPGFALMPDQRSCTDIDECEDNPNICDGGQCTNIPGEYRCLCYDGFMASEDMKTCVDVNECDLNPNICLSGTCENTKGSFICHCDMGYSGKKGKTGCTDINECEIGAHNCGKHAVCTNTAGSFKCSCSPGWIGDGIKCTDLDECSNGTHMCSQHADCKNTMGSYRCLCKEGYTGDGFTCTDLDECSENLNLCGNGQCLNAPGGYRCECDMGFVPSADGKACEDIDECSLPNICVFGTCHNLPGLFRCECEIGYELDRSGGNCTDVNECLDPTTCISGNCVNTPGSYICDCPPDFELNPTRVGCVDTRSGNCYLDIRPRGDNGDTACSNEIGVGVSKASCCCSLGKAWGTPCEMCPAVNTSEYKILCPGGEGFRPNPITVILEDIDECQELPGLCQGGKCINTFGSFQCRCPTGYYLNEDTRVCDDVNECETPGICGPGTCYNTVGNYTCICPPDYMQVNGGNNCMDMRRSLCYRNYYADNQTCDGELLFNMTKKMCCCSYNIGRAWNKPCEQCPIPSTDEFATLCGSQRPGFVIDIYTGLPVDIDECREIPGVCENGVCINMVGSFRCECPVGFFYNDKLLVCEDIDECQNGPVCQRNAECINTAGSYRCDCKPGYRFTSTGQCNDRNECQEIPNICSHGQCIDTVGSFYCLCHTGFKTNDDQTMCLDINECERDACGNGTCRNTIGSFNCRCNHGFILSHNNDCIDVDECASGNGNLCRNGQCINTVGSFQCQCNEGYEVAPDGRTCVDINECLLEPRKCAPGTCQNLDGSYRCICPPGYSLQNEKCEDIDECVEEPEICALGTCSNTEGSFKCLCPEGFSLSSSGRRCQDLRMSYCYAKFEGGKCSSPKSRNHSKQECCCALKGEGWGDPCELCPTEPDEAFRQICPYGSGIIVGPDDSAVDMDECKEPDVCKHGQCINTDGSYRCECPFGYILAGNECVDTDECSVGNPCGNGTCKNVIGGFECTCEEGFEPGPMMTCEDINECAQNPLLCAFRCVNTYGSYECKCPVGYVLREDRRMCKDEDECEEGKHDCTEKQMECKNLIGTYMCICGPGYQRRPDGEGCVDENECQTKPGICENGRCLNTRGSYTCECNDGFTASPNQDECLDNREGYCFTEVLQNMCQIGSSNRNPVTKSECCCDGGRGWGPHCEICPFQGTVAFKKLCPHGRGFMTNGADIDECKVIHDVCRNGECVNDRGSYHCICKTGYTPDITGTSCVDLNECNQAPKPCNFICKNTEGSYQCSCPKGYILQEDGRSCKDLDECATKQHNCQFLCVNTIGGFTCKCPPGFTQHHTSCIDNNECTSDINLCGSKGICQNTPGSFTCECQRGFSLDQTGSSCEDVDECEGNHRCQHGCQNIIGGYRCSCPQGYLQHYQWNQCVDENECLSAHICGGASCHNTLGSYKCMCPAGFQYEQFSGGCQDINECGSAQAPCSYGCSNTEGGYLCGCPPGYFRIGQGHCVSGMGMGRGNPEPPVSGEMDDNSLSPEACYECKINGYPKRGRKRRSTNETDASNIEDQSETEANVSLASWDVEKTAIFAFNISHVSNKVRILELLPALTTLTNHNRYLIESGNEDGFFKINQKEGISYLHFTKKKPVAGTYSLQISSTPLYKKKELNQLEDKYDKDYLSGELGDNLKMKIQVLLHtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue