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Fibrillin-1 [Cleaved into: Asprosin]

 FBN1_HUMAN              Reviewed;        2871 AA.
P35555; B2RUU0; D2JYH6; Q15972; Q75N87;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
27-SEP-2017, entry version 212.
RecName: Full=Fibrillin-1;
Contains:
RecName: Full=Asprosin {ECO:0000303|PubMed:27087445};
Flags: Precursor;
Name=FBN1; Synonyms=FBN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TYR-472.
TISSUE=Placenta;
PubMed=8364578; DOI=10.1093/hmg/2.7.961;
Pereira L.V., D'Alessio M., Ramirez F., Lynch J.R., Sykes B.,
Pangilinan T., Bonadio J.;
"Genomic organization of the sequence coding for fibrillin, the
defective gene product in Marfan syndrome.";
Hum. Mol. Genet. 2:961-968(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MFS SER-2663.
PubMed=15221638; DOI=10.1007/s10038-004-0168-x;
Uyeda T., Takahashi T., Eto S., Sato T., Xu G., Kanezaki R., Toki T.,
Yonesaka S., Ito E.;
"Three novel mutations of the fibrillin-1 gene and ten single
nucleotide polymorphisms of the fibrillin-3 gene in Marfan syndrome
patients.";
J. Hum. Genet. 49:404-407(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-472.
Rieder M.J., Bertucci C., Stanaway I.B., Johnson E.J., Swanson J.E.,
Siegel D.L., da Ponte S.H., Igartua C., Patterson K., Nickerson D.A.;
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TYR-472.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-472.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55,
AND VARIANT TYR-472.
TISSUE=Fibroblast, and Placenta;
PubMed=7691719; DOI=10.1006/geno.1993.1350;
Corson G.M., Chalberg S.C., Dietz H.C., Charbonneau N.L., Sakai L.Y.;
"Fibrillin binds calcium and is coded by cDNAs that reveal a
multidomain structure and alternatively spliced exons at the 5' end.";
Genomics 17:476-484(1993).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 899-2871.
PubMed=1852207; DOI=10.1038/352334a0;
Maslen C.L., Corson G.M., Maddox B.K., Glanville R.W., Sakai L.Y.;
"Partial sequence of a candidate gene for the Marfan syndrome.";
Nature 352:334-337(1991).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 813-1313.
PubMed=1852206; DOI=10.1038/352330a0;
Lee B., Godfrey M., Vitale E., Hori H., Mattei M.-G., Sarfarazi M.,
Tsipouras P., Ramirez F., Hollister D.W.;
"Linkage of Marfan syndrome and a phenotypically related disorder to
two different fibrillin genes.";
Nature 352:330-334(1991).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2086-2194.
PubMed=8430317; DOI=10.1126/science.8430317;
Dietz H.C., Valle D., Francomano C.A., Kendzior R.J. Jr.,
Pyeritz R.E., Cutting G.R.;
"The skipping of constitutive exons in vivo induced by nonsense
mutations.";
Science 259:680-683(1993).
[11]
PROTEIN SEQUENCE OF 25-36 AND 45-56, AND CLEAVAGE OF SIGNAL PEPTIDE
AFTER GLY-24.
PubMed=10636927; DOI=10.1074/jbc.275.3.2205;
Reinhardt D.P., Gambee J.E., Ono R.N., Baechinger H.P., Sakai L.Y.;
"Initial steps in assembly of microfibrils. Formation of disulfide-
cross-linked multimers containing fibrillin-1.";
J. Biol. Chem. 275:2205-2210(2000).
[12]
PROTEIN SEQUENCE OF 2732-2746, PROTEOLYTIC PROCESSING, MUTAGENESIS OF
ARG-2728; ARG-2731 AND SER-2732, AND CHARACTERIZATION OF VARIANT
TRP-2726.
PubMed=9817919; DOI=10.1093/hmg/7.13.2039;
Loennqvist L., Reinhardt D., Sakai L., Peltonen L.;
"Evidence for furin-type activity-mediated C-terminal processing of
profibrillin-1 and interference in the processing by certain
mutations.";
Hum. Mol. Genet. 7:2039-2044(1998).
[13]
INVOLVEMENT IN OCTD.
PubMed=2739055; DOI=10.1001/jama.1989.03430040095032;
Glesby M.J., Pyeritz R.E.;
"Association of mitral valve prolapse and systemic abnormalities of
connective tissue: a phenotypic continuum.";
JAMA 262:523-528(1989).
[14]
FUNCTION.
PubMed=1860873;
Sakai L.Y., Keene D.R., Glanville R.W., Bachinger H.P.;
"Purification and partial characterization of fibrillin, a cysteine-
rich structural component of connective tissue microfibrils.";
J. Biol. Chem. 266:14763-14770(1991).
[15]
HEPARIN-BINDING, N-TERMINAL REGION DOMAIN, C-TERMINAL REGION DOMAIN,
AND SUBCELLULAR LOCATION.
PubMed=11461921; DOI=10.1074/jbc.M104985200;
Tiedemann K., Baetge B., Mueller P.K., Reinhardt D.P.;
"Interactions of fibrillin-1 with heparin/heparan sulfate,
implications for microfibrillar assembly.";
J. Biol. Chem. 276:36035-36042(2001).
[16]
FUNCTION, CELL ATTACHMENT SITE, MUTAGENESIS OF GLY-1542, AND
INTERACTION WITH ITGA5; ITGAV; ITGB1 AND ITGB3.
PubMed=12807887; DOI=10.1074/jbc.M303159200;
Bax D.V., Bernard S.E., Lomas A., Morgan A., Humphries J.,
Shuttleworth C.A., Humphries M.J., Kielty C.M.;
"Cell adhesion to fibrillin-1 molecules and microfibrils is mediated
by alpha 5 beta 1 and alpha v beta 3 integrins.";
J. Biol. Chem. 278:34605-34616(2003).
[17]
INTERACTION WITH MFAP2 AND MFAP5.
PubMed=15131124; DOI=10.1074/jbc.M313672200;
Hanssen E., Hew F.H., Moore E., Gibson M.A.;
"MAGP-2 has multiple binding regions on fibrillins and has covalent
periodic association with fibrillin-containing microfibrils.";
J. Biol. Chem. 279:29185-29194(2004).
[18]
INTERACTION WITH COL16A1.
PubMed=15165854; DOI=10.1016/j.jmb.2004.03.042;
Kassner A., Tiedemann K., Notbohm H., Ludwig T., Morgelin M.,
Reinhardt D.P., Chu M.-L., Bruckner P., Grassel S.;
"Molecular structure and interaction of recombinant human type XVI
collagen.";
J. Mol. Biol. 339:835-853(2004).
[19]
INTERACTION WITH FBLN5 AND ELN.
PubMed=15790312; DOI=10.1042/BJ20050368;
Freeman L.J., Lomas A., Hodson N., Sherratt M.J., Mellody K.T.,
Weiss A.S., Shuttleworth A., Kielty C.M.;
"Fibulin-5 interacts with fibrillin-1 molecules and microfibrils.";
Biochem. J. 388:1-5(2005).
[20]
FUNCTION, AND INTERACTION WITH ITGA5; ITGAV; ITGB1 AND ITGB6.
PubMed=17158881; DOI=10.1074/jbc.M607008200;
Jovanovic J., Takagi J., Choulier L., Abrescia N.G., Stuart D.I.,
van der Merwe P.A., Mardon H.J., Handford P.A.;
"alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative
studies of molecular determinants underlying integrin-rgd affinity and
specificity.";
J. Biol. Chem. 282:6743-6751(2007).
[21]
INTERACTION WITH ELN; FBLN2; FBLN4 AND FBLN5.
PubMed=17255108; DOI=10.1074/jbc.M608204200;
El-Hallous E., Sasaki T., Hubmacher D., Getie M., Tiedemann K.,
Brinckmann J., Baetge B., Davis E.C., Reinhardt D.P.;
"Fibrillin-1 interactions with fibulins depend on the first hybrid
domain and provide an adaptor function to tropoelastin.";
J. Biol. Chem. 282:8935-8946(2007).
[22]
INTERACTION WITH LTBP1 AND LTBP2, AND TISSUE SPECIFICITY.
PubMed=17293099; DOI=10.1016/j.matbio.2006.12.006;
Hirani R., Hanssen E., Gibson M.A.;
"LTBP-2 specifically interacts with the amino-terminal region of
fibrillin-1 and competes with LTBP-1 for binding to this
microfibrillar protein.";
Matrix Biol. 26:213-223(2007).
[23]
INTERACTION WITH BMP2; BMP4; BMP7; BMP10 AND GDF5.
PubMed=18339631; DOI=10.1074/jbc.M707820200;
Sengle G., Charbonneau N.L., Ono R.N., Sasaki T., Alvarez J.,
Keene D.R., Baechinger H.P., Sakai L.Y.;
"Targeting of bone morphogenetic protein growth factor complexes to
fibrillin.";
J. Biol. Chem. 283:13874-13888(2008).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-448; ASN-1067; ASN-1484
AND ASN-1581.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[25]
INVOLVEMENT IN MFLS (ASPROSIN).
PubMed=20979188; DOI=10.1002/ajmg.a.33690;
Graul-Neumann L.M., Kienitz T., Robinson P.N., Baasanjav S., Karow B.,
Gillessen-Kaesbach G., Fahsold R., Schmidt H., Hoffmann K.,
Passarge E.;
"Marfan syndrome with neonatal progeroid syndrome-like lipodystrophy
associated with a novel frameshift mutation at the 3' terminus of the
FBN1-gene.";
Am. J. Med. Genet. A 152A:2749-2755(2010).
[26]
INVOLVEMENT IN MFLS (ASPROSIN).
PubMed=21594992; DOI=10.1002/ajmg.a.33906;
Goldblatt J., Hyatt J., Edwards C., Walpole I.;
"Further evidence for a marfanoid syndrome with neonatal progeroid
features and severe generalized lipodystrophy due to frameshift
mutations near the 3' end of the FBN1 gene.";
Am. J. Med. Genet. A 155A:717-720(2011).
[27]
INVOLVEMENT IN MFLS (ASPROSIN).
PubMed=21594993; DOI=10.1002/ajmg.a.33905;
Horn D., Robinson P.N.;
"Progeroid facial features and lipodystrophy associated with a novel
splice site mutation in the final intron of the FBN1 gene.";
Am. J. Med. Genet. A 155A:721-724(2011).
[28]
INTERACTION WITH ADAMTS10.
PubMed=21402694; DOI=10.1074/jbc.M111.231571;
Kutz W.E., Wang L.W., Bader H.L., Majors A.K., Iwata K.,
Traboulsi E.I., Sakai L.Y., Keene D.R., Apte S.S.;
"ADAMTS10 protein interacts with fibrillin-1 and promotes its
deposition in extracellular matrix of cultured fibroblasts.";
J. Biol. Chem. 286:17156-17167(2011).
[29]
INTERACTION WITH ADAMTSL5.
PubMed=23010571; DOI=10.1016/j.matbio.2012.09.003;
Bader H.L., Wang L.W., Ho J.C., Tran T., Holden P., Fitzgerald J.,
Atit R.P., Reinhardt D.P., Apte S.S.;
"A disintegrin-like and metalloprotease domain containing
thrombospondin type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-,
fibrillin-2-, and heparin-binding member of the ADAMTS superfamily
containing a netrin-like module.";
Matrix Biol. 31:398-411(2012).
[30]
FUNCTION, AND INTERACTION WITH TNFSF11.
PubMed=24039232; DOI=10.1242/jcs.127571;
Tiedemann K., Boraschi-Diaz I., Rajakumar I., Kaur J., Roughley P.,
Reinhardt D.P., Komarova S.V.;
"Fibrillin-1 directly regulates osteoclast formation and function by a
dual mechanism.";
J. Cell Sci. 126:4187-4194(2013).
[31]
INVOLVEMENT IN MFLS (ASPROSIN), AND VARIANT MFLS THR-2741.
PubMed=24665001; DOI=10.1002/ajmg.a.36449;
Garg A., Xing C.;
"De novo heterozygous FBN1 mutations in the extreme C-terminal region
cause progeroid fibrillinopathy.";
Am. J. Med. Genet. A 164A:1341-1345(2014).
[32]
INVOLVEMENT IN MFLS (ASPROSIN).
PubMed=24039054; DOI=10.1002/ajmg.a.36157;
Takenouchi T., Hida M., Sakamoto Y., Torii C., Kosaki R.,
Takahashi T., Kosaki K.;
"Severe congenital lipodystrophy and a progeroid appearance: Mutation
in the penultimate exon of FBN1 causing a recognizable phenotype.";
Am. J. Med. Genet. A 161A:3057-3062(2013).
[33]
INVOLVEMENT IN MFLS (ASPROSIN).
PubMed=24613577; DOI=10.1016/j.ejmg.2014.02.012;
Jacquinet A., Verloes A., Callewaert B., Coremans C., Coucke P.,
de Paepe A., Kornak U., Lebrun F., Lombet J., Pierard G.E.,
Robinson P.N., Symoens S., Van Maldergem L., Debray F.G.;
"Neonatal progeroid variant of Marfan syndrome with congenital
lipodystrophy results from mutations at the 3' end of FBN1 gene.";
Eur. J. Med. Genet. 57:230-234(2014).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2702, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND CHARACTERIZATION OF
VARIANTS 2776-ARG--LEU-2781 DEL; PRO-2780; 2849-TYR--HIS-2871 DEL AND
2867-GLN--HIS-2871 DEL.
PubMed=24982166; DOI=10.1073/pnas.1401697111;
Jensen S.A., Aspinall G., Handford P.A.;
"C-terminal propeptide is required for fibrillin-1 secretion and
blocks premature assembly through linkage to domains cbEGF41-43.";
Proc. Natl. Acad. Sci. U.S.A. 111:10155-10160(2014).
[36]
PHOSPHORYLATION AT SER-2702.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[37]
REVIEW.
PubMed=27026396; DOI=10.1042/BJ20151108;
Jensen S.A., Handford P.A.;
"New insights into the structure, assembly and biological roles of 10-
12 nm connective tissue microfibrils from fibrillin-1 studies.";
Biochem. J. 473:827-838(2016).
[38]
FUNCTION (ASPROSIN), SUBCELLULAR LOCATION (ASPROSIN), AND INVOLVEMENT
IN MFLS (ASPROSIN).
PubMed=27087445; DOI=10.1016/j.cell.2016.02.063;
Romere C., Duerrschmid C., Bournat J., Constable P., Jain M., Xia F.,
Saha P.K., Del Solar M., Zhu B., York B., Sarkar P., Rendon D.A.,
Gaber M.W., LeMaire S.A., Coselli J.S., Milewicz D.M., Sutton V.R.,
Butte N.F., Moore D.D., Chopra A.R.;
"Asprosin, a fasting-induced glucogenic protein hormone.";
Cell 165:566-579(2016).
[39]
INVOLVEMENT IN MFLS (ASPROSIN).
PubMed=26860060; DOI=10.1038/ejhg.2016.6;
Passarge E., Robinson P.N., Graul-Neumann L.M.;
"Marfanoid-progeroid-lipodystrophy syndrome: a newly recognized
fibrillinopathy.";
Eur. J. Hum. Genet. 24:1244-1247(2016).
[40]
INTERACTION WITH MFAP4.
PubMed=26601954; DOI=10.1074/jbc.M115.681775;
Pilecki B., Holm A.T., Schlosser A., Moeller J.B., Wohl A.P.,
Zuk A.V., Heumueller S.E., Wallis R., Moestrup S.K., Sengle G.,
Holmskov U., Sorensen G.L.;
"Characterization of microfibrillar-associated protein 4 (MFAP4) as a
tropoelastin- and fibrillin-binding protein involved in elastic fiber
formation.";
J. Biol. Chem. 291:1103-1114(2016).
[41]
STRUCTURE BY NMR OF 2054-2125, AND DISULFIDE BONDS.
PubMed=9362480; DOI=10.1093/emboj/16.22.6659;
Yuan X., Downing A.K., Knott V., Handford P.A.;
"Solution structure of the transforming growth factor beta-binding
protein-like module, a domain associated with matrix fibrils.";
EMBO J. 16:6659-6666(1997).
[42]
STRUCTURE BY NMR OF 2124-2205.
PubMed=8568869; DOI=10.1006/jmbi.1996.0003;
Knott V., Downing A.K., Cardy C.M., Handford P.A.;
"Calcium binding properties of an epidermal growth factor-like domain
pair from human fibrillin-1.";
J. Mol. Biol. 255:22-27(1996).
[43]
STRUCTURE BY NMR OF 2124-2205.
PubMed=8653794; DOI=10.1016/S0092-8674(00)81259-3;
Downing A.K., Knott V., Werner J.M., Cardy C.M., Campbell I.D.,
Handford P.A.;
"Solution structure of a pair of calcium-binding epidermal growth
factor-like domains: implications for the Marfan syndrome and other
genetic disorders.";
Cell 85:597-605(1996).
[44]
STRUCTURE BY NMR OF 1069-1154 IN COMPLEX WITH CALCIUM, AND DISULFIDE
BONDS.
PubMed=12511552; DOI=10.1074/jbc.M208266200;
Smallridge R.S., Whiteman P., Werner J.M., Campbell I.D.,
Handford P.A., Downing A.K.;
"Solution structure and dynamics of a calcium binding epidermal growth
factor-like domain pair from the neonatal region of human fibrillin-
1.";
J. Biol. Chem. 278:12199-12206(2003).
[45]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1486-1647 IN COMPLEX WITH
CALCIUM IONS, FUNCTION, INTERACTION WITH INTEGRIN ALPHA-V/BETA-3, AND
DISULFIDE BONDS.
PubMed=15062093; DOI=10.1016/j.str.2004.02.023;
Lee S.S., Knott V., Jovanovic J., Harlos K., Grimes J.M., Choulier L.,
Mardon H.J., Stuart D.I., Handford P.A.;
"Structure of the integrin binding fragment from fibrillin-1 gives new
insights into microfibril organization.";
Structure 12:717-729(2004).
[46]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 807-951 IN COMPLEX WITH
CALCIUM, AND DISULFIDE BONDS.
PubMed=19446531; DOI=10.1016/j.str.2009.03.014;
Jensen S.A., Iqbal S., Lowe E.D., Redfield C., Handford P.A.;
"Structure and interdomain interactions of a hybrid domain: a
disulphide-rich module of the fibrillin/LTBP superfamily of matrix
proteins.";
Structure 17:759-768(2009).
[47]
STRUCTURE BY NMR OF 45-178, AND DISULFIDE BONDS.
PubMed=24035709; DOI=10.1016/j.str.2013.08.004;
Yadin D.A., Robertson I.B., McNaught-Davis J., Evans P., Stoddart D.,
Handford P.A., Jensen S.A., Redfield C.;
"Structure of the fibrillin-1 N-terminal domains suggests that heparan
sulfate regulates the early stages of microfibril assembly.";
Structure 21:1743-1756(2013).
[48]
REVIEW ON MFS VARIANTS.
PubMed=8594563; DOI=10.1093/nar/24.1.137;
Collod G., Beroud C., Soussi T., Junien C., Boileau C.;
"Software and database for the analysis of mutations in the human FBN1
gene.";
Nucleic Acids Res. 24:137-141(1996).
[49]
REVIEW ON MFS.
PubMed=10633129; DOI=10.1136/jmg.37.1.9;
Robinson P.N., Godfrey M.;
"The molecular genetics of Marfan syndrome and related
microfibrillopathies.";
J. Med. Genet. 37:9-25(2000).
[50]
REVIEW ON VARIANTS.
PubMed=12203987; DOI=10.1002/humu.10113;
Robinson P.N., Booms P., Katzke S., Ladewig M., Neumann L., Palz M.,
Pregla R., Tiecke F., Rosenberg T.;
"Mutations of FBN1 and genotype-phenotype correlations in Marfan
syndrome and related fibrillinopathies.";
Hum. Mutat. 20:153-161(2002).
[51]
VARIANT MFS PRO-1137.
PubMed=1852208; DOI=10.1038/352337a0;
Dietz H.C., Cutting G.R., Pyeritz R.E., Maslen C.L., Sakai L.Y.,
Corson G.M., Puffenberger E.G., Hamosh A., Nanthakumar E.J.,
Curristin S.M., Stetten G., Meyers D.A., Francomano C.A.;
"Marfan syndrome caused by a recurrent de novo missense mutation in
the fibrillin gene.";
Nature 352:337-339(1991).
[52]
VARIANTS MFS SER-1249; ARG-1663; SER-2221 AND SER-2307.
PubMed=1301946; DOI=10.1002/humu.1380010504;
Dietz H.C., Saraiva J.M., Pyeritz R.E., Cutting G.R., Francomano C.A.;
"Clustering of fibrillin (FBN1) missense mutations in Marfan syndrome
patients at cysteine residues in EGF-like domains.";
Hum. Mutat. 1:366-374(1992).
[53]
VARIANT MFS SER-2307.
PubMed=1569206; DOI=10.1172/JCI115766;
Dietz H.C., Pyeritz R.E., Puffenberger E.G., Kendzior R.J. Jr.,
Corson G.M., Maslen C.L., Sakai L.Y., Francomano C.A., Cutting G.R.;
"Marfan phenotype variability in a family segregating a missense
mutation in the epidermal growth factor-like motif of the fibrillin
gene.";
J. Clin. Invest. 89:1674-1680(1992).
[54]
VARIANTS MFS ILE-548 AND ALA-723.
PubMed=8406497; DOI=10.1006/geno.1993.1349;
Dietz H.C., McIntosh I., Sakai L.Y., Corson G.M., Chalberg S.C.,
Pyeritz R.E., Francomano C.A.;
"Four novel FBN1 mutations: significance for mutant transcript level
and EGF-like domain calcium binding in the pathogenesis of Marfan
syndrome.";
Genomics 17:468-475(1993).
[55]
VARIANT MFS SER-2144.
PubMed=8504310; DOI=10.1093/hmg/2.4.475;
Hewett D.R., Lynch J.R., Smith R., Sykes B.C.;
"A novel fibrillin mutation in the Marfan syndrome which could disrupt
calcium binding of the epidermal growth factor-like module.";
Hum. Mol. Genet. 2:475-477(1993).
[56]
VARIANTS MFS ARG-862; TYR-1117; PRO-1137 AND PHE-1589, AND VARIANT
ALA-1148.
PubMed=8281141; DOI=10.1093/hmg/2.11.1813;
Tynan K., Comeau K., Pearson M., Wilgenbus P., Levitt D., Gasner C.,
Berg M.A., Miller D.C., Francke U.;
"Mutation screening of complete fibrillin-1 coding sequence: report of
five new mutations, including two in 8-cysteine domains.";
Hum. Mol. Genet. 2:1813-1821(1993).
[57]
VARIANTS MFS GLY-217 AND ARG-2627.
PubMed=7977366;
Karttunen L., Raghunath M., Loennqvist L., Peltonen L.;
"A compound-heterozygous Marfan patient: two defective fibrillin
alleles result in a lethal phenotype.";
Am. J. Hum. Genet. 55:1083-1091(1994).
[58]
VARIANT ECTOL1 LYS-2447.
PubMed=8188302; DOI=10.1006/geno.1994.1110;
Lonnqvist L., Child A., Kainulainen K., Davidson R., Puhakka L.,
Peltonen L.;
"A novel mutation of the fibrillin gene causing ectopia lentis.";
Genomics 19:573-576(1994).
[59]
VARIANT MFS CYS-627.
PubMed=8004112; DOI=10.1093/hmg/3.2.373;
Hayward C., Rae A.L., Porteous M.E.M., Logie L.J., Brock L.J.;
"Two 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.";
Hum. Mol. Genet. 3:373-375(1994).
[60]
VARIANT MFS GLY-476.
PubMed=7951214; DOI=10.1093/hmg/3.6.1013;
Piersall L.D., Dietz H.C., Hall B.D., Cadle R.G., Pyeritz R.E.,
Francomano C.A., McIntosh I.;
"Substitution of a cysteine residue in a non-calcium binding, EGF-like
domain of fibrillin segregates with the Marfan syndrome in a large
kindred.";
Hum. Mol. Genet. 3:1013-1014(1994).
[61]
VARIANT 2776-ARG--LEU-2781 DEL.
PubMed=7911051; DOI=10.1002/humu.1380030212;
Hayward C., Porteous M.E., Brock D.J.;
"Identification of a novel nonsense mutation in the fibrillin gene
(FBN1) using nonisotopic techniques.";
Hum. Mutat. 3:159-162(1994).
[62]
VARIANT MFS CYS-122.
PubMed=8040326; DOI=10.1172/JCI117389;
Stahl-Hallengren C., Ukkonen T., Kainulainen K., Kristofersson U.,
Saxne T., Tornqvist K., Peltonen L.;
"An 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.";
J. Clin. Invest. 94:709-713(1994).
[63]
VARIANT MFS TYR-1223.
PubMed=8071963; DOI=10.1136/jmg.31.4.338;
Hewett D.R., Lynch J.R., Child A., Sykes B.C.;
"A new missense mutation of fibrillin in a patient with Marfan
syndrome.";
J. Med. Genet. 31:338-339(1994).
[64]
VARIANT MFS HIS-1170.
PubMed=7870075; DOI=10.1006/mcpr.1994.1045;
Hayward C., Porteous M.E.M., Brock D.J.H.;
"A novel mutation in the fibrillin gene (FBN1) in familial
arachnodactyly.";
Mol. Cell. Probes 8:325-327(1994).
[65]
VARIANTS MFS GLY-217; ASN-1023; ARG-1074; TYR-1242; ARG-1513;
GLU-2127; TRP-2151; LYS-2447 AND ARG-2511.
PubMed=8136837; DOI=10.1038/ng0194-64;
Kainulainen K., Karttunen L., Puhakka L., Sakai L., Peltonen L.;
"Mutations in the fibrillin gene responsible for dominant ectopia
lentis and neonatal Marfan syndrome.";
Nat. Genet. 6:64-69(1994).
[66]
VARIANT MFS SER-1127.
PubMed=7762551;
Francke U., Berg M.A., Tynan K., Brenn T., Liu W., Aoyama T.,
Gasner C., Miller D.C., Furthmayr H.;
"A Gly1127Ser mutation in an EGF-like domain of the fibrillin-1 gene
is a risk factor for ascending aortic aneurysm and dissection.";
Am. J. Hum. Genet. 56:1287-1296(1995).
[67]
VARIANTS MFS TYR-129; PHE-166; CYS-746; ARG-926; ARG-1013; LYS-1073;
SER-1382 AND ARG-1928.
PubMed=7611299;
Nijbroek G., Sood S., McIntosh I., Francomano C.A., Bull E.,
Pereira L., Ramirez F., Pyeritz R.E., Dietz H.C.;
"Fifteen novel FBN1 mutations causing Marfan syndrome detected by
heteroduplex analysis of genomic amplicons.";
Am. J. Hum. Genet. 57:8-21(1995).
[68]
VARIANT MFS TYR-1223.
Dietz H.C., Sood I., McIntosh I.;
"The phenotypic continuum associated with FBN1 mutations includes the
Shprintzen-Goldberg syndrome.";
Am. J. Hum. Genet. 57:A211-A211(1995).
[69]
VARIANT TRP-2726, CHARACTERIZATION OF VARIANT TRP-2726, AND
INVOLVEMENT IN MFS.
PubMed=7738200; DOI=10.1172/JCI117930;
Milewicz D.M., Grossfield J., Cao S.-N., Kielty C., Covitz W.,
Jewett T.;
"A mutation in FBN1 disrupts profibrillin processing and results in
isolated skeletal features of the Marfan syndrome.";
J. Clin. Invest. 95:2373-2378(1995).
[70]
VARIANTS MFS ARG-1053; GLY-1072; LYS-1073 AND GLY-1117.
PubMed=8882780;
DOI=10.1002/(SICI)1096-8628(19960329)62:3<233::AID-AJMG7>3.0.CO;2-U;
Putnam E.A., Cho M., Zinn A.B., Towbin J.A., Byers P.H.,
Milewicz D.M.;
"Delineation of the Marfan phenotype associated with mutations in
exons 23-32 of the FBN1 gene.";
Am. J. Med. Genet. 62:233-242(1996).
[71]
VARIANTS MFS THR-705; TYR-711; GLY-1055 AND TYR-1153.
PubMed=8863159; DOI=10.1136/jmg.33.8.665;
Ades L.C., Haan E.A., Colley A.F., Richards R.I.;
"Characterisation of four novel fibrillin-1 (FBN1) mutations in Marfan
syndrome.";
J. Med. Genet. 33:665-671(1996).
[72]
VARIANT MFS TYR-587.
PubMed=9254848; DOI=10.1007/s004390050489;
Booms P., Withers A.P., Boxer M., Kaufmann U.C., Hagemeier C.,
Vetter U., Robinson P.N.;
"A 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.";
Hum. Genet. 100:195-200(1997).
[73]
VARIANT ALA-1148.
PubMed=9150726; DOI=10.1007/s004390050414;
Schrijver I., Liu W., Francke U.;
"The pathogenicity of the Pro1148Ala substitution in the FBN1 gene:
causing or predisposing to Marfan syndrome and aortic aneurysm, or
clinically innocent?";
Hum. Genet. 99:607-611(1997).
[74]
VARIANTS 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-2489.
PubMed=9338581;
DOI=10.1002/(SICI)1098-1004(1997)10:4<280::AID-HUMU3>3.3.CO;2-L;
Hayward C., Porteous M.E.M., Brock D.J.H.;
"Mutation screening of all 65 exons of the fibrillin-1 gene in 60
patients with Marfan syndrome: report of 12 novel mutations.";
Hum. Mutat. 10:280-289(1997).
[75]
VARIANT ALA-1148.
PubMed=9338588;
DOI=10.1002/(SICI)1098-1004(1997)10:4<326::AID-HUMU10>3.0.CO;2-1;
Watanabe Y., Yano S., Koga Y., Yukizane S., Nishiyori A., Yoshino M.,
Kato H.;
"P1148A in fibrillin-1 is not a mutation leading to Shprintzen-
Goldberg syndrome.";
Hum. Mutat. 10:326-327(1997).
[76]
VARIANTS MFS ARG-996; THR-1048; THR-1048 DEL; CYS-1058 INS; TRP-1086;
SER-1837 AND CYS-2680.
PubMed=9401003;
DOI=10.1002/(SICI)1098-1004(1997)10:6<415::AID-HUMU1>3.3.CO;2-2;
Hayward C., Brock D.J.H.;
"Fibrillin-1 mutations in Marfan syndrome and other type-1
fibrillinopathies.";
Hum. Mutat. 10:415-423(1997).
[77]
VARIANT ALA-1148.
PubMed=8988160; DOI=10.1038/ng0197-12;
Wang M., Mathews K.R., Imaizumi K., Beiraghi S., Blumberg B.,
Scheuner M., Graham J.M. Jr., Godfrey M.;
"P1148A in fibrillin-1 is not a mutation anymore.";
Nat. Genet. 15:12-12(1997).
[78]
VARIANTS MFS ARG-661; ARG-1043 AND ARG-2511.
PubMed=9016526; DOI=10.1093/nar/25.1.147;
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.;
"Marfan Database (second edition): software and database for the
analysis of mutations in the human FBN1 gene.";
Nucleic Acids Res. 25:147-150(1997).
[79]
VARIANT MFS ARG-1265.
PubMed=9837823; DOI=10.1086/302144;
Montgomery R.A., Geraghty M.T., Bull E., Gelb B.D., Johnson M.,
McIntosh I., Francomano C.A., Dietz H.C.;
"Multiple molecular mechanisms underlying subdiagnostic variants of
Marfan syndrome.";
Am. J. Hum. Genet. 63:1703-1711(1998).
[80]
VARIANT MFS CYS-122.
PubMed=9452085;
Black C., Withers A.P., Gray J.R., Bridges A.B., Craig A., Baty D.U.,
Boxer M.;
"Correlation of a recurrent FBN1 mutation (R122C) with an atypical
familial Marfan syndrome phenotype.";
Hum. Mutat. Suppl. 1:S198-S200(1998).
[81]
VARIANT MFS ILE-984.
PubMed=10694921;
DOI=10.1002/(SICI)1098-1004(1998)12:2<137::AID-HUMU14>3.3.CO;2-G;
Grau U., Klein H.-G., Detter C., Mair H., Welz A., Seidel D.,
Reichart B.;
"A novel mutation in the neonatal region of the fibrillin (FBN) 1 gene
associated with a classical phenotype of Marfan syndrome (MfS).";
Hum. Mutat. 12:137-137(1998).
[82]
VARIANT MFS GLU-985.
PubMed=10441597; DOI=10.1086/302545;
Collod-Beroud G., Lackmy-Port-Lys M., Jondeau G., Mathieu M.,
Maingourd Y., Coulon M., Guillotel M., Junien C., Boileau C.;
"Demonstration of the recurrence of Marfan-like skeletal and
cardiovascular manifestations due to germline mosaicism for an FBN1
mutation.";
Am. J. Hum. Genet. 65:917-921(1999).
[83]
VARIANTS MFS PHE-504; TYR-1129; CYS-1261; SER-1833 AND TYR-2142.
PubMed=10425041;
DOI=10.1002/(SICI)1098-1004(1999)14:2<181::AID-HUMU10>3.3.CO;2-Y;
El-Aleem A.A., Karck M., Haverich A., Schmidtke J.,
Arslan-Kirchner M.;
"Identification of 9 novel FBN1 mutations in German patients with
Marfan syndrome.";
Hum. Mutat. 14:181-181(1999).
[84]
VARIANTS 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-2668, VARIANT ECTOL1 ARG-2154, VARIANT MITRAL VALVE PROLAPSE
ILE-1128, AND VARIANT CYS-1530.
PubMed=11700157; DOI=10.1001/archinte.161.20.2447;
Loeys B., Nuytinck L., Delvaux I., De Bie S., De Paepe A.;
"Genotype and phenotype analysis of 171 patients referred for
molecular study of the fibrillin-1 gene FBN1 because of suspected
Marfan syndrome.";
Arch. Intern. Med. 161:2447-2454(2001).
[85]
VARIANTS 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-2335, VARIANTS ECTOL1 CYS-115; TYR-661 AND TYR-2339,
AND VARIANT MET-2101.
PubMed=12203992; DOI=10.1002/humu.10112;
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.;
"TGGE screening of the entire FBN1 coding sequence in 126 individuals
with Marfan syndrome and related fibrillinopathies.";
Hum. Mutat. 20:197-208(2002).
[86]
VARIANTS MFS 429-ARG--HIS-2871 DEL; ILE-449; SER-880; CYS-1101;
TYR-1806; ILE-1908; ASP-1919 AND ARG-2251.
PubMed=12402346; DOI=10.1002/humu.9075;
Rommel K., Karck M., Haverich A., Schmidtke J., Arslan-Kirchner M.;
"Mutation 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.";
Hum. Mutat. 20:406-407(2002).
[87]
VARIANTS MFS CYS-114; ARG-890; GLY-1200; TYR-1835; ARG-2111; CYS-2474
AND GLY-2652, AND VARIANT ECTOL1 CYS-240.
PubMed=11826022; DOI=10.1136/jmg.39.1.34;
Koerkkoe J., Kaitila I., Loennqvist L., Peltonen L., Ala-Kokko L.;
"Sensitivity of conformation sensitive gel electrophoresis in
detecting mutations in Marfan syndrome and related conditions.";
J. Med. Genet. 39:34-41(2002).
[88]
VARIANTS 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 DEL, AND VARIANT
PRO-2780.
PubMed=12161601; DOI=10.1136/jmg.39.8.589;
Halliday D.J., Hutchinson S., Lonie L., Hurst J.A., Firth H.,
Handford P.A., Wordsworth P.;
"Twelve novel FBN1 mutations in Marfan syndrome and Marfan related
phenotypes test the feasibility of FBN1 mutation testing in clinical
practice.";
J. Med. Genet. 39:589-593(2002).
[89]
VARIANT WMS2 1692-ARG--TYR-1699 DEL.
PubMed=12525539; DOI=10.1136/jmg.40.1.34;
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.;
"In frame fibrillin-1 gene deletion in autosomal dominant Weill-
Marchesani syndrome.";
J. Med. Genet. 40:34-36(2003).
[90]
VARIANTS 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; TYR-1564; PHE-1770; TRP-1793; GLU-1796; TRP-2442;
THR-2585 AND PRO-2623, AND VARIANT CYS-1530.
PubMed=14695540; DOI=10.1002/humu.9207;
Biggin A., Holman K., Brett M., Bennetts B., Ades L.;
"Detection of thirty novel FBN1 mutations in patients with Marfan
syndrome or a related fibrillinopathy.";
Hum. Mutat. 23:99-99(2004).
[91]
CHARACTERIZATION OF VARIANTS MFS CYS-627; GLY-750 AND ARG-926.
PubMed=15161917; DOI=10.1074/jbc.M405239200;
Vollbrandt T., Tiedemann K., El-Hallous E., Lin G., Brinckmann J.,
John H., Baetge B., Notbohm H., Reinhardt D.P.;
"Consequences of cysteine mutations in calcium-binding epidermal
growth factor modules of fibrillin-1.";
J. Biol. Chem. 279:32924-32931(2004).
[92]
VARIANTS 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-2629.
PubMed=16222657; DOI=10.1002/humu.9377;
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.;
"Identification of sixty-two novel and twelve known FBN1 mutations in
eighty-one unrelated probands with Marfan syndrome and other
fibrillinopathies.";
Hum. Mutat. 26:494-494(2005).
[93]
VARIANTS 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-2605.
PubMed=16220557; DOI=10.1002/humu.20239;
Rommel K., Karck M., Haverich A., von Kodolitsch Y., Rybczynski M.,
Muller G., Singh K.K., Schmidtke J., Arslan-Kirchner M.;
"Identification of 29 novel and nine recurrent fibrillin-1 (FBN1)
mutations and genotype-phenotype correlations in 76 patients with
Marfan syndrome.";
Hum. Mutat. 26:529-539(2005).
[94]
VARIANTS 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-2618, VARIANTS 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-2448, AND VARIANTS 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 DEL.
PubMed=17657824; DOI=10.1002/humu.9505;
Comeglio P., Johnson P., Arno G., Brice G., Evans A.,
Aragon-Martin J., da Silva F.P., Kiotsekoglou A., Child A.;
"The importance of mutation detection in Marfan syndrome and Marfan-
related disorders: report of 193 FBN1 mutations.";
Hum. Mutat. 28:928-928(2007).
[95]
VARIANTS 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 DEL, AND
VARIANTS PRO-39; ARG-937; ALA-1020; TRP-2726 AND 2774-LYS--HIS-2871
DEL.
PubMed=18435798; DOI=10.1111/j.1399-0004.2008.01007.x;
Attanasio M., Lapini I., Evangelisti L., Lucarini L., Giusti B.,
Porciani M., Fattori R., Anichini C., Abbate R., Gensini G., Pepe G.;
"FBN1 mutation screening of patients with Marfan syndrome and related
disorders: detection of 46 novel FBN1 mutations.";
Clin. Genet. 74:39-46(2008).
[96]
VARIANTS 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-2708.
PubMed=19533785; DOI=10.1002/ajmg.a.32918;
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.;
"Identification of novel FBN1 and TGFBR2 mutations in 65 probands with
Marfan syndrome or Marfan-like phenotypes.";
Am. J. Med. Genet. A 149A:1452-1459(2009).
[97]
VARIANT 2867-GLN--HIS-2871 DEL.
PubMed=19293843; DOI=10.1038/ejhg.2009.36;
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.;
"Identification of the minimal combination of clinical features in
probands for efficient mutation detection in the FBN1 gene.";
Eur. J. Hum. Genet. 17:1121-1128(2009).
[98]
VARIANT MFS GLY-1068.
PubMed=20803651; DOI=10.1002/ajmg.a.33406;
Barnett C.P., Wilson G.J., Chiasson D.A., Gross G.J., Hinek A.,
Hawkins C., Chitayat D.;
"Central nervous system abnormalities in two cases with neonatal
Marfan syndrome with novel mutations in the fibrillin-1 gene.";
Am. J. Med. Genet. A 152:2409-2412(2010).
[99]
VARIANT 2849-TYR--HIS-2871 DEL.
PubMed=21034599;
Gao L.G., Zhang L., Song L., Wang H., Chang Q., Wu Y.B., Hui R.T.,
Zhou X.L.;
"Identification of a novel lethal fibrillin-1 gene mutation in a
Chinese Marfan family and correlation of 3' fibrillin-1 gene mutations
with phenotype.";
Chin. Med. J. 123:2874-2878(2010).
[100]
VARIANT ALA-1148.
PubMed=20547088; DOI=10.1016/j.legalmed.2010.04.001;
Yuasa I., Umetsu K., Matsusue A., Nishimukai H., Harihara S.,
Fukumori Y., Saitou N., Jin F., Chattopadhyay P.K., Henke L.,
Henke J.;
"A Japanese-specific allele in the GALNT11 gene.";
Leg. Med. 12:208-211(2010).
[101]
VARIANTS SSKS SER-1564; CYS-1570; GLY-1577 AND ASP-1594.
PubMed=20375004; DOI=10.1126/scitranslmed.3000488;
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.;
"Mutations in fibrillin-1 cause congenital scleroderma: stiff skin
syndrome.";
Sci. Transl. Med. 2:23RA20-23RA20(2010).
[102]
VARIANTS GPHYSD2 CYS-1696; ASP-1699; CYS-1699; TYR-1706; TRP-1719;
THR-1728; VAL-1728; TYR-1733 AND SER-1762, AND VARIANTS ACMICD
CYS-1699; CYS-1700; ARG-1714; CYS-1722; VAL-1726; THR-1728; GLN-1735
INS; ARG-1750 AND VAL-1758.
PubMed=21683322; DOI=10.1016/j.ajhg.2011.05.012;
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.;
"Mutations in the TGFbeta binding-protein-like domain 5 of FBN1 are
responsible for acromicric and geleophysic dysplasias.";
Am. J. Hum. Genet. 89:7-14(2011).
[103]
VARIANTS 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-2646, AND VARIANTS GLY-1481 AND HIS-2793.
PubMed=21542060; DOI=10.1002/humu.21525;
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.;
"Applying massive parallel sequencing to molecular diagnosis of Marfan
and Loeys-Dietz syndromes.";
Hum. Mutat. 32:1053-1062(2011).
[104]
VARIANTS 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 DEL.
PubMed=22772377; DOI=10.1007/s00109-012-0931-y;
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.;
"Exon 47 skipping of fibrillin-1 leads preferentially to
cardiovascular defects in patients with thoracic aortic aneurysms and
dissections.";
J. Mol. Med. 91:37-47(2013).
-!- FUNCTION: Fibrillin-1: Structural 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. 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. 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. 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. This
leads to disruption of TNFSF11-induced Ca2+ 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). {ECO:0000250|UniProtKB:Q61554,
ECO:0000269|PubMed:11461921, ECO:0000269|PubMed:12807887,
ECO:0000269|PubMed:15062093, ECO:0000269|PubMed:17158881,
ECO:0000269|PubMed:1860873, ECO:0000269|PubMed:24039232,
ECO:0000303|PubMed:27026396}.
-!- FUNCTION: Asprosin: Hormone that targets the liver to increase
plasma glucose levels. Secreted by white adipose tissue and
circulates in the plasma. Acts in response to fasting and promotes
blood glucose elevation by binding to the surface of hepatocytes.
Promotes hepatocyte glucose release by activating the protein
kinase A activity in the liver, resulting in rapid glucose release
into the circulation. {ECO:0000269|PubMed:27087445}.
-!- SUBUNIT: 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, FBLN4 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). {ECO:0000250|UniProtKB:Q61554,
ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:15062093,
ECO:0000269|PubMed:15131124, ECO:0000269|PubMed:15165854,
ECO:0000269|PubMed:15790312, ECO:0000269|PubMed:17158881,
ECO:0000269|PubMed:17255108, ECO:0000269|PubMed:17293099,
ECO:0000269|PubMed:18339631, ECO:0000269|PubMed:21402694,
ECO:0000269|PubMed:23010571, ECO:0000269|PubMed:24039232,
ECO:0000269|PubMed:26601954}.
-!- INTERACTION:
O95967:EFEMP2; NbExp=3; IntAct=EBI-2505934, EBI-743414;
Q9UBX5:FBLN5; NbExp=3; IntAct=EBI-2505934, EBI-947897;
P35556:FBN2; NbExp=2; IntAct=EBI-2505934, EBI-6164392;
P02751:FN1; NbExp=2; IntAct=EBI-2505934, EBI-1220319;
P28300:LOX; NbExp=2; IntAct=EBI-2505934, EBI-3893481;
Q14766-2:LTBP1; NbExp=2; IntAct=EBI-2505934, EBI-11173832;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24982166}.
Note=Fibrillin-1 and Asprosin chains are still linked together
during the secretion from cells, but are subsequently separated by
furin (PubMed:24982166). {ECO:0000269|PubMed:24982166}.
-!- SUBCELLULAR LOCATION: Asprosin: Secreted
{ECO:0000269|PubMed:27087445}. Note=Secreted into the plasma.
{ECO:0000269|PubMed:27087445}.
-!- SUBCELLULAR LOCATION: Fibrillin-1: Secreted, extracellular space,
extracellular matrix {ECO:0000269|PubMed:11461921,
ECO:0000269|PubMed:24982166}.
-!- PTM: Fibrillin-1: 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). {ECO:0000269|PubMed:10636927,
ECO:0000269|PubMed:24982166, ECO:0000303|PubMed:27026396}.
-!- PTM: Fibrillin-1: Forms intermolecular disulfide bonds either with
other fibrillin-1 molecules or with other components of the
microfibrils. {ECO:0000269|PubMed:9362480}.
-!- DISEASE: Marfan syndrome (MFS) [MIM:154700]: A hereditary disorder
of connective tissue that affects the skeletal, ocular, and
cardiovascular systems. A wide variety of skeletal abnormalities
occurs with Marfan syndrome, including scoliosis, chest wall
deformity, tall stature, abnormal joint mobility. Ectopia lentis
occurs in most of the patients and is almost always bilateral. The
leading cause of premature death is progressive dilation of the
aortic root and ascending aorta, causing aortic incompetence and
dissection. Neonatal Marfan syndrome is the most severe form
resulting in death from cardiorespiratory failure in the first few
years of life. {ECO:0000269|PubMed:10425041,
ECO:0000269|PubMed:10441597, ECO:0000269|PubMed:10694921,
ECO:0000269|PubMed:11700157, ECO:0000269|PubMed:11826022,
ECO:0000269|PubMed:12161601, ECO:0000269|PubMed:12203992,
ECO:0000269|PubMed:12402346, ECO:0000269|PubMed:1301946,
ECO:0000269|PubMed:14695540, ECO:0000269|PubMed:15161917,
ECO:0000269|PubMed:15221638, ECO:0000269|PubMed:1569206,
ECO:0000269|PubMed:16220557, ECO:0000269|PubMed:16222657,
ECO:0000269|PubMed:17657824, ECO:0000269|PubMed:18435798,
ECO:0000269|PubMed:1852208, ECO:0000269|PubMed:19533785,
ECO:0000269|PubMed:20803651, ECO:0000269|PubMed:21542060,
ECO:0000269|PubMed:22772377, ECO:0000269|PubMed:7611299,
ECO:0000269|PubMed:7738200, ECO:0000269|PubMed:7762551,
ECO:0000269|PubMed:7870075, ECO:0000269|PubMed:7951214,
ECO:0000269|PubMed:7977366, ECO:0000269|PubMed:8004112,
ECO:0000269|PubMed:8040326, ECO:0000269|PubMed:8071963,
ECO:0000269|PubMed:8136837, ECO:0000269|PubMed:8281141,
ECO:0000269|PubMed:8406497, ECO:0000269|PubMed:8504310,
ECO:0000269|PubMed:8863159, ECO:0000269|PubMed:8882780,
ECO:0000269|PubMed:9016526, ECO:0000269|PubMed:9254848,
ECO:0000269|PubMed:9338581, ECO:0000269|PubMed:9401003,
ECO:0000269|PubMed:9452085, ECO:0000269|PubMed:9837823,
ECO:0000269|Ref.68}. Note=The disease is caused by mutations
affecting the gene represented in this entry. The majority of the
more than 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.
-!- DISEASE: Ectopia lentis 1, isolated, autosomal dominant (ECTOL1)
[MIM:129600]: An ocular abnormality characterized by partial or
complete displacement of the lens from its space resulting from
defective zonule formation. {ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:11826022, ECO:0000269|PubMed:12203992,
ECO:0000269|PubMed:17657824, ECO:0000269|PubMed:8188302}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Weill-Marchesani syndrome 2 (WMS2) [MIM:608328]: A rare
connective tissue disorder characterized by short stature,
brachydactyly, joint stiffness, and eye abnormalities including
microspherophakia, ectopia lentis, severe myopia and glaucoma.
{ECO:0000269|PubMed:12525539}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Overlap connective tissue disease (OCTD) [MIM:604308]:
Heritable disorder of connective tissue characterized by
involvement of the mitral valve, aorta, skeleton, and skin. MASS
syndrome is closely resembling both the Marfan syndrome and the
Barlow syndrome. However, no dislocation of the lenses or
aneurysmal changes occur in the aorta, and the mitral valve
prolapse is by no means invariable. {ECO:0000269|PubMed:2739055}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Stiff skin syndrome (SSKS) [MIM:184900]: A syndrome
characterized by hard, thick skin, usually over the entire body,
which limits joint mobility and causes flexion contractures. Other
occasional findings include lipodystrophy and muscle weakness.
{ECO:0000269|PubMed:20375004}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Geleophysic dysplasia 2 (GPHYSD2) [MIM:614185]: An
autosomal dominant disorder characterized by severe short stature,
short hands and feet, joint limitations, and skin thickening.
Radiologic features include delayed bone age, cone-shaped
epiphyses, shortened long tubular bones, and ovoid vertebral
bodies. Affected individuals have characteristic facial features
including a 'happy' face with full cheeks, shortened nose,
hypertelorism, long and flat philtrum, and thin upper lip. Other
distinctive features include progressive cardiac valvular
thickening often leading to an early death, toe walking, tracheal
stenosis, respiratory insufficiency, and lysosomal-like storage
vacuoles in various tissues. {ECO:0000269|PubMed:21683322}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Acromicric dysplasia (ACMICD) [MIM:102370]: An autosomal
dominant disorder characterized by severe short stature, short
hands and feet, joint limitations, and skin thickening. Radiologic
features include delayed bone age, cone-shaped epiphyses,
shortened long tubular bones, and ovoid vertebral bodies. Affected
individuals have distinct facial features, including round face,
well-defined eyebrows, long eyelashes, bulbous nose with
anteverted nostrils, long and prominent philtrum, and thick lips
with a small mouth. Other characteristic features include hoarse
voice and pseudomuscular build, and there are distinct skeletal
features as well, including an internal notch of the femoral head,
internal notch of the second metacarpal, and external notch of the
fifth metacarpal. {ECO:0000269|PubMed:21683322}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Marfan lipodystrophy syndrome (MFLS) [MIM:616914]: A
syndrome characterized by congenital lipodystrophy, a progeroid
facial appearance due to lack of subcutaneous fat, and variable
signs of Marfan syndrome. Clinical features include premature
birth with an accelerated linear growth disproportionate to the
weight gain, ectopia lentis, aortic dilatation, dural ectasia, and
arachnodactyly. Mental and motor development are within normal
limits. {ECO:0000269|PubMed:20979188, ECO:0000269|PubMed:21594992,
ECO:0000269|PubMed:21594993, ECO:0000269|PubMed:24039054,
ECO:0000269|PubMed:24613577, ECO:0000269|PubMed:24665001,
ECO:0000269|PubMed:26860060, ECO:0000269|PubMed:27087445}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. Asprosin: Mutations specifically affect
Asprosin, a hormone peptide present at the C-terminus of
Fibrillin-1 chain, which is cleaved from Fibrillin-1 following
secretion (PubMed:27087445). {ECO:0000269|PubMed:27087445}.
-!- MISCELLANEOUS: Asprosin: Was named after the Greek word for white,
because of the reduction in subcutaneous white adipose tissue that
is displayed by asprosin-deficient patients.
{ECO:0000303|PubMed:27087445}.
-!- SIMILARITY: Belongs to the fibrillin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA45118.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L13923; AAB02036.1; -; mRNA.
EMBL; AB177803; BAD16739.1; -; Genomic_DNA.
EMBL; GU143398; ACZ58372.1; -; Genomic_DNA.
EMBL; AC022467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471082; EAW77354.1; -; Genomic_DNA.
EMBL; BC146854; AAI46855.1; -; mRNA.
EMBL; L19896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X63556; CAA45118.1; ALT_INIT; mRNA.
EMBL; X62008; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S54426; AAB25244.1; -; Genomic_DNA.
EMBL; S54425; AAB25244.1; JOINED; Genomic_DNA.
CCDS; CCDS32232.1; -.
PIR; A47221; A47221.
RefSeq; NP_000129.3; NM_000138.4.
UniGene; Hs.591133; -.
PDB; 1APJ; NMR; -; A=2052-2125.
PDB; 1EMN; NMR; -; A=2124-2205.
PDB; 1EMO; NMR; -; A=2124-2205.
PDB; 1LMJ; NMR; -; A=1069-1154.
PDB; 1UZJ; X-ray; 2.25 A; A/B/C=1486-1647.
PDB; 1UZK; X-ray; 1.35 A; A=1486-1647.
PDB; 1UZP; X-ray; 1.78 A; A=1486-1647.
PDB; 1UZQ; X-ray; 2.40 A; A=1486-1647.
PDB; 2M74; NMR; -; A=45-178.
PDB; 2W86; X-ray; 1.80 A; A=807-951.
PDBsum; 1APJ; -.
PDBsum; 1EMN; -.
PDBsum; 1EMO; -.
PDBsum; 1LMJ; -.
PDBsum; 1UZJ; -.
PDBsum; 1UZK; -.
PDBsum; 1UZP; -.
PDBsum; 1UZQ; -.
PDBsum; 2M74; -.
PDBsum; 2W86; -.
ProteinModelPortal; P35555; -.
SMR; P35555; -.
BioGrid; 108494; 11.
DIP; DIP-29985N; -.
ELM; P35555; -.
IntAct; P35555; 26.
MINT; MINT-206075; -.
STRING; 9606.ENSP00000325527; -.
iPTMnet; P35555; -.
PhosphoSitePlus; P35555; -.
BioMuta; FBN1; -.
DMDM; 311033452; -.
EPD; P35555; -.
MaxQB; P35555; -.
PaxDb; P35555; -.
PeptideAtlas; P35555; -.
PRIDE; P35555; -.
Ensembl; ENST00000316623; ENSP00000325527; ENSG00000166147.
GeneID; 2200; -.
KEGG; hsa:2200; -.
UCSC; uc001zwx.3; human.
CTD; 2200; -.
DisGeNET; 2200; -.
EuPathDB; HostDB:ENSG00000166147.13; -.
GeneCards; FBN1; -.
GeneReviews; FBN1; -.
HGNC; HGNC:3603; FBN1.
HPA; CAB002670; -.
HPA; CAB058696; -.
HPA; CAB068188; -.
HPA; HPA017759; -.
HPA; HPA021057; -.
MalaCards; FBN1; -.
MIM; 102370; phenotype.
MIM; 129600; phenotype.
MIM; 134797; gene.
MIM; 154700; phenotype.
MIM; 184900; phenotype.
MIM; 604308; phenotype.
MIM; 608328; phenotype.
MIM; 614185; phenotype.
MIM; 616914; phenotype.
neXtProt; NX_P35555; -.
Orphanet; 969; Acromicric dysplasia.
Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection.
Orphanet; 2623; Geleophysic dysplasia.
Orphanet; 2084; Glaucoma - ectopia - microspherophakia - stiff joints - short stature.
Orphanet; 1885; Isolated ectopia lentis.
Orphanet; 284963; Marfan syndrome type 1.
Orphanet; 284979; Neonatal Marfan syndrome.
Orphanet; 300382; Progeroid and marfanoid aspect-lipodystrophy syndrome.
Orphanet; 2462; Shprintzen-Goldberg syndrome.
Orphanet; 2833; Stiff skin syndrome.
Orphanet; 3449; Weill-Marchesani syndrome.
PharmGKB; PA28016; -.
eggNOG; ENOG410IR7H; Eukaryota.
eggNOG; ENOG410XSTY; LUCA.
HOGENOM; HOG000231768; -.
HOVERGEN; HBG005643; -.
InParanoid; P35555; -.
KO; K06825; -.
OrthoDB; EOG091G002H; -.
PhylomeDB; P35555; -.
TreeFam; TF316849; -.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1566948; Elastic fibre formation.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P35555; -.
ChiTaRS; FBN1; human.
EvolutionaryTrace; P35555; -.
GeneWiki; FBN1; -.
GenomeRNAi; 2200; -.
PRO; PR:P35555; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000166147; -.
CleanEx; HS_FBN1; -.
ExpressionAtlas; P35555; baseline and differential.
Genevisible; P35555; HS.
GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0001527; C:microfibril; IDA:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; IC:UniProtKB.
GO; GO:0005201; F:extracellular matrix structural constituent; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0005179; F:hormone activity; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IPI:UniProtKB.
GO; GO:0034199; P:activation of protein kinase A activity; IDA:UniProtKB.
GO; GO:0043010; P:camera-type eye development; IEP:UniProtKB.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0048048; P:embryonic eye morphogenesis; IEP:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; IDA:UniProtKB.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0001656; P:metanephros development; IEA:Ensembl.
GO; GO:2001205; P:negative regulation of osteoclast development; IDA:UniProtKB.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:UniProtKB.
GO; GO:0048050; P:post-embryonic eye morphogenesis; IEP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0010737; P:protein kinase A signaling; IDA:UniProtKB.
GO; GO:0090287; P:regulation of cellular response to growth factor stimulus; IBA:GO_Central.
GO; GO:0035582; P:sequestering of BMP in extracellular matrix; ISS:BHF-UCL.
GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; ISS:BHF-UCL.
GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
Gene3D; 3.90.290.10; -; 9.
InterPro; IPR026823; cEGF.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR011398; FBN.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR017878; TB_dom.
PANTHER; PTHR24039; PTHR24039; 1.
Pfam; PF12662; cEGF; 2.
Pfam; PF07645; EGF_CA; 38.
Pfam; PF00683; TB; 9.
SMART; SM00181; EGF; 47.
SMART; SM00179; EGF_CA; 44.
SUPFAM; SSF57184; SSF57184; 10.
SUPFAM; SSF57581; SSF57581; 9.
PROSITE; PS00010; ASX_HYDROXYL; 43.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 38.
PROSITE; PS50026; EGF_3; 44.
PROSITE; PS01187; EGF_CA; 43.
PROSITE; PS51364; TB; 9.
1: Evidence at protein level;
3D-structure; Aortic aneurysm; Calcium; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond; Dwarfism;
EGF-like domain; Extracellular matrix; Glycoprotein; Heparin-binding;
Hormone; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:10636927}.
PROPEP 25 44 {ECO:0000269|PubMed:10636927}.
/FTId=PRO_0000436881.
CHAIN 45 2731 Fibrillin-1.
{ECO:0000305|PubMed:10636927,
ECO:0000305|PubMed:24982166}.
/FTId=PRO_0000007581.
CHAIN 2732 2871 Asprosin. {ECO:0000305|PubMed:27087445,
ECO:0000305|PubMed:9817919}.
/FTId=PRO_0000436882.
DOMAIN 81 112 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 115 146 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 147 178 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 184 236 TB 1.
DOMAIN 246 287 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 288 329 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 334 389 TB 2.
DOMAIN 449 489 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 490 529 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 530 571 EGF-like 8; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 572 612 EGF-like 9; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 613 653 EGF-like 10; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 659 711 TB 3.
DOMAIN 723 764 EGF-like 11; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 765 806 EGF-like 12; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 807 846 EGF-like 13; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 851 902 TB 4.
DOMAIN 910 951 EGF-like 14; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 956 1008 TB 5.
DOMAIN 1028 1069 EGF-like 15; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1070 1112 EGF-like 16; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1113 1154 EGF-like 17; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1155 1196 EGF-like 18; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1197 1237 EGF-like 19; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1238 1279 EGF-like 20; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1280 1321 EGF-like 21; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1322 1362 EGF-like 22; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1363 1403 EGF-like 23; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1404 1445 EGF-like 24; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1446 1486 EGF-like 25; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1487 1527 EGF-like 26; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1532 1589 TB 6.
DOMAIN 1606 1647 EGF-like 27; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1648 1688 EGF-like 28; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1693 1748 TB 7.
DOMAIN 1766 1807 EGF-like 29; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1808 1848 EGF-like 30; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1849 1890 EGF-like 31; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1891 1929 EGF-like 32; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1930 1972 EGF-like 33; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1973 2012 EGF-like 34; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2013 2054 EGF-like 35; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2059 2111 TB 8.
DOMAIN 2127 2165 EGF-like 36; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2166 2205 EGF-like 37; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2206 2246 EGF-like 38; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2247 2290 EGF-like 39; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2291 2332 EGF-like 40; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2337 2390 TB 9.
DOMAIN 2402 2443 EGF-like 41; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2444 2484 EGF-like 42; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2485 2523 EGF-like 43; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2524 2566 EGF-like 44; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2567 2606 EGF-like 45; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2607 2647 EGF-like 46; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2648 2687 EGF-like 47; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REGION 45 450 N-terminal domain.
{ECO:0000269|PubMed:11461921}.
REGION 45 81 Fibrillin unique N-terminal (FUN) domain.
{ECO:0000305|PubMed:24035709}.
REGION 119 329 Interaction with MFAP4.
{ECO:0000269|PubMed:26601954}.
REGION 195 221 Hybrid domain 1.
{ECO:0000305|PubMed:19446531}.
REGION 862 887 Hybrid domain 2.
{ECO:0000305|PubMed:19446531}.
REGION 1528 2731 C-terminal domain.
{ECO:0000269|PubMed:11461921}.
MOTIF 1541 1543 Cell attachment site.
{ECO:0000269|PubMed:12807887}.
COMPBIAS 402 446 Pro-rich.
SITE 44 45 Cleavage; by furin.
{ECO:0000305|PubMed:10636927}.
SITE 2731 2732 Cleavage; by furin.
{ECO:0000269|PubMed:24982166,
ECO:0000269|PubMed:9817919}.
MOD_RES 2702 2702 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
MOD_RES 2709 2709 Phosphoserine.
{ECO:0000250|UniProtKB:Q61554}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1067 1067 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1149 1149 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1369 1369 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1484 1484 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1581 1581 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1669 1669 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1703 1703 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1713 1713 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1902 1902 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2077 2077 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2178 2178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2734 2734 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2750 2750 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2767 2767 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 59 68 {ECO:0000269|PubMed:24035709}.
DISULFID 67 80 {ECO:0000269|PubMed:24035709}.
DISULFID 85 94 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:24035709}.
DISULFID 89 100 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:24035709}.
DISULFID 102 111 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:24035709}.
DISULFID 119 129 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:24035709}.
DISULFID 123 134 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:24035709}.
DISULFID 136 145 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:24035709}.
DISULFID 150 160 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:24035709}.
DISULFID 154 166 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:24035709}.
DISULFID 168 177 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:24035709}.
DISULFID 250 262 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 257 271 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 273 286 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 292 304 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 299 313 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 315 328 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 453 465 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 460 474 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 476 488 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 494 504 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 499 513 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 515 528 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 534 546 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 541 555 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 557 570 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 576 587 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 582 596 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 598 611 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 617 628 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 623 637 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 639 652 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 727 739 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 734 748 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 750 763 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 769 781 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 776 790 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 792 805 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 811 821 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:19446531}.
DISULFID 816 830 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:19446531}.
DISULFID 832 845 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:19446531}.
DISULFID 853 875 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:19446531}.
DISULFID 862 887 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:19446531}.
DISULFID 876 890 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:19446531}.
DISULFID 896 908 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:19446531}.
DISULFID 914 926 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:19446531}.
DISULFID 921 935 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:19446531}.
DISULFID 937 950 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:19446531}.
DISULFID 1032 1044 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1039 1053 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1055 1068 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1074 1086 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:12511552}.
DISULFID 1081 1095 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:12511552}.
DISULFID 1097 1111 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:12511552}.
DISULFID 1117 1129 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:12511552}.
DISULFID 1124 1138 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:12511552}.
DISULFID 1140 1153 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1159 1171 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1166 1180 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1182 1195 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1201 1212 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1208 1221 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1223 1236 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1242 1254 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1249 1263 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1265 1278 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1284 1296 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1291 1305 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1307 1320 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1326 1339 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1333 1348 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1350 1361 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1367 1380 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1374 1389 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1391 1402 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1408 1420 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1415 1429 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1431 1444 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1450 1461 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1456 1470 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1472 1485 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1491 1502 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:15062093}.
DISULFID 1497 1511 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:15062093}.
DISULFID 1513 1526 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:15062093}.
DISULFID 1534 1562 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:15062093}.
DISULFID 1549 1574 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:15062093}.
DISULFID 1563 1577 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:15062093}.
DISULFID 1564 1589 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:15062093}.
DISULFID 1610 1622 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:15062093}.
DISULFID 1617 1631 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:15062093}.
DISULFID 1633 1646 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:15062093}.
DISULFID 1652 1663 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1658 1672 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1674 1687 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1770 1782 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1777 1791 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1793 1806 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1812 1824 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1818 1833 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1835 1847 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1853 1865 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1860 1874 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1876 1889 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1895 1905 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1900 1914 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1916 1928 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1934 1947 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1942 1956 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1958 1971 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1977 1989 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1984 1998 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2000 2011 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2017 2029 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2024 2038 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2040 2053 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2061 2083 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:9362480}.
DISULFID 2070 2096 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:9362480}.
DISULFID 2084 2099 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:9362480}.
DISULFID 2085 2111 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:9362480}.
DISULFID 2131 2142 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2137 2151 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2153 2164 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2170 2181 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2176 2190 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2192 2204 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2210 2221 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2217 2230 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2232 2245 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2251 2265 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2258 2274 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2276 2289 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2295 2307 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2302 2316 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2318 2331 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2406 2418 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2413 2427 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2429 2442 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2448 2459 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2455 2468 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2470 2483 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2489 2500 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2496 2509 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2511 2522 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2528 2541 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2535 2550 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2552 2565 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2571 2581 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2577 2590 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2592 2605 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2611 2622 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2617 2631 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2633 2646 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2652 2663 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2659 2672 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2674 2686 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VARIANT 20 20 Y -> C (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023859.
VARIANT 27 27 A -> T (in dbSNP:rs25397).
/FTId=VAR_014663.
VARIANT 39 39 A -> P (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_075984.
VARIANT 55 55 G -> E (in MFS).
{ECO:0000269|PubMed:22772377}.
/FTId=VAR_075985.
VARIANT 57 57 N -> D (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_075986.
VARIANT 62 62 R -> C (in MFS; also in a patient with
ectopia lentis and retinal detachment;
dbSNP:rs25403).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017967.
VARIANT 63 63 Y -> C (in ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_075987.
VARIANT 68 68 C -> S (in ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_075988.
VARIANT 80 80 C -> G (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065981.
VARIANT 89 89 C -> F (in MFS; dbSNP:rs112660651).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_017968.
VARIANT 100 100 C -> Y (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_075989.
VARIANT 111 111 C -> R (in MFS).
{ECO:0000269|PubMed:9338581}.
/FTId=VAR_002276.
VARIANT 114 114 R -> C (in MFS).
{ECO:0000269|PubMed:11826022}.
/FTId=VAR_017969.
VARIANT 115 115 S -> C (in ECTOL1).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017970.
VARIANT 122 122 R -> C (in MFS; dbSNP:rs137854467).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:8040326,
ECO:0000269|PubMed:9452085}.
/FTId=VAR_002277.
VARIANT 123 123 C -> Y (in MFS).
{ECO:0000269|PubMed:16222657,
ECO:0000269|PubMed:18435798}.
/FTId=VAR_023860.
VARIANT 127 127 G -> D (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_075990.
VARIANT 129 129 C -> Y (in MFS; severe neonatal).
{ECO:0000269|PubMed:19533785,
ECO:0000269|PubMed:7611299}.
/FTId=VAR_002278.
VARIANT 133 133 H -> Q (in dbSNP:rs363850).
/FTId=VAR_055723.
VARIANT 136 136 C -> S (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_075991.
VARIANT 154 154 C -> S (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_017971.
VARIANT 160 160 C -> R (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_075992.
VARIANT 164 164 N -> S (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_075993.
VARIANT 166 166 C -> F (in MFS).
{ECO:0000269|PubMed:7611299}.
/FTId=VAR_002279.
VARIANT 166 166 C -> S (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_002280.
VARIANT 177 177 C -> R (in MFS; dbSNP:rs363853).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023861.
VARIANT 177 177 C -> S (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_075994.
VARIANT 177 177 C -> Y (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_075995.
VARIANT 214 214 G -> S (in MFS).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:18435798}.
/FTId=VAR_075996.
VARIANT 215 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_075997.
VARIANT 217 217 W -> G (in MFS).
{ECO:0000269|PubMed:7977366,
ECO:0000269|PubMed:8136837}.
/FTId=VAR_002281.
VARIANT 219 219 H -> Q (in MFS).
{ECO:0000269|PubMed:22772377}.
/FTId=VAR_075998.
VARIANT 224 224 C -> R (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023862.
VARIANT 240 240 R -> C (in MFS and ECTOL1;
dbSNP:rs137854480).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:11826022,
ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:17657824}.
/FTId=VAR_017972.
VARIANT 248 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_075999.
VARIANT 329 329 I -> T (in dbSNP:rs12324002).
/FTId=VAR_055724.
VARIANT 348 2871 Missing (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076000.
VARIANT 351 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076001.
VARIANT 363 363 G -> S (in dbSNP:rs363855).
/FTId=VAR_055725.
VARIANT 364 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076002.
VARIANT 365 365 C -> R (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076003.
VARIANT 365 365 C -> W (in ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076004.
VARIANT 366 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076005.
VARIANT 366 366 W -> C (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_017973.
VARIANT 429 2871 Missing (in MFS).
{ECO:0000269|PubMed:12402346,
ECO:0000269|PubMed:18435798}.
/FTId=VAR_076006.
VARIANT 439 439 R -> G (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023863.
VARIANT 449 449 V -> I (in MFS).
{ECO:0000269|PubMed:12402346}.
/FTId=VAR_076007.
VARIANT 472 472 C -> Y (in dbSNP:rs4775765).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7691719,
ECO:0000269|PubMed:8364578,
ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
/FTId=VAR_058090.
VARIANT 474 474 C -> W (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076008.
VARIANT 476 476 C -> G (in MFS).
{ECO:0000269|PubMed:7951214}.
/FTId=VAR_002282.
VARIANT 488 488 C -> R (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076009.
VARIANT 490 490 D -> Y (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_002283.
VARIANT 499 499 C -> Y (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065982.
VARIANT 504 504 C -> F (in MFS).
{ECO:0000269|PubMed:10425041}.
/FTId=VAR_010776.
VARIANT 504 504 C -> R (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076010.
VARIANT 507 507 Missing (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023864.
VARIANT 541 541 C -> Y (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023865.
VARIANT 545 545 R -> C (in MFS and ECTOL1).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:9338581}.
/FTId=VAR_002284.
VARIANT 546 546 C -> W (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076011.
VARIANT 548 548 N -> I (in MFS; dbSNP:rs137854462).
{ECO:0000269|PubMed:8406497}.
/FTId=VAR_002285.
VARIANT 560 560 G -> S (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_017974.
VARIANT 565 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076012.
VARIANT 570 570 C -> Y (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_017975.
VARIANT 576 576 C -> Y (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076013.
VARIANT 582 582 C -> R (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076014.
VARIANT 587 587 C -> Y (in MFS).
{ECO:0000269|PubMed:12203992,
ECO:0000269|PubMed:9254848}.
/FTId=VAR_002286.
VARIANT 592 592 G -> D (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_017976.
VARIANT 596 596 C -> R (in ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076015.
VARIANT 596 596 C -> Y (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017977.
VARIANT 598 598 C -> W (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_017978.
VARIANT 611 611 C -> R (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065983.
VARIANT 617 617 C -> G (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065984.
VARIANT 623 623 C -> F (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076016.
VARIANT 627 627 R -> C (in MFS; enhances proteolytic
degradation).
{ECO:0000269|PubMed:12161601,
ECO:0000269|PubMed:15161917,
ECO:0000269|PubMed:16220557,
ECO:0000269|PubMed:8004112,
ECO:0000269|PubMed:9338581}.
/FTId=VAR_002287.
VARIANT 629 633 Missing (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023867.
VARIANT 634 634 S -> P (in ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076017.
VARIANT 635 635 Y -> C (in MFS).
{ECO:0000269|PubMed:16222657,
ECO:0000269|PubMed:18435798}.
/FTId=VAR_023868.
VARIANT 636 636 R -> I (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023869.
VARIANT 652 652 C -> S (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_017979.
VARIANT 652 652 C -> Y (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076018.
VARIANT 653 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076019.
VARIANT 654 654 D -> N (in MFS).
{ECO:0000269|PubMed:12161601,
ECO:0000269|PubMed:12203992}.
/FTId=VAR_017980.
VARIANT 661 661 C -> R (in MFS).
{ECO:0000269|PubMed:9016526}.
/FTId=VAR_002288.
VARIANT 661 661 C -> Y (in ECTOL1; patient presenting
also mitral valve prolapse).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017981.
VARIANT 681 681 S -> Y (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017982.
VARIANT 683 683 C -> R (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017983.
VARIANT 684 684 C -> Y (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076020.
VARIANT 685 685 C -> W (in MFS; dbSNP:rs140603).
{ECO:0000269|PubMed:12203992,
ECO:0000269|PubMed:21542060}.
/FTId=VAR_017984.
VARIANT 685 685 C -> Y (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065985.
VARIANT 699 699 C -> S (in MFS).
{ECO:0000269|PubMed:22772377}.
/FTId=VAR_076021.
VARIANT 705 705 A -> T (in MFS).
{ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:8863159}.
/FTId=VAR_002289.
VARIANT 711 711 C -> Y (in MFS).
{ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:8863159}.
/FTId=VAR_002290.
VARIANT 721 721 G -> C (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076022.
VARIANT 723 723 D -> A (in MFS; dbSNP:rs137854463).
{ECO:0000269|PubMed:8406497}.
/FTId=VAR_002291.
VARIANT 723 723 D -> V (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017985.
VARIANT 727 727 C -> Y (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076023.
VARIANT 734 734 C -> F (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017986.
VARIANT 746 746 Y -> C (in MFS).
{ECO:0000269|PubMed:7611299}.
/FTId=VAR_002292.
VARIANT 748 748 C -> Y (in MFS).
{ECO:0000269|PubMed:12161601,
ECO:0000269|PubMed:12203992}.
/FTId=VAR_017987.
VARIANT 750 750 C -> G (in MFS; enhances proteolytic
degradation).
{ECO:0000269|PubMed:15161917,
ECO:0000269|PubMed:9338581}.
/FTId=VAR_002293.
VARIANT 752 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076024.
VARIANT 776 776 C -> G (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017988.
VARIANT 776 776 C -> Y (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_017989.
VARIANT 781 781 C -> R (in MFS).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:12203992}.
/FTId=VAR_017990.
VARIANT 781 781 C -> Y (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023870.
VARIANT 790 790 C -> Y (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065986.
VARIANT 811 811 C -> Y (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065987.
VARIANT 816 816 C -> R (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076025.
VARIANT 816 816 C -> S (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_017991.
VARIANT 828 828 F -> C (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076026.
VARIANT 832 832 C -> Y (in MFS).
{ECO:0000269|PubMed:16222657,
ECO:0000269|PubMed:17657824}.
/FTId=VAR_023871.
VARIANT 853 853 C -> S (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065988.
VARIANT 861 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:19533785}.
/FTId=VAR_076027.
VARIANT 862 862 C -> R (in MFS).
{ECO:0000269|PubMed:8281141}.
/FTId=VAR_002294.
VARIANT 880 880 G -> S (in MFS).
{ECO:0000269|PubMed:12402346,
ECO:0000269|PubMed:18435798,
ECO:0000269|PubMed:22772377}.
/FTId=VAR_076028.
VARIANT 882 882 A -> V (in MFS and ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076029.
VARIANT 884 884 G -> E (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076030.
VARIANT 890 890 C -> G (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023872.
VARIANT 890 890 C -> R (in MFS).
{ECO:0000269|PubMed:11826022}.
/FTId=VAR_017992.
VARIANT 908 908 C -> R (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017993.
VARIANT 908 908 C -> Y (in MFS).
{ECO:0000269|PubMed:22772377}.
/FTId=VAR_076031.
VARIANT 910 910 D -> H (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076032.
VARIANT 913 913 E -> G (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_017994.
VARIANT 921 2871 Missing (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076033.
VARIANT 921 921 C -> G (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_017995.
VARIANT 926 926 C -> R (in MFS; enhances proteolytic
degradation).
{ECO:0000269|PubMed:15161917,
ECO:0000269|PubMed:7611299}.
/FTId=VAR_002295.
VARIANT 926 926 C -> Y (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065989.
VARIANT 937 937 C -> R (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076034.
VARIANT 954 954 R -> C (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076035.
VARIANT 966 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076036.
VARIANT 974 974 R -> C (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076037.
VARIANT 976 976 R -> H (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076038.
VARIANT 984 984 V -> I (in MFS).
{ECO:0000269|PubMed:10694921}.
/FTId=VAR_002296.
VARIANT 985 985 G -> E (in MFS; atypical;
dbSNP:rs137854477).
{ECO:0000269|PubMed:10441597}.
/FTId=VAR_018319.
VARIANT 985 985 G -> R (in MFS).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:16220557}.
/FTId=VAR_017996.
VARIANT 988 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076039.
VARIANT 994 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076040.
VARIANT 996 996 C -> R (in MFS; dbSNP:rs140592).
{ECO:0000269|PubMed:9401003}.
/FTId=VAR_002297.
VARIANT 1008 1008 C -> Y (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076041.
VARIANT 1013 1013 G -> R (in MFS; severe neonatal;
dbSNP:rs140593).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:16220557,
ECO:0000269|PubMed:7611299}.
/FTId=VAR_002298.
VARIANT 1020 1020 T -> A (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076042.
VARIANT 1023 1023 K -> N (in MFS; severe neonatal).
{ECO:0000269|PubMed:8136837}.
/FTId=VAR_002299.
VARIANT 1028 1028 D -> G (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076043.
VARIANT 1032 1032 C -> Y (in MFS; severe neonatal).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076044.
VARIANT 1042 1042 G -> S (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076045.
VARIANT 1043 1043 K -> R (in MFS; dbSNP:rs137854472).
{ECO:0000269|PubMed:9016526}.
/FTId=VAR_002300.
VARIANT 1044 1044 C -> Y (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_017997.
VARIANT 1048 1048 I -> T (in MFS; severe neonatal).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:9401003}.
/FTId=VAR_002301.
VARIANT 1048 1048 I -> V (in dbSNP:rs2229324).
/FTId=VAR_055726.
VARIANT 1048 1048 Missing (in MFS).
{ECO:0000269|PubMed:9401003}.
/FTId=VAR_002302.
VARIANT 1053 1053 C -> R (in MFS).
{ECO:0000269|PubMed:8882780}.
/FTId=VAR_002303.
VARIANT 1055 1055 C -> G (in MFS; neonatal).
{ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:8863159}.
/FTId=VAR_002304.
VARIANT 1055 1055 C -> W (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_017998.
VARIANT 1055 1055 C -> Y (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_017999.
VARIANT 1058 1058 G -> D (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023873.
VARIANT 1058 1058 G -> GC (in MFS).
{ECO:0000269|PubMed:9401003}.
/FTId=VAR_002305.
VARIANT 1068 1068 C -> G (in MFS; neonatal form).
{ECO:0000269|PubMed:20803651}.
/FTId=VAR_064503.
VARIANT 1072 1072 D -> G (in MFS).
{ECO:0000269|PubMed:8882780}.
/FTId=VAR_002306.
VARIANT 1073 1073 E -> K (in MFS; severe neonatal;
dbSNP:rs137854478).
{ECO:0000269|PubMed:7611299,
ECO:0000269|PubMed:8882780}.
/FTId=VAR_002307.
VARIANT 1074 1074 C -> R (in MFS; severe neonatal;
dbSNP:rs137854465).
{ECO:0000269|PubMed:8136837,
ECO:0000269|PubMed:9338581}.
/FTId=VAR_002308.
VARIANT 1074 1074 C -> Y (in MFS; severe neonatal).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076046.
VARIANT 1086 2871 Missing (in ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076047.
VARIANT 1086 1086 C -> W (in MFS).
{ECO:0000269|PubMed:9401003}.
/FTId=VAR_002309.
VARIANT 1088 1088 N -> I (in MFS; severe neonatal).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076048.
VARIANT 1090 1090 P -> S (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065990.
VARIANT 1101 1101 Y -> C (in MFS).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:12402346,
ECO:0000269|PubMed:14695540}.
/FTId=VAR_018000.
VARIANT 1113 1113 D -> G (in dbSNP:rs140597).
/FTId=VAR_055727.
VARIANT 1113 1113 D -> V (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023874.
VARIANT 1117 1117 C -> G (in MFS).
{ECO:0000269|PubMed:8882780}.
/FTId=VAR_002310.
VARIANT 1117 1117 C -> R (in MFS).
{ECO:0000269|PubMed:22772377}.
/FTId=VAR_076049.
VARIANT 1117 1117 C -> Y (in MFS; dbSNP:rs137854470).
{ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:8281141}.
/FTId=VAR_002311.
VARIANT 1125 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:18435798}.
/FTId=VAR_076050.
VARIANT 1127 1127 G -> S (in MFS; mild form;
dbSNP:rs137854468).
{ECO:0000269|PubMed:7762551}.
/FTId=VAR_002312.
VARIANT 1128 1128 V -> I (in a patient with mitral valve
prolapse). {ECO:0000269|PubMed:11700157}.
/FTId=VAR_018001.
VARIANT 1129 1129 C -> Y (in MFS; dbSNP:rs137854482).
{ECO:0000269|PubMed:10425041}.
/FTId=VAR_010777.
VARIANT 1130 1130 H -> P (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076051.
VARIANT 1131 1131 N -> Y (in dbSNP:rs137854473).
/FTId=VAR_002313.
VARIANT 1136 2871 Missing (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076052.
VARIANT 1137 1137 R -> P (in MFS; dbSNP:rs137854456).
{ECO:0000269|PubMed:1852208,
ECO:0000269|PubMed:8281141}.
/FTId=VAR_002314.
VARIANT 1138 1138 C -> Y (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076053.
VARIANT 1140 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076054.
VARIANT 1148 1148 P -> A (in dbSNP:rs140598).
{ECO:0000269|PubMed:20547088,
ECO:0000269|PubMed:8281141,
ECO:0000269|PubMed:8988160,
ECO:0000269|PubMed:9150726,
ECO:0000269|PubMed:9338588}.
/FTId=VAR_002315.
VARIANT 1153 1153 C -> S (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023875.
VARIANT 1153 1153 C -> Y (in MFS; severe; dbSNP:rs140599).
{ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:8863159}.
/FTId=VAR_002316.
VARIANT 1155 1155 D -> N (in MFS and ECTOL1).
{ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:17657824}.
/FTId=VAR_002317.
VARIANT 1158 1158 E -> G (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076055.
VARIANT 1170 1170 R -> H (in MFS; dbSNP:rs137854475).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:7870075,
ECO:0000269|PubMed:9338581}.
/FTId=VAR_002318.
VARIANT 1171 1171 C -> W (in MFS).
{ECO:0000269|PubMed:9338581}.
/FTId=VAR_002319.
VARIANT 1173 1173 N -> K (in MFS).
{ECO:0000269|PubMed:9338581}.
/FTId=VAR_002320.
VARIANT 1182 1182 C -> W (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076056.
VARIANT 1185 1185 G -> D (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065991.
VARIANT 1199 1199 D -> A (in MFS).
{ECO:0000269|PubMed:22772377}.
/FTId=VAR_076057.
VARIANT 1200 1200 E -> G (in MFS).
{ECO:0000269|PubMed:11826022}.
/FTId=VAR_018002.
VARIANT 1211 1211 Missing (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023876.
VARIANT 1219 1219 Y -> C (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023877.
VARIANT 1223 1223 C -> R (in MFS; severe neonatal).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076058.
VARIANT 1223 1223 C -> Y (in MFS; also found in a patient
with Shprintzen-Goldberg craniosynostosis
syndrome; dbSNP:rs137854469).
{ECO:0000269|PubMed:8071963,
ECO:0000269|Ref.68}.
/FTId=VAR_002321.
VARIANT 1242 1242 C -> Y (in MFS; dbSNP:rs137854471).
{ECO:0000269|PubMed:8136837}.
/FTId=VAR_002322.
VARIANT 1249 1249 C -> R (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076059.
VARIANT 1249 1249 C -> S (in MFS; dbSNP:rs137854458).
{ECO:0000269|PubMed:1301946}.
/FTId=VAR_002323.
VARIANT 1261 1261 Y -> C (in MFS).
{ECO:0000269|PubMed:10425041}.
/FTId=VAR_010778.
VARIANT 1261 1261 Y -> D (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023878.
VARIANT 1265 1265 C -> R (in MFS; dbSNP:rs137854474).
{ECO:0000269|PubMed:9837823}.
/FTId=VAR_018320.
VARIANT 1265 1265 C -> Y (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076060.
VARIANT 1278 1278 C -> S (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023879.
VARIANT 1282 1282 N -> S (in dbSNP:rs140647).
/FTId=VAR_055728.
VARIANT 1284 1284 C -> G (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023880.
VARIANT 1284 1284 C -> Y (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065992.
VARIANT 1307 1307 C -> Y (in MFS; severe neonatal).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076061.
VARIANT 1320 1320 C -> R (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076062.
VARIANT 1325 1325 E -> Q (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_018003.
VARIANT 1326 1326 C -> R (in MFS; severe neonatal).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076063.
VARIANT 1333 1333 C -> S (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023881.
VARIANT 1337 1337 A -> P (in MFS; neonatal).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018004.
VARIANT 1339 1339 C -> Y (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018005.
VARIANT 1346 1346 F -> L (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076064.
VARIANT 1350 1350 C -> F (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065993.
VARIANT 1366 1366 E -> K (in MFS).
{ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:17657824}.
/FTId=VAR_018006.
VARIANT 1374 1374 C -> S (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_018007.
VARIANT 1382 1382 N -> S (in MFS).
{ECO:0000269|PubMed:7611299}.
/FTId=VAR_002324.
VARIANT 1389 1389 C -> R (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_018008.
VARIANT 1394 1396 Missing (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_018009.
VARIANT 1401 1401 T -> A (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065994.
VARIANT 1402 1402 C -> R (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023882.
VARIANT 1402 1402 C -> Y (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076065.
VARIANT 1404 1404 D -> Y (in MFS).
{ECO:0000269|PubMed:9338581}.
/FTId=VAR_002325.
VARIANT 1406 1406 D -> G (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076066.
VARIANT 1424 1424 P -> A (in MFS).
{ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:17657824}.
/FTId=VAR_018010.
VARIANT 1424 1424 P -> S (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023883.
VARIANT 1427 1427 Y -> D (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076067.
VARIANT 1429 1429 C -> S (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018011.
VARIANT 1431 1431 C -> W (in MFS; dbSNP:rs112375043).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065995.
VARIANT 1431 1431 C -> Y (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065996.
VARIANT 1475 1475 G -> E (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023884.
VARIANT 1475 1475 G -> S (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023885.
VARIANT 1481 1481 S -> G (in dbSNP:rs61730054).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065997.
VARIANT 1485 1485 C -> R (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076068.
VARIANT 1487 1487 D -> A (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065998.
VARIANT 1489 1489 N -> K (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_065999.
VARIANT 1513 1513 C -> R (in MFS).
{ECO:0000269|PubMed:8136837}.
/FTId=VAR_002326.
VARIANT 1528 1528 D -> Y (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076069.
VARIANT 1530 1530 R -> C (found in patients with ectopia
lensis; dbSNP:rs111401431).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:14695540}.
/FTId=VAR_018012.
VARIANT 1534 2871 Missing (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076070.
VARIANT 1539 2871 Missing (in MFS).
{ECO:0000269|PubMed:18435798,
ECO:0000269|PubMed:22772377}.
/FTId=VAR_076071.
VARIANT 1541 2871 Missing (in MFS).
{ECO:0000269|PubMed:12161601,
ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:18435798}.
/FTId=VAR_076072.
VARIANT 1564 1564 C -> F (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023886.
VARIANT 1564 1564 C -> S (in SSKS).
{ECO:0000269|PubMed:20375004}.
/FTId=VAR_064046.
VARIANT 1564 1564 C -> Y (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_018013.
VARIANT 1570 1570 W -> C (in SSKS).
{ECO:0000269|PubMed:20375004}.
/FTId=VAR_064047.
VARIANT 1576 1576 M -> T (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023887.
VARIANT 1577 1577 C -> G (in SSKS).
{ECO:0000269|PubMed:20375004}.
/FTId=VAR_064048.
VARIANT 1589 1589 C -> F (in MFS).
{ECO:0000269|PubMed:8281141}.
/FTId=VAR_002327.
VARIANT 1594 1594 G -> D (in SSKS).
{ECO:0000269|PubMed:20375004}.
/FTId=VAR_064049.
VARIANT 1610 1610 C -> G (in MFS).
{ECO:0000269|PubMed:9338581}.
/FTId=VAR_002328.
VARIANT 1622 1622 C -> R (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076073.
VARIANT 1631 1631 C -> G (in MFS).
{ECO:0000269|PubMed:16222657,
ECO:0000269|PubMed:18435798}.
/FTId=VAR_023888.
VARIANT 1633 1633 C -> S (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076074.
VARIANT 1642 1642 D -> G (in MFS).
{ECO:0000269|PubMed:22772377}.
/FTId=VAR_076075.
VARIANT 1644 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076076.
VARIANT 1663 1663 C -> R (in MFS; dbSNP:rs137854459).
{ECO:0000269|PubMed:1301946}.
/FTId=VAR_002329.
VARIANT 1663 1663 C -> Y (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023889.
VARIANT 1672 1672 C -> F (in dbSNP:rs140627).
/FTId=VAR_055729.
VARIANT 1672 1672 C -> R (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076077.
VARIANT 1672 1672 C -> Y (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076078.
VARIANT 1674 1674 C -> G (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076079.
VARIANT 1692 1699 Missing (in WMS2).
{ECO:0000269|PubMed:12525539}.
/FTId=VAR_018014.
VARIANT 1692 1692 Missing (in ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076080.
VARIANT 1696 1696 Y -> C (in GPHYSD2).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066527.
VARIANT 1699 1699 Y -> C (in GPHYSD2 and ACMICD).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066528.
VARIANT 1699 1699 Y -> D (in GPHYSD2).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066529.
VARIANT 1700 1700 Y -> C (in ACMICD).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066530.
VARIANT 1706 1706 C -> Y (in GPHYSD2).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066531.
VARIANT 1714 1714 M -> R (in ACMICD).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066532.
VARIANT 1719 1719 C -> W (in GPHYSD2).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066533.
VARIANT 1720 1720 C -> Y (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076081.
VARIANT 1722 1722 S -> C (in ACMICD).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066534.
VARIANT 1726 1726 G -> V (in ACMICD).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066535.
VARIANT 1728 1728 A -> T (in GPHYSD2 and ACMICD).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066536.
VARIANT 1728 1728 A -> V (in GPHYSD2).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066537.
VARIANT 1733 1733 C -> Y (in GPHYSD2).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066538.
VARIANT 1735 2871 Missing (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076082.
VARIANT 1735 1735 Q -> QQ (in ACMICD).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066539.
VARIANT 1750 1750 S -> R (in ACMICD).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066540.
VARIANT 1758 1758 D -> V (in ACMICD).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066541.
VARIANT 1762 1762 G -> S (in GPHYSD2).
{ECO:0000269|PubMed:21683322}.
/FTId=VAR_066542.
VARIANT 1770 1770 C -> F (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_018015.
VARIANT 1777 1777 C -> F (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076083.
VARIANT 1790 2871 Missing (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076084.
VARIANT 1790 1790 R -> P (in MFS).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:12203992}.
/FTId=VAR_018016.
VARIANT 1791 1791 C -> R (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023890.
VARIANT 1791 1791 C -> Y (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018017.
VARIANT 1793 1793 C -> W (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_018018.
VARIANT 1793 1793 C -> Y (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076085.
VARIANT 1796 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076086.
VARIANT 1796 1796 G -> E (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_018019.
VARIANT 1796 1796 G -> V (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076087.
VARIANT 1806 1806 C -> S (in MFS).
{ECO:0000269|PubMed:12203992,
ECO:0000269|PubMed:17657824}.
/FTId=VAR_018020.
VARIANT 1806 1806 C -> Y (in MFS).
{ECO:0000269|PubMed:12402346}.
/FTId=VAR_023891.
VARIANT 1811 1811 E -> K (in MFS).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:18435798}.
/FTId=VAR_076088.
VARIANT 1812 1812 C -> R (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076089.
VARIANT 1812 1812 C -> Y (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076090.
VARIANT 1826 1826 N -> S (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076091.
VARIANT 1830 1830 S -> C (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076092.
VARIANT 1833 1833 C -> S (in MFS).
{ECO:0000269|PubMed:10425041}.
/FTId=VAR_010779.
VARIANT 1835 1835 C -> F (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076093.
VARIANT 1835 1835 C -> Y (in MFS; dbSNP:rs111929350).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:11826022,
ECO:0000269|PubMed:12161601}.
/FTId=VAR_018021.
VARIANT 1837 1837 P -> S (in MFS).
{ECO:0000269|PubMed:9401003}.
/FTId=VAR_002330.
VARIANT 1838 1838 G -> C (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066000.
VARIANT 1847 1847 C -> R (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076094.
VARIANT 1847 1847 C -> W (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076095.
VARIANT 1860 1860 C -> Y (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076096.
VARIANT 1865 1865 C -> R (in MFS).
{ECO:0000269|PubMed:22772377}.
/FTId=VAR_076097.
VARIANT 1876 1876 C -> Y (in MFS; dbSNP:rs112728248).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023892.
VARIANT 1879 1879 G -> D (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076098.
VARIANT 1887 1887 T -> I (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023893.
VARIANT 1893 1893 N -> K (in MFS).
{ECO:0000269|PubMed:9338581}.
/FTId=VAR_002331.
VARIANT 1894 1894 E -> K (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076099.
VARIANT 1895 1895 C -> R (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023894.
VARIANT 1900 1900 C -> Y (in MFS).
{ECO:0000269|PubMed:16222657,
ECO:0000269|PubMed:18435798,
ECO:0000269|PubMed:21542060}.
/FTId=VAR_023895.
VARIANT 1907 1907 N -> S (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076100.
VARIANT 1908 1908 T -> I (in MFS).
{ECO:0000269|PubMed:12402346}.
/FTId=VAR_076101.
VARIANT 1909 1909 I -> T (in MFS).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:21542060}.
/FTId=VAR_018022.
VARIANT 1915 1915 R -> S (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018023.
VARIANT 1919 1919 G -> D (in MFS).
{ECO:0000269|PubMed:12402346}.
/FTId=VAR_076102.
VARIANT 1928 1928 C -> G (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023896.
VARIANT 1928 1928 C -> R (in MFS).
{ECO:0000269|PubMed:7611299}.
/FTId=VAR_002332.
VARIANT 1928 1928 C -> Y (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023897.
VARIANT 1930 1930 D -> H (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076103.
VARIANT 1931 1931 Missing (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_018024.
VARIANT 1934 1934 C -> G (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076104.
VARIANT 1934 1934 C -> S (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066001.
VARIANT 1971 1971 C -> Y (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018025.
VARIANT 1976 1976 E -> G (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066002.
VARIANT 1977 1977 C -> R (in MFS).
{ECO:0000269|PubMed:12161601}.
/FTId=VAR_076105.
VARIANT 1977 1977 C -> W (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076106.
VARIANT 1977 1977 C -> Y (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018026.
VARIANT 1984 1984 C -> R (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066003.
VARIANT 1987 1987 G -> R (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076107.
VARIANT 1998 1998 C -> Y (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_018027.
VARIANT 2018 2018 V -> I (in dbSNP:rs363802).
/FTId=VAR_055730.
VARIANT 2038 2038 C -> Y (in MFS; dbSNP:rs363804).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023898.
VARIANT 2053 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076108.
VARIANT 2053 2053 C -> F (in dbSNP:rs363805).
/FTId=VAR_055731.
VARIANT 2057 2871 Missing (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076109.
VARIANT 2062 2871 Missing (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076110.
VARIANT 2064 2871 Missing (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076111.
VARIANT 2081 2871 Missing (in MFS).
{ECO:0000269|PubMed:22772377}.
/FTId=VAR_076112.
VARIANT 2084 2084 C -> W (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076113.
VARIANT 2084 2084 C -> Y (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076114.
VARIANT 2085 2085 C -> R (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023899.
VARIANT 2099 2099 C -> W (in MFS).
{ECO:0000269|PubMed:9338581}.
/FTId=VAR_002333.
VARIANT 2101 2101 T -> M (in dbSNP:rs200816828).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_018028.
VARIANT 2105 2105 E -> K (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076115.
VARIANT 2111 2111 C -> R (in MFS; dbSNP:rs363815).
{ECO:0000269|PubMed:11826022}.
/FTId=VAR_018029.
VARIANT 2111 2111 C -> Y (in MFS).
{ECO:0000269|PubMed:9338581}.
/FTId=VAR_002334.
VARIANT 2113 2113 Y -> F (in dbSNP:rs363816).
/FTId=VAR_055732.
VARIANT 2118 2118 I -> M (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076116.
VARIANT 2127 2127 D -> E (in MFS).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:8136837}.
/FTId=VAR_002335.
VARIANT 2130 2130 E -> K (in MFS).
{ECO:0000269|PubMed:18435798,
ECO:0000269|PubMed:19533785}.
/FTId=VAR_076117.
VARIANT 2136 2136 V -> D (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076118.
VARIANT 2142 2142 C -> Y (in MFS).
{ECO:0000269|PubMed:10425041}.
/FTId=VAR_010780.
VARIANT 2144 2144 N -> D (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076119.
VARIANT 2144 2144 N -> S (in MFS; dbSNP:rs137854461).
{ECO:0000269|PubMed:16220557,
ECO:0000269|PubMed:19533785,
ECO:0000269|PubMed:8504310}.
/FTId=VAR_002336.
VARIANT 2145 2145 T -> P (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076120.
VARIANT 2151 2151 C -> W (in MFS).
{ECO:0000269|PubMed:8136837}.
/FTId=VAR_002337.
VARIANT 2153 2153 C -> Y (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076121.
VARIANT 2154 2154 P -> R (in ECTOL1).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018030.
VARIANT 2160 2160 A -> P (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023900.
VARIANT 2166 2166 D -> N (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066004.
VARIANT 2169 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076122.
VARIANT 2170 2170 C -> F (in dbSNP:rs363821).
/FTId=VAR_055733.
VARIANT 2185 2185 I -> T (in MFS).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:21542060}.
/FTId=VAR_066005.
VARIANT 2195 2195 G -> R (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076123.
VARIANT 2220 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:22772377}.
/FTId=VAR_076124.
VARIANT 2221 2221 C -> F (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023901.
VARIANT 2221 2221 C -> G (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_018031.
VARIANT 2221 2221 C -> R (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076125.
VARIANT 2221 2221 C -> S (in MFS; dbSNP:rs137854460).
{ECO:0000269|PubMed:1301946}.
/FTId=VAR_002338.
VARIANT 2223 2223 N -> H (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018032.
VARIANT 2224 2224 T -> P (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076126.
VARIANT 2229 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076127.
VARIANT 2232 2232 C -> Y (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076128.
VARIANT 2234 2234 V -> M (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076129.
VARIANT 2247 2247 D -> G (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066006.
VARIANT 2250 2250 E -> G (in ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076130.
VARIANT 2251 2251 C -> R (in MFS; dbSNP:rs112836174).
{ECO:0000269|PubMed:12402346}.
/FTId=VAR_023902.
VARIANT 2258 2258 C -> R (in MFS).
{ECO:0000269|PubMed:9338581}.
/FTId=VAR_002339.
VARIANT 2258 2258 C -> Y (in MFS).
{ECO:0000269|PubMed:12161601}.
/FTId=VAR_076131.
VARIANT 2269 2269 I -> T (in MFS).
{ECO:0000269|PubMed:12203992,
ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:18435798}.
/FTId=VAR_018033.
VARIANT 2272 2272 Y -> C (in ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076132.
VARIANT 2273 2273 M -> T (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076133.
VARIANT 2274 2274 C -> W (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076134.
VARIANT 2278 2278 P -> S (in dbSNP:rs363835).
/FTId=VAR_055734.
VARIANT 2282 2282 R -> W (in MFS).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:9338581}.
/FTId=VAR_002340.
VARIANT 2284 2284 P -> T (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076135.
VARIANT 2289 2289 C -> W (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076136.
VARIANT 2298 2871 Missing (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076137.
VARIANT 2302 2302 C -> Y (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076138.
VARIANT 2307 2307 C -> S (in MFS; dbSNP:rs137854457).
{ECO:0000269|PubMed:1301946,
ECO:0000269|PubMed:1569206}.
/FTId=VAR_002341.
VARIANT 2318 2318 C -> R (in MFS; dbSNP:rs111588631).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066007.
VARIANT 2329 2329 D -> E (in dbSNP:rs363831).
/FTId=VAR_055735.
VARIANT 2335 2335 R -> W (in MFS).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_018034.
VARIANT 2339 2339 C -> Y (in ECTOL1; patient presenting
also flat corneas).
{ECO:0000269|PubMed:12203992}.
/FTId=VAR_018035.
VARIANT 2365 2365 C -> Y (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076139.
VARIANT 2385 2385 A -> T (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023903.
VARIANT 2394 2871 Missing (in MFS).
{ECO:0000269|PubMed:12161601}.
/FTId=VAR_076140.
VARIANT 2406 2406 C -> Y (in MFS).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:21542060}.
/FTId=VAR_018036.
VARIANT 2442 2442 C -> S (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066008.
VARIANT 2442 2442 C -> W (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_018037.
VARIANT 2447 2447 E -> K (in ECTOL1 and MFS;
dbSNP:rs137854464).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:8136837,
ECO:0000269|PubMed:8188302}.
/FTId=VAR_002342.
VARIANT 2448 2448 C -> R (in ECTOL1).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076141.
VARIANT 2466 2871 Missing (in MFS).
{ECO:0000269|PubMed:12161601}.
/FTId=VAR_076142.
VARIANT 2467 2871 Missing (in MFS).
{ECO:0000269|PubMed:12161601}.
/FTId=VAR_076143.
VARIANT 2470 2470 C -> W (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076144.
VARIANT 2470 2470 C -> Y (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076145.
VARIANT 2474 2474 Y -> C (in MFS).
{ECO:0000269|PubMed:11826022}.
/FTId=VAR_018038.
VARIANT 2489 2489 C -> R (in MFS).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:9338581}.
/FTId=VAR_002343.
VARIANT 2500 2500 C -> R (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023904.
VARIANT 2500 2500 C -> Y (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023905.
VARIANT 2511 2511 C -> R (in MFS).
{ECO:0000269|PubMed:21542060,
ECO:0000269|PubMed:8136837,
ECO:0000269|PubMed:9016526}.
/FTId=VAR_002344.
VARIANT 2516 2516 T -> I (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076146.
VARIANT 2520 2520 T -> M (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076147.
VARIANT 2522 2522 C -> Y (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076148.
VARIANT 2526 2526 N -> S (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076149.
VARIANT 2535 2535 C -> W (in MFS; dbSNP:rs113544411).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023906.
VARIANT 2536 2536 G -> R (in MFS).
{ECO:0000269|PubMed:16220557,
ECO:0000269|PubMed:17657824}.
/FTId=VAR_023907.
VARIANT 2541 2541 C -> F (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076150.
VARIANT 2542 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076151.
VARIANT 2554 2554 R -> W (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076152.
VARIANT 2555 2555 G -> V (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076153.
VARIANT 2561 2561 T -> P (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076154.
VARIANT 2570 2570 E -> K (in MFS).
{ECO:0000269|PubMed:16222657,
ECO:0000269|PubMed:18435798}.
/FTId=VAR_023908.
VARIANT 2571 2871 Missing (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076155.
VARIANT 2571 2571 C -> R (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023909.
VARIANT 2577 2577 C -> R (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076156.
VARIANT 2577 2577 C -> Y (in MFS).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076157.
VARIANT 2581 2581 C -> F (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018039.
VARIANT 2585 2585 I -> T (in MFS).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:14695540,
ECO:0000269|PubMed:17657824}.
/FTId=VAR_018040.
VARIANT 2592 2592 C -> S (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023910.
VARIANT 2605 2605 C -> Y (in MFS).
{ECO:0000269|PubMed:16220557}.
/FTId=VAR_023912.
VARIANT 2606 2606 Missing (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066009.
VARIANT 2610 2610 E -> K (in MFS; dbSNP:rs111984349).
{ECO:0000269|PubMed:16222657,
ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:21542060}.
/FTId=VAR_023913.
VARIANT 2618 2618 G -> R (in MFS; dbSNP:rs141133182).
{ECO:0000269|PubMed:11700157,
ECO:0000269|PubMed:17657824}.
/FTId=VAR_018041.
VARIANT 2623 2623 H -> P (in MFS).
{ECO:0000269|PubMed:14695540}.
/FTId=VAR_002345.
VARIANT 2624 2624 N -> K (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018042.
VARIANT 2627 2627 G -> R (in MFS).
{ECO:0000269|PubMed:7977366}.
/FTId=VAR_002346.
VARIANT 2629 2629 Y -> C (in MFS).
{ECO:0000269|PubMed:16222657}.
/FTId=VAR_023914.
VARIANT 2646 2646 C -> R (in MFS).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066010.
VARIANT 2652 2652 C -> G (in MFS).
{ECO:0000269|PubMed:11826022}.
/FTId=VAR_018043.
VARIANT 2663 2663 C -> S (in MFS).
{ECO:0000269|PubMed:15221638}.
/FTId=VAR_023915.
VARIANT 2668 2668 G -> C (in MFS).
{ECO:0000269|PubMed:11700157}.
/FTId=VAR_018044.
VARIANT 2680 2680 R -> C (in MFS).
{ECO:0000269|PubMed:9401003}.
/FTId=VAR_002347.
VARIANT 2694 2871 Missing (in MFS).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076158.
VARIANT 2708 2708 N -> S (in MFS).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076159.
VARIANT 2726 2726 R -> W (probable disease-associated
mutation found in a patient with Marfan-
like syndrome; defects in protein
processing; dbSNP:rs61746008).
{ECO:0000269|PubMed:17657824,
ECO:0000269|PubMed:18435798,
ECO:0000269|PubMed:7738200,
ECO:0000269|PubMed:9817919}.
/FTId=VAR_002348.
VARIANT 2741 2741 I -> T (in MFLS).
{ECO:0000269|PubMed:24665001}.
/FTId=VAR_076160.
VARIANT 2774 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:18435798}.
/FTId=VAR_076161.
VARIANT 2776 2781 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome; prevents secretion into
the extracellular matrix).
{ECO:0000269|PubMed:24982166,
ECO:0000269|PubMed:7911051}.
/FTId=VAR_076162.
VARIANT 2780 2780 L -> P (probable disease-associated
mutation found in a patient with Marfan-
like syndrome; prevents secretion into
the extracellular matrix).
{ECO:0000269|PubMed:12161601,
ECO:0000269|PubMed:24982166}.
/FTId=VAR_076163.
VARIANT 2793 2793 Y -> H (probable disease-associated
mutation found in a patient with Marfan-
like syndrome; dbSNP:rs113722038).
{ECO:0000269|PubMed:21542060}.
/FTId=VAR_066011.
VARIANT 2840 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome).
{ECO:0000269|PubMed:17657824}.
/FTId=VAR_076164.
VARIANT 2849 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome; prevents secretion into
the extracellular matrix).
{ECO:0000269|PubMed:21034599,
ECO:0000269|PubMed:24982166}.
/FTId=VAR_076165.
VARIANT 2867 2871 Missing (probable disease-associated
mutation found in a patient with Marfan-
like syndrome; prevents secretion into
the extracellular matrix).
{ECO:0000269|PubMed:19293843,
ECO:0000269|PubMed:24982166}.
/FTId=VAR_076166.
MUTAGEN 1542 1542 G->D: Loss of integrin-mediated cell
adhesion. {ECO:0000269|PubMed:12807887}.
MUTAGEN 2728 2728 R->A: Abolishes furin cleavage site,
leading to defects in protein processing
at the C-terminus.
{ECO:0000269|PubMed:9817919}.
MUTAGEN 2731 2731 R->K: Abolishes furin cleavage site,
leading to defects in protein processing
at the C-terminus.
{ECO:0000269|PubMed:9817919}.
MUTAGEN 2732 2732 S->T: Defects in protein processing at
the C-terminus.
{ECO:0000269|PubMed:9817919}.
CONFLICT 207 207 T -> Q (in Ref. 1; AAB02036).
{ECO:0000305}.
CONFLICT 2158 2158 I -> T (in Ref. 1; AAB02036 and 7;
CAA45118). {ECO:0000305}.
STRAND 50 52 {ECO:0000244|PDB:2M74}.
STRAND 54 56 {ECO:0000244|PDB:2M74}.
STRAND 58 60 {ECO:0000244|PDB:2M74}.
STRAND 92 96 {ECO:0000244|PDB:2M74}.
STRAND 99 101 {ECO:0000244|PDB:2M74}.
STRAND 107 110 {ECO:0000244|PDB:2M74}.
TURN 118 120 {ECO:0000244|PDB:2M74}.
TURN 142 145 {ECO:0000244|PDB:2M74}.
STRAND 155 157 {ECO:0000244|PDB:2M74}.
STRAND 159 162 {ECO:0000244|PDB:2M74}.
STRAND 165 167 {ECO:0000244|PDB:2M74}.
STRAND 174 176 {ECO:0000244|PDB:2M74}.
HELIX 810 813 {ECO:0000244|PDB:2W86}.
STRAND 819 824 {ECO:0000244|PDB:2W86}.
STRAND 827 831 {ECO:0000244|PDB:2W86}.
STRAND 836 838 {ECO:0000244|PDB:2W86}.
STRAND 842 847 {ECO:0000244|PDB:2W86}.
STRAND 851 858 {ECO:0000244|PDB:2W86}.
STRAND 861 870 {ECO:0000244|PDB:2W86}.
HELIX 872 876 {ECO:0000244|PDB:2W86}.
TURN 877 879 {ECO:0000244|PDB:2W86}.
STRAND 881 883 {ECO:0000244|PDB:2W86}.
TURN 884 887 {ECO:0000244|PDB:2W86}.
TURN 894 896 {ECO:0000244|PDB:2W86}.
STRAND 900 904 {ECO:0000244|PDB:2W86}.
STRAND 907 910 {ECO:0000244|PDB:2W86}.
HELIX 913 916 {ECO:0000244|PDB:2W86}.
STRAND 921 929 {ECO:0000244|PDB:2W86}.
STRAND 932 936 {ECO:0000244|PDB:2W86}.
TURN 1073 1076 {ECO:0000244|PDB:1LMJ}.
TURN 1080 1083 {ECO:0000244|PDB:1LMJ}.
STRAND 1086 1089 {ECO:0000244|PDB:1LMJ}.
STRAND 1092 1095 {ECO:0000244|PDB:1LMJ}.
STRAND 1099 1103 {ECO:0000244|PDB:1LMJ}.
TURN 1105 1107 {ECO:0000244|PDB:1LMJ}.
STRAND 1108 1113 {ECO:0000244|PDB:1LMJ}.
HELIX 1116 1119 {ECO:0000244|PDB:1LMJ}.
TURN 1123 1126 {ECO:0000244|PDB:1LMJ}.
STRAND 1127 1132 {ECO:0000244|PDB:1LMJ}.
STRAND 1135 1140 {ECO:0000244|PDB:1LMJ}.
STRAND 1148 1150 {ECO:0000244|PDB:1LMJ}.
HELIX 1490 1492 {ECO:0000244|PDB:1UZK}.
STRAND 1496 1498 {ECO:0000244|PDB:1UZK}.
STRAND 1500 1505 {ECO:0000244|PDB:1UZK}.
STRAND 1508 1512 {ECO:0000244|PDB:1UZK}.
STRAND 1523 1527 {ECO:0000244|PDB:1UZK}.
STRAND 1532 1537 {ECO:0000244|PDB:1UZK}.
STRAND 1544 1546 {ECO:0000244|PDB:1UZJ}.
STRAND 1550 1557 {ECO:0000244|PDB:1UZK}.
HELIX 1559 1563 {ECO:0000244|PDB:1UZK}.
TURN 1564 1566 {ECO:0000244|PDB:1UZK}.
STRAND 1568 1570 {ECO:0000244|PDB:1UZP}.
TURN 1571 1574 {ECO:0000244|PDB:1UZK}.
HELIX 1583 1588 {ECO:0000244|PDB:1UZK}.
STRAND 1595 1597 {ECO:0000244|PDB:1UZK}.
TURN 1599 1601 {ECO:0000244|PDB:1UZK}.
STRAND 1604 1606 {ECO:0000244|PDB:1UZK}.
HELIX 1609 1612 {ECO:0000244|PDB:1UZK}.
HELIX 1614 1617 {ECO:0000244|PDB:1UZK}.
STRAND 1620 1624 {ECO:0000244|PDB:1UZK}.
STRAND 1629 1632 {ECO:0000244|PDB:1UZK}.
TURN 1641 1643 {ECO:0000244|PDB:1UZK}.
HELIX 2054 2056 {ECO:0000244|PDB:1APJ}.
STRAND 2061 2065 {ECO:0000244|PDB:1APJ}.
STRAND 2070 2073 {ECO:0000244|PDB:1APJ}.
HELIX 2080 2084 {ECO:0000244|PDB:1APJ}.
STRAND 2090 2092 {ECO:0000244|PDB:1APJ}.
TURN 2093 2096 {ECO:0000244|PDB:1APJ}.
HELIX 2105 2110 {ECO:0000244|PDB:1APJ}.
STRAND 2130 2133 {ECO:0000244|PDB:1EMN}.
STRAND 2138 2142 {ECO:0000244|PDB:1EMN}.
STRAND 2157 2160 {ECO:0000244|PDB:1EMN}.
STRAND 2163 2166 {ECO:0000244|PDB:1EMN}.
HELIX 2169 2171 {ECO:0000244|PDB:1EMN}.
STRAND 2177 2179 {ECO:0000244|PDB:1EMN}.
STRAND 2181 2183 {ECO:0000244|PDB:1EMN}.
STRAND 2185 2190 {ECO:0000244|PDB:1EMN}.
STRAND 2193 2196 {ECO:0000244|PDB:1EMN}.
STRAND 2200 2202 {ECO:0000244|PDB:1EMN}.
SEQUENCE 2871 AA; 312237 MW; 3E6BEF0F1E9A479F CRC64;
MRRGRLLEIA LGFTVLLASY TSHGADANLE AGNVKETRAS RAKRRGGGGH DALKGPNVCG
SRYNAYCCPG WKTLPGGNQC IVPICRHSCG DGFCSRPNMC TCPSGQIAPS CGSRSIQHCN
IRCMNGGSCS DDHCLCQKGY IGTHCGQPVC ESGCLNGGRC VAPNRCACTY GFTGPQCERD
YRTGPCFTVI SNQMCQGQLS GIVCTKTLCC ATVGRAWGHP CEMCPAQPHP CRRGFIPNIR
TGACQDVDEC QAIPGLCQGG NCINTVGSFE CKCPAGHKLN EVSQKCEDID ECSTIPGICE
GGECTNTVSS YFCKCPPGFY TSPDGTRCID VRPGYCYTAL TNGRCSNQLP QSITKMQCCC
DAGRCWSPGV TVAPEMCPIR ATEDFNKLCS VPMVIPGRPE YPPPPLGPIP PVLPVPPGFP
PGPQIPVPRP PVEYLYPSRE PPRVLPVNVT DYCQLVRYLC QNGRCIPTPG SCRCECNKGF
QLDLRGECID VDECEKNPCA GGECINNQGS YTCQCRAGYQ STLTRTECRD IDECLQNGRI
CNNGRCINTD GSFHCVCNAG FHVTRDGKNC EDMDECSIRN MCLNGMCINE DGSFKCICKP
GFQLASDGRY CKDINECETP GICMNGRCVN TDGSYRCECF PGLAVGLDGR VCVDTHMRST
CYGGYKRGQC IKPLFGAVTK SECCCASTEY AFGEPCQPCP AQNSAEYQAL CSSGPGMTSA
GSDINECALD PDICPNGICE NLRGTYKCIC NSGYEVDSTG KNCVDINECV LNSLLCDNGQ
CRNTPGSFVC TCPKGFIYKP DLKTCEDIDE CESSPCINGV CKNSPGSFIC ECSSESTLDP
TKTICIETIK GTCWQTVIDG RCEININGAT LKSQCCSSLG AAWGSPCTLC QVDPICGKGY
SRIKGTQCED IDECEVFPGV CKNGLCVNTR GSFKCQCPSG MTLDATGRIC LDIRLETCFL
RYEDEECTLP IAGRHRMDAC CCSVGAAWGT EECEECPMRN TPEYEELCPR GPGFATKEIT
NGKPFFKDIN ECKMIPSLCT HGKCRNTIGS FKCRCDSGFA LDSEERNCTD IDECRISPDL
CGRGQCVNTP GDFECKCDEG YESGFMMMKN CMDIDECQRD PLLCRGGVCH NTEGSYRCEC
PPGHQLSPNI SACIDINECE LSAHLCPNGR CVNLIGKYQC ACNPGYHSTP DRLFCVDIDE
CSIMNGGCET FCTNSEGSYE CSCQPGFALM PDQRSCTDID ECEDNPNICD GGQCTNIPGE
YRCLCYDGFM ASEDMKTCVD VNECDLNPNI CLSGTCENTK GSFICHCDMG YSGKKGKTGC
TDINECEIGA HNCGKHAVCT NTAGSFKCSC SPGWIGDGIK CTDLDECSNG THMCSQHADC
KNTMGSYRCL CKEGYTGDGF TCTDLDECSE NLNLCGNGQC LNAPGGYRCE CDMGFVPSAD
GKACEDIDEC SLPNICVFGT CHNLPGLFRC ECEIGYELDR SGGNCTDVNE CLDPTTCISG
NCVNTPGSYI CDCPPDFELN PTRVGCVDTR SGNCYLDIRP RGDNGDTACS NEIGVGVSKA
SCCCSLGKAW GTPCEMCPAV NTSEYKILCP GGEGFRPNPI TVILEDIDEC QELPGLCQGG
KCINTFGSFQ CRCPTGYYLN EDTRVCDDVN ECETPGICGP GTCYNTVGNY TCICPPDYMQ
VNGGNNCMDM RRSLCYRNYY ADNQTCDGEL LFNMTKKMCC CSYNIGRAWN KPCEQCPIPS
TDEFATLCGS QRPGFVIDIY TGLPVDIDEC REIPGVCENG VCINMVGSFR CECPVGFFYN
DKLLVCEDID ECQNGPVCQR NAECINTAGS YRCDCKPGYR FTSTGQCNDR NECQEIPNIC
SHGQCIDTVG SFYCLCHTGF KTNDDQTMCL DINECERDAC GNGTCRNTIG SFNCRCNHGF
ILSHNNDCID VDECASGNGN LCRNGQCINT VGSFQCQCNE GYEVAPDGRT CVDINECLLE
PRKCAPGTCQ NLDGSYRCIC PPGYSLQNEK CEDIDECVEE PEICALGTCS NTEGSFKCLC
PEGFSLSSSG RRCQDLRMSY CYAKFEGGKC SSPKSRNHSK QECCCALKGE GWGDPCELCP
TEPDEAFRQI CPYGSGIIVG PDDSAVDMDE CKEPDVCKHG QCINTDGSYR CECPFGYILA
GNECVDTDEC SVGNPCGNGT CKNVIGGFEC TCEEGFEPGP MMTCEDINEC AQNPLLCAFR
CVNTYGSYEC KCPVGYVLRE DRRMCKDEDE CEEGKHDCTE KQMECKNLIG TYMCICGPGY
QRRPDGEGCV DENECQTKPG ICENGRCLNT RGSYTCECND GFTASPNQDE CLDNREGYCF
TEVLQNMCQI GSSNRNPVTK SECCCDGGRG WGPHCEICPF QGTVAFKKLC PHGRGFMTNG
ADIDECKVIH DVCRNGECVN DRGSYHCICK TGYTPDITGT SCVDLNECNQ APKPCNFICK
NTEGSYQCSC PKGYILQEDG RSCKDLDECA TKQHNCQFLC VNTIGGFTCK CPPGFTQHHT
SCIDNNECTS DINLCGSKGI CQNTPGSFTC ECQRGFSLDQ TGSSCEDVDE CEGNHRCQHG
CQNIIGGYRC SCPQGYLQHY QWNQCVDENE CLSAHICGGA SCHNTLGSYK CMCPAGFQYE
QFSGGCQDIN ECGSAQAPCS YGCSNTEGGY LCGCPPGYFR IGQGHCVSGM GMGRGNPEPP
VSGEMDDNSL SPEACYECKI NGYPKRGRKR RSTNETDASN IEDQSETEAN VSLASWDVEK
TAIFAFNISH VSNKVRILEL LPALTTLTNH NRYLIESGNE DGFFKINQKE GISYLHFTKK
KPVAGTYSLQ ISSTPLYKKK ELNQLEDKYD KDYLSGELGD NLKMKIQVLL H


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