P35555 (FBN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibrillin-1

Gene names

Name:	FBN1
Synonyms:	FBN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2871 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively. Ref.25
Subunit structure	Interacts with COL16A1. Interacts with integrin alpha-V/beta-3. Interacts with ADAMTSL4. Interacts with ADAMTS10; this interaction promotes microfibrils assembly. Interacts with THSD4; this interaction promotes fibril formation By similarity. Ref.12 Ref.14 Ref.15 Ref.25
Subcellular location	Secreted › extracellular space › extracellular matrix Ref.15.
Post-translational modification	Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. The majority of the more than 600 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. Ref.2 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.43 Ref.44 Ref.45 Ref.46 Ref.48 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.67 Ectopia lentis, 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34 Ref.56 Ref.57 Ref.58 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.59 Shprintzen-Goldberg craniosynostosis syndrome (SGS) [MIM:182212]: A very rare syndrome characterized by a marfanoid habitus, craniosynostosis, characteristic dysmorphic facial features, skeletal and cardiovascular abnormalities, mental retardation, developmental delay and learning disabilities. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.42 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.65 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.66 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.66
Sequence similarities	Belongs to the fibrillin family. Contains 47 EGF-like domains. Contains 9 TB (TGF-beta binding) domains.
Sequence caution	The sequence CAA45118.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Aortic aneurysm Craniosynostosis Disease mutation Dwarfism
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	extracellular matrix organization Traceable author statement. Source: Reactome heart development Inferred from mutant phenotype PubMed 15781745. Source: UniProtKB sequestering of BMP in extracellular matrix Inferred from sequence or structural similarity. Source: BHF-UCL sequestering of TGFbeta in extracellular matrix Inferred from sequence or structural similarity. Source: BHF-UCL skeletal system development Inferred from mutant phenotype Ref.34. Source: UniProtKB
Cellular_component	basement membrane Inferred from direct assay PubMed 3536967. Source: UniProtKB extracellular space Inferred from direct assay PubMed 3536967. Source: UniProtKB microfibril Inferred from direct assay Ref.11PubMed 3536967. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from direct assay Ref.7. Source: UniProtKB extracellular matrix structural constituent Inferred from direct assay PubMed 3536967. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EFEMP2	O95967	3	EBI-2505934,EBI-743414
FBLN5	Q9UBX5	3	EBI-2505934,EBI-947897
LOX	P28300	2	EBI-2505934,EBI-3893481

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Potential

Chain

28 – 2871

2844

Fibrillin-1

PRO_0000007581

Regions

Domain

81 – 112

32

EGF-like 1

Domain

115 – 146

32

EGF-like 2

Domain

147 – 178

32

EGF-like 3

Domain

184 – 236

53

TB 1

Domain

246 – 287

42

EGF-like 4; calcium-binding

Domain

288 – 329

42

EGF-like 5; calcium-binding

Domain

334 – 389

56

TB 2

Domain

449 – 489

41

EGF-like 6

Domain

490 – 529

40

EGF-like 7; calcium-binding

Domain

530 – 571

42

EGF-like 8; calcium-binding

Domain

572 – 612

41

EGF-like 9; calcium-binding

Domain

613 – 653

41

EGF-like 10; calcium-binding

Domain

659 – 711

53

TB 3

Domain

723 – 764

42

EGF-like 11; calcium-binding

Domain

765 – 806

42

EGF-like 12; calcium-binding

Domain

807 – 846

40

EGF-like 13; calcium-binding

Domain

851 – 902

52

TB 4

Domain

910 – 951

42

EGF-like 14; calcium-binding

Domain

956 – 1008

53

TB 5

Domain

1028 – 1069

42

EGF-like 15; calcium-binding

Domain

1070 – 1112

43

EGF-like 16; calcium-binding

Domain

1113 – 1154

42

EGF-like 17; calcium-binding

Domain

1155 – 1196

42

EGF-like 18; calcium-binding

Domain

1197 – 1237

41

EGF-like 19; calcium-binding

Domain

1238 – 1279

42

EGF-like 20; calcium-binding

Domain

1280 – 1321

42

EGF-like 21; calcium-binding

Domain

1322 – 1362

41

EGF-like 22; calcium-binding

Domain

1363 – 1403

41

EGF-like 23; calcium-binding

Domain

1404 – 1445

42

EGF-like 24; calcium-binding

Domain

1446 – 1486

41

EGF-like 25; calcium-binding

Domain

1487 – 1527

41

EGF-like 26; calcium-binding

Domain

1532 – 1589

58

TB 6

Domain

1606 – 1647

42

EGF-like 27; calcium-binding

Domain

1648 – 1688

41

EGF-like 28; calcium-binding

Domain

1693 – 1748

56

TB 7

Domain

1766 – 1807

42

EGF-like 29; calcium-binding

Domain

1808 – 1848

41

EGF-like 30; calcium-binding

Domain

1849 – 1890

42

EGF-like 31; calcium-binding

Domain

1891 – 1929

39

EGF-like 32; calcium-binding

Domain

1930 – 1972

43

EGF-like 33; calcium-binding

Domain

1973 – 2012

40

EGF-like 34; calcium-binding

Domain

2013 – 2054

42

EGF-like 35; calcium-binding

Domain

2059 – 2111

53

TB 8

Domain

2127 – 2165

39

EGF-like 36; calcium-binding

Domain

2166 – 2205

40

EGF-like 37; calcium-binding

Domain

2206 – 2246

41

EGF-like 38; calcium-binding

Domain

2247 – 2290

44

EGF-like 39; calcium-binding

Domain

2291 – 2332

42

EGF-like 40; calcium-binding

Domain

2337 – 2390

54

TB 9

Domain

2402 – 2443

42

EGF-like 41; calcium-binding

Domain

2444 – 2484

41

EGF-like 42; calcium-binding

Domain

2485 – 2523

39

EGF-like 43; calcium-binding

Domain

2524 – 2566

43

EGF-like 44; calcium-binding

Domain

2567 – 2606

40

EGF-like 45; calcium-binding

Domain

2607 – 2647

41

EGF-like 46; calcium-binding

Domain

2648 – 2687

40

EGF-like 47; calcium-binding

Compositional bias

402 – 446

45

Pro-rich

Amino acid modifications

Modified residue

1103

1

Phosphoserine By similarity

Modified residue

2071

1

Phosphoserine By similarity

Glycosylation

448

1

N-linked (GlcNAc...) Ref.13

Glycosylation

1067

1

N-linked (GlcNAc...) Ref.13

Glycosylation

1149

1

N-linked (GlcNAc...) Potential

Glycosylation

1369

1

N-linked (GlcNAc...) Potential

Glycosylation

1484

1

N-linked (GlcNAc...) Ref.13

Glycosylation

1581

1

N-linked (GlcNAc...) Ref.13

Glycosylation

1669

1

N-linked (GlcNAc...) Potential

Glycosylation

1703

1

N-linked (GlcNAc...) Potential

Glycosylation

1713

1

N-linked (GlcNAc...) Potential

Glycosylation

1902

1

N-linked (GlcNAc...) Potential

Glycosylation

2077

1

N-linked (GlcNAc...) Potential

Glycosylation

2178

1

N-linked (GlcNAc...) Potential

Glycosylation

2734

1

N-linked (GlcNAc...) Potential

Glycosylation

2750

1

N-linked (GlcNAc...) Potential

Glycosylation

2767

1

N-linked (GlcNAc...) Potential

Disulfide bond

85 ↔ 94

By similarity

Disulfide bond

89 ↔ 100

By similarity

Disulfide bond

102 ↔ 111

By similarity

Disulfide bond

119 ↔ 129

By similarity

Disulfide bond

123 ↔ 134

By similarity

Disulfide bond

136 ↔ 145

By similarity

Disulfide bond

150 ↔ 160

By similarity

Disulfide bond

154 ↔ 166

By similarity

Disulfide bond

168 ↔ 177

By similarity

Disulfide bond

250 ↔ 262

By similarity

Disulfide bond

257 ↔ 271

By similarity

Disulfide bond

273 ↔ 286

By similarity

Disulfide bond

292 ↔ 304

By similarity

Disulfide bond

299 ↔ 313

By similarity

Disulfide bond

315 ↔ 328

By similarity

Disulfide bond

453 ↔ 465

By similarity

Disulfide bond

460 ↔ 474

By similarity

Disulfide bond

476 ↔ 488

By similarity

Disulfide bond

494 ↔ 504

By similarity

Disulfide bond

499 ↔ 513

By similarity

Disulfide bond

515 ↔ 528

By similarity

Disulfide bond

534 ↔ 546

By similarity

Disulfide bond

541 ↔ 555

By similarity

Disulfide bond

557 ↔ 570

By similarity

Disulfide bond

576 ↔ 587

By similarity

Disulfide bond

582 ↔ 596

By similarity

Disulfide bond

598 ↔ 611

By similarity

Disulfide bond

617 ↔ 628

By similarity

Disulfide bond

623 ↔ 637

By similarity

Disulfide bond

639 ↔ 652

By similarity

Disulfide bond

727 ↔ 739

By similarity

Disulfide bond

734 ↔ 748

By similarity

Disulfide bond

750 ↔ 763

By similarity

Disulfide bond

769 ↔ 781

By similarity

Disulfide bond

776 ↔ 790

By similarity

Disulfide bond

792 ↔ 805

By similarity

Disulfide bond

811 ↔ 821

Ref.25 Ref.26

Disulfide bond

816 ↔ 830

Ref.25 Ref.26

Disulfide bond

832 ↔ 845

Ref.25 Ref.26

Disulfide bond

853 ↔ 875

Ref.25 Ref.26

Disulfide bond

862 ↔ 887

Ref.25 Ref.26

Disulfide bond

876 ↔ 890

Ref.25 Ref.26

Disulfide bond

896 ↔ 908

Ref.25 Ref.26

Disulfide bond

914 ↔ 926

Ref.25 Ref.26

Disulfide bond

921 ↔ 935

Ref.25 Ref.26

Disulfide bond

937 ↔ 950

Ref.25 Ref.26

Disulfide bond

1032 ↔ 1044

By similarity

Disulfide bond

1039 ↔ 1053

By similarity

Disulfide bond

1055 ↔ 1068

By similarity

Disulfide bond

1074 ↔ 1086

By similarity

Disulfide bond

1081 ↔ 1095

By similarity

Disulfide bond

1097 ↔ 1111

By similarity

Disulfide bond

1117 ↔ 1129

By similarity

Disulfide bond

1124 ↔ 1138

By similarity

Disulfide bond

1140 ↔ 1153

By similarity

Disulfide bond

1159 ↔ 1171

By similarity

Disulfide bond

1166 ↔ 1180

By similarity

Disulfide bond

1182 ↔ 1195

By similarity

Disulfide bond

1201 ↔ 1212

By similarity

Disulfide bond

1208 ↔ 1221

By similarity

Disulfide bond

1223 ↔ 1236

By similarity

Disulfide bond

1242 ↔ 1254

By similarity

Disulfide bond

1249 ↔ 1263

By similarity

Disulfide bond

1265 ↔ 1278

By similarity

Disulfide bond

1284 ↔ 1296

By similarity

Disulfide bond

1291 ↔ 1305

By similarity

Disulfide bond

1307 ↔ 1320

By similarity

Disulfide bond

1326 ↔ 1339

By similarity

Disulfide bond

1333 ↔ 1348

By similarity

Disulfide bond

1350 ↔ 1361

By similarity

Disulfide bond

1367 ↔ 1380

By similarity

Disulfide bond

1374 ↔ 1389

By similarity

Disulfide bond

1391 ↔ 1402

By similarity

Disulfide bond

1408 ↔ 1420

By similarity

Disulfide bond

1415 ↔ 1429

By similarity

Disulfide bond

1431 ↔ 1444

By similarity

Disulfide bond

1450 ↔ 1461

By similarity

Disulfide bond

1456 ↔ 1470

By similarity

Disulfide bond

1472 ↔ 1485

By similarity

Disulfide bond

1491 ↔ 1502

Ref.25 Ref.26

Disulfide bond

1497 ↔ 1511

Ref.25 Ref.26

Disulfide bond

1513 ↔ 1526

Ref.25 Ref.26

Disulfide bond

1534 ↔ 1562

Ref.25 Ref.26

Disulfide bond

1549 ↔ 1574

Ref.25 Ref.26

Disulfide bond

1563 ↔ 1577

Ref.25 Ref.26

Disulfide bond

1564 ↔ 1589

Ref.25 Ref.26

Disulfide bond

1610 ↔ 1622

Ref.25 Ref.26

Disulfide bond

1617 ↔ 1631

Ref.25 Ref.26

Disulfide bond

1633 ↔ 1646

Ref.25 Ref.26

Disulfide bond

1652 ↔ 1663

By similarity

Disulfide bond

1658 ↔ 1672

By similarity

Disulfide bond

1674 ↔ 1687

By similarity

Disulfide bond

1770 ↔ 1782

By similarity

Disulfide bond

1777 ↔ 1791

By similarity

Disulfide bond

1793 ↔ 1806

By similarity

Disulfide bond

1812 ↔ 1824

By similarity

Disulfide bond

1818 ↔ 1833

By similarity

Disulfide bond

1835 ↔ 1847

By similarity

Disulfide bond

1853 ↔ 1865

By similarity

Disulfide bond

1860 ↔ 1874

By similarity

Disulfide bond

1876 ↔ 1889

By similarity

Disulfide bond

1895 ↔ 1905

By similarity

Disulfide bond

1900 ↔ 1914

By similarity

Disulfide bond

1916 ↔ 1928

By similarity

Disulfide bond

1934 ↔ 1947

By similarity

Disulfide bond

1942 ↔ 1956

By similarity

Disulfide bond

1958 ↔ 1971

By similarity

Disulfide bond

1977 ↔ 1989

By similarity

Disulfide bond

1984 ↔ 1998

By similarity

Disulfide bond

2000 ↔ 2011

By similarity

Disulfide bond

2017 ↔ 2029

By similarity

Disulfide bond

2024 ↔ 2038

By similarity

Disulfide bond

2040 ↔ 2053

By similarity

Disulfide bond

2061 ↔ 2083

Ref.25 Ref.26

Disulfide bond

2070 ↔ 2096

Ref.25 Ref.26

Disulfide bond

2084 ↔ 2099

Ref.25 Ref.26

Disulfide bond

2085 ↔ 2111

Ref.25 Ref.26

Disulfide bond

2131 ↔ 2142

By similarity

Disulfide bond

2137 ↔ 2151

By similarity

Disulfide bond

2153 ↔ 2164

By similarity

Disulfide bond

2170 ↔ 2181

By similarity

Disulfide bond

2176 ↔ 2190

By similarity

Disulfide bond

2192 ↔ 2204

By similarity

Disulfide bond

2210 ↔ 2221

By similarity

Disulfide bond

2217 ↔ 2230

By similarity

Disulfide bond

2232 ↔ 2245

By similarity

Disulfide bond

2251 ↔ 2265

By similarity

Disulfide bond

2258 ↔ 2274

By similarity

Disulfide bond

2276 ↔ 2289

By similarity

Disulfide bond

2295 ↔ 2307

By similarity

Disulfide bond

2302 ↔ 2316

By similarity

Disulfide bond

2318 ↔ 2331

By similarity

Disulfide bond

2406 ↔ 2418

By similarity

Disulfide bond

2413 ↔ 2427

By similarity

Disulfide bond

2429 ↔ 2442

By similarity

Disulfide bond

2448 ↔ 2459

By similarity

Disulfide bond

2455 ↔ 2468

By similarity

Disulfide bond

2470 ↔ 2483

By similarity

Disulfide bond

2489 ↔ 2500

By similarity

Disulfide bond

2496 ↔ 2509

By similarity

Disulfide bond

2511 ↔ 2522

By similarity

Disulfide bond

2528 ↔ 2541

By similarity

Disulfide bond

2535 ↔ 2550

By similarity

Disulfide bond

2552 ↔ 2565

By similarity

Disulfide bond

2571 ↔ 2581

By similarity

Disulfide bond

2577 ↔ 2590

By similarity

Disulfide bond

2592 ↔ 2605

By similarity

Disulfide bond

2611 ↔ 2622

By similarity

Disulfide bond

2617 ↔ 2631

By similarity

Disulfide bond

2633 ↔ 2646

By similarity

Disulfide bond

2652 ↔ 2663

By similarity

Disulfide bond

2659 ↔ 2672

By similarity

Disulfide bond

2674 ↔ 2686

By similarity

Natural variations

Natural variant

20

1

Y → C in MFS. Ref.62

VAR_023859

Natural variant

27

1

A → T.
Corresponds to variant rs25397 [ dbSNP | Ensembl ].

VAR_014663

Natural variant

62

1

R → C in MFS; also in a patient with ectopia lentis and retinal detachment. Ref.57
Corresponds to variant rs25403 [ dbSNP | Ensembl ].

VAR_017967

Natural variant

80

1

C → G in MFS. Ref.67

VAR_065981

Natural variant

89

1

C → F in MFS. Ref.56
Corresponds to variant rs112660651 [ dbSNP | Ensembl ].

VAR_017968

Natural variant

111

1

C → R in MFS. Ref.48

VAR_002276

Natural variant

114

1

R → C in MFS. Ref.58

VAR_017969

Natural variant

115

1

S → C in ECTOL1. Ref.57

VAR_017970

Natural variant

122

1

R → C in MFS. Ref.36 Ref.52 Ref.56
Corresponds to variant rs137854467 [ dbSNP | Ensembl ].

VAR_002277

Natural variant

123

1

C → Y in MFS. Ref.62

VAR_023860

Natural variant

129

1

C → Y in MFS; severe neonatal. Ref.41

VAR_002278

Natural variant

133

1

H → Q.
Corresponds to variant rs363850 [ dbSNP | Ensembl ].

VAR_055723

Natural variant

154

1

C → S in MFS. Ref.60

VAR_017971

Natural variant

166

1

C → F in MFS. Ref.41

VAR_002279

Natural variant

166

1

C → S in MFS. Ref.60

VAR_002280

Natural variant

177

1

C → R in MFS. Ref.62
Corresponds to variant rs363853 [ dbSNP | Ensembl ].

VAR_023861

Natural variant

217

1

W → G in MFS. Ref.33 Ref.39

VAR_002281

Natural variant

224

1

C → R in MFS. Ref.62

VAR_023862

Natural variant

240

1

R → C in MFS and ECTOL1. Ref.56 Ref.58 Ref.60
Corresponds to variant rs137854480 [ dbSNP | Ensembl ].

VAR_017972

Natural variant

329

1

I → T.
Corresponds to variant rs12324002 [ dbSNP | Ensembl ].

VAR_055724

Natural variant

363

1

G → S.
Corresponds to variant rs363855 [ dbSNP | Ensembl ].

VAR_055725

Natural variant

366

1

W → C in MFS. Ref.56

VAR_017973

Natural variant

439

1

R → G in MFS. Ref.62

VAR_023863

Natural variant

472

1

C → Y. Ref.1 Ref.3 Ref.5 Ref.6 Ref.7
Corresponds to variant rs4775765 [ dbSNP | Ensembl ].

VAR_058090

Natural variant

476

1

C → G in MFS.

VAR_002282

Natural variant

490

1

D → Y in MFS. Ref.67

VAR_002283

Natural variant

499

1

C → Y in MFS. Ref.67

VAR_065982

Natural variant

504

1

C → F in MFS. Ref.55

VAR_010776

Natural variant

507

1

Missing in MFS. Ref.63

VAR_023864

Natural variant

541

1

C → Y in MFS. Ref.63

VAR_023865

Natural variant

545

1

R → C in MFS. Ref.48 Ref.56

VAR_002284

Natural variant

548

1

N → I in MFS. Ref.30
Corresponds to variant rs137854462 [ dbSNP | Ensembl ].

VAR_002285

Natural variant

560

1

G → S in MFS. Ref.56

VAR_017974

Natural variant

570

1

C → Y in MFS. Ref.56

VAR_017975

Natural variant

587

1

C → Y in MFS. Ref.46 Ref.57

VAR_002286

Natural variant

592

1

G → D in MFS. Ref.56

VAR_017976

Natural variant

596

1

C → Y in MFS. Ref.57

VAR_017977

Natural variant

598

1

C → W in MFS. Ref.56

VAR_017978

Natural variant

611

1

C → R in MFS. Ref.67

VAR_065983

Natural variant

617

1

C → G in MFS. Ref.67

VAR_065984

Natural variant

627

1

R → C in MFS; enhances proteolytic degradation. Ref.35 Ref.48 Ref.61 Ref.63

VAR_002287

Natural variant

628

1

C → K in MFS; requires 2 nucleotide substitutions.

VAR_023866

Natural variant

629 – 633

5

Missing in MFS.

VAR_023867

Natural variant

635

1

Y → C in MFS. Ref.62

VAR_023868

Natural variant

636

1

R → I in MFS. Ref.62

VAR_023869

Natural variant

652

1

C → S in MFS. Ref.60

VAR_017979

Natural variant

654

1

D → N in MFS. Ref.57

VAR_017980

Natural variant

661

1

C → R in MFS.

VAR_002288

Natural variant

661

1

C → Y in ECTOL1; patient presenting also mitral valve prolapse. Ref.57

VAR_017981

Natural variant

681

1

S → Y in MFS. Ref.57

VAR_017982

Natural variant

683

1

C → R in MFS. Ref.57

VAR_017983

Natural variant

685

1

C → W in MFS. Ref.57 Ref.67

VAR_017984

Natural variant

685

1

C → Y in MFS. Ref.67

VAR_065985

Natural variant

705

1

A → T in MFS. Ref.45 Ref.60

VAR_002289

Natural variant

711

1

C → Y in MFS. Ref.45 Ref.60

VAR_002290

Natural variant

723

1

D → A in MFS. Ref.30
Corresponds to variant rs137854463 [ dbSNP | Ensembl ].

VAR_002291

Natural variant

723

1

D → V in MFS. Ref.57

VAR_017985

Natural variant

734

1

C → F in MFS. Ref.57

VAR_017986

Natural variant

746

1

Y → C in MFS. Ref.41

VAR_002292

Natural variant

748

1

C → Y in MFS. Ref.57

VAR_017987

Natural variant

750

1

C → G in MFS; enhances proteolytic degradation. Ref.48 Ref.61

VAR_002293

Natural variant

776

1

C → G in MFS. Ref.57

VAR_017988

Natural variant

776

1

C → Y in MFS. Ref.56

VAR_017989

Natural variant

781

1

C → R in MFS. Ref.56 Ref.57

VAR_017990

Natural variant

781

1

C → Y in MFS. Ref.63

VAR_023870

Natural variant

790

1

C → Y in MFS. Ref.67

VAR_065986

Natural variant

811

1

C → Y in MFS. Ref.67

VAR_065987

Natural variant

816

1

C → S in MFS. Ref.60

VAR_017991

Natural variant

832

1

C → Y in MFS. Ref.62

VAR_023871

Natural variant

853

1

C → S in MFS. Ref.67

VAR_065988

Natural variant

862

1

C → R in MFS. Ref.32

VAR_002294

Natural variant

890

1

C → G in MFS. Ref.62

VAR_023872

Natural variant

890

1

C → R in MFS. Ref.58

VAR_017992

Natural variant

908

1

C → R in MFS. Ref.57

VAR_017993

Natural variant

913

1

E → G in MFS. Ref.56

VAR_017994

Natural variant

921

1

C → G in MFS. Ref.57

VAR_017995

Natural variant

926

1

C → R in MFS; enhances proteolytic degradation. Ref.41 Ref.61

VAR_002295

Natural variant

926

1

C → Y in MFS. Ref.67

VAR_065989

Natural variant

984

1

V → I in MFS. Ref.53

VAR_002296

Natural variant

985

1

G → E in MFS; atypical. Ref.54
Corresponds to variant rs137854477 [ dbSNP | Ensembl ].

VAR_018319

Natural variant

985

1

G → R in MFS. Ref.56 Ref.63

VAR_017996

Natural variant

996

1

C → R in MFS.
Corresponds to variant rs140592 [ dbSNP | Ensembl ].

VAR_002297

Natural variant

1013

1

G → R in MFS; severe neonatal. Ref.41 Ref.56 Ref.60 Ref.63
Corresponds to variant rs140593 [ dbSNP | Ensembl ].

VAR_002298

Natural variant

1023

1

K → N in MFS; severe neonatal. Ref.39

VAR_002299

Natural variant

1043

1

K → R in MFS.
Corresponds to variant rs137854472 [ dbSNP | Ensembl ].

VAR_002300

Natural variant

1044

1

C → Y in MFS. Ref.60

VAR_017997

Natural variant

1048

1

I → T in MFS.

VAR_002301

Natural variant

1048

1

I → V.
Corresponds to variant rs2229324 [ dbSNP | Ensembl ].

VAR_055726

Natural variant

1048

1

Missing in MFS.

VAR_002302

Natural variant

1053

1

C → R in MFS. Ref.44

VAR_002303

Natural variant

1055

1

C → G in MFS; neonatal. Ref.45 Ref.60

VAR_002304

Natural variant

1055

1

C → W in MFS. Ref.56

VAR_017998

Natural variant

1055

1

C → Y in MFS. Ref.56

VAR_017999

Natural variant

1058

1

G → D in MFS. Ref.62

VAR_023873

Natural variant

1058

1

G → GC in MFS.

VAR_002305

Natural variant

1068

1

C → G in MFS; neonatal form. Ref.64

VAR_064503

Natural variant

1072

1

D → G in MFS. Ref.44

VAR_002306

Natural variant

1073

1

E → K in MFS; severe neonatal. Ref.41 Ref.44
Corresponds to variant rs137854478 [ dbSNP | Ensembl ].

VAR_002307

Natural variant

1074

1

C → R in MFS; severe neonatal. Ref.39 Ref.48
Corresponds to variant rs137854465 [ dbSNP | Ensembl ].

VAR_002308

Natural variant

1086

1

C → W in MFS.

VAR_002309

Natural variant

1090

1

P → S in MFS. Ref.67

VAR_065990

Natural variant

1101

1

Y → C in MFS. Ref.56 Ref.60

VAR_018000

Natural variant

1113

1

D → G.
Corresponds to variant rs140597 [ dbSNP | Ensembl ].

VAR_055727

Natural variant

1113

1

D → V in MFS. Ref.63

VAR_023874

Natural variant

1117

1

C → G in MFS. Ref.44

VAR_002310

Natural variant

1117

1

C → Y in MFS. Ref.32 Ref.60
Corresponds to variant rs137854470 [ dbSNP | Ensembl ].

VAR_002311

Natural variant

1127

1

G → S in a mild form of inherited weakness of elastic tissue that predisposes to ascending aortic aneurysm and dissection later in life. Ref.40
Corresponds to variant rs137854468 [ dbSNP | Ensembl ].

VAR_002312

Natural variant

1128

1

V → I in a patient with mitral valve prolapse. Ref.56

VAR_018001

Natural variant

1129

1

C → Y in MFS. Ref.55
Corresponds to variant rs137854482 [ dbSNP | Ensembl ].

VAR_010777

Natural variant

1131

1

N → Y in MFS.
Corresponds to variant rs137854473 [ dbSNP | Ensembl ].

VAR_002313

Natural variant

1137

1

R → P in MFS. Ref.27 Ref.32
Corresponds to variant rs137854456 [ dbSNP | Ensembl ].

VAR_002314

Natural variant

1148

1

P → A. Ref.32 Ref.47 Ref.49 Ref.50
Corresponds to variant rs140598 [ dbSNP | Ensembl ].

VAR_002315

Natural variant

1153

1

C → S in MFS. Ref.62

VAR_023875

Natural variant

1153

1

C → Y in MFS; severe. Ref.45 Ref.60
Corresponds to variant rs140599 [ dbSNP | Ensembl ].

VAR_002316

Natural variant

1155

1

D → N in MFS. Ref.60

VAR_002317

Natural variant

1170

1

R → H in MFS; mild. Ref.38 Ref.48
Corresponds to variant rs137854475 [ dbSNP | Ensembl ].

VAR_002318

Natural variant

1171

1

C → W in MFS. Ref.48

VAR_002319

Natural variant

1173

1

N → K in MFS. Ref.48

VAR_002320

Natural variant

1185

1

G → D in MFS. Ref.67

VAR_065991

Natural variant

1200

1

E → G in MFS. Ref.58

VAR_018002

Natural variant

1211

1

Missing in MFS. Ref.62

VAR_023876

Natural variant

1219

1

Y → C in MFS. Ref.62

VAR_023877

Natural variant

1223

1

C → Y in MFS and SGS. Ref.37 Ref.42
Corresponds to variant rs137854469 [ dbSNP | Ensembl ].

VAR_002321

Natural variant

1242

1

C → Y in MFS. Ref.39
Corresponds to variant rs137854471 [ dbSNP | Ensembl ].

VAR_002322

Natural variant

1249

1

C → S in MFS. Ref.28
Corresponds to variant rs137854458 [ dbSNP | Ensembl ].

VAR_002323

Natural variant

1261

1

Y → C in MFS. Ref.55

VAR_010778

Natural variant

1261

1

Y → D in MFS. Ref.62

VAR_023878

Natural variant

1265

1

C → R in MFS. Ref.51
Corresponds to variant rs137854474 [ dbSNP | Ensembl ].

VAR_018320

Natural variant

1278

1

C → S in MFS. Ref.62

VAR_023879

Natural variant

1282

1

N → S.
Corresponds to variant rs140647 [ dbSNP | Ensembl ].

VAR_055728

Natural variant

1284

1

C → G in MFS. Ref.63

VAR_023880

Natural variant

1284

1

C → Y in MFS. Ref.67

VAR_065992

Natural variant

1325

1

E → Q in MFS. Ref.60

VAR_018003

Natural variant

1333

1

C → S in MFS. Ref.62

VAR_023881

Natural variant

1337

1

A → P in MFS; neonatal. Ref.56

VAR_018004

Natural variant

1339

1

C → Y in MFS. Ref.56

VAR_018005

Natural variant

1350

1

C → F in MFS. Ref.67

VAR_065993

Natural variant

1366

1

E → K in MFS. Ref.60

VAR_018006

Natural variant

1374

1

C → S in MFS. Ref.60

VAR_018007

Natural variant

1382

1

N → S in MFS. Ref.41

VAR_002324

Natural variant

1389

1

C → R in MFS. Ref.60

VAR_018008

Natural variant

1394 – 1396

3

Missing in MFS.

VAR_018009

Natural variant

1401

1

T → A in MFS. Ref.67

VAR_065994

Natural variant

1402

1

C → R in MFS. Ref.62

VAR_023882

Natural variant

1404

1

D → Y in MFS. Ref.48

VAR_002325

Natural variant

1424

1

P → A in MFS. Ref.60

VAR_018010

Natural variant

1424

1

P → S in MFS. Ref.62

VAR_023883

Natural variant

1429

1

C → S in MFS. Ref.56

VAR_018011

Natural variant

1431

1

C → W in MFS. Ref.67
Corresponds to variant rs112375043 [ dbSNP | Ensembl ].

VAR_065995

Natural variant

1431

1

C → Y in MFS. Ref.67

VAR_065996

Natural variant

1475

1

G → E in MFS. Ref.63

VAR_023884

Natural variant

1475

1

G → S in MFS. Ref.63

VAR_023885

Natural variant

1481

1

S → G. Ref.67
Corresponds to variant rs61730054 [ dbSNP | Ensembl ].

VAR_065997

Natural variant

1487

1

D → A in MFS. Ref.67

VAR_065998

Natural variant

1489

1

N → K in MFS. Ref.67

VAR_065999

Natural variant

1513

1

C → R in MFS. Ref.39

VAR_002326

Natural variant

1530

1

R → C Found in patients with ectopia lensis. Ref.56 Ref.60
Corresponds to variant rs111401431 [ dbSNP | Ensembl ].

VAR_018012

Natural variant

1564

1

C → F in MFS. Ref.62

VAR_023886

Natural variant

1564

1

C → S in SSKS. Ref.65

VAR_064046

Natural variant

1564

1

C → Y in MFS. Ref.60

VAR_018013

Natural variant

1570

1

W → C in SSKS. Ref.65

VAR_064047

Natural variant

1576

1

M → T in MFS. Ref.63

VAR_023887

Natural variant

1577

1

C → G in SSKS. Ref.65

VAR_064048

Natural variant

1589

1

C → F in MFS. Ref.32

VAR_002327

Natural variant

1594

1

G → D in SSKS. Ref.65

VAR_064049

Natural variant

1610

1

C → G in MFS. Ref.48

VAR_002328

Natural variant

1631

1

C → G in MFS. Ref.62

VAR_023888

Natural variant

1663

1

C → R in MFS. Ref.28
Corresponds to variant rs137854459 [ dbSNP | Ensembl ].

VAR_002329

Natural variant

1663

1

C → Y in MFS. Ref.62

VAR_023889

Natural variant

1672

1

C → F.
Corresponds to variant rs140627 [ dbSNP | Ensembl ].

VAR_055729

Natural variant

1692 – 1699

8

Missing in WMS2.

VAR_018014

Natural variant

1696

1

Y → C in GPHYSD2. Ref.66

VAR_066527

Natural variant

1699

1

Y → C in GPHYSD2 and ACMICD. Ref.66

VAR_066528

Natural variant

1699

1

Y → D in GPHYSD2. Ref.66

VAR_066529

Natural variant

1700

1

Y → C in ACMICD. Ref.66

VAR_066530

Natural variant

1706

1

C → Y in GPHYSD2. Ref.66

VAR_066531

Natural variant

1714

1

M → R in ACMICD. Ref.66

VAR_066532

Natural variant

1719

1

C → W in GPHYSD2. Ref.66

VAR_066533

Natural variant

1722

1

S → C in ACMICD. Ref.66

VAR_066534

Natural variant

1726

1

G → V in ACMICD. Ref.66

VAR_066535

Natural variant

1728

1

A → T in GPHYSD2 and ACMICD. Ref.66

VAR_066536

Natural variant

1728

1

A → V in GPHYSD2. Ref.66

VAR_066537

Natural variant

1733

1

C → Y in GPHYSD2. Ref.66

VAR_066538

Natural variant

1735

1

Q → QQ in ACMICD. Ref.66

VAR_066539

Natural variant

1750

1

S → R in ACMICD. Ref.66

VAR_066540

Natural variant

1758

1

D → V in ACMICD. Ref.66

VAR_066541

Natural variant

1762

1

G → S in GPHYSD2. Ref.66

VAR_066542

Natural variant

1770

1

C → F in MFS. Ref.60

VAR_018015

Natural variant

1790

1

R → P in MFS. Ref.56 Ref.57

VAR_018016

Natural variant

1791

1

C → R in MFS. Ref.63

VAR_023890

Natural variant

1791

1

C → Y in MFS. Ref.56

VAR_018017

Natural variant

1793

1

C → W in MFS. Ref.60

VAR_018018

Natural variant

1796

1

G → E in MFS. Ref.60

VAR_018019

Natural variant

1806

1

C → S in MFS. Ref.57

VAR_018020

Natural variant

1806

1

C → Y in MFS.

VAR_023891

Natural variant

1833

1

C → S in MFS. Ref.55

VAR_010779

Natural variant

1835

1

C → Y in MFS. Ref.56 Ref.58
Corresponds to variant rs111929350 [ dbSNP | Ensembl ].

VAR_018021

Natural variant

1837

1

P → S in MFS.

VAR_002330

Natural variant

1838

1

G → C in MFS. Ref.67

VAR_066000

Natural variant

1876

1

C → Y in MFS. Ref.62
Corresponds to variant rs112728248 [ dbSNP | Ensembl ].

VAR_023892

Natural variant

1887

1

T → I in MFS. Ref.62

VAR_023893

Natural variant

1893

1

N → K in MFS. Ref.48

VAR_002331

Natural variant

1895

1

C → R in MFS. Ref.62

VAR_023894

Natural variant

1900

1

C → Y in MFS. Ref.62 Ref.67

VAR_023895

Natural variant

1909

1

I → T in MFS. Ref.56 Ref.67

VAR_018022

Natural variant

1915

1

R → S in MFS. Ref.56

VAR_018023

Natural variant

1928

1

C → G in MFS. Ref.63

VAR_023896

Natural variant

1928

1

C → R in MFS. Ref.41

VAR_002332

Natural variant

1928

1

C → Y in MFS. Ref.63

VAR_023897

Natural variant

1931

1

Missing in MFS. Ref.57

VAR_018024

Natural variant

1934

1

C → S in MFS. Ref.67

VAR_066001

Natural variant

1971

1

C → Y in MFS. Ref.56

VAR_018025

Natural variant

1976

1

E → G in MFS. Ref.67

VAR_066002

Natural variant

1977

1

C → Y in MFS. Ref.56

VAR_018026

Natural variant

1984

1

C → R in MFS. Ref.67

VAR_066003

Natural variant

1998

1

C → Y in MFS. Ref.57

VAR_018027

Natural variant

2018

1

V → I.
Corresponds to variant rs363802 [ dbSNP | Ensembl ].

VAR_055730

Natural variant

2038

1

C → Y in MFS. Ref.63
Corresponds to variant rs363804 [ dbSNP | Ensembl ].

VAR_023898

Natural variant

2053

1

C → F.
Corresponds to variant rs363805 [ dbSNP | Ensembl ].

VAR_055731

Natural variant

2085

1

C → R in MFS. Ref.63

VAR_023899

Natural variant

2099

1

C → W in MFS. Ref.48

VAR_002333

Natural variant

2101

1

T → M. Ref.57

VAR_018028

Natural variant

2111

1

C → R in MFS. Ref.58
Corresponds to variant rs363815 [ dbSNP | Ensembl ].

VAR_018029

Natural variant

2111

1

C → Y in MFS. Ref.48

VAR_002334

Natural variant

2113

1

Y → F.
Corresponds to variant rs363816 [ dbSNP | Ensembl ].

VAR_055732

Natural variant

2127

1

D → E in MFS. Ref.39

VAR_002335

Natural variant

2142

1

C → Y in MFS. Ref.55

VAR_010780

Natural variant

2144

1

N → S in MFS. Ref.31 Ref.63
Corresponds to variant rs137854461 [ dbSNP | Ensembl ].

VAR_002336

Natural variant

2151

1

C → W in MFS. Ref.39

VAR_002337

Natural variant

2154

1

P → R in ECTOL1. Ref.56

VAR_018030

Natural variant

2160

1

A → P in MFS. Ref.62

VAR_023900

Natural variant

2166

1

D → N in MFS. Ref.67

VAR_066004

Natural variant

2170

1

C → F.
Corresponds to variant rs363821 [ dbSNP | Ensembl ].

VAR_055733

Natural variant

2185

1

I → T in MFS. Ref.67

VAR_066005

Natural variant

2221

1

C → F in MFS. Ref.62

VAR_023901

Natural variant

2221

1

C → G in MFS. Ref.57

VAR_018031

Natural variant

2221

1

C → S in MFS. Ref.28
Corresponds to variant rs137854460 [ dbSNP | Ensembl ].

VAR_002338

Natural variant

2223

1

N → H in MFS. Ref.56

VAR_018032

Natural variant

2247

1

D → G in MFS. Ref.67

VAR_066006

Natural variant

2251

1

C → R in MFS.
Corresponds to variant rs112836174 [ dbSNP | Ensembl ].

VAR_023902

Natural variant

2258

1

C → R in MFS. Ref.48

VAR_002339

Natural variant

2269

1

I → T in MFS. Ref.57

VAR_018033

Natural variant

2278

1

P → S.
Corresponds to variant rs363835 [ dbSNP | Ensembl ].

VAR_055734

Natural variant

2282

1

R → W in MFS. Ref.48 Ref.56

VAR_002340

Natural variant

2307

1

C → S in MFS. Ref.28 Ref.29
Corresponds to variant rs137854457 [ dbSNP | Ensembl ].

VAR_002341

Natural variant

2318

1

C → R Found in patients with Marfan syndrome. Ref.67
Corresponds to variant rs111588631 [ dbSNP | Ensembl ].

VAR_066007

Natural variant

2329

1

D → E.
Corresponds to variant rs363831 [ dbSNP | Ensembl ].

VAR_055735

Natural variant

2335

1

R → W in MFS. Ref.57

VAR_018034

Natural variant

2339

1

C → Y in ECTOL1; patient presenting also flat corneas. Ref.57

VAR_018035

Natural variant

2385

1

A → T in MFS. Ref.62

VAR_023903

Natural variant

2406

1

C → Y in MFS. Ref.56 Ref.67

VAR_018036

Natural variant

2442

1

C → S in MFS. Ref.67

VAR_066008

Natural variant

2442

1

C → W in MFS. Ref.60

VAR_018037

Natural variant

2447

1

E → K in ECTOL1. Ref.34 Ref.39
Corresponds to variant rs137854464 [ dbSNP | Ensembl ].

VAR_002342

Natural variant

2474

1

Y → C in MFS. Ref.58

VAR_018038

Natural variant

2489

1

C → R in MFS. Ref.48

VAR_002343

Natural variant

2500

1

C → R in MFS. Ref.62

VAR_023904

Natural variant

2500

1

C → Y in MFS. Ref.62

VAR_023905

Natural variant

2511

1

C → R in MFS. Ref.39 Ref.67

VAR_002344

Natural variant

2535

1

C → W in MFS. Ref.62
Corresponds to variant rs113544411 [ dbSNP | Ensembl ].

VAR_023906

Natural variant

2536

1

G → R in MFS. Ref.63

VAR_023907

Natural variant

2570

1

E → K in MFS. Ref.62

VAR_023908

Natural variant

2571

1

C → R in MFS. Ref.62

VAR_023909

Natural variant

2581

1

C → F in MFS. Ref.56

VAR_018039

Natural variant

2585

1

I → T in MFS. Ref.56 Ref.60

VAR_018040

Natural variant

2592

1

C → S in MFS. Ref.62

VAR_023910

Natural variant

2605

1

C → R in MFS.

VAR_023911

Natural variant

2605

1

C → Y in MFS. Ref.63

VAR_023912

Natural variant

2606

1

Missing in MFS. Ref.67

VAR_066009

Natural variant

2610

1

E → K in MFS; unclear pathological significance. Ref.62 Ref.67
Corresponds to variant rs111984349 [ dbSNP | Ensembl ].

VAR_023913

Natural variant

2618

1

G → R in MFS. Ref.56
Corresponds to variant rs141133182 [ dbSNP | Ensembl ].

VAR_018041

Natural variant

2623

1

H → P in MFS. Ref.60

VAR_002345

Natural variant

2624

1

N → K in MFS. Ref.56

VAR_018042

Natural variant

2627

1

G → R in MFS. Ref.33

VAR_002346

Natural variant

2629

1

Y → C in MFS. Ref.62

VAR_023914

Natural variant

2646

1

C → R in MFS. Ref.67

VAR_066010

Natural variant

2652

1

C → G in MFS. Ref.58

VAR_018043

Natural variant

2663

1

C → S in MFS. Ref.2

VAR_023915

Natural variant

2668

1

G → C in MFS. Ref.56

VAR_018044

Natural variant

2680

1

R → C in MFS.

VAR_002347

Natural variant

2726

1

R → W in MFS; defects in protein processing. Ref.43
Corresponds to variant rs61746008 [ dbSNP | Ensembl ].

VAR_002348

Natural variant

2793

1

Y → H Found in a patient with Marfan syndrome; unclear pathological significance. Ref.67
Corresponds to variant rs113722038 [ dbSNP | Ensembl ].

VAR_066011

Experimental info

Sequence conflict

207

1

T → Q in AAB02036. Ref.1

Sequence conflict

2158

1

I → T in AAB02036. Ref.1

Sequence conflict

2158

1

I → T in CAA45118. Ref.7

Secondary structure

1

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2871

Helix Strand Turn

Details...

Helix

810 – 813

4

Beta strand

819 – 824

6

Beta strand

827 – 831

5

Beta strand

836 – 838

3

Beta strand

842 – 847

6

Beta strand

851 – 858

8

Beta strand

861 – 870

10

Helix

872 – 876

5

Turn

877 – 879

3

Beta strand

881 – 883

3

Turn

884 – 887

4

Turn

894 – 896

3

Beta strand

900 – 904

5

Beta strand

907 – 910

4

Helix

913 – 916

4

Beta strand

921 – 929

9

Beta strand

932 – 936

5

Turn

1073 – 1076

4

Turn

1080 – 1083

4

Beta strand

1086 – 1089

4

Beta strand

1092 – 1095

4

Beta strand

1099 – 1103

5

Turn

1105 – 1107

3

Beta strand

1108 – 1113

6

Helix

1116 – 1119

4

Turn

1123 – 1126

4

Beta strand

1127 – 1132

6

Beta strand

1135 – 1140

6

Beta strand

1148 – 1150

3

Helix

1490 – 1492

3

Beta strand

1496 – 1498

3

Beta strand

1500 – 1505

6

Beta strand

1508 – 1512

5

Beta strand

1523 – 1527

5

Beta strand

1532 – 1537

6

Beta strand

1544 – 1546

3

Beta strand

1550 – 1557

8

Helix

1559 – 1563

5

Turn

1564 – 1566

3

Beta strand

1568 – 1570

3

Turn

1571 – 1574

4

Helix

1583 – 1588

6

Beta strand

1595 – 1597

3

Turn

1599 – 1601

3

Beta strand

1604 – 1606

3

Helix

1609 – 1612

4

Helix

1614 – 1617

4

Beta strand

1620 – 1624

5

Beta strand

1629 – 1632

4

Turn

1641 – 1643

3

Helix

2054 – 2056

3

Beta strand

2061 – 2065

5

Beta strand

2070 – 2073

4

Helix

2080 – 2084

5

Beta strand

2090 – 2092

3

Turn

2093 – 2096

4

Helix

2105 – 2110

6

Beta strand

2130 – 2133

4

Beta strand

2138 – 2142

5

Beta strand

2157 – 2160

4

Beta strand

2163 – 2166

4

Helix

2169 – 2171

3

Beta strand

2177 – 2179

3

Beta strand

2181 – 2183

3

Beta strand

2185 – 2190

6

Beta strand

2193 – 2196

4

Beta strand

2200 – 2202

3

Sequences

	Sequence		Length	Mass (Da)
	P35555 [UniParc]. Last modified November 2, 2010. Version 3. Checksum: 3E6BEF0F1E9A479F	FASTA	2,871	312,237
	10 20 30 40 50 60 MRRGRLLEIA LGFTVLLASY TSHGADANLE AGNVKETRAS RAKRRGGGGH DALKGPNVCG 70 80 90 100 110 120 SRYNAYCCPG WKTLPGGNQC IVPICRHSCG DGFCSRPNMC TCPSGQIAPS CGSRSIQHCN 130 140 150 160 170 180 IRCMNGGSCS DDHCLCQKGY IGTHCGQPVC ESGCLNGGRC VAPNRCACTY GFTGPQCERD 190 200 210 220 230 240 YRTGPCFTVI SNQMCQGQLS GIVCTKTLCC ATVGRAWGHP CEMCPAQPHP CRRGFIPNIR 250 260 270 280 290 300 TGACQDVDEC QAIPGLCQGG NCINTVGSFE CKCPAGHKLN EVSQKCEDID ECSTIPGICE 310 320 330 340 350 360 GGECTNTVSS YFCKCPPGFY TSPDGTRCID VRPGYCYTAL TNGRCSNQLP QSITKMQCCC 370 380 390 400 410 420 DAGRCWSPGV TVAPEMCPIR ATEDFNKLCS VPMVIPGRPE YPPPPLGPIP PVLPVPPGFP 430 440 450 460 470 480 PGPQIPVPRP PVEYLYPSRE PPRVLPVNVT DYCQLVRYLC QNGRCIPTPG SCRCECNKGF 490 500 510 520 530 540 QLDLRGECID VDECEKNPCA GGECINNQGS YTCQCRAGYQ STLTRTECRD IDECLQNGRI 550 560 570 580 590 600 CNNGRCINTD GSFHCVCNAG FHVTRDGKNC EDMDECSIRN MCLNGMCINE DGSFKCICKP 610 620 630 640 650 660 GFQLASDGRY CKDINECETP GICMNGRCVN TDGSYRCECF PGLAVGLDGR VCVDTHMRST 670 680 690 700 710 720 CYGGYKRGQC IKPLFGAVTK SECCCASTEY AFGEPCQPCP AQNSAEYQAL CSSGPGMTSA 730 740 750 760 770 780 GSDINECALD PDICPNGICE NLRGTYKCIC NSGYEVDSTG KNCVDINECV LNSLLCDNGQ 790 800 810 820 830 840 CRNTPGSFVC TCPKGFIYKP DLKTCEDIDE CESSPCINGV CKNSPGSFIC ECSSESTLDP 850 860 870 880 890 900 TKTICIETIK GTCWQTVIDG RCEININGAT LKSQCCSSLG AAWGSPCTLC QVDPICGKGY 910 920 930 940 950 960 SRIKGTQCED IDECEVFPGV CKNGLCVNTR GSFKCQCPSG MTLDATGRIC LDIRLETCFL 970 980 990 1000 1010 1020 RYEDEECTLP IAGRHRMDAC CCSVGAAWGT EECEECPMRN TPEYEELCPR GPGFATKEIT 1030 1040 1050 1060 1070 1080 NGKPFFKDIN ECKMIPSLCT HGKCRNTIGS FKCRCDSGFA LDSEERNCTD IDECRISPDL 1090 1100 1110 1120 1130 1140 CGRGQCVNTP GDFECKCDEG YESGFMMMKN CMDIDECQRD PLLCRGGVCH NTEGSYRCEC 1150 1160 1170 1180 1190 1200 PPGHQLSPNI SACIDINECE LSAHLCPNGR CVNLIGKYQC ACNPGYHSTP DRLFCVDIDE 1210 1220 1230 1240 1250 1260 CSIMNGGCET FCTNSEGSYE CSCQPGFALM PDQRSCTDID ECEDNPNICD GGQCTNIPGE 1270 1280 1290 1300 1310 1320 YRCLCYDGFM ASEDMKTCVD VNECDLNPNI CLSGTCENTK GSFICHCDMG YSGKKGKTGC 1330 1340 1350 1360 1370 1380 TDINECEIGA HNCGKHAVCT NTAGSFKCSC SPGWIGDGIK CTDLDECSNG THMCSQHADC 1390 1400 1410 1420 1430 1440 KNTMGSYRCL CKEGYTGDGF TCTDLDECSE NLNLCGNGQC LNAPGGYRCE CDMGFVPSAD 1450 1460 1470 1480 1490 1500 GKACEDIDEC SLPNICVFGT CHNLPGLFRC ECEIGYELDR SGGNCTDVNE CLDPTTCISG 1510 1520 1530 1540 1550 1560 NCVNTPGSYI CDCPPDFELN PTRVGCVDTR SGNCYLDIRP RGDNGDTACS NEIGVGVSKA 1570 1580 1590 1600 1610 1620 SCCCSLGKAW GTPCEMCPAV NTSEYKILCP GGEGFRPNPI TVILEDIDEC QELPGLCQGG 1630 1640 1650 1660 1670 1680 KCINTFGSFQ CRCPTGYYLN EDTRVCDDVN ECETPGICGP GTCYNTVGNY TCICPPDYMQ 1690 1700 1710 1720 1730 1740 VNGGNNCMDM RRSLCYRNYY ADNQTCDGEL LFNMTKKMCC CSYNIGRAWN KPCEQCPIPS 1750 1760 1770 1780 1790 1800 TDEFATLCGS QRPGFVIDIY TGLPVDIDEC REIPGVCENG VCINMVGSFR CECPVGFFYN 1810 1820 1830 1840 1850 1860 DKLLVCEDID ECQNGPVCQR NAECINTAGS YRCDCKPGYR FTSTGQCNDR NECQEIPNIC 1870 1880 1890 1900 1910 1920 SHGQCIDTVG SFYCLCHTGF KTNDDQTMCL DINECERDAC GNGTCRNTIG SFNCRCNHGF 1930 1940 1950 1960 1970 1980 ILSHNNDCID VDECASGNGN LCRNGQCINT VGSFQCQCNE GYEVAPDGRT CVDINECLLE 1990 2000 2010 2020 2030 2040 PRKCAPGTCQ NLDGSYRCIC PPGYSLQNEK CEDIDECVEE PEICALGTCS NTEGSFKCLC 2050 2060 2070 2080 2090 2100 PEGFSLSSSG RRCQDLRMSY CYAKFEGGKC SSPKSRNHSK QECCCALKGE GWGDPCELCP 2110 2120 2130 2140 2150 2160 TEPDEAFRQI CPYGSGIIVG PDDSAVDMDE CKEPDVCKHG QCINTDGSYR CECPFGYILA 2170 2180 2190 2200 2210 2220 GNECVDTDEC SVGNPCGNGT CKNVIGGFEC TCEEGFEPGP MMTCEDINEC AQNPLLCAFR 2230 2240 2250 2260 2270 2280 CVNTYGSYEC KCPVGYVLRE DRRMCKDEDE CEEGKHDCTE KQMECKNLIG TYMCICGPGY 2290 2300 2310 2320 2330 2340 QRRPDGEGCV DENECQTKPG ICENGRCLNT RGSYTCECND GFTASPNQDE CLDNREGYCF 2350 2360 2370 2380 2390 2400 TEVLQNMCQI GSSNRNPVTK SECCCDGGRG WGPHCEICPF QGTVAFKKLC PHGRGFMTNG 2410 2420 2430 2440 2450 2460 ADIDECKVIH DVCRNGECVN DRGSYHCICK TGYTPDITGT SCVDLNECNQ APKPCNFICK 2470 2480 2490 2500 2510 2520 NTEGSYQCSC PKGYILQEDG RSCKDLDECA TKQHNCQFLC VNTIGGFTCK CPPGFTQHHT 2530 2540 2550 2560 2570 2580 SCIDNNECTS DINLCGSKGI CQNTPGSFTC ECQRGFSLDQ TGSSCEDVDE CEGNHRCQHG 2590 2600 2610 2620 2630 2640 CQNIIGGYRC SCPQGYLQHY QWNQCVDENE CLSAHICGGA SCHNTLGSYK CMCPAGFQYE 2650 2660 2670 2680 2690 2700 QFSGGCQDIN ECGSAQAPCS YGCSNTEGGY LCGCPPGYFR IGQGHCVSGM GMGRGNPEPP 2710 2720 2730 2740 2750 2760 VSGEMDDNSL SPEACYECKI NGYPKRGRKR RSTNETDASN IEDQSETEAN VSLASWDVEK 2770 2780 2790 2800 2810 2820 TAIFAFNISH VSNKVRILEL LPALTTLTNH NRYLIESGNE DGFFKINQKE GISYLHFTKK 2830 2840 2850 2860 2870 KPVAGTYSLQ ISSTPLYKKK ELNQLEDKYD KDYLSGELGD NLKMKIQVLL H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome." Pereira L.V., D'Alessio M., Ramirez F., Lynch J.R., Sykes B., Pangilinan T., Bonadio J. Hum. Mol. Genet. 2:961-968(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-472. Tissue: Placenta.
[2]	"Three novel mutations of the fibrillin-1 gene and ten single nucleotide polymorphisms of the fibrillin-3 gene in Marfan syndrome patients." Uyeda T., Takahashi T., Eto S., Sato T., Xu G., Kanezaki R., Toki T., Yonesaka S., Ito E. J. Hum. Genet. 49:404-407(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MFS SER-2663.
[3]	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 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-472.
[4]	"Analysis of the DNA sequence and duplication history of human chromosome 15." 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. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TYR-472.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-472.
[7]	"Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5' end." Corson G.M., Chalberg S.C., Dietz H.C., Charbonneau N.L., Sakai L.Y. Genomics 17:476-484(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55, VARIANT TYR-472. Tissue: Fibroblast and Placenta.
[8]	"Partial sequence of a candidate gene for the Marfan syndrome." Maslen C.L., Corson G.M., Maddox B.K., Glanville R.W., Sakai L.Y. Nature 352:334-337(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 899-2871.
[9]	"Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes." Lee B., Godfrey M., Vitale E., Hori H., Mattei M.-G., Sarfarazi M., Tsipouras P., Ramirez F., Hollister D.W. Nature 352:330-334(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 813-1313.
[10]	"The skipping of constitutive exons in vivo induced by nonsense mutations." Dietz H.C., Valle D., Francomano C.A., Kendzior R.J. Jr., Pyeritz R.E., Cutting G.R. Science 259:680-683(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2086-2194.
[11]	"Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils." Sakai L.Y., Keene D.R., Glanville R.W., Bachinger H.P. J. Biol. Chem. 266:14763-14770(1991) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[12]	"Molecular structure and interaction of recombinant human type XVI collagen." Kassner A., Tiedemann K., Notbohm H., Ludwig T., Morgelin M., Reinhardt D.P., Chu M.-L., Bruckner P., Grassel S. J. Mol. Biol. 339:835-853(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH COL16A1.
[13]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-448; ASN-1067; ASN-1484 AND ASN-1581, MASS SPECTROMETRY. Tissue: Liver.
[14]	"ADAMTS10 protein interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts." 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. J. Biol. Chem. 286:17156-17167(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ADAMTS10.
[15]	"ADAMTSL4, a secreted glycoprotein widely distributed in the eye, binds Fibrillin-1 microfibrils and accelerates microfibril biogenesis." Gabriel L.A., Wang L.W., Bader H., Ho J.C., Majors A.K., Hollyfield J.G., Traboulsi E.I., Apte S.S. Invest. Ophthalmol. Vis. Sci. 53:461-469(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ADAMTSL4.
[16]	"Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils." Yuan X., Downing A.K., Knott V., Handford P.A. EMBO J. 16:6659-6666(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2054-2125.
[17]	"Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1." Knott V., Downing A.K., Cardy C.M., Handford P.A. J. Mol. Biol. 255:22-27(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2124-2205.
[18]	"Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders." Downing A.K., Knott V., Werner J.M., Cardy C.M., Campbell I.D., Handford P.A. Cell 85:597-605(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2124-2205.
[19]	"Software and database for the analysis of mutations in the human FBN1 gene." Collod G., Beroud C., Soussi T., Junien C., Boileau C. Nucleic Acids Res. 24:137-141(1996) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON MFS VARIANTS.
[20]	"Marfan Database (second edition): software and database for the analysis of mutations in the human FBN1 gene." Collod-Beroud G., Beroud C., Ades L., Black C., Boxer M., Brock D.J., Godfrey M., Hayward C., Karttunen L., Milewicz D., Peltonen L., Richards R.I., Wang W., Junien C., Boileau C. Nucleic Acids Res. 25:147-150(1997) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON MFS VARIANTS.
[21]	"Fibrillin-1 mutations in Marfan syndrome and other type-1 fibrillinopathies." Hayward C., Brock D.J.H. Hum. Mutat. 10:415-423(1997) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[22]	"The molecular genetics of Marfan syndrome and related microfibrillopathies." Robinson P.N., Godfrey M. J. Med. Genet. 37:9-25(2000) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON MFS.
[23]	"Mutations of FBN1 and genotype-phenotype correlations in Marfan syndrome and related fibrillinopathies." Robinson P.N., Booms P., Katzke S., Ladewig M., Neumann L., Palz M., Pregla R., Tiecke F., Rosenberg T. Hum. Mutat. 20:153-161(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[24]	"Association of mitral valve prolapse and systemic abnormalities of connective tissue: a phenotypic continuum." Glesby M.J., Pyeritz R.E. JAMA 262:523-528(1989) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN OCTD.
[25]	"Structure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organization." Lee S.S., Knott V., Jovanovic J., Harlos K., Grimes J.M., Choulier L., Mardon H.J., Stuart D.I., Handford P.A. Structure 12:717-729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1486-1647 IN COMPLEX WITH CALCIUM IONS, FUNCTION, INTERACTION WITH INTEGRIN ALPHA-V/BETA-3, DISULFIDE BONDS.
[26]	"Structure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteins." Jensen S.A., Iqbal S., Lowe E.D., Redfield C., Handford P.A. Structure 17:759-768(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 807-951 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS.
[27]	"Marfan syndrome caused by a recurrent de novo missense mutation in the fibrillin gene." 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. Nature 352:337-339(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS PRO-1137.
[28]	"Clustering of fibrillin (FBN1) missense mutations in Marfan syndrome patients at cysteine residues in EGF-like domains." Dietz H.C., Saraiva J.M., Pyeritz R.E., Cutting G.R., Francomano C.A. Hum. Mutat. 1:366-374(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MFS SER-1249; ARG-1663; SER-2221 AND SER-2307.
[29]	"Marfan phenotype variability in a family segregating a missense mutation in the epidermal growth factor-like motif of the fibrillin gene." 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. J. Clin. Invest. 89:1674-1680(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS SER-2307.
[30]	"Four novel FBN1 mutations: significance for mutant transcript level and EGF-like domain calcium binding in the pathogenesis of Marfan syndrome." Dietz H.C., McIntosh I., Sakai L.Y., Corson G.M., Chalberg S.C., Pyeritz R.E., Francomano C.A. Genomics 17:468-475(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MFS ILE-548 AND ALA-723.
[31]	"A novel fibrillin mutation in the Marfan syndrome which could disrupt calcium binding of the epidermal growth factor-like module." Hewett D.R., Lynch J.R., Smith R., Sykes B.C. Hum. Mol. Genet. 2:475-477(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS SER-2144.
[32]	"Mutation screening of complete fibrillin-1 coding sequence: report of five new mutations, including two in 8-cysteine domains." Tynan K., Comeau K., Pearson M., Wilgenbus P., Levitt D., Gasner C., Berg M.A., Miller D.C., Francke U. Hum. Mol. Genet. 2:1813-1821(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MFS ARG-862; TYR-1117; PRO-1137 AND PHE-1589, VARIANT ALA-1148.
[33]	"A compound-heterozygous Marfan patient: two defective fibrillin alleles result in a lethal phenotype." Karttunen L., Raghunath M., Loennqvist L., Peltonen L. Am. J. Hum. Genet. 55:1083-1091(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MFS GLY-217 AND ARG-2627.
[34]	"A novel mutation of the fibrillin gene causing ectopia lentis." Lonnqvist L., Child A., Kainulainen K., Davidson R., Puhakka L., Peltonen L. Genomics 19:573-576(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ECTOL1 LYS-2447.
[35]	"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." Hayward C., Rae A.L., Porteous M.E.M., Logie L.J., Brock L.J. Hum. Mol. Genet. 3:373-375(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS CYS-627.
[36]	"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." Stahl-Hallengren C., Ukkonen T., Kainulainen K., Kristofersson U., Saxne T., Tornqvist K., Peltonen L. J. Clin. Invest. 94:709-713(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS CYS-122.
[37]	"A new missense mutation of fibrillin in a patient with Marfan syndrome." Hewett D.R., Lynch J.R., Child A., Sykes B.C. J. Med. Genet. 31:338-339(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS TYR-1223.
[38]	"A novel mutation in the fibrillin gene (FBN1) in familial arachnodactyly." Hayward C., Porteous M.E.M., Brock D.J.H. Mol. Cell. Probes 8:325-327(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS HIS-1170.
[39]	"Mutations in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome." Kainulainen K., Karttunen L., Puhakka L., Sakai L., Peltonen L. Nat. Genet. 6:64-69(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MFS GLY-217; ASN-1023; ARG-1074; TYR-1242; ARG-1513; GLU-2127; TRP-2151; LYS-2447 AND ARG-2511.
[40]	"A Gly1127Ser mutation in an EGF-like domain of the fibrillin-1 gene is a risk factor for ascending aortic aneurysm and dissection." Francke U., Berg M.A., Tynan K., Brenn T., Liu W., Aoyama T., Gasner C., Miller D.C., Furthmayr H. Am. J. Hum. Genet. 56:1287-1296(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-1127.
[41]	"Fifteen novel FBN1 mutations causing Marfan syndrome detected by heteroduplex analysis of genomic amplicons." Nijbroek G., Sood S., McIntosh I., Francomano C.A., Bull E., Pereira L., Ramirez F., Pyeritz R.E., Dietz H.C. Am. J. Hum. Genet. 57:8-21(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MFS TYR-129; PHE-166; CYS-746; ARG-926; ARG-1013; LYS-1073; SER-1382 AND ARG-1928.
[42]	"The phenotypic continuum associated with FBN1 mutations includes the Shprintzen-Goldberg syndrome." Dietz H.C., Sood I., McIntosh I. Am. J. Hum. Genet. 57:A211-A211(1995) Cited for: VARIANT SGS TYR-1223.
[43]	"A mutation in FBN1 disrupts profibrillin processing and results in isolated skeletal features of the Marfan syndrome." Milewicz D.M., Grossfield J., Cao S.-N., Kielty C., Covitz W., Jewett T. J. Clin. Invest. 95:2373-2378(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS TRP-2726.
[44]	"Delineation of the Marfan phenotype associated with mutations in exons 23-32 of the FBN1 gene." Putnam E.A., Cho M., Zinn A.B., Towbin J.A., Byers P.H., Milewicz D.M. Am. J. Med. Genet. 62:233-242(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MFS ARG-1053; GLY-1072; LYS-1073 AND GLY-1117.
[45]	"Characterisation of four novel fibrillin-1 (FBN1) mutations in Marfan syndrome." Ades L.C., Haan E.A., Colley A.F., Richards R.I. J. Med. Genet. 33:665-671(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MFS THR-705; TYR-711; GLY-1055 AND TYR-1153.
[46]	"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." Booms P., Withers A.P., Boxer M., Kaufmann U.C., Hagemeier C., Vetter U., Robinson P.N. Hum. Genet. 100:195-200(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS TYR-587.
[47]	"The pathogenicity of the Pro1148Ala substitution in the FBN1 gene: causing or predisposing to Marfan syndrome and aortic aneurysm, or clinically innocent?" Schrijver I., Liu W., Francke U. Hum. Genet. 99:607-611(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-1148.
[48]	"Mutation screening of all 65 exons of the fibrillin-1 gene in 60 patients with Marfan syndrome: report of 12 novel mutations." Hayward C., Porteous M.E.M., Brock D.J.H. Hum. Mutat. 10:280-289(1997) [PubMed] [Europe PMC] [Abstract] Cited for: 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.
[49]	"P1148A in fibrillin-1 is not a mutation leading to Shprintzen-Goldberg syndrome." Watanabe Y., Yano S., Koga Y., Yukizane S., Nishiyori A., Yoshino M., Kato H. Hum. Mutat. 10:326-327(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-1148.
[50]	"P1148A in fibrillin-1 is not a mutation anymore." Wang M., Mathews K.R., Imaizumi K., Beiraghi S., Blumberg B., Scheuner M., Graham J.M. Jr., Godfrey M. Nat. Genet. 15:12-12(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-1148.
[51]	"Multiple molecular mechanisms underlying subdiagnostic variants of Marfan syndrome." Montgomery R.A., Geraghty M.T., Bull E., Gelb B.D., Johnson M., McIntosh I., Francomano C.A., Dietz H.C. Am. J. Hum. Genet. 63:1703-1711(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS ARG-1265.
[52]	"Correlation of a recurrent FBN1 mutation (R122C) with an atypical familial Marfan syndrome phenotype." Black C., Withers A.P., Gray J.R., Bridges A.B., Craig A., Baty D.U., Boxer M. Hum. Mutat. Suppl. 1:S198-S200(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS CYS-122.
[53]	"A novel mutation in the neonatal region of the fibrillin (FBN) 1 gene associated with a classical phenotype of Marfan syndrome (MfS)." Grau U., Klein H.-G., Detter C., Mair H., Welz A., Seidel D., Reichart B. Hum. Mutat. 12:137-137(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS ILE-984.
[54]	"Demonstration of the recurrence of Marfan-like skeletal and cardiovascular manifestations due to germline mosaicism for an FBN1 mutation." Collod-Beroud G., Lackmy-Port-Lys M., Jondeau G., Mathieu M., Maingourd Y., Coulon M., Guillotel M., Junien C., Boileau C. Am. J. Hum. Genet. 65:917-921(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS GLU-985.
[55]	"Identification of 9 novel FBN1 mutations in German patients with Marfan syndrome." El-Aleem A.A., Karck M., Haverich A., Schmidtke J., Arslan-Kirchner M. Hum. Mutat. 14:181-181(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MFS PHE-504; TYR-1129; CYS-1261; SER-1833 AND TYR-2142.
[56]	"Genotype and phenotype analysis of 171 patients referred for molecular study of the fibrillin-1 gene FBN1 because of suspected Marfan syndrome." Loeys B., Nuytinck L., Delvaux I., De Bie S., De Paepe A. Arch. Intern. Med. 161:2447-2454(2001) [PubMed] [Europe PMC] [Abstract] Cited for: 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, VARIANT CYS-1530.
[57]	"TGGE screening of the entire FBN1 coding sequence in 126 individuals with Marfan syndrome and related fibrillinopathies." Katzke S., Booms P., Tiecke F., Palz M., Pletschacher A., Turkmen S., Neumann L.M., Pregla R., Leitner C., Schramm C., Lorenz P., Hagemeier C., Fuchs J., Skovby F., Rosenberg T., Robinson P.N. Hum. Mutat. 20:197-208(2002) [PubMed] [Europe PMC] [Abstract] Cited for: 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, VARIANT MET-2101.
[58]	"Sensitivity of conformation sensitive gel electrophoresis in detecting mutations in Marfan syndrome and related conditions." Koerkkoe J., Kaitila I., Loennqvist L., Peltonen L., Ala-Kokko L. J. Med. Genet. 39:34-41(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MFS CYS-114; ARG-890; GLY-1200; TYR-1835; ARG-2111; CYS-2474 AND GLY-2652, VARIANT ECTOL1 CYS-240.
[59]	"In frame fibrillin-1 gene deletion in autosomal dominant Weill-Marchesani syndrome." Faivre L., Gorlin R.J., Wirtz M.K., Godfrey M., Dagoneau N., Samples J.R., Le Merrer M., Collod-Beroud G., Boileau C., Munnich A., Cormier-Daire V. J. Med. Genet. 40:34-36(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WMS2 1692-ARG--TYR-1699 DEL.
[60]	"Detection of thirty novel FBN1 mutations in patients with Marfan syndrome or a related fibrillinopathy." Biggin A., Holman K., Brett M., Bennetts B., Ades L. Hum. Mutat. 23:99-99(2004) [PubMed] [Europe PMC] [Abstract] Cited for: 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, VARIANT CYS-1530.
[61]	"Consequences of cysteine mutations in calcium-binding epidermal growth factor modules of fibrillin-1." Vollbrandt T., Tiedemann K., El-Hallous E., Lin G., Brinckmann J., John H., Baetge B., Notbohm H., Reinhardt D.P. J. Biol. Chem. 279:32924-32931(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS MFS CYS-627; GLY-750 AND ARG-926.
[62]	"Identification of sixty-two novel and twelve known FBN1 mutations in eighty-one unrelated probands with Marfan syndrome and other fibrillinopathies." Arbustini E., Grasso M., Ansaldi S., Malattia C., Pilotto A., Porcu E., Disabella E., Marziliano N., Pisani A., Lanzarini L., Mannarino S., Larizza D., Mosconi M., Antoniazzi E., Zoia M.C., Meloni G., Magrassi L., Brega A. , Bedeschi M.F., Torrente I., Mari F., Tavazzi L. Hum. Mutat. 26:494-494(2005) [PubMed] [Europe PMC] [Abstract] Cited for: 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.
[63]	"Identification of 29 novel and nine recurrent fibrillin-1 (FBN1) mutations and genotype-phenotype correlations in 76 patients with Marfan syndrome." Rommel K., Karck M., Haverich A., von Kodolitsch Y., Rybczynski M., Muller G., Singh K.K., Schmidtke J., Arslan-Kirchner M. Hum. Mutat. 26:529-539(2005) [PubMed] [Europe PMC] [Abstract] Cited for: 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.
[64]	"Central nervous system abnormalities in two cases with neonatal Marfan syndrome with novel mutations in the fibrillin-1 gene." Barnett C.P., Wilson G.J., Chiasson D.A., Gross G.J., Hinek A., Hawkins C., Chitayat D. Am. J. Med. Genet. A 152:2409-2412(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MFS GLY-1068.
[65]	"Mutations in fibrillin-1 cause congenital scleroderma: stiff skin syndrome." Loeys B.L., Gerber E.E., Riegert-Johnson D., Iqbal S., Whiteman P., McConnell V., Chillakuri C.R., Macaya D., Coucke P.J., De Paepe A., Judge D.P., Wigley F., Davis E.C., Mardon H.J., Handford P., Keene D.R., Sakai L.Y., Dietz H.C. Sci. Transl. Med. 2:23RA20-23RA20(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SSKS SER-1564; CYS-1570; GLY-1577 AND ASP-1594.
[66]	"Mutations in the TGFbeta binding-protein-like domain 5 of FBN1 are responsible for acromicric and geleophysic dysplasias." Le Goff C., Mahaut C., Wang L.W., Allali S., Abhyankar A., Jensen S., Zylberberg L., Collod-Beroud G., Bonnet D., Alanay Y., Brady A.F., Cordier M.P., Devriendt K., Genevieve D., Kiper P.O., Kitoh H., Krakow D., Lynch S.A. , Le Merrer M., Megarbane A., Mortier G., Odent S., Polak M., Rohrbach M., Sillence D., Stolte-Dijkstra I., Superti-Furga A., Rimoin D.L., Topouchian V., Unger S., Zabel B., Bole-Feysot C., Nitschke P., Handford P., Casanova J.L., Boileau C., Apte S.S., Munnich A., Cormier-Daire V. Am. J. Hum. Genet. 89:7-14(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GPHYSD2 CYS-1696; ASP-1699; CYS-1699; TYR-1706; TRP-1719; THR-1728; VAL-1728; TYR-1733 AND SER-1762, VARIANTS ACMICD CYS-1699; CYS-1700; ARG-1714; CYS-1722; VAL-1726; THR-1728; GLN-1735 INS; ARG-1750 AND VAL-1758.
[67]	"Applying massive parallel sequencing to molecular diagnosis of Marfan and Loeys-Dietz syndromes." Baetens M., Van Laer L., De Leeneer K., Hellemans J., De Schrijver J., Van De Voorde H., Renard M., Dietz H., Lacro R.V., Menten B., Van Criekinge W., De Backer J., De Paepe A., Loeys B., Coucke P.J. Hum. Mutat. 0:0-0(2011) [PubMed] [Europe PMC] [Abstract] Cited for: 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; TYR-2406; SER-2442; ARG-2511; VAL-2606 DEL; LYS-2610 AND ARG-2646, VARIANTS GLY-1481; ARG-2318 AND HIS-2793.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L13923 mRNA. Translation: AAB02036.1.
AB177803 Genomic DNA. Translation: BAD16739.1.
GU143398 Genomic DNA. Translation: ACZ58372.1.
AC022467 Genomic DNA. No translation available.
AC084757 Genomic DNA. No translation available.
AC084758 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77354.1.
BC146854 mRNA. Translation: AAI46855.1.
L19896 Genomic DNA. No translation available.
X63556 mRNA. Translation: CAA45118.1. Different initiation.
X62008 mRNA. No translation available.
S54426, S54425 Genomic DNA. Translation: AAB25244.1.

IPI

IPI00328113.

PIR

A47221.

RefSeq

NP_000129.3. NM_000138.4.

UniGene

Hs.591133.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1APJ	NMR	-	A	2054-2125	[»]
1EMN	NMR	-	A	2124-2205	[»]
1EMO	NMR	-	A	2124-2205	[»]
1LMJ	NMR	-	A	1069-1154	[»]
1UZJ	X-ray	2.25	A/B/C	1486-1647	[»]
1UZK	X-ray	1.35	A	1486-1647	[»]
1UZP	X-ray	1.78	A	1486-1647	[»]
1UZQ	X-ray	2.40	A	1486-1647	[»]
2W86	X-ray	1.80	A	807-951	[»]

ProteinModelPortal

P35555.

SMR

P35555. Positions 807-951, 1069-1154, 1486-1647, 2054-2205.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29985N.

IntAct

P35555. 15 interactions.

MINT

MINT-206075.

STRING

9606.ENSP00000325527.

PTM databases

PhosphoSite

P35555.

Polymorphism databases

DMDM

311033452.

Proteomic databases

PaxDb

P35555.

PRIDE

P35555.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316623; ENSP00000325527; ENSG00000166147.

GeneID

2200.

KEGG

hsa:2200.

UCSC

uc001zwx.2. human.

Organism-specific databases

CTD

2200.

GeneCards

GC15M048700.

HGNC

HGNC:3603. FBN1.

HPA

CAB002670.
CAB058696.
HPA017759.
HPA021057.

MIM

102370. phenotype.
129600. phenotype.
134797. gene.
154700. phenotype.
182212. phenotype.
184900. phenotype.
604308. phenotype.
608328. phenotype.
614185. phenotype.

neXtProt

NX_P35555.

Orphanet

969. Acromicric dysplasia.
1885. Ectopia lentis syndrome.
91387. Familial thoracic aortic aneurysm and aortic dissection.
2623. Geleophysic dysplasia.
2084. Glaucoma - ectopia - microspherophakia - stiff joints - short stature.
284963. Marfan syndrome type 1.
284979. Neonatal Marfan syndrome.
300382. Progeroid and marfanoid aspect-lipodystrophy syndrome.
2462. Shprintzen-Goldberg syndrome.
2833. Stiff skin syndrome.
3449. Weill-Marchesani syndrome.

PharmGKB

PA28016.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOGENOM

HOG000231768.

HOVERGEN

HBG005643.

InParanoid

P35555.

KO

K06825.

OMA

DATGRIC.

OrthoDB

EOG45TCM7.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P35555.

Bgee

P35555.

CleanEx

HS_FBN1.

Genevestigator

P35555.

GermOnline

ENSG00000166147. Homo sapiens.

Family and domain databases

Gene3D

3.90.290.10. 10 hits.

InterPro

IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view]

PANTHER

PTHR24039:SF0. PTHR24039:SF0. 1 hit.

Pfam

PF12662. cEGF. 2 hits.
PF07645. EGF_CA. 38 hits.
PF00683. TB. 9 hits.
[Graphical view]

PIRSF

PIRSF036312. Fibrillin. 1 hit.

SMART

SM00181. EGF. 4 hits.
SM00179. EGF_CA. 42 hits.
[Graphical view]

SUPFAM

SSF57581. Fibril-assoc. 9 hits.
SSF57184. Grow_fac_recept. 1 hit.

PROSITE

PS00010. ASX_HYDROXYL. 43 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 38 hits.
PS50026. EGF_3. 44 hits.
PS01187. EGF_CA. 43 hits.
PS51364. TB. 9 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FBN1. human.

EvolutionaryTrace

P35555.

GenomeRNAi

2200.

NextBio

8891.

SOURCE

Search...

Entry information

Entry name

FBN1_HUMAN

Accession

Primary (citable) accession number: P35555
Secondary accession number(s): B2RUU0 , D2JYH6, Q15972, Q75N87

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 2, 2010
Last modified:	May 29, 2013
This is version 165 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.