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P35555 (FBN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibrillin-1
Gene names
Name:FBN1
Synonyms:FBN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2871 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular 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.68

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.
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.66

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.67

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.67

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 componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DiseaseAortic aneurysm
Craniosynostosis
Disease mutation
Dwarfism
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processextracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

heart development

Inferred from mutant phenotype PubMed 15781745. Source: UniProtKB

kidney development

Inferred from electronic annotation. Source: Ensembl

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_componentbasement membrane

Inferred from direct assay PubMed 3536967. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 3536967. Source: UniProtKB

microfibril

Inferred from direct assay Ref.11PubMed 3536967. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from direct assay PubMed 3536967. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from direct assay Ref.7. Source: UniProtKB

extracellular matrix structural constituent

Inferred from direct assay PubMed 3536967. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 28712844Fibrillin-1
PRO_0000007581

Regions

Domain81 – 11232EGF-like 1
Domain115 – 14632EGF-like 2
Domain147 – 17832EGF-like 3
Domain184 – 23653TB 1
Domain246 – 28742EGF-like 4; calcium-binding
Domain288 – 32942EGF-like 5; calcium-binding
Domain334 – 38956TB 2
Domain449 – 48941EGF-like 6
Domain490 – 52940EGF-like 7; calcium-binding
Domain530 – 57142EGF-like 8; calcium-binding
Domain572 – 61241EGF-like 9; calcium-binding
Domain613 – 65341EGF-like 10; calcium-binding
Domain659 – 71153TB 3
Domain723 – 76442EGF-like 11; calcium-binding
Domain765 – 80642EGF-like 12; calcium-binding
Domain807 – 84640EGF-like 13; calcium-binding
Domain851 – 90252TB 4
Domain910 – 95142EGF-like 14; calcium-binding
Domain956 – 100853TB 5
Domain1028 – 106942EGF-like 15; calcium-binding
Domain1070 – 111243EGF-like 16; calcium-binding
Domain1113 – 115442EGF-like 17; calcium-binding
Domain1155 – 119642EGF-like 18; calcium-binding
Domain1197 – 123741EGF-like 19; calcium-binding
Domain1238 – 127942EGF-like 20; calcium-binding
Domain1280 – 132142EGF-like 21; calcium-binding
Domain1322 – 136241EGF-like 22; calcium-binding
Domain1363 – 140341EGF-like 23; calcium-binding
Domain1404 – 144542EGF-like 24; calcium-binding
Domain1446 – 148641EGF-like 25; calcium-binding
Domain1487 – 152741EGF-like 26; calcium-binding
Domain1532 – 158958TB 6
Domain1606 – 164742EGF-like 27; calcium-binding
Domain1648 – 168841EGF-like 28; calcium-binding
Domain1693 – 174856TB 7
Domain1766 – 180742EGF-like 29; calcium-binding
Domain1808 – 184841EGF-like 30; calcium-binding
Domain1849 – 189042EGF-like 31; calcium-binding
Domain1891 – 192939EGF-like 32; calcium-binding
Domain1930 – 197243EGF-like 33; calcium-binding
Domain1973 – 201240EGF-like 34; calcium-binding
Domain2013 – 205442EGF-like 35; calcium-binding
Domain2059 – 211153TB 8
Domain2127 – 216539EGF-like 36; calcium-binding
Domain2166 – 220540EGF-like 37; calcium-binding
Domain2206 – 224641EGF-like 38; calcium-binding
Domain2247 – 229044EGF-like 39; calcium-binding
Domain2291 – 233242EGF-like 40; calcium-binding
Domain2337 – 239054TB 9
Domain2402 – 244342EGF-like 41; calcium-binding
Domain2444 – 248441EGF-like 42; calcium-binding
Domain2485 – 252339EGF-like 43; calcium-binding
Domain2524 – 256643EGF-like 44; calcium-binding
Domain2567 – 260640EGF-like 45; calcium-binding
Domain2607 – 264741EGF-like 46; calcium-binding
Domain2648 – 268740EGF-like 47; calcium-binding
Compositional bias402 – 44645Pro-rich

Amino acid modifications

Glycosylation4481N-linked (GlcNAc...) Ref.13
Glycosylation10671N-linked (GlcNAc...) Ref.13
Glycosylation11491N-linked (GlcNAc...) Potential
Glycosylation13691N-linked (GlcNAc...) Potential
Glycosylation14841N-linked (GlcNAc...) Ref.13
Glycosylation15811N-linked (GlcNAc...) Ref.13
Glycosylation16691N-linked (GlcNAc...) Potential
Glycosylation17031N-linked (GlcNAc...) Potential
Glycosylation17131N-linked (GlcNAc...) Potential
Glycosylation19021N-linked (GlcNAc...) Potential
Glycosylation20771N-linked (GlcNAc...) Potential
Glycosylation21781N-linked (GlcNAc...) Potential
Glycosylation27341N-linked (GlcNAc...) Potential
Glycosylation27501N-linked (GlcNAc...) Potential
Glycosylation27671N-linked (GlcNAc...) Potential
Disulfide bond85 ↔ 94 By similarity
Disulfide bond89 ↔ 100 By similarity
Disulfide bond102 ↔ 111 By similarity
Disulfide bond119 ↔ 129 By similarity
Disulfide bond123 ↔ 134 By similarity
Disulfide bond136 ↔ 145 By similarity
Disulfide bond150 ↔ 160 By similarity
Disulfide bond154 ↔ 166 By similarity
Disulfide bond168 ↔ 177 By similarity
Disulfide bond250 ↔ 262 By similarity
Disulfide bond257 ↔ 271 By similarity
Disulfide bond273 ↔ 286 By similarity
Disulfide bond292 ↔ 304 By similarity
Disulfide bond299 ↔ 313 By similarity
Disulfide bond315 ↔ 328 By similarity
Disulfide bond453 ↔ 465 By similarity
Disulfide bond460 ↔ 474 By similarity
Disulfide bond476 ↔ 488 By similarity
Disulfide bond494 ↔ 504 By similarity
Disulfide bond499 ↔ 513 By similarity
Disulfide bond515 ↔ 528 By similarity
Disulfide bond534 ↔ 546 By similarity
Disulfide bond541 ↔ 555 By similarity
Disulfide bond557 ↔ 570 By similarity
Disulfide bond576 ↔ 587 By similarity
Disulfide bond582 ↔ 596 By similarity
Disulfide bond598 ↔ 611 By similarity
Disulfide bond617 ↔ 628 By similarity
Disulfide bond623 ↔ 637 By similarity
Disulfide bond639 ↔ 652 By similarity
Disulfide bond727 ↔ 739 By similarity
Disulfide bond734 ↔ 748 By similarity
Disulfide bond750 ↔ 763 By similarity
Disulfide bond769 ↔ 781 By similarity
Disulfide bond776 ↔ 790 By similarity
Disulfide bond792 ↔ 805 By similarity
Disulfide bond811 ↔ 821 Ref.25 Ref.26
Disulfide bond816 ↔ 830 Ref.25 Ref.26
Disulfide bond832 ↔ 845 Ref.25 Ref.26
Disulfide bond853 ↔ 875 Ref.25 Ref.26
Disulfide bond862 ↔ 887 Ref.25 Ref.26
Disulfide bond876 ↔ 890 Ref.25 Ref.26
Disulfide bond896 ↔ 908 Ref.25 Ref.26
Disulfide bond914 ↔ 926 Ref.25 Ref.26
Disulfide bond921 ↔ 935 Ref.25 Ref.26
Disulfide bond937 ↔ 950 Ref.25 Ref.26
Disulfide bond1032 ↔ 1044 By similarity
Disulfide bond1039 ↔ 1053 By similarity
Disulfide bond1055 ↔ 1068 By similarity
Disulfide bond1074 ↔ 1086 By similarity
Disulfide bond1081 ↔ 1095 By similarity
Disulfide bond1097 ↔ 1111 By similarity
Disulfide bond1117 ↔ 1129 By similarity
Disulfide bond1124 ↔ 1138 By similarity
Disulfide bond1140 ↔ 1153 By similarity
Disulfide bond1159 ↔ 1171 By similarity
Disulfide bond1166 ↔ 1180 By similarity
Disulfide bond1182 ↔ 1195 By similarity
Disulfide bond1201 ↔ 1212 By similarity
Disulfide bond1208 ↔ 1221 By similarity
Disulfide bond1223 ↔ 1236 By similarity
Disulfide bond1242 ↔ 1254 By similarity
Disulfide bond1249 ↔ 1263 By similarity
Disulfide bond1265 ↔ 1278 By similarity
Disulfide bond1284 ↔ 1296 By similarity
Disulfide bond1291 ↔ 1305 By similarity
Disulfide bond1307 ↔ 1320 By similarity
Disulfide bond1326 ↔ 1339 By similarity
Disulfide bond1333 ↔ 1348 By similarity
Disulfide bond1350 ↔ 1361 By similarity
Disulfide bond1367 ↔ 1380 By similarity
Disulfide bond1374 ↔ 1389 By similarity
Disulfide bond1391 ↔ 1402 By similarity
Disulfide bond1408 ↔ 1420 By similarity
Disulfide bond1415 ↔ 1429 By similarity
Disulfide bond1431 ↔ 1444 By similarity
Disulfide bond1450 ↔ 1461 By similarity
Disulfide bond1456 ↔ 1470 By similarity
Disulfide bond1472 ↔ 1485 By similarity
Disulfide bond1491 ↔ 1502 Ref.25 Ref.26
Disulfide bond1497 ↔ 1511 Ref.25 Ref.26
Disulfide bond1513 ↔ 1526 Ref.25 Ref.26
Disulfide bond1534 ↔ 1562 Ref.25 Ref.26
Disulfide bond1549 ↔ 1574 Ref.25 Ref.26
Disulfide bond1563 ↔ 1577 Ref.25 Ref.26
Disulfide bond1564 ↔ 1589 Ref.25 Ref.26
Disulfide bond1610 ↔ 1622 Ref.25 Ref.26
Disulfide bond1617 ↔ 1631 Ref.25 Ref.26
Disulfide bond1633 ↔ 1646 Ref.25 Ref.26
Disulfide bond1652 ↔ 1663 By similarity
Disulfide bond1658 ↔ 1672 By similarity
Disulfide bond1674 ↔ 1687 By similarity
Disulfide bond1770 ↔ 1782 By similarity
Disulfide bond1777 ↔ 1791 By similarity
Disulfide bond1793 ↔ 1806 By similarity
Disulfide bond1812 ↔ 1824 By similarity
Disulfide bond1818 ↔ 1833 By similarity
Disulfide bond1835 ↔ 1847 By similarity
Disulfide bond1853 ↔ 1865 By similarity
Disulfide bond1860 ↔ 1874 By similarity
Disulfide bond1876 ↔ 1889 By similarity
Disulfide bond1895 ↔ 1905 By similarity
Disulfide bond1900 ↔ 1914 By similarity
Disulfide bond1916 ↔ 1928 By similarity
Disulfide bond1934 ↔ 1947 By similarity
Disulfide bond1942 ↔ 1956 By similarity
Disulfide bond1958 ↔ 1971 By similarity
Disulfide bond1977 ↔ 1989 By similarity
Disulfide bond1984 ↔ 1998 By similarity
Disulfide bond2000 ↔ 2011 By similarity
Disulfide bond2017 ↔ 2029 By similarity
Disulfide bond2024 ↔ 2038 By similarity
Disulfide bond2040 ↔ 2053 By similarity
Disulfide bond2061 ↔ 2083 Ref.25 Ref.26
Disulfide bond2070 ↔ 2096 Ref.25 Ref.26
Disulfide bond2084 ↔ 2099 Ref.25 Ref.26
Disulfide bond2085 ↔ 2111 Ref.25 Ref.26
Disulfide bond2131 ↔ 2142 By similarity
Disulfide bond2137 ↔ 2151 By similarity
Disulfide bond2153 ↔ 2164 By similarity
Disulfide bond2170 ↔ 2181 By similarity
Disulfide bond2176 ↔ 2190 By similarity
Disulfide bond2192 ↔ 2204 By similarity
Disulfide bond2210 ↔ 2221 By similarity
Disulfide bond2217 ↔ 2230 By similarity
Disulfide bond2232 ↔ 2245 By similarity
Disulfide bond2251 ↔ 2265 By similarity
Disulfide bond2258 ↔ 2274 By similarity
Disulfide bond2276 ↔ 2289 By similarity
Disulfide bond2295 ↔ 2307 By similarity
Disulfide bond2302 ↔ 2316 By similarity
Disulfide bond2318 ↔ 2331 By similarity
Disulfide bond2406 ↔ 2418 By similarity
Disulfide bond2413 ↔ 2427 By similarity
Disulfide bond2429 ↔ 2442 By similarity
Disulfide bond2448 ↔ 2459 By similarity
Disulfide bond2455 ↔ 2468 By similarity
Disulfide bond2470 ↔ 2483 By similarity
Disulfide bond2489 ↔ 2500 By similarity
Disulfide bond2496 ↔ 2509 By similarity
Disulfide bond2511 ↔ 2522 By similarity
Disulfide bond2528 ↔ 2541 By similarity
Disulfide bond2535 ↔ 2550 By similarity
Disulfide bond2552 ↔ 2565 By similarity
Disulfide bond2571 ↔ 2581 By similarity
Disulfide bond2577 ↔ 2590 By similarity
Disulfide bond2592 ↔ 2605 By similarity
Disulfide bond2611 ↔ 2622 By similarity
Disulfide bond2617 ↔ 2631 By similarity
Disulfide bond2633 ↔ 2646 By similarity
Disulfide bond2652 ↔ 2663 By similarity
Disulfide bond2659 ↔ 2672 By similarity
Disulfide bond2674 ↔ 2686 By similarity

Natural variations

Natural variant201Y → C in MFS. Ref.62
VAR_023859
Natural variant271A → T.
Corresponds to variant rs25397 [ dbSNP | Ensembl ].
VAR_014663
Natural variant621R → C in MFS; also in a patient with ectopia lentis and retinal detachment. Ref.57
Corresponds to variant rs25403 [ dbSNP | Ensembl ].
VAR_017967
Natural variant801C → G in MFS. Ref.68
VAR_065981
Natural variant891C → F in MFS. Ref.56
Corresponds to variant rs112660651 [ dbSNP | Ensembl ].
VAR_017968
Natural variant1111C → R in MFS. Ref.48
VAR_002276
Natural variant1141R → C in MFS. Ref.58
VAR_017969
Natural variant1151S → C in ECTOL1. Ref.57
VAR_017970
Natural variant1221R → C in MFS. Ref.36 Ref.52 Ref.56
Corresponds to variant rs137854467 [ dbSNP | Ensembl ].
VAR_002277
Natural variant1231C → Y in MFS. Ref.62
VAR_023860
Natural variant1291C → Y in MFS; severe neonatal. Ref.41
VAR_002278
Natural variant1331H → Q.
Corresponds to variant rs363850 [ dbSNP | Ensembl ].
VAR_055723
Natural variant1541C → S in MFS. Ref.60
VAR_017971
Natural variant1661C → F in MFS. Ref.41
VAR_002279
Natural variant1661C → S in MFS. Ref.60
VAR_002280
Natural variant1771C → R in MFS. Ref.62
Corresponds to variant rs363853 [ dbSNP | Ensembl ].
VAR_023861
Natural variant2171W → G in MFS. Ref.33 Ref.39
VAR_002281
Natural variant2241C → R in MFS. Ref.62
VAR_023862
Natural variant2401R → C in MFS and ECTOL1. Ref.56 Ref.58 Ref.60
Corresponds to variant rs137854480 [ dbSNP | Ensembl ].
VAR_017972
Natural variant3291I → T.
Corresponds to variant rs12324002 [ dbSNP | Ensembl ].
VAR_055724
Natural variant3631G → S.
Corresponds to variant rs363855 [ dbSNP | Ensembl ].
VAR_055725
Natural variant3661W → C in MFS. Ref.56
VAR_017973
Natural variant4391R → G in MFS. Ref.62
VAR_023863
Natural variant4721C → Y. Ref.1 Ref.3 Ref.5 Ref.6 Ref.7
Corresponds to variant rs4775765 [ dbSNP | Ensembl ].
VAR_058090
Natural variant4761C → G in MFS.
VAR_002282
Natural variant4901D → Y in MFS. Ref.68
VAR_002283
Natural variant4991C → Y in MFS. Ref.68
VAR_065982
Natural variant5041C → F in MFS. Ref.55
VAR_010776
Natural variant5071Missing in MFS. Ref.63
VAR_023864
Natural variant5411C → Y in MFS. Ref.63
VAR_023865
Natural variant5451R → C in MFS. Ref.48 Ref.56
VAR_002284
Natural variant5481N → I in MFS. Ref.30
Corresponds to variant rs137854462 [ dbSNP | Ensembl ].
VAR_002285
Natural variant5601G → S in MFS. Ref.56
VAR_017974
Natural variant5701C → Y in MFS. Ref.56
VAR_017975
Natural variant5871C → Y in MFS. Ref.46 Ref.57
VAR_002286
Natural variant5921G → D in MFS. Ref.56
VAR_017976
Natural variant5961C → Y in MFS. Ref.57
VAR_017977
Natural variant5981C → W in MFS. Ref.56
VAR_017978
Natural variant6111C → R in MFS. Ref.68
VAR_065983
Natural variant6171C → G in MFS. Ref.68
VAR_065984
Natural variant6271R → C in MFS; enhances proteolytic degradation. Ref.35 Ref.48 Ref.61 Ref.63
VAR_002287
Natural variant6281C → K in MFS; requires 2 nucleotide substitutions.
VAR_023866
Natural variant629 – 6335Missing in MFS.
VAR_023867
Natural variant6351Y → C in MFS. Ref.62
VAR_023868
Natural variant6361R → I in MFS. Ref.62
VAR_023869
Natural variant6521C → S in MFS. Ref.60
VAR_017979
Natural variant6541D → N in MFS. Ref.57
VAR_017980
Natural variant6611C → R in MFS.
VAR_002288
Natural variant6611C → Y in ECTOL1; patient presenting also mitral valve prolapse. Ref.57
VAR_017981
Natural variant6811S → Y in MFS. Ref.57
VAR_017982
Natural variant6831C → R in MFS. Ref.57
VAR_017983
Natural variant6851C → W in MFS. Ref.57 Ref.68
Corresponds to variant rs140603 [ dbSNP | Ensembl ].
VAR_017984
Natural variant6851C → Y in MFS. Ref.68
VAR_065985
Natural variant7051A → T in MFS. Ref.45 Ref.60
VAR_002289
Natural variant7111C → Y in MFS. Ref.45 Ref.60
VAR_002290
Natural variant7231D → A in MFS. Ref.30
Corresponds to variant rs137854463 [ dbSNP | Ensembl ].
VAR_002291
Natural variant7231D → V in MFS. Ref.57
VAR_017985
Natural variant7341C → F in MFS. Ref.57
VAR_017986
Natural variant7461Y → C in MFS. Ref.41
VAR_002292
Natural variant7481C → Y in MFS. Ref.57
VAR_017987
Natural variant7501C → G in MFS; enhances proteolytic degradation. Ref.48 Ref.61
VAR_002293
Natural variant7761C → G in MFS. Ref.57
VAR_017988
Natural variant7761C → Y in MFS. Ref.56
VAR_017989
Natural variant7811C → R in MFS. Ref.56 Ref.57
VAR_017990
Natural variant7811C → Y in MFS. Ref.63
VAR_023870
Natural variant7901C → Y in MFS. Ref.68
VAR_065986
Natural variant8111C → Y in MFS. Ref.68
VAR_065987
Natural variant8161C → S in MFS. Ref.60
VAR_017991
Natural variant8321C → Y in MFS. Ref.62
VAR_023871
Natural variant8531C → S in MFS. Ref.68
VAR_065988
Natural variant8621C → R in MFS. Ref.32
VAR_002294
Natural variant8901C → G in MFS. Ref.62
VAR_023872
Natural variant8901C → R in MFS. Ref.58
VAR_017992
Natural variant9081C → R in MFS. Ref.57
VAR_017993
Natural variant9131E → G in MFS. Ref.56
VAR_017994
Natural variant9211C → G in MFS. Ref.57
VAR_017995
Natural variant9261C → R in MFS; enhances proteolytic degradation. Ref.41 Ref.61
VAR_002295
Natural variant9261C → Y in MFS. Ref.68
VAR_065989
Natural variant9841V → I in MFS. Ref.53
VAR_002296
Natural variant9851G → E in MFS; atypical. Ref.54
Corresponds to variant rs137854477 [ dbSNP | Ensembl ].
VAR_018319
Natural variant9851G → R in MFS. Ref.56 Ref.63
VAR_017996
Natural variant9961C → R in MFS.
Corresponds to variant rs140592 [ dbSNP | Ensembl ].
VAR_002297
Natural variant10131G → R in MFS; severe neonatal. Ref.41 Ref.56 Ref.60 Ref.63
Corresponds to variant rs140593 [ dbSNP | Ensembl ].
VAR_002298
Natural variant10231K → N in MFS; severe neonatal. Ref.39
VAR_002299
Natural variant10431K → R in MFS.
Corresponds to variant rs137854472 [ dbSNP | Ensembl ].
VAR_002300
Natural variant10441C → Y in MFS. Ref.60
VAR_017997
Natural variant10481I → T in MFS.
VAR_002301
Natural variant10481I → V.
Corresponds to variant rs2229324 [ dbSNP | Ensembl ].
VAR_055726
Natural variant10481Missing in MFS.
VAR_002302
Natural variant10531C → R in MFS. Ref.44
VAR_002303
Natural variant10551C → G in MFS; neonatal. Ref.45 Ref.60
VAR_002304
Natural variant10551C → W in MFS. Ref.56
VAR_017998
Natural variant10551C → Y in MFS. Ref.56
VAR_017999
Natural variant10581G → D in MFS. Ref.62
VAR_023873
Natural variant10581G → GC in MFS.
VAR_002305
Natural variant10681C → G in MFS; neonatal form. Ref.64
VAR_064503
Natural variant10721D → G in MFS. Ref.44
VAR_002306
Natural variant10731E → K in MFS; severe neonatal. Ref.41 Ref.44
Corresponds to variant rs137854478 [ dbSNP | Ensembl ].
VAR_002307
Natural variant10741C → R in MFS; severe neonatal. Ref.39 Ref.48
Corresponds to variant rs137854465 [ dbSNP | Ensembl ].
VAR_002308
Natural variant10861C → W in MFS.
VAR_002309
Natural variant10901P → S in MFS. Ref.68
VAR_065990
Natural variant11011Y → C in MFS. Ref.56 Ref.60
VAR_018000
Natural variant11131D → G.
Corresponds to variant rs140597 [ dbSNP | Ensembl ].
VAR_055727
Natural variant11131D → V in MFS. Ref.63
VAR_023874
Natural variant11171C → G in MFS. Ref.44
VAR_002310
Natural variant11171C → Y in MFS. Ref.32 Ref.60
Corresponds to variant rs137854470 [ dbSNP | Ensembl ].
VAR_002311
Natural variant11271G → 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 variant11281V → I in a patient with mitral valve prolapse. Ref.56
VAR_018001
Natural variant11291C → Y in MFS. Ref.55
Corresponds to variant rs137854482 [ dbSNP | Ensembl ].
VAR_010777
Natural variant11311N → Y in MFS.
Corresponds to variant rs137854473 [ dbSNP | Ensembl ].
VAR_002313
Natural variant11371R → P in MFS. Ref.27 Ref.32
Corresponds to variant rs137854456 [ dbSNP | Ensembl ].
VAR_002314
Natural variant11481P → A. Ref.32 Ref.47 Ref.49 Ref.50 Ref.65
Corresponds to variant rs140598 [ dbSNP | Ensembl ].
VAR_002315
Natural variant11531C → S in MFS. Ref.62
VAR_023875
Natural variant11531C → Y in MFS; severe. Ref.45 Ref.60
Corresponds to variant rs140599 [ dbSNP | Ensembl ].
VAR_002316
Natural variant11551D → N in MFS. Ref.60
VAR_002317
Natural variant11701R → H in MFS; mild. Ref.38 Ref.48
Corresponds to variant rs137854475 [ dbSNP | Ensembl ].
VAR_002318
Natural variant11711C → W in MFS. Ref.48
VAR_002319
Natural variant11731N → K in MFS. Ref.48
VAR_002320
Natural variant11851G → D in MFS. Ref.68
VAR_065991
Natural variant12001E → G in MFS. Ref.58
VAR_018002
Natural variant12111Missing in MFS. Ref.62
VAR_023876
Natural variant12191Y → C in MFS. Ref.62
VAR_023877
Natural variant12231C → Y in MFS and SGS. Ref.37 Ref.42
Corresponds to variant rs137854469 [ dbSNP | Ensembl ].
VAR_002321
Natural variant12421C → Y in MFS. Ref.39
Corresponds to variant rs137854471 [ dbSNP | Ensembl ].
VAR_002322
Natural variant12491C → S in MFS. Ref.28
Corresponds to variant rs137854458 [ dbSNP | Ensembl ].
VAR_002323
Natural variant12611Y → C in MFS. Ref.55
VAR_010778
Natural variant12611Y → D in MFS. Ref.62
VAR_023878
Natural variant12651C → R in MFS. Ref.51
Corresponds to variant rs137854474 [ dbSNP | Ensembl ].
VAR_018320
Natural variant12781C → S in MFS. Ref.62
VAR_023879
Natural variant12821N → S.
Corresponds to variant rs140647 [ dbSNP | Ensembl ].
VAR_055728
Natural variant12841C → G in MFS. Ref.63
VAR_023880
Natural variant12841C → Y in MFS. Ref.68
VAR_065992
Natural variant13251E → Q in MFS. Ref.60
VAR_018003
Natural variant13331C → S in MFS. Ref.62
VAR_023881
Natural variant13371A → P in MFS; neonatal. Ref.56
VAR_018004
Natural variant13391C → Y in MFS. Ref.56
VAR_018005
Natural variant13501C → F in MFS. Ref.68
VAR_065993
Natural variant13661E → K in MFS. Ref.60
VAR_018006
Natural variant13741C → S in MFS. Ref.60
VAR_018007
Natural variant13821N → S in MFS. Ref.41
VAR_002324
Natural variant13891C → R in MFS. Ref.60
VAR_018008
Natural variant1394 – 13963Missing in MFS.
VAR_018009
Natural variant14011T → A in MFS. Ref.68
VAR_065994
Natural variant14021C → R in MFS. Ref.62
VAR_023882
Natural variant14041D → Y in MFS. Ref.48
VAR_002325
Natural variant14241P → A in MFS. Ref.60
VAR_018010
Natural variant14241P → S in MFS. Ref.62
VAR_023883
Natural variant14291C → S in MFS. Ref.56
VAR_018011
Natural variant14311C → W in MFS. Ref.68
Corresponds to variant rs112375043 [ dbSNP | Ensembl ].
VAR_065995
Natural variant14311C → Y in MFS. Ref.68
VAR_065996
Natural variant14751G → E in MFS. Ref.63
VAR_023884
Natural variant14751G → S in MFS. Ref.63
VAR_023885
Natural variant14811S → G. Ref.68
Corresponds to variant rs61730054 [ dbSNP | Ensembl ].
VAR_065997
Natural variant14871D → A in MFS. Ref.68
VAR_065998
Natural variant14891N → K in MFS. Ref.68
VAR_065999
Natural variant15131C → R in MFS. Ref.39
VAR_002326
Natural variant15301R → C Found in patients with ectopia lensis. Ref.56 Ref.60
Corresponds to variant rs111401431 [ dbSNP | Ensembl ].
VAR_018012
Natural variant15641C → F in MFS. Ref.62
VAR_023886
Natural variant15641C → S in SSKS. Ref.66
VAR_064046
Natural variant15641C → Y in MFS. Ref.60
VAR_018013
Natural variant15701W → C in SSKS. Ref.66
VAR_064047
Natural variant15761M → T in MFS. Ref.63
VAR_023887
Natural variant15771C → G in SSKS. Ref.66
VAR_064048
Natural variant15891C → F in MFS. Ref.32
VAR_002327
Natural variant15941G → D in SSKS. Ref.66
VAR_064049
Natural variant16101C → G in MFS. Ref.48
VAR_002328
Natural variant16311C → G in MFS. Ref.62
VAR_023888
Natural variant16631C → R in MFS. Ref.28
Corresponds to variant rs137854459 [ dbSNP | Ensembl ].
VAR_002329
Natural variant16631C → Y in MFS. Ref.62
VAR_023889
Natural variant16721C → F.
Corresponds to variant rs140627 [ dbSNP | Ensembl ].
VAR_055729
Natural variant1692 – 16998Missing in WMS2.
VAR_018014
Natural variant16961Y → C in GPHYSD2. Ref.67
VAR_066527
Natural variant16991Y → C in GPHYSD2 and ACMICD. Ref.67
VAR_066528
Natural variant16991Y → D in GPHYSD2. Ref.67
VAR_066529
Natural variant17001Y → C in ACMICD. Ref.67
VAR_066530
Natural variant17061C → Y in GPHYSD2. Ref.67
VAR_066531
Natural variant17141M → R in ACMICD. Ref.67
VAR_066532
Natural variant17191C → W in GPHYSD2. Ref.67
VAR_066533
Natural variant17221S → C in ACMICD. Ref.67
VAR_066534
Natural variant17261G → V in ACMICD. Ref.67
VAR_066535
Natural variant17281A → T in GPHYSD2 and ACMICD. Ref.67
VAR_066536
Natural variant17281A → V in GPHYSD2. Ref.67
VAR_066537
Natural variant17331C → Y in GPHYSD2. Ref.67
VAR_066538
Natural variant17351Q → QQ in ACMICD. Ref.67
VAR_066539
Natural variant17501S → R in ACMICD. Ref.67
VAR_066540
Natural variant17581D → V in ACMICD. Ref.67
VAR_066541
Natural variant17621G → S in GPHYSD2. Ref.67
VAR_066542
Natural variant17701C → F in MFS. Ref.60
VAR_018015
Natural variant17901R → P in MFS. Ref.56 Ref.57
VAR_018016
Natural variant17911C → R in MFS. Ref.63
VAR_023890
Natural variant17911C → Y in MFS. Ref.56
VAR_018017
Natural variant17931C → W in MFS. Ref.60
VAR_018018
Natural variant17961G → E in MFS. Ref.60
VAR_018019
Natural variant18061C → S in MFS. Ref.57
VAR_018020
Natural variant18061C → Y in MFS.
VAR_023891
Natural variant18331C → S in MFS. Ref.55
VAR_010779
Natural variant18351C → Y in MFS. Ref.56 Ref.58
Corresponds to variant rs111929350 [ dbSNP | Ensembl ].
VAR_018021
Natural variant18371P → S in MFS.
VAR_002330
Natural variant18381G → C in MFS. Ref.68
VAR_066000
Natural variant18761C → Y in MFS. Ref.62
Corresponds to variant rs112728248 [ dbSNP | Ensembl ].
VAR_023892
Natural variant18871T → I in MFS. Ref.62
VAR_023893
Natural variant18931N → K in MFS. Ref.48
VAR_002331
Natural variant18951C → R in MFS. Ref.62
VAR_023894
Natural variant19001C → Y in MFS. Ref.62 Ref.68
VAR_023895
Natural variant19091I → T in MFS. Ref.56 Ref.68
VAR_018022
Natural variant19151R → S in MFS. Ref.56
VAR_018023
Natural variant19281C → G in MFS. Ref.63
VAR_023896
Natural variant19281C → R in MFS. Ref.41
VAR_002332
Natural variant19281C → Y in MFS. Ref.63
VAR_023897
Natural variant19311Missing in MFS. Ref.57
VAR_018024
Natural variant19341C → S in MFS. Ref.68
VAR_066001
Natural variant19711C → Y in MFS. Ref.56
VAR_018025
Natural variant19761E → G in MFS. Ref.68
VAR_066002
Natural variant19771C → Y in MFS. Ref.56
VAR_018026
Natural variant19841C → R in MFS. Ref.68
VAR_066003
Natural variant19981C → Y in MFS. Ref.57
VAR_018027
Natural variant20181V → I.
Corresponds to variant rs363802 [ dbSNP | Ensembl ].
VAR_055730
Natural variant20381C → Y in MFS. Ref.63
Corresponds to variant rs363804 [ dbSNP | Ensembl ].
VAR_023898
Natural variant20531C → F.
Corresponds to variant rs363805 [ dbSNP | Ensembl ].
VAR_055731
Natural variant20851C → R in MFS. Ref.63
VAR_023899
Natural variant20991C → W in MFS. Ref.48
VAR_002333
Natural variant21011T → M. Ref.57
Corresponds to variant rs200816828 [ dbSNP | Ensembl ].
VAR_018028
Natural variant21111C → R in MFS. Ref.58
Corresponds to variant rs363815 [ dbSNP | Ensembl ].
VAR_018029
Natural variant21111C → Y in MFS. Ref.48
VAR_002334
Natural variant21131Y → F.
Corresponds to variant rs363816 [ dbSNP | Ensembl ].
VAR_055732
Natural variant21271D → E in MFS. Ref.39
VAR_002335
Natural variant21421C → Y in MFS. Ref.55
VAR_010780
Natural variant21441N → S in MFS. Ref.31 Ref.63
Corresponds to variant rs137854461 [ dbSNP | Ensembl ].
VAR_002336
Natural variant21511C → W in MFS. Ref.39
VAR_002337
Natural variant21541P → R in ECTOL1. Ref.56
VAR_018030
Natural variant21601A → P in MFS. Ref.62
VAR_023900
Natural variant21661D → N in MFS. Ref.68
VAR_066004
Natural variant21701C → F.
Corresponds to variant rs363821 [ dbSNP | Ensembl ].
VAR_055733
Natural variant21851I → T in MFS. Ref.68
VAR_066005
Natural variant22211C → F in MFS. Ref.62
VAR_023901
Natural variant22211C → G in MFS. Ref.57
VAR_018031
Natural variant22211C → S in MFS. Ref.28
Corresponds to variant rs137854460 [ dbSNP | Ensembl ].
VAR_002338
Natural variant22231N → H in MFS. Ref.56
VAR_018032
Natural variant22471D → G in MFS. Ref.68
VAR_066006
Natural variant22511C → R in MFS.
Corresponds to variant rs112836174 [ dbSNP | Ensembl ].
VAR_023902
Natural variant22581C → R in MFS. Ref.48
VAR_002339
Natural variant22691I → T in MFS. Ref.57
VAR_018033
Natural variant22781P → S.
Corresponds to variant rs363835 [ dbSNP | Ensembl ].
VAR_055734
Natural variant22821R → W in MFS. Ref.48 Ref.56
VAR_002340
Natural variant23071C → S in MFS. Ref.28 Ref.29
Corresponds to variant rs137854457 [ dbSNP | Ensembl ].
VAR_002341
Natural variant23181C → R in MFS. Ref.68
Corresponds to variant rs111588631 [ dbSNP | Ensembl ].
VAR_066007
Natural variant23291D → E.
Corresponds to variant rs363831 [ dbSNP | Ensembl ].
VAR_055735
Natural variant23351R → W in MFS. Ref.57
VAR_018034
Natural variant23391C → Y in ECTOL1; patient presenting also flat corneas. Ref.57
VAR_018035
Natural variant23851A → T in MFS. Ref.62
VAR_023903
Natural variant24061C → Y in MFS. Ref.56 Ref.68
VAR_018036
Natural variant24421C → S in MFS. Ref.68
VAR_066008
Natural variant24421C → W in MFS. Ref.60
VAR_018037
Natural variant24471E → K in ECTOL1. Ref.34 Ref.39
Corresponds to variant rs137854464 [ dbSNP | Ensembl ].
VAR_002342
Natural variant24741Y → C in MFS. Ref.58
VAR_018038
Natural variant24891C → R in MFS. Ref.48
VAR_002343
Natural variant25001C → R in MFS. Ref.62
VAR_023904
Natural variant25001C → Y in MFS. Ref.62
VAR_023905
Natural variant25111C → R in MFS. Ref.39 Ref.68
VAR_002344
Natural variant25351C → W in MFS. Ref.62
Corresponds to variant rs113544411 [ dbSNP | Ensembl ].
VAR_023906
Natural variant25361G → R in MFS. Ref.63
VAR_023907
Natural variant25701E → K in MFS. Ref.62
VAR_023908
Natural variant25711C → R in MFS. Ref.62
VAR_023909
Natural variant25811C → F in MFS. Ref.56
VAR_018039
Natural variant25851I → T in MFS. Ref.56 Ref.60
VAR_018040
Natural variant25921C → S in MFS. Ref.62
VAR_023910
Natural variant26051C → R in MFS.
VAR_023911
Natural variant26051C → Y in MFS. Ref.63
VAR_023912
Natural variant26061Missing in MFS. Ref.68
VAR_066009
Natural variant26101E → K in MFS; unclear pathological significance. Ref.62 Ref.68
Corresponds to variant rs111984349 [ dbSNP | Ensembl ].
VAR_023913
Natural variant26181G → R in MFS. Ref.56
Corresponds to variant rs141133182 [ dbSNP | Ensembl ].
VAR_018041
Natural variant26231H → P in MFS. Ref.60
VAR_002345
Natural variant26241N → K in MFS. Ref.56
VAR_018042
Natural variant26271G → R in MFS. Ref.33
VAR_002346
Natural variant26291Y → C in MFS. Ref.62
VAR_023914
Natural variant26461C → R in MFS. Ref.68
VAR_066010
Natural variant26521C → G in MFS. Ref.58
VAR_018043
Natural variant26631C → S in MFS. Ref.2
VAR_023915
Natural variant26681G → C in MFS. Ref.56
VAR_018044
Natural variant26801R → C in MFS.
VAR_002347
Natural variant27261R → W in MFS; defects in protein processing. Ref.43
Corresponds to variant rs61746008 [ dbSNP | Ensembl ].
VAR_002348
Natural variant27931Y → H Found in a patient with Marfan syndrome; unclear pathological significance. Ref.68
Corresponds to variant rs113722038 [ dbSNP | Ensembl ].
VAR_066011

Experimental info

Sequence conflict2071T → Q in AAB02036. Ref.1
Sequence conflict21581I → T in AAB02036. Ref.1
Sequence conflict21581I → T in CAA45118. Ref.7

Secondary structure

........................................................................................................................................................ 2871
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35555 [UniParc].

Last modified November 2, 2010. Version 3.
Checksum: 3E6BEF0F1E9A479F

FASTA2,871312,237
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
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. expand/collapse author list , 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]"A Japanese-specific allele in the GALNT11 gene."
Yuasa I., Umetsu K., Matsusue A., Nishimukai H., Harihara S., Fukumori Y., Saitou N., Jin F., Chattopadhyay P.K., Henke L., Henke J.
Leg. Med. 12:208-211(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-1148.
[66]"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.
[67]"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. expand/collapse author list , 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.
[68]"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. 32:1053-1062(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; ARG-2318; TYR-2406; SER-2442; ARG-2511; VAL-2606 DEL; LYS-2610 AND ARG-2646, VARIANTS GLY-1481 AND HIS-2793.
+Additional computationally mapped references.

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.
CCDSCCDS32232.1.
PIRA47221.
RefSeqNP_000129.3. NM_000138.4.
UniGeneHs.591133.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1APJNMR-A2052-2125[»]
1EMNNMR-A2124-2205[»]
1EMONMR-A2124-2205[»]
1LMJNMR-A1069-1154[»]
1UZJX-ray2.25A/B/C1486-1647[»]
1UZKX-ray1.35A1486-1647[»]
1UZPX-ray1.78A1486-1647[»]
1UZQX-ray2.40A1486-1647[»]
2M74NMR-A45-178[»]
2W86X-ray1.80A807-951[»]
ProteinModelPortalP35555.
SMRP35555. Positions 45-178, 807-951, 1069-1154, 1486-1647, 2054-2205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108494. 7 interactions.
DIPDIP-29985N.
IntActP35555. 18 interactions.
MINTMINT-206075.
STRING9606.ENSP00000325527.

PTM databases

PhosphoSiteP35555.

Polymorphism databases

DMDM311033452.

Proteomic databases

MaxQBP35555.
PaxDbP35555.
PRIDEP35555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316623; ENSP00000325527; ENSG00000166147.
GeneID2200.
KEGGhsa:2200.
UCSCuc001zwx.2. human.

Organism-specific databases

CTD2200.
GeneCardsGC15M048700.
GeneReviewsFBN1.
HGNCHGNC:3603. FBN1.
HPACAB002670.
CAB058696.
HPA017759.
HPA021057.
MIM102370. phenotype.
129600. phenotype.
134797. gene.
154700. phenotype.
182212. phenotype.
184900. phenotype.
604308. phenotype.
608328. phenotype.
614185. phenotype.
neXtProtNX_P35555.
Orphanet969. Acromicric dysplasia.
91387. Familial thoracic aortic aneurysm and aortic dissection.
2623. Geleophysic dysplasia.
2084. Glaucoma - ectopia - microspherophakia - stiff joints - short stature.
1885. Isolated ectopia lentis.
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.
PharmGKBPA28016.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000231768.
HOVERGENHBG005643.
InParanoidP35555.
KOK06825.
OMAGGSCSDD.
OrthoDBEOG7RV9F6.
PhylomeDBP35555.
TreeFamTF316849.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP35555.
BgeeP35555.
CleanExHS_FBN1.
GenevestigatorP35555.

Family and domain databases

Gene3D3.90.290.10. 10 hits.
InterProIPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN/EtMIC4.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view]
PANTHERPTHR24039. PTHR24039. 1 hit.
PfamPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 39 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFPIRSF036312. Fibrillin. 1 hit.
SMARTSM00181. EGF. 4 hits.
SM00179. EGF_CA. 42 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 10 hits.
SSF57581. SSF57581. 9 hits.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

ChiTaRSFBN1. human.
EvolutionaryTraceP35555.
GeneWikiFBN1.
GenomeRNAi2200.
NextBio8891.
PROP35555.
SOURCESearch...

Entry information

Entry nameFBN1_HUMAN
AccessionPrimary (citable) accession number: P35555
Secondary accession number(s): B2RUU0 expand/collapse secondary AC list , D2JYH6, Q15972, Q75N87
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 178 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM