Details for: FBN1

Gene ID: 2200

Symbol: FBN1

Ensembl ID: ENSG00000166147

Description: fibrillin 1

Associated with

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: syncytiotrophoblast cell (CL0000525)
    Fold Change: 4.59
    Marker Score: 3773
  • Cell Name: skeletal muscle fibroblast (CL0011027)
    Fold Change: 3.72
    Marker Score: 2447
  • Cell Name: endocardial cell (CL0002350)
    Fold Change: 3.62
    Marker Score: 2048
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 3.2
    Marker Score: 935
  • Cell Name: alveolar type 2 fibroblast cell (CL4028006)
    Fold Change: 2.78
    Marker Score: 1547
  • Cell Name: kidney interstitial fibroblast (CL1000692)
    Fold Change: 2.66
    Marker Score: 5120
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: 2.63
    Marker Score: 11006
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: 2.6
    Marker Score: 1523
  • Cell Name: bronchus fibroblast of lung (CL2000093)
    Fold Change: 2.41
    Marker Score: 3314
  • Cell Name: retinal cone cell (CL0000573)
    Fold Change: 2.4
    Marker Score: 6879
  • Cell Name: skin fibroblast (CL0002620)
    Fold Change: 2.39
    Marker Score: 621
  • Cell Name: skeletal muscle satellite stem cell (CL0008011)
    Fold Change: 2.35
    Marker Score: 2506
  • Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
    Fold Change: 2.22
    Marker Score: 33260
  • Cell Name: sncg GABAergic cortical interneuron (CL4023015)
    Fold Change: 2.21
    Marker Score: 16940
  • Cell Name: fibroblast of lung (CL0002553)
    Fold Change: 2.19
    Marker Score: 5738
  • Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
    Fold Change: 2.18
    Marker Score: 80529
  • Cell Name: sst GABAergic cortical interneuron (CL4023017)
    Fold Change: 2.14
    Marker Score: 42649
  • Cell Name: vip GABAergic cortical interneuron (CL4023016)
    Fold Change: 2.07
    Marker Score: 78640.5
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: 2.07
    Marker Score: 2504
  • Cell Name: caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 1.96
    Marker Score: 7560
  • Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
    Fold Change: 1.93
    Marker Score: 18180
  • Cell Name: fat cell (CL0000136)
    Fold Change: 1.93
    Marker Score: 1080
  • Cell Name: keratocyte (CL0002363)
    Fold Change: 1.9
    Marker Score: 438
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: 1.88
    Marker Score: 641
  • Cell Name: chandelier pvalb GABAergic cortical interneuron (CL4023036)
    Fold Change: 1.88
    Marker Score: 7785
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 1.88
    Marker Score: 115433
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 1.82
    Marker Score: 61865.5
  • Cell Name: neuron (CL0000540)
    Fold Change: 1.78
    Marker Score: 7265
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: 1.76
    Marker Score: 18214
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 1.76
    Marker Score: 19793
  • Cell Name: mesenchymal stem cell (CL0000134)
    Fold Change: 1.74
    Marker Score: 2677
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: 1.72
    Marker Score: 6766
  • Cell Name: cardiac neuron (CL0010022)
    Fold Change: 1.7
    Marker Score: 2114
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: 1.66
    Marker Score: 14290
  • Cell Name: oligodendrocyte (CL0000128)
    Fold Change: 1.63
    Marker Score: 3900
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: 1.62
    Marker Score: 15419
  • Cell Name: decidual cell (CL2000002)
    Fold Change: 1.62
    Marker Score: 6970.5
  • Cell Name: adventitial cell (CL0002503)
    Fold Change: 1.6
    Marker Score: 394
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 1.59
    Marker Score: 1156
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: 1.52
    Marker Score: 9916
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 1.52
    Marker Score: 1516
  • Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
    Fold Change: 1.52
    Marker Score: 2347
  • Cell Name: mesodermal cell (CL0000222)
    Fold Change: 1.51
    Marker Score: 19973
  • Cell Name: vascular leptomeningeal cell (CL4023051)
    Fold Change: 1.5
    Marker Score: 1721
  • Cell Name: mural cell (CL0008034)
    Fold Change: 1.46
    Marker Score: 168043
  • Cell Name: stromal cell of lamina propria of small intestine (CL0009022)
    Fold Change: 1.37
    Marker Score: 309
  • Cell Name: type EC enteroendocrine cell (CL0000577)
    Fold Change: 1.36
    Marker Score: 1283
  • Cell Name: Leydig cell (CL0000178)
    Fold Change: 1.31
    Marker Score: 1407
  • Cell Name: skeletal muscle satellite cell (CL0000594)
    Fold Change: 1.3
    Marker Score: 872
  • Cell Name: pancreatic stellate cell (CL0002410)
    Fold Change: 1.28
    Marker Score: 806
  • Cell Name: astrocyte of the cerebral cortex (CL0002605)
    Fold Change: 1.27
    Marker Score: 27181.5
  • Cell Name: Purkinje cell (CL0000121)
    Fold Change: 1.27
    Marker Score: 42790.5
  • Cell Name: fibroblast of breast (CL4006000)
    Fold Change: 1.26
    Marker Score: 716
  • Cell Name: cerebral cortex neuron (CL0010012)
    Fold Change: 1.21
    Marker Score: 3464
  • Cell Name: immature innate lymphoid cell (CL0001082)
    Fold Change: 1.17
    Marker Score: 2379
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: 1.14
    Marker Score: 4785
  • Cell Name: adipocyte of epicardial fat of left ventricle (CL1000311)
    Fold Change: 1.11
    Marker Score: 291
  • Cell Name: kidney capillary endothelial cell (CL1000892)
    Fold Change: 1.1
    Marker Score: 346
  • Cell Name: preosteoblast (CL0007010)
    Fold Change: 1.09
    Marker Score: 310
  • Cell Name: fibroblast of cardiac tissue (CL0002548)
    Fold Change: 1.09
    Marker Score: 6572
  • Cell Name: smooth muscle cell of large intestine (CL1000279)
    Fold Change: 1.09
    Marker Score: 412
  • Cell Name: fibroblast (CL0000057)
    Fold Change: 1.09
    Marker Score: 1048
  • Cell Name: astrocyte (CL0000127)
    Fold Change: 1.08
    Marker Score: 936
  • Cell Name: inflammatory cell (CL0009002)
    Fold Change: 1.08
    Marker Score: 464
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 1.06
    Marker Score: 16627
  • Cell Name: adipose microvascular endothelial cell (CL2000072)
    Fold Change: 1.03
    Marker Score: 306
  • Cell Name: OFF retinal ganglion cell (CL4023033)
    Fold Change: 1.02
    Marker Score: 427.5
  • Cell Name: extravillous trophoblast (CL0008036)
    Fold Change: 1
    Marker Score: 892
  • Cell Name: cerebral cortex GABAergic interneuron (CL0010011)
    Fold Change: 1
    Marker Score: 71782
  • Cell Name: forebrain radial glial cell (CL0013000)
    Fold Change: 1
    Marker Score: 48008
  • Cell Name: subcutaneous fat cell (CL0002521)
    Fold Change: 0.98
    Marker Score: 360
  • Cell Name: renal interstitial pericyte (CL1001318)
    Fold Change: 0.98
    Marker Score: 937
  • Cell Name: interstitial cell of Cajal (CL0002088)
    Fold Change: 0.98
    Marker Score: 340
  • Cell Name: absorptive cell (CL0000212)
    Fold Change: 0.98
    Marker Score: 30404
  • Cell Name: retinal blood vessel endothelial cell (CL0002585)
    Fold Change: 0.97
    Marker Score: 234
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.97
    Marker Score: 499
  • Cell Name: fibroblast of connective tissue of nonglandular part of prostate (CL1000304)
    Fold Change: 0.97
    Marker Score: 824
  • Cell Name: BEST4+ intestinal epithelial cell, human (CL4030026)
    Fold Change: 0.96
    Marker Score: 454
  • Cell Name: smooth muscle cell of prostate (CL1000487)
    Fold Change: 0.95
    Marker Score: 243
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.95
    Marker Score: 2412
  • Cell Name: mesothelial cell of epicardium (CL0011019)
    Fold Change: 0.92
    Marker Score: 295
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: 0.92
    Marker Score: 368
  • Cell Name: oligodendrocyte precursor cell (CL0002453)
    Fold Change: 0.91
    Marker Score: 1130
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: 0.91
    Marker Score: 2734
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: 0.91
    Marker Score: 288
  • Cell Name: myofibroblast cell (CL0000186)
    Fold Change: 0.9
    Marker Score: 1116.5
  • Cell Name: transit amplifying cell (CL0009010)
    Fold Change: 0.9
    Marker Score: 5115
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.89
    Marker Score: 321
  • Cell Name: ON retinal ganglion cell (CL4023032)
    Fold Change: 0.88
    Marker Score: 240
  • Cell Name: reticular cell (CL0000432)
    Fold Change: 0.87
    Marker Score: 319
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.87
    Marker Score: 5274
  • Cell Name: fibroblast of connective tissue of glandular part of prostate (CL1000305)
    Fold Change: 0.87
    Marker Score: 362
  • Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
    Fold Change: 0.87
    Marker Score: 520
  • Cell Name: epithelial cell of alveolus of lung (CL0010003)
    Fold Change: 0.84
    Marker Score: 375
  • Cell Name: early T lineage precursor (CL0002425)
    Fold Change: 0.83
    Marker Score: 631.5
  • Cell Name: vein endothelial cell (CL0002543)
    Fold Change: 0.81
    Marker Score: 736
  • Cell Name: enteric smooth muscle cell (CL0002504)
    Fold Change: 0.81
    Marker Score: 1912
  • Cell Name: primitive red blood cell (CL0002355)
    Fold Change: 0.81
    Marker Score: 605
  • Cell Name: interneuron (CL0000099)
    Fold Change: 0.79
    Marker Score: 359
  • Cell Name: intestinal epithelial cell (CL0002563)
    Fold Change: 0.77
    Marker Score: 1253

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Other Information

**Key characteristics:** * FBN1 is a secreted protein that is produced by epithelial cells and some other cell types. * It is a large protein (140 kDa) that is composed of three different types of polypeptide chains. * FBN1 is a transmembrane protein that is expressed on the surface of cells. * It is a key component of the extracellular matrix, where it helps to maintain the structural integrity of tissues. **Pathways and functions:** * FBN1 is involved in the regulation of cell migration, proliferation, and differentiation. * It is also involved in the formation and maintenance of blood vessels and the extracellular matrix. * Mutations in FBN1 have been linked to a number of human diseases, including Marfan syndrome, which is characterized by structural abnormalities in the skin, blood vessels, and eyes. **Clinical significance:** * FBN1 is a promising target for the treatment of a variety of diseases that are characterized by abnormal cell migration and proliferation. * For example, FBN1 mutations have been linked to the development of aortic dissection, a condition in which the aorta (the main artery that carries blood from the heart to the body) tears or bursts. * FBN1 inhibitors are being investigated as a treatment for aortic dissection and other diseases that are characterized by abnormal cell migration and proliferation. **Additional notes:** * FBN1 is a highly conserved protein, with a similar protein found in humans, mice, and birds. * It is a well-studied protein that has been extensively characterized in both experimental and clinical settings.

Genular Protein ID: 1230546517

Symbol: FBN1_HUMAN

Name: N/A

UniProtKB Accession Codes:

P35555 B2RUU0 D2JYH6 Q15972 Q75N87

Database IDs:

AGR 1 Antibodypedia 1 BMRB 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 1 CDD 1 CORUM 1 CPTAC 6 CPTC 1 CTD 1 ChiTaRS 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 ELM 1 EMBL 13 EPD 1 Ensembl 1 EvolutionaryTrace 1 ExpressionAtlas 1 GO 29 Gene3D 2 GeneCards 1 GeneReviews 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 HGNC 2 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 12 KEGG 1 MANE-Select 1 MIM 17 MINT 1 MalaCards 1 MassIVE 1 MaxQB 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 11 OrthoDB 1 PANTHER 2 PDB 20 PDBsum 11 PIR 1 PIRSF 1 PRO 1 PROSITE 6 PROSITE-ProRule 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 8 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 1 Pumba 1 RNAct 1 Reactome 7 RefSeq 1 SAM 1 SASBDB 1 SIGNOR 1 SMART 2 SMR 1 STRING 1 SUPFAM 3 SignaLink 1 SwissPalm 1 TreeFam 1 UCSC 1 UniProtKB 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 8364578

Title: Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome.

PubMed ID: 8364578

DOI: 10.1093/hmg/2.7.961

PubMed ID: 15221638

Title: Three novel mutations of the fibrillin-1 gene and ten single nucleotide polymorphisms of the fibrillin-3 gene in Marfan syndrome patients.

PubMed ID: 15221638

DOI: 10.1007/s10038-004-0168-x

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7691719

Title: Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5' end.

PubMed ID: 7691719

DOI: 10.1006/geno.1993.1350

PubMed ID: 1852207

Title: Partial sequence of a candidate gene for the Marfan syndrome.

PubMed ID: 1852207

DOI: 10.1038/352334a0

PubMed ID: 1852206

Title: Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes.

PubMed ID: 1852206

DOI: 10.1038/352330a0

PubMed ID: 8430317

Title: The skipping of constitutive exons in vivo induced by nonsense mutations.

PubMed ID: 8430317

DOI: 10.1126/science.8430317

PubMed ID: 10636927

Title: Initial steps in assembly of microfibrils. Formation of disulfide-cross-linked multimers containing fibrillin-1.

PubMed ID: 10636927

DOI: 10.1074/jbc.275.3.2205

PubMed ID: 9817919

Title: Evidence for furin-type activity-mediated C-terminal processing of profibrillin-1 and interference in the processing by certain mutations.

PubMed ID: 9817919

DOI: 10.1093/hmg/7.13.2039

PubMed ID: 2739055

Title: Association of mitral valve prolapse and systemic abnormalities of connective tissue: a phenotypic continuum.

PubMed ID: 2739055

DOI: 10.1001/jama.262.4.523

PubMed ID: 1860873

Title: Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils.

PubMed ID: 1860873

DOI: 10.1016/s0021-9258(18)98752-1

PubMed ID: 11461921

Title: Interactions of fibrillin-1 with heparin/heparan sulfate, implications for microfibrillar assembly.

PubMed ID: 11461921

DOI: 10.1074/jbc.m104985200

PubMed ID: 12807887

Title: Cell adhesion to fibrillin-1 molecules and microfibrils is mediated by alpha 5 beta 1 and alpha v beta 3 integrins.

PubMed ID: 12807887

DOI: 10.1074/jbc.m303159200

PubMed ID: 15131124

Title: MAGP-2 has multiple binding regions on fibrillins and has covalent periodic association with fibrillin-containing microfibrils.

PubMed ID: 15131124

DOI: 10.1074/jbc.m313672200

PubMed ID: 15165854

Title: Molecular structure and interaction of recombinant human type XVI collagen.

PubMed ID: 15165854

DOI: 10.1016/j.jmb.2004.03.042

PubMed ID: 15790312

Title: Fibulin-5 interacts with fibrillin-1 molecules and microfibrils.

PubMed ID: 15790312

DOI: 10.1042/bj20050368

PubMed ID: 17158881

Title: alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative studies of molecular determinants underlying integrin-rgd affinity and specificity.

PubMed ID: 17158881

DOI: 10.1074/jbc.m607008200

PubMed ID: 17255108

Title: Fibrillin-1 interactions with fibulins depend on the first hybrid domain and provide an adaptor function to tropoelastin.

PubMed ID: 17255108

DOI: 10.1074/jbc.m608204200

PubMed ID: 17293099

Title: LTBP-2 specifically interacts with the amino-terminal region of fibrillin-1 and competes with LTBP-1 for binding to this microfibrillar protein.

PubMed ID: 17293099

DOI: 10.1016/j.matbio.2006.12.006

PubMed ID: 18339631

Title: Targeting of bone morphogenetic protein growth factor complexes to fibrillin.

PubMed ID: 18339631

DOI: 10.1074/jbc.m707820200

PubMed ID: 19349279

Title: Latent transforming growth factor beta-binding proteins and fibulins compete for fibrillin-1 and exhibit exquisite specificities in binding sites.

PubMed ID: 19349279

DOI: 10.1074/jbc.m809348200

PubMed ID: 19570982

Title: Differential regulation of elastic fiber formation by fibulin-4 and -5.

PubMed ID: 19570982

DOI: 10.1074/jbc.m109.019364

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 20979188

Title: Marfan syndrome with neonatal progeroid syndrome-like lipodystrophy associated with a novel frameshift mutation at the 3' terminus of the FBN1-gene.

PubMed ID: 20979188

DOI: 10.1002/ajmg.a.33690

PubMed ID: 21594992

Title: Further evidence for a marfanoid syndrome with neonatal progeroid features and severe generalized lipodystrophy due to frameshift mutations near the 3' end of the FBN1 gene.

PubMed ID: 21594992

DOI: 10.1002/ajmg.a.33906

PubMed ID: 21594993

Title: Progeroid facial features and lipodystrophy associated with a novel splice site mutation in the final intron of the FBN1 gene.

PubMed ID: 21594993

DOI: 10.1002/ajmg.a.33905

PubMed ID: 21402694

Title: ADAMTS10 protein interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts.

PubMed ID: 21402694

DOI: 10.1074/jbc.m111.231571

PubMed ID: 23010571

Title: A disintegrin-like and metalloprotease domain containing thrombospondin type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-, fibrillin-2-, and heparin-binding member of the ADAMTS superfamily containing a netrin-like module.

PubMed ID: 23010571

DOI: 10.1016/j.matbio.2012.09.003

PubMed ID: 24039232

Title: Fibrillin-1 directly regulates osteoclast formation and function by a dual mechanism.

PubMed ID: 24039232

DOI: 10.1242/jcs.127571

PubMed ID: 24665001

Title: De novo heterozygous FBN1 mutations in the extreme C-terminal region cause progeroid fibrillinopathy.

PubMed ID: 24665001

DOI: 10.1002/ajmg.a.36449

PubMed ID: 24039054

Title: Severe congenital lipodystrophy and a progeroid appearance: Mutation in the penultimate exon of FBN1 causing a recognizable phenotype.

PubMed ID: 24039054

DOI: 10.1002/ajmg.a.36157

PubMed ID: 24613577

Title: Neonatal progeroid variant of Marfan syndrome with congenital lipodystrophy results from mutations at the 3' end of FBN1 gene.

PubMed ID: 24613577

DOI: 10.1016/j.ejmg.2014.02.012

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24982166

Title: C-terminal propeptide is required for fibrillin-1 secretion and blocks premature assembly through linkage to domains cbEGF41-43.

PubMed ID: 24982166

DOI: 10.1073/pnas.1401697111

PubMed ID: 26091039

Title: A single kinase generates the majority of the secreted phosphoproteome.

PubMed ID: 26091039

DOI: 10.1016/j.cell.2015.05.028

PubMed ID: 27026396

Title: New insights into the structure, assembly and biological roles of 10-12 nm connective tissue microfibrils from fibrillin-1 studies.

PubMed ID: 27026396

DOI: 10.1042/bj20151108

PubMed ID: 27087445

Title: Asprosin, a fasting-induced glucogenic protein hormone.

PubMed ID: 27087445

DOI: 10.1016/j.cell.2016.02.063

PubMed ID: 31230984

Title: OLFR734 mediates glucose metabolism as a receptor of asprosin.

PubMed ID: 31230984

DOI: 10.1016/j.cmet.2019.05.022

PubMed ID: 31775140

Title: Serum Asprosin Concentrations Are Increased and Associated with Insulin Resistance in Children with Obesity.

PubMed ID: 31775140

DOI: 10.1159/000503808

PubMed ID: 29104036

Title: Circulating asprosin concentrations are increased in type 2 diabetes mellitus and independently associated with fasting glucose and triglyceride.

PubMed ID: 29104036

DOI: 10.1016/j.cca.2017.10.034

PubMed ID: 30853600

Title: Asprosin impairs insulin secretion in response to glucose and viability through TLR4/JNK-mediated inflammation.

PubMed ID: 30853600

DOI: 10.1016/j.mce.2019.03.001

PubMed ID: 33904407

Title: Asprosin-neutralizing antibodies as a treatment for metabolic syndrome.

PubMed ID: 33904407

DOI: 10.7554/elife.63784

PubMed ID: 26860060

Title: Marfanoid-progeroid-lipodystrophy syndrome: a newly recognized fibrillinopathy.

PubMed ID: 26860060

DOI: 10.1038/ejhg.2016.6

PubMed ID: 26601954

Title: Characterization of microfibrillar-associated protein 4 (MFAP4) as a tropoelastin- and fibrillin-binding protein involved in elastic fiber formation.

PubMed ID: 26601954

DOI: 10.1074/jbc.m115.681775

PubMed ID: 34411563

Title: POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1.

PubMed ID: 34411563

DOI: 10.1016/j.jbc.2021.101055

PubMed ID: 9362480

Title: Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils.

PubMed ID: 9362480

DOI: 10.1093/emboj/16.22.6659

PubMed ID: 8568869

Title: Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1.

PubMed ID: 8568869

DOI: 10.1006/jmbi.1996.0003

PubMed ID: 8653794

Title: Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders.

PubMed ID: 8653794

DOI: 10.1016/s0092-8674(00)81259-3

PubMed ID: 12511552

Title: Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1.

PubMed ID: 12511552

DOI: 10.1074/jbc.m208266200

PubMed ID: 15062093

Title: Structure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organization.

PubMed ID: 15062093

DOI: 10.1016/j.str.2004.02.023

PubMed ID: 19446531

Title: Structure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteins.

PubMed ID: 19446531

DOI: 10.1016/j.str.2009.03.014

PubMed ID: 24035709

Title: Structure of the fibrillin-1 N-terminal domains suggests that heparan sulfate regulates the early stages of microfibril assembly.

PubMed ID: 24035709

DOI: 10.1016/j.str.2013.08.004

PubMed ID: 8594563

Title: Software and database for the analysis of mutations in the human FBN1 gene.

PubMed ID: 8594563

DOI: 10.1093/nar/24.1.137

PubMed ID: 10633129

Title: The molecular genetics of Marfan syndrome and related microfibrillopathies.

PubMed ID: 10633129

DOI: 10.1136/jmg.37.1.9

PubMed ID: 12203987

Title: Mutations of FBN1 and genotype-phenotype correlations in Marfan syndrome and related fibrillinopathies.

PubMed ID: 12203987

DOI: 10.1002/humu.10113

PubMed ID: 1852208

Title: Marfan syndrome caused by a recurrent de novo missense mutation in the fibrillin gene.

PubMed ID: 1852208

DOI: 10.1038/352337a0

PubMed ID: 1301946

Title: Clustering of fibrillin (FBN1) missense mutations in Marfan syndrome patients at cysteine residues in EGF-like domains.

PubMed ID: 1301946

DOI: 10.1002/humu.1380010504

PubMed ID: 1569206

Title: Marfan phenotype variability in a family segregating a missense mutation in the epidermal growth factor-like motif of the fibrillin gene.

PubMed ID: 1569206

DOI: 10.1172/jci115766

PubMed ID: 8406497

Title: Four novel FBN1 mutations: significance for mutant transcript level and EGF-like domain calcium binding in the pathogenesis of Marfan syndrome.

PubMed ID: 8406497

DOI: 10.1006/geno.1993.1349

PubMed ID: 8504310

Title: A novel fibrillin mutation in the Marfan syndrome which could disrupt calcium binding of the epidermal growth factor-like module.

PubMed ID: 8504310

DOI: 10.1093/hmg/2.4.475

PubMed ID: 8281141

Title: Mutation screening of complete fibrillin-1 coding sequence: report of five new mutations, including two in 8-cysteine domains.

PubMed ID: 8281141

DOI: 10.1093/hmg/2.11.1813

PubMed ID: 7977366

Title: A compound-heterozygous Marfan patient: two defective fibrillin alleles result in a lethal phenotype.

PubMed ID: 7977366

PubMed ID: 8188302

Title: A novel mutation of the fibrillin gene causing ectopia lentis.

PubMed ID: 8188302

DOI: 10.1006/geno.1994.1110

PubMed ID: 8004112

Title: 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.

PubMed ID: 8004112

DOI: 10.1093/hmg/3.2.373

PubMed ID: 7951214

Title: Substitution of a cysteine residue in a non-calcium binding, EGF-like domain of fibrillin segregates with the Marfan syndrome in a large kindred.

PubMed ID: 7951214

DOI: 10.1093/hmg/3.6.1013

PubMed ID: 7911051

Title: Identification of a novel nonsense mutation in the fibrillin gene (FBN1) using nonisotopic techniques.

PubMed ID: 7911051

DOI: 10.1002/humu.1380030212

PubMed ID: 8040326

Title: 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.

PubMed ID: 8040326

DOI: 10.1172/jci117389

PubMed ID: 8071963

Title: A new missense mutation of fibrillin in a patient with Marfan syndrome.

PubMed ID: 8071963

DOI: 10.1136/jmg.31.4.338

PubMed ID: 7870075

Title: A novel mutation in the fibrillin gene (FBN1) in familial arachnodactyly.

PubMed ID: 7870075

DOI: 10.1006/mcpr.1994.1045

PubMed ID: 8136837

Title: Mutations in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome.

PubMed ID: 8136837

DOI: 10.1038/ng0194-64

PubMed ID: 7762551

Title: A Gly1127Ser mutation in an EGF-like domain of the fibrillin-1 gene is a risk factor for ascending aortic aneurysm and dissection.

PubMed ID: 7762551

PubMed ID: 7611299

Title: Fifteen novel FBN1 mutations causing Marfan syndrome detected by heteroduplex analysis of genomic amplicons.

PubMed ID: 7611299

PubMed ID: 7738200

Title: A mutation in FBN1 disrupts profibrillin processing and results in isolated skeletal features of the Marfan syndrome.

PubMed ID: 7738200

DOI: 10.1172/jci117930

PubMed ID: 8882780

Title: Delineation of the Marfan phenotype associated with mutations in exons 23-32 of the FBN1 gene.

PubMed ID: 8882780

DOI: 10.1002/(sici)1096-8628(19960329)62:3<233::aid-ajmg7>3.0.co;2-u

PubMed ID: 8863159

Title: Characterisation of four novel fibrillin-1 (FBN1) mutations in Marfan syndrome.

PubMed ID: 8863159

DOI: 10.1136/jmg.33.8.665

PubMed ID: 9254848

Title: 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.

PubMed ID: 9254848

DOI: 10.1007/s004390050489

PubMed ID: 9150726

Title: The pathogenicity of the Pro1148Ala substitution in the FBN1 gene: causing or predisposing to Marfan syndrome and aortic aneurysm, or clinically innocent?

PubMed ID: 9150726

DOI: 10.1007/s004390050414

PubMed ID: 9338581

Title: Mutation screening of all 65 exons of the fibrillin-1 gene in 60 patients with Marfan syndrome: report of 12 novel mutations.

PubMed ID: 9338581

DOI: 10.1002/(sici)1098-1004(1997)10:4<280::aid-humu3>3.0.co;2-l

PubMed ID: 9338588

Title: P1148A in fibrillin-1 is not a mutation leading to Shprintzen-Goldberg syndrome.

PubMed ID: 9338588

DOI: 10.1002/(sici)1098-1004(1997)10:4<326::aid-humu10>3.0.co;2-1

PubMed ID: 9401003

Title: Fibrillin-1 mutations in Marfan syndrome and other type-1 fibrillinopathies.

PubMed ID: 9401003

DOI: 10.1002/(sici)1098-1004(1997)10:6<415::aid-humu1>3.0.co;2-c

PubMed ID: 8988160

Title: P1148A in fibrillin-1 is not a mutation anymore.

PubMed ID: 8988160

DOI: 10.1038/ng0197-12

PubMed ID: 9016526

Title: Marfan Database (second edition): software and database for the analysis of mutations in the human FBN1 gene.

PubMed ID: 9016526

DOI: 10.1093/nar/25.1.147

PubMed ID: 9837823

Title: Multiple molecular mechanisms underlying subdiagnostic variants of Marfan syndrome.

PubMed ID: 9837823

DOI: 10.1086/302144

PubMed ID: 9452085

Title: Correlation of a recurrent FBN1 mutation (R122C) with an atypical familial Marfan syndrome phenotype.

PubMed ID: 9452085

DOI: 10.1002/humu.1380110164

PubMed ID: 10694921

Title: A novel mutation in the neonatal region of the fibrillin (FBN) 1 gene associated with a classical phenotype of Marfan syndrome (MfS).

PubMed ID: 10694921

DOI: 10.1002/(sici)1098-1004(1998)12:2%3c137::aid-humu14%3e3.0.co;2-p

PubMed ID: 10441597

Title: Demonstration of the recurrence of Marfan-like skeletal and cardiovascular manifestations due to germline mosaicism for an FBN1 mutation.

PubMed ID: 10441597

DOI: 10.1086/302545

PubMed ID: 10425041

Title: Identification of 9 novel FBN1 mutations in German patients with Marfan syndrome.

PubMed ID: 10425041

DOI: 10.1002/(sici)1098-1004(1999)14:2<181::aid-humu10>3.0.co;2-6

PubMed ID: 11700157

Title: Genotype and phenotype analysis of 171 patients referred for molecular study of the fibrillin-1 gene FBN1 because of suspected Marfan syndrome.

PubMed ID: 11700157

DOI: 10.1001/archinte.161.20.2447

PubMed ID: 12203992

Title: TGGE screening of the entire FBN1 coding sequence in 126 individuals with Marfan syndrome and related fibrillinopathies.

PubMed ID: 12203992

DOI: 10.1002/humu.10112

PubMed ID: 12402346

Title: Mutation screening of the fibrillin-1 (FBN1) gene in 76 unrelated patients with Marfan syndrome or Marfanoid features leads to the identification of 11 novel and three previously reported mutations.

PubMed ID: 12402346

DOI: 10.1002/humu.9075

PubMed ID: 11826022

Title: Sensitivity of conformation sensitive gel electrophoresis in detecting mutations in Marfan syndrome and related conditions.

PubMed ID: 11826022

DOI: 10.1136/jmg.39.1.34

PubMed ID: 12161601

Title: Twelve novel FBN1 mutations in Marfan syndrome and Marfan related phenotypes test the feasibility of FBN1 mutation testing in clinical practice.

PubMed ID: 12161601

DOI: 10.1136/jmg.39.8.589

PubMed ID: 12525539

Title: In frame fibrillin-1 gene deletion in autosomal dominant Weill-Marchesani syndrome.

PubMed ID: 12525539

DOI: 10.1136/jmg.40.1.34

PubMed ID: 14695540

Title: Detection of thirty novel FBN1 mutations in patients with Marfan syndrome or a related fibrillinopathy.

PubMed ID: 14695540

DOI: 10.1002/humu.9207

PubMed ID: 15161917

Title: Consequences of cysteine mutations in calcium-binding epidermal growth factor modules of fibrillin-1.

PubMed ID: 15161917

DOI: 10.1074/jbc.m405239200

PubMed ID: 16222657

Title: Identification of sixty-two novel and twelve known FBN1 mutations in eighty-one unrelated probands with Marfan syndrome and other fibrillinopathies.

PubMed ID: 16222657

DOI: 10.1002/humu.9377

PubMed ID: 16220557

Title: Identification of 29 novel and nine recurrent fibrillin-1 (FBN1) mutations and genotype-phenotype correlations in 76 patients with Marfan syndrome.

PubMed ID: 16220557

DOI: 10.1002/humu.20239

PubMed ID: 17657824

Title: The importance of mutation detection in Marfan syndrome and Marfan-related disorders: report of 193 FBN1 mutations.

PubMed ID: 17657824

DOI: 10.1002/humu.9505

PubMed ID: 18435798

Title: FBN1 mutation screening of patients with Marfan syndrome and related disorders: detection of 46 novel FBN1 mutations.

PubMed ID: 18435798

DOI: 10.1111/j.1399-0004.2008.01007.x

Sequence Information:

  • Length: 2871
  • Mass: 312298
  • Checksum: 501258AF1756B9F7
  • Sequence:
    • MRRGRLLEIA LGFTVLLASY TSHGADANLE AGNVKETRAS RAKRRGGGGH DALKGPNVCG 
SRYNAYCCPG WKTLPGGNQC IVPICRHSCG DGFCSRPNMC TCPSGQIAPS CGSRSIQHCN 
IRCMNGGSCS DDHCLCQKGY IGTHCGQPVC ESGCLNGGRC VAPNRCACTY GFTGPQCERD 
YRTGPCFTVI SNQMCQGQLS GIVCTKTLCC ATVGRAWGHP CEMCPAQPHP CRRGFIPNIR 
TGACQDVDEC QAIPGLCQGG NCINTVGSFE CKCPAGHKLN EVSQKCEDID ECSTIPGICE 
GGECTNTVSS YFCKCPPGFY TSPDGTRCID VRPGYCYTAL TNGRCSNQLP QSITKMQCCC 
DAGRCWSPGV TVAPEMCPIR ATEDFNKLCS VPMVIPGRPE YPPPPLGPIP PVLPVPPGFP 
PGPQIPVPRP PVEYLYPSRE PPRVLPVNVT DYCQLVRYLC QNGRCIPTPG SYRCECNKGF 
QLDLRGECID VDECEKNPCA GGECINNQGS YTCQCRAGYQ STLTRTECRD IDECLQNGRI 
CNNGRCINTD GSFHCVCNAG FHVTRDGKNC EDMDECSIRN MCLNGMCINE DGSFKCICKP 
GFQLASDGRY CKDINECETP GICMNGRCVN TDGSYRCECF PGLAVGLDGR VCVDTHMRST 
CYGGYKRGQC IKPLFGAVTK SECCCASTEY AFGEPCQPCP AQNSAEYQAL CSSGPGMTSA 
GSDINECALD PDICPNGICE NLRGTYKCIC NSGYEVDSTG KNCVDINECV LNSLLCDNGQ 
CRNTPGSFVC TCPKGFIYKP DLKTCEDIDE CESSPCINGV CKNSPGSFIC ECSSESTLDP 
TKTICIETIK GTCWQTVIDG RCEININGAT LKSQCCSSLG AAWGSPCTLC QVDPICGKGY 
SRIKGTQCED IDECEVFPGV CKNGLCVNTR GSFKCQCPSG MTLDATGRIC LDIRLETCFL 
RYEDEECTLP IAGRHRMDAC CCSVGAAWGT EECEECPMRN TPEYEELCPR GPGFATKEIT 
NGKPFFKDIN ECKMIPSLCT HGKCRNTIGS FKCRCDSGFA LDSEERNCTD IDECRISPDL 
CGRGQCVNTP GDFECKCDEG YESGFMMMKN CMDIDECQRD PLLCRGGVCH NTEGSYRCEC 
PPGHQLSPNI SACIDINECE LSAHLCPNGR CVNLIGKYQC ACNPGYHSTP DRLFCVDIDE 
CSIMNGGCET FCTNSEGSYE CSCQPGFALM PDQRSCTDID ECEDNPNICD GGQCTNIPGE 
YRCLCYDGFM ASEDMKTCVD VNECDLNPNI CLSGTCENTK GSFICHCDMG YSGKKGKTGC 
TDINECEIGA HNCGKHAVCT NTAGSFKCSC SPGWIGDGIK CTDLDECSNG THMCSQHADC 
KNTMGSYRCL CKEGYTGDGF TCTDLDECSE NLNLCGNGQC LNAPGGYRCE CDMGFVPSAD 
GKACEDIDEC SLPNICVFGT CHNLPGLFRC ECEIGYELDR SGGNCTDVNE CLDPTTCISG 
NCVNTPGSYI CDCPPDFELN PTRVGCVDTR SGNCYLDIRP RGDNGDTACS NEIGVGVSKA 
SCCCSLGKAW GTPCEMCPAV NTSEYKILCP GGEGFRPNPI TVILEDIDEC QELPGLCQGG 
KCINTFGSFQ CRCPTGYYLN EDTRVCDDVN ECETPGICGP GTCYNTVGNY TCICPPDYMQ 
VNGGNNCMDM RRSLCYRNYY ADNQTCDGEL LFNMTKKMCC CSYNIGRAWN KPCEQCPIPS 
TDEFATLCGS QRPGFVIDIY TGLPVDIDEC REIPGVCENG VCINMVGSFR CECPVGFFYN 
DKLLVCEDID ECQNGPVCQR NAECINTAGS YRCDCKPGYR FTSTGQCNDR NECQEIPNIC 
SHGQCIDTVG SFYCLCHTGF KTNDDQTMCL DINECERDAC GNGTCRNTIG SFNCRCNHGF 
ILSHNNDCID VDECASGNGN LCRNGQCINT VGSFQCQCNE GYEVAPDGRT CVDINECLLE 
PRKCAPGTCQ NLDGSYRCIC PPGYSLQNEK CEDIDECVEE PEICALGTCS NTEGSFKCLC 
PEGFSLSSSG RRCQDLRMSY CYAKFEGGKC SSPKSRNHSK QECCCALKGE GWGDPCELCP 
TEPDEAFRQI CPYGSGIIVG PDDSAVDMDE CKEPDVCKHG QCINTDGSYR CECPFGYILA 
GNECVDTDEC SVGNPCGNGT CKNVIGGFEC TCEEGFEPGP MMTCEDINEC AQNPLLCAFR 
CVNTYGSYEC KCPVGYVLRE DRRMCKDEDE CEEGKHDCTE KQMECKNLIG TYMCICGPGY 
QRRPDGEGCV DENECQTKPG ICENGRCLNT RGSYTCECND GFTASPNQDE CLDNREGYCF 
TEVLQNMCQI GSSNRNPVTK SECCCDGGRG WGPHCEICPF QGTVAFKKLC PHGRGFMTNG 
ADIDECKVIH DVCRNGECVN DRGSYHCICK TGYTPDITGT SCVDLNECNQ APKPCNFICK 
NTEGSYQCSC PKGYILQEDG RSCKDLDECA TKQHNCQFLC VNTIGGFTCK CPPGFTQHHT 
SCIDNNECTS DINLCGSKGI CQNTPGSFTC ECQRGFSLDQ TGSSCEDVDE CEGNHRCQHG 
CQNIIGGYRC SCPQGYLQHY QWNQCVDENE CLSAHICGGA SCHNTLGSYK CMCPAGFQYE 
QFSGGCQDIN ECGSAQAPCS YGCSNTEGGY LCGCPPGYFR IGQGHCVSGM GMGRGNPEPP 
VSGEMDDNSL SPEACYECKI NGYPKRGRKR RSTNETDASN IEDQSETEAN VSLASWDVEK 
TAIFAFNISH VSNKVRILEL LPALTTLTNH NRYLIESGNE DGFFKINQKE GISYLHFTKK 
KPVAGTYSLQ ISSTPLYKKK ELNQLEDKYD KDYLSGELGD NLKMKIQVLL H

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.