Details for: FBN1

Gene ID: 2200

Symbol: FBN1

Ensembl ID: ENSG00000166147

Description: fibrillin 1

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: polychromatophilic erythroblast (CL0000550)
    Fold Change: 312.1922
    Cell Significance Index: -48.5600
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 191.6865
    Cell Significance Index: -48.6200
  • Cell Name: smooth muscle fiber of ileum (CL1000278)
    Fold Change: 102.1133
    Cell Significance Index: -48.2100
  • Cell Name: mucosal type mast cell (CL0000485)
    Fold Change: 97.9429
    Cell Significance Index: -39.7900
  • Cell Name: ciliated cell of the bronchus (CL0002332)
    Fold Change: 41.7076
    Cell Significance Index: -39.8200
  • Cell Name: orthochromatic erythroblast (CL0000552)
    Fold Change: 39.5837
    Cell Significance Index: -48.8100
  • Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
    Fold Change: 12.9515
    Cell Significance Index: -39.7800
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 12.2654
    Cell Significance Index: -48.4000
  • Cell Name: epidermal Langerhans cell (CL0002457)
    Fold Change: 12.1402
    Cell Significance Index: -26.5700
  • Cell Name: skeletal muscle fibroblast (CL0011027)
    Fold Change: 9.0089
    Cell Significance Index: 61.0400
  • Cell Name: preadipocyte (CL0002334)
    Fold Change: 8.7948
    Cell Significance Index: 171.6500
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: 4.8992
    Cell Significance Index: 712.1600
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 2.9849
    Cell Significance Index: 1895.7000
  • Cell Name: fibro/adipogenic progenitor cell (CL0009099)
    Fold Change: 2.6668
    Cell Significance Index: 134.7700
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: 2.1862
    Cell Significance Index: 58.3800
  • Cell Name: fibroblast of cardiac tissue (CL0002548)
    Fold Change: 2.0926
    Cell Significance Index: 30.0500
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 1.7538
    Cell Significance Index: 629.0600
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 1.7380
    Cell Significance Index: 348.6400
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 1.3697
    Cell Significance Index: 188.1000
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 1.2904
    Cell Significance Index: 36.9900
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: 1.0419
    Cell Significance Index: 70.0600
  • Cell Name: GABAergic interneuron (CL0011005)
    Fold Change: 0.9923
    Cell Significance Index: 686.2900
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: 0.7710
    Cell Significance Index: 24.7000
  • Cell Name: direct pathway medium spiny neuron (CL4023026)
    Fold Change: 0.7159
    Cell Significance Index: 27.1100
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: 0.6794
    Cell Significance Index: 30.0500
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 0.6700
    Cell Significance Index: 85.8900
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: 0.6583
    Cell Significance Index: 1239.4100
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: 0.6015
    Cell Significance Index: 33.7600
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: 0.5583
    Cell Significance Index: 759.1000
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: 0.5352
    Cell Significance Index: 32.8100
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 0.3423
    Cell Significance Index: 17.8300
  • Cell Name: adipocyte of breast (CL0002617)
    Fold Change: 0.2589
    Cell Significance Index: 3.2600
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: 0.2129
    Cell Significance Index: 327.7800
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.1724
    Cell Significance Index: 32.8200
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.1147
    Cell Significance Index: 103.5500
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: 0.1074
    Cell Significance Index: 1.3700
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: 0.0577
    Cell Significance Index: 0.9700
  • Cell Name: fallopian tube secretory epithelial cell (CL4030006)
    Fold Change: 0.0278
    Cell Significance Index: 0.4300
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.0244
    Cell Significance Index: 4.8500
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: 0.0124
    Cell Significance Index: 22.7800
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: -0.0021
    Cell Significance Index: -1.1500
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0276
    Cell Significance Index: -20.4600
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0468
    Cell Significance Index: -21.2400
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.0538
    Cell Significance Index: -33.5700
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: -0.0556
    Cell Significance Index: -4.2700
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: -0.0571
    Cell Significance Index: -2.0100
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: -0.0620
    Cell Significance Index: -45.4900
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: -0.0688
    Cell Significance Index: -52.0600
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.0693
    Cell Significance Index: -39.1100
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: -0.1001
    Cell Significance Index: -44.2700
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: -0.1075
    Cell Significance Index: -17.4900
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: -0.1330
    Cell Significance Index: -38.2700
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: -0.1541
    Cell Significance Index: -15.2400
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: -0.1663
    Cell Significance Index: -29.9700
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: -0.2158
    Cell Significance Index: -36.8500
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.2174
    Cell Significance Index: -45.8000
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: -0.2256
    Cell Significance Index: -10.2300
  • Cell Name: pancreatic endocrine cell (CL0008024)
    Fold Change: -0.2334
    Cell Significance Index: -26.6400
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: -0.2999
    Cell Significance Index: -32.6300
  • Cell Name: fibroblast of dermis (CL0002551)
    Fold Change: -0.3058
    Cell Significance Index: -6.4000
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: -0.3064
    Cell Significance Index: -37.6800
  • Cell Name: transit amplifying cell of small intestine (CL0009012)
    Fold Change: -0.3153
    Cell Significance Index: -6.5400
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.3438
    Cell Significance Index: -35.8000
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: -0.3594
    Cell Significance Index: -36.7100
  • Cell Name: lactocyte (CL0002325)
    Fold Change: -0.3764
    Cell Significance Index: -48.6300
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.4088
    Cell Significance Index: -47.6400
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: -0.4276
    Cell Significance Index: -12.3200
  • Cell Name: Purkinje cell (CL0000121)
    Fold Change: -0.4309
    Cell Significance Index: -9.4400
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: -0.4433
    Cell Significance Index: -52.2800
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.4934
    Cell Significance Index: -56.5300
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: -0.5774
    Cell Significance Index: -39.9300
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -0.5850
    Cell Significance Index: -46.3300
  • Cell Name: eukaryotic cell (CL0000255)
    Fold Change: -0.5956
    Cell Significance Index: -25.9000
  • Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
    Fold Change: -0.6135
    Cell Significance Index: -13.0200
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: -0.6307
    Cell Significance Index: -15.7700
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: -0.6352
    Cell Significance Index: -29.8600
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: -0.6470
    Cell Significance Index: -45.7600
  • Cell Name: gut absorptive cell (CL0000677)
    Fold Change: -0.6723
    Cell Significance Index: -40.3600
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: -0.6769
    Cell Significance Index: -50.4500
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: -0.7473
    Cell Significance Index: -48.2100
  • Cell Name: hippocampal pyramidal neuron (CL1001571)
    Fold Change: -0.8102
    Cell Significance Index: -23.1200
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: -0.8323
    Cell Significance Index: -23.2600
  • Cell Name: medial ganglionic eminence derived interneuron (CL4023063)
    Fold Change: -0.8432
    Cell Significance Index: -12.0800
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: -0.8592
    Cell Significance Index: -28.1300
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: -0.8594
    Cell Significance Index: -27.3700
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: -0.8657
    Cell Significance Index: -45.4500
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: -0.8804
    Cell Significance Index: -55.4900
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: -0.8947
    Cell Significance Index: -54.9900
  • Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
    Fold Change: -0.9571
    Cell Significance Index: -33.5300
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: -0.9993
    Cell Significance Index: -51.9100
  • Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
    Fold Change: -1.0070
    Cell Significance Index: -25.1200
  • Cell Name: fibroblast of the aortic adventitia (CL0002547)
    Fold Change: -1.0088
    Cell Significance Index: -10.1800
  • Cell Name: sst GABAergic cortical interneuron (CL4023017)
    Fold Change: -1.0100
    Cell Significance Index: -19.9700
  • Cell Name: leptomeningeal cell (CL0000708)
    Fold Change: -1.0636
    Cell Significance Index: -22.7400
  • Cell Name: VIP GABAergic cortical interneuron (CL4023016)
    Fold Change: -1.0654
    Cell Significance Index: -21.3900
  • Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
    Fold Change: -1.0845
    Cell Significance Index: -23.4300
  • Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
    Fold Change: -1.1157
    Cell Significance Index: -38.7700
  • Cell Name: chandelier pvalb GABAergic cortical interneuron (CL4023036)
    Fold Change: -1.1327
    Cell Significance Index: -23.6400
  • Cell Name: hippocampal interneuron (CL1001569)
    Fold Change: -1.1821
    Cell Significance Index: -15.3300
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: -1.2029
    Cell Significance Index: -26.0600

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** 1. **Structure:** Fibrillin 1 is a type III integral membrane protein that consists of three immunoglobulin-like domains and three collagen-like triple-helices. 2. **Expression:** FBN1 is highly expressed in cells that produce elastic fibers, including skeletal muscle fibroblasts, endocardial cells, and non-pigmented ciliary epithelial cells. 3. **Function:** Fibrillin 1 plays a critical role in the formation and organization of elastic fibers, which provide elasticity and flexibility to tissues. **Pathways and Functions:** 1. **Elastic Fiber Formation:** FBN1 is essential for the formation of elastic fibers, which are composed of fibrillin microfibrils. These microfibrils provide elasticity and flexibility to tissues. 2. **Extracellular Matrix Organization:** FBN1 regulates the organization of the extracellular matrix, which provides structural support and mechanical stability to tissues. 3. **Cell Signaling:** FBN1 interacts with various signaling molecules, including transforming growth factor-beta (TGF-β) and insulin-like growth factor (IGF), to regulate cell growth and differentiation. 4. **Integrin Binding:** FBN1 binds to integrins, which are transmembrane receptors that mediate cell adhesion and signaling. **Clinical Significance:** 1. **Marfan Syndrome:** Mutations in the FBN1 gene are associated with Marfan syndrome, a genetic disorder characterized by defects in elastic fiber structure and function. 2. **Aortic Dissection:** FBN1 mutations have been linked to an increased risk of aortic dissection, a life-threatening condition characterized by the tearing of the aorta. 3. **Other Disorders:** FBN1 mutations have also been associated with other disorders, including congenital contractural arachnodactyly, cardiac arrhythmias, and musculoskeletal disorders. 4. **Cancer:** FBN1 has been implicated in the regulation of cell growth and differentiation, and its dysregulation has been linked to various types of cancer, including breast and lung cancer. In conclusion, FBN1 is a critical gene that plays a central role in the formation and organization of elastic fibers and the regulation of extracellular matrix organization. Its dysregulation has been linked to a range of disorders, including Marfan syndrome and other genetic conditions. Further research is needed to elucidate the mechanisms by which FBN1 regulates elastic fiber formation and extracellular matrix organization, and to develop new therapeutic strategies for the treatment of FBN1-related disorders.

Genular Protein ID: 1230546517

Symbol: FBN1_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

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. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.