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FBLN1 (fibulin 1)

Written2010-09Lorenzo Castagnoli, Elda Tagliabue, Serenella M Pupa
Fondazione IRCCS Istituto Nazionale Dei Tumori - Molecular Targeting Unit, Dept of Experimental Oncology, Molecular Medicine, Via Amadeo 42, Milan, Italy
Updated2012-05Lorenzo Castagnoli, Elda Tagliabue, Serenella M Pupa
Fondazione IRCCS Istituto Nazionale Dei Tumori - Molecular Targeting Unit, Dept of Experimental Oncology, Molecular Medicine, Via Amadeo 42, Milan, Italy

(Note : for Links provided by Atlas : click)

Identity

Alias_symbol (synonym)FBLN
Other aliasFIBL-1
HGNC (Hugo) FBLN1
LocusID (NCBI) 2192
Atlas_Id 44462
Location 22q13.31  [Link to chromosome band 22q13]
Location_base_pair Starts at 45502839 and ends at 45563362 bp from pter ( according to hg19-Feb_2009)  [Mapping FBLN1.png]
Local_order Orientation: plus strand.
 
Fusion genes
(updated 2016)		ATXN10 (22q13.31) / FBLN1 (22q13.31)CSRNP2 (12q13.12) / FBLN1 (22q13.31)FBLN1 (22q13.31) / CSRNP2 (12q13.12)
FBLN1 (22q13.31) / FBLN1 (22q13.31)FBLN1 (22q13.31) / H19 (11p15.5)FBLN1 (22q13.31) / MAP3K4 (6q26)
FBLN1 (22q13.31) / PTPN12 (7q11.23)FBLN1 (22q13.31) / RIBC2 (22q13.31)HACE1 (6q16.3) / FBLN1 (22q13.31)
LARP1B (4q28.2) / FBLN1 (22q13.31)PLA2G2A (1p36.13) / FBLN1 (22q13.31)
Note Fibulin-1 is an extracellular matrix (ECM) and blood glycoprotein. It is a member of the fibulin glycoprotein family which includes 7 proteins thought to function as bridges in the organization of ECM supramolecular structures (Argraves et al., 1990; Timpl et al., 2003; De Vega et al., 2009).

DNA/RNA

 
  Transcription factor.
Description Sequence length: 97,71 Kb, 20 exons, max. exon length 818, min. exon length: 50. Number of SNPs: 1038. Four splice variants have been identified which differ in the 3' end and encode different isoforms (A, B, C and D) (Pan et al., 1999).
Variant D: This variant is considered the canonic transcript form: 2947 bp;
- Including exons 18, 19 and 20;
- Lacking exons 15 and 16.
Variant B: 2530 bp;
- Including exon 17;
- Lacking exons 16,18, 19 and 20.
Variant A: 2350bp;
- Including exon 15;
- Lackings exons 16 to 20.
Variant C: 2313bp;
- Including exon 16;
- Lacking exons 15 and 17 to 20.

Protein

Note Name: Fibulin-1.
 
Description
PositionLengthDescription
36-7641Anaphylatoxin-like 1
77-11135Anaphylatoxin-like 2
112-14433Anaphylatoxin-like 3
176-21540EGF-like 1
216-26146EGF-like 2; calcium-binding
262-30746EGF-like 3; calcium-binding
308-35548EGF-like 4; calcium-binding
356-39843EGF-like 5; calcium-binding
399-44042EGF-like 6; calcium-binding
441-48040EGF-like 7; calcium-binding
481-52444EGF-like 8; calcium-binding
525-57854EGF-like 9; calcium-binding

Glycosylation98; 535; 539
Disulfide bond36↔61; 37↔68; 50↔69; 78↔109; 91↔110; 112↔136; 113↔143; 126↔144; 180↔190; 186↔199; 201↔214; 220↔233; 227↔242; 248↔260; 266↔279; 273↔288; 294↔306; 312↔325; 319↔334; 341↔354; 360↔373; 367↔382; 384↔397; 403↔415; 411↔424; 426↔439; 445↔454; 450↔463; 465↔479; 485↔498; 494↔507; 509↔523; 529↔542; 536↔551; 556↔577
Amino acid modifications (UNIPROT)

Fibulin-1 homomultimerizes and interacts with various ECM components such as fibronectin (FN) (Balbona et al., 1992), laminin subunits alpha-1 and alpha-2 (LAMA1 and LAMA2), nidogen (NID), Aggrecan core protein (ACAN), versican core protein (CSPG2) and type IV collagen proteins (Timpl et al., 2003). Fibulin-1 also interacts with amyloid beta A4 (APP) (Ohsawa et al., 2001), insulin-like growth factor-binding protein 9 (NOV) (Perbal et al., 1999), fibrinogen (FGB) (Tran et al., 1995), and human papillomavirus (HPV) type 16, 18, 31 proteins (Du et al., 2002).

 
Localisation Secreted, extracellular space, extracellular matrix.
Function Fibulin-1 is incorporated into FN-containing matrix fibers. It plays a role in cell adhesion and migration along protein fibers within the ECM and is important for certain developmental processes. Fibulin-1 contributes to the supramolecular organization of ECM architecture, in particular to that of the basement membrane. It is implicated in cellular transformation and tumor invasion, and can behave both as an oncosuppressor and oncogene depending on tissue environment. It also plays a role in hemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots and plays a significant role in modulating the neurotrophic activities of APP, particularly soluble APP (Timpl et al., 2003).
Homology Paralogs: Latent-transforming growth factor beta-binding protein 1 (LTBP1), LTBP2, LTBP3, LTBP4, fibrillin-1 (FBN1), FBN2, FBN3, FBLN5, fibulin-2 (FBLN2), epidermal growth factor-like protein 6 (EGFL6), nephronectin (NPNT), EGF-containing fibulin-like extracellular matrix protein 2 (EFEMP2), Von Willebrand factor C (VWCE).

Mutations

Note - Location: exon 19 (acceptor splice site)
- Substitution: G-A
- Phenotype: Bernard-Soulier syndrome
 

Implicated in

Note
  
Entity Epithelial cancers
  
  
Entity Various cancers
Note Several studies have reported that fibulin-1 is overexpressed in various human neoplasias and it is implicated in processes such as invasion, motility, and in vivo tumor growth (Du et al., 2002; Greene et al., 2003; Moll et al., 2002; Qing et al., 1997; Twal et al., 2001). Fibulin-1 inhibits in vitro adhesion and motility of various carcinoma cell lines (Twal et al., 2001).
  
  
Entity Breast cancer
Prognosis Fibulin-1 was found aberrantly expressed in ~35% of 528 human primary breast cancers. Its expression is associated with improved survival in patients with lymphoid infiltrate at the tumor site (Pupa et al., 2004), suggesting a possible involvement in triggering a protective antitumor immune response. Fibulin-1 induces specific B- and T-cell-mediated responses in breast cancer patients (Forti et al., 2002; Pupa et al., 2004). Its overexpression can serve as a tool for early detection of breast cancer (Pupa et al., 2002) and acts to promote breast cancer cell survival during doxorubicin treatment (Pupa et al., 2007). In a series of 36 primary breast carcinomas, the expression of mature fibulin-1 polypeptide (100 kDa) did not correlate with estrogen receptor-alpha (ERα) or progesterone receptor (PR) levels, whereas a positive correlation was found between fibulin-1 processing (50 kDa fragment) and ERα and PR protein levels (Greene et al., 2003).
  
  
Entity Ovarian cancer
Disease The molecular mechanisms involved in ovarian carcinogenesis remain unclear, but growing evidence indicates that estrogens promote progression of ovarian cancer and increase expression levels of some secreted proteins. Differential overexpression of ERα versus -ERβ has been demonstrated during ovarian carcinogenesis (Clinton et al., 1996; Moll et al., 2002), suggesting that estrogen-induced proteins, including fibulin-1, may act as ovarian tumor-promoting agents. In ovarian tissues and cancer cell lines, fibulin-1C and -1D are the predominant forms, whereas fibulin-1A and -1B are weakly expressed. An increased fibulin-1C:-1D mRNA ratio in ovarian cancer cells as compared to that in normal ovaries has been observed, suggesting that the C variant is the main one involved in ovarian carcinogenesis. Fibulin-1C overexpression might provide a clue in understanding the putative role of estrogens in ERα-promoted ovarian tumor progression (Moll et al., 2002). In addition, quantitative proteomic analysis integrated with microarray data reveals that fibulin-1 is one of the ECM-related molecules important for chemotherapy response (Pan et al., 2009).
  
  
Entity Hypermethylation of fibulin-1 gene in epithelial cancers
Note It has been previously reported both in gastric and prostate cancer models that Fibulin-1 acts as a tumor suppressor gene and is regulated by promoter hypermethylation (Cheng et al., 2008; Wlazlinski et al., 2007). Very recently, also in hepatocellular carcinoma (HCC) model, a downmodulation of fibulin-1 expression caused by its promoter hypermethylation has been proposed as a marker of HCC progression (Kanda et al., 2011).
  
  
Entity Mesenchymal cancers
  
  
Entity Osteosarcoma
Disease Recently, a distinct gene expression pattern of osteoblastic and non osteoblastic osteosarcoma groups has been proposed. In particular, they found significantly modulated the expression of several genes involved in the formation of extracellular matrix, including fibulin-1, already known to be involved in cell morphology modulation, growth and invasion of sarcoma cells (Qing et al., 1997) and suggest that fibulin-1 could be exploited as potential therapeutic target in the future (Kubista et al., 2011).
  
  
Entity Hematological cancers
  
  
Entity Lymphoma
Disease Using a chemical proteomic approach in Hodgkin Lymphoma (HL), Kischel and coauthors identified several extracellular matrix proteins, including fibulin-1, overexpressed in HL (Kischel et al., 2011). Based on its high expression levels in HL biopsy samples fibulin-1 has been suggested as a potential targets for HL immunotherapy.
  
  
Entity Synpolydactyly
Disease Synpolydactyly is a rare genetic disorder characterized by malformations in the hands and feet, with abnormalities including increased finger and toe numbers and fusion of digits into a single digit. Molecular analysis of the reciprocal chromosomal translocation t(12;22)(p11.2;q13.3) cosegregating with a complex type of synpolydactyly indicated involvement of an alternatively spliced exon of the fibulin-1 gene (FBLN1 located in 22q13.3). Investigation of the possible functional involvement of the fibulin-1 protein in the observed phenotype showed that fibulin-1 is expressed in the ECM in association with the digits in the developing limb (Debeer et al., 2002). Thus, t(12;22) might result in haplo-insufficiency of the fibulin-1D variant, leading to the observed limb malformations.
  
  
Entity Bernard-Soulier syndrome
Disease Bernard-Soulier syndrome is an autosomic-dominant disease that causes alterations of the megakaryocyte/platelet lineage and is characterized by bleeding tendency, giant blood platelets and low platelet counts. An unexpected mutation in the splice acceptor site of fibulin-1 exon 19 was found in affected individuals of the Israeli Fechtner family. In all affected individuals from eight families, expression of fibulin-1 variant D was inhibited by putative antisense RNA (Lanza, 2006), raising the possibility that these autosomal-dominant giant platelet syndromes are associated with aberrant antisense gene regulation of fibulin-1.
  
  
Entity Placenta dysplasia
Disease Placental dysplasia is a rare human placental disorder in which the placenta is enlarged and contains cystic villi and dilated vasculature. A significant correlation was observed between fibulin-1 gene overexpression and murine placental overgrowth (Singh et al., 2006), suggesting that the gene and its product have a functional role in placenta development.
  
  
Entity Morphogenesis of neural crest-derived structures
Disease A significant negative correlation between fibulin-1 gene expression and some morphogenic anomalies of neural crest-derived structures in mice has been reported (Cooley et al., 2008). Such fibulin-1-deficient mice exhibit cardiac ventricular wall thinning and ventricular septal defects, with double outlet right ventricle or overriding aorta, as well as aortic arch arteries anomalies, hypoplasia of the thymus and thyroid, underdeveloped skull bones, malformations of cranial nerves and hemorrhagic blood vessels in the head and neck. The spectrum of malformations is consistent with a role for fibulin-1 in neural crest cell-dependent development of these tissues.
  
  
Entity Acute aortic dissection
Disease Acute aortic dissection (AAD) is a tear in the wall of the aorta that causes blood to flow between the layers of the wall of the aorta and force the layers apart. AAD is a life-threatening condition with high mortality and a mostly unclear pathophysiological mechanism. Downregulation of fibulin-1 noted in AAD compared to control samples might determine a weakening of ECM in the aorta and/or interfere with the transmission of cellular signals causing AAD (Mohamed et al., 2009).
  
  
Entity Atherosclerotic lesions
Disease Fibulin-1 deposits were found in association with fibrinogen in atherosclerotic lesions and in regions containing fresh thrombi. By contrast, fibulin-1 was not detected in sclerotic regions and low levels were associated with smooth muscle cells within and outside lesions (Argraves et al., 2009). Further, an accumulation of fibulin-1 deposits were found in the arterial wall and in plasma of patients with type 2 diabetes and appears to be a factor associated with arterial extracellular matrix alterations (Cangemi et al., 2011).
  
  
Entity Thrombosis
Disease Thrombosis, the formation of a blood clot (thrombus) inside a blood vessel, obstructs blood flow through the circulatory system. Analyses of blood plasma revealed an interaction between fibulin-1 and fibrinogen (Tran et al., 1995), pointing to potential new roles for fibulin-1 in hemostasis as well as thrombosis.
  
  
Entity Infection disease
Note Streptococcus Pyogenes, which belongs to the group A of streptococcus, has been found to interact with the host fibulin 1 through its major serum opacity factor (SOF) receptor that is a major fibronectin binding protein involved in adhesion to host cells. The SOF-fibulin-1 interaction can lead to initial bacterial adhesion (Courtney et al., 2009).
  

Breakpoints

Note Description: Translocation t(12;22)(p11.2;q13.3)
Phenotype: Synpolydactyly
Analysis of a Belgian family with a complex type of synpolydactyly (SPD2) and a t(12;22)(p11.2;q13.3) translocation identified the breakpoints located in the intron between the last 2 exons of the fibulin-1D splice variant isoform (exons 19, 20) and the 5' UTR of the C12ORF2 gene. Fibroblasts derived from the patients displayed decreased levels of ECM-related fibulin-1D secreted into the culture medium, whereas levels of the fibulin-1C variant were normal. The findings are consistent with the notion that the t(12;22)(p11.2;q13.3) translocation results in haplo-insufficiency of the fibulin-1D variant, leading to the observed limb malformations. The authors noted that the entire fibulin-1 gene is deleted in the chromosome 22q13.3 deletion syndrome (Debeer et al 2002).

Bibliography

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Fibulin-1 is a marker for arterial extracellular matrix alterations in type 2 diabetes.
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Fibulin 1 is downregulated through promoter hypermethylation in gastric cancer.
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Estrogens increase the expression of fibulin-1, an extracellular matrix protein secreted by human ovarian cancer cells.
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Fibulin-1 is required for morphogenesis of neural crest-derived structures.
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Serum opacity factor is a streptococcal receptor for the extracellular matrix protein fibulin-1.
Courtney HS, Li Y, Twal WO, Argraves WS.
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PMID 19276078
 
The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated with a complex type of synpolydactyly.
Debeer P, Schoenmakers EF, Twal WO, Argraves WS, De Smet L, Fryns JP, Van De Ven WJ.
J Med Genet. 2002 Feb;39(2):98-104.
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Interaction of oncogenic papillomavirus E6 proteins with fibulin-1.
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Identification of breast cancer-restricted antigens by antibody screening of SKBR3 cDNA library using a preselected patient's serum.
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Elevated expression and altered processing of fibulin-1 protein in human breast cancer.
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Promoter hypermethylation of fibulin 1 gene is associated with tumor progression in hepatocellular carcinoma.
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PMID 11850827
 
Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein and modulates its physiological function.
Ohsawa I, Takamura C, Kohsaka S.
J Neurochem. 2001 Mar;76(5):1411-20.
PMID 11238726
 
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The C-terminal domain of the regulatory protein NOVH is sufficient to promote interaction with fibulin 1C: a clue for a role of NOVH in cell-adhesion signaling.
Perbal B, Martinerie C, Sainson R, Werner M, He B, Roizman B.
Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):869-74.
PMID 9927660
 
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Regulation of breast cancer response to chemotherapy by fibulin-1.
Pupa SM, Giuffre S, Castiglioni F, Bertola L, Cantu M, Bongarzone I, Baldassari P, Mortarini R, Argraves WS, Anichini A, Menard S, Tagliabue E.
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Citation

This paper should be referenced as such :
Castagnoli, L ; Tagliabue, E ; Pupa, SM
FBLN1 (fibulin 1)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(11):796-801.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/FBLN1ID44462ch22q13.html
History of this paper:
Castagnoli, L ; Tagliabue, E ; Pupa, SM. FBLN1 (fibulin 1). Atlas Genet Cytogenet Oncol Haematol. 2011;15(5):450-454.
http://documents.irevues.inist.fr/bitstream/handle/2042/45023/09-2010-FBLN1ID44462ch22q13.pdf

External links

Nomenclature
HGNC (Hugo)FBLN1   3600
Cards
AtlasFBLN1ID44462ch22q13
Entrez_Gene (NCBI)FBLN1  2192  fibulin 1
AliasesFBLN; FIBL1
GeneCards (Weizmann)FBLN1
Ensembl hg19 (Hinxton)ENSG00000077942 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000077942 [Gene_View]  chr22:45502839-45563362 [Contig_View]  FBLN1 [Vega]
ICGC DataPortalENSG00000077942
TCGA cBioPortalFBLN1
AceView (NCBI)FBLN1
Genatlas (Paris)FBLN1
WikiGenes2192
SOURCE (Princeton)FBLN1
Genetics Home Reference (NIH)FBLN1
Genomic and cartography
GoldenPath hg38 (UCSC)FBLN1  -     chr22:45502839-45563362 +  22q13.31   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)FBLN1  -     22q13.31   [Description]    (hg19-Feb_2009)
EnsemblFBLN1 - 22q13.31 [CytoView hg19]  FBLN1 - 22q13.31 [CytoView hg38]
Mapping of homologs : NCBIFBLN1 [Mapview hg19]  FBLN1 [Mapview hg38]
OMIM135820   608180   
Gene and transcription
Genbank (Entrez)AF126110 AF217999 AI092723 AK075460 AK075566
RefSeq transcript (Entrez)NM_001996 NM_006485 NM_006486 NM_006487
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)FBLN1
Cluster EST : UnigeneHs.24601 [ NCBI ]
CGAP (NCI)Hs.24601
Alternative Splicing GalleryENSG00000077942
Gene ExpressionFBLN1 [ NCBI-GEO ]   FBLN1 [ EBI - ARRAY_EXPRESS ]   FBLN1 [ SEEK ]   FBLN1 [ MEM ]
Gene Expression Viewer (FireBrowse)FBLN1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2192
GTEX Portal (Tissue expression)FBLN1
Protein : pattern, domain, 3D structure
UniProt/SwissProtP23142   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP23142  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP23142
Splice isoforms : SwissVarP23142
PhosPhoSitePlusP23142
Domaine pattern : Prosite (Expaxy)ANAPHYLATOXIN_1 (PS01177)    ANAPHYLATOXIN_2 (PS01178)    ASX_HYDROXYL (PS00010)    EGF_2 (PS01186)    EGF_3 (PS50026)    EGF_CA (PS01187)   
Domains : Interpro (EBI)Anaphylatoxin/fibulin    cEGF    EGF-like_Ca-bd_dom    EGF-like_CS    EGF-like_dom    EGF-type_Asp/Asn_hydroxyl_site    EGF_Ca-bd_CS    Fibulin-1    Growth_fac_rcpt_   
Domain families : Pfam (Sanger)cEGF (PF12662)    EGF_CA (PF07645)   
Domain families : Pfam (NCBI)pfam12662    pfam07645   
Domain families : Smart (EMBL)ANATO (SM00104)  EGF (SM00181)  EGF_CA (SM00179)  
Conserved Domain (NCBI)FBLN1
DMDM Disease mutations2192
Blocks (Seattle)FBLN1
SuperfamilyP23142
Human Protein AtlasENSG00000077942
Peptide AtlasP23142
HPRD00629
IPIIPI00296534   IPI00333852   IPI00218803   IPI00296537   IPI01025069   IPI00889740   IPI00413623   IPI00889637   IPI00894386   IPI00894529   IPI00889714   IPI00893821   IPI01010857   IPI00889648   IPI00893588   
Protein Interaction databases
DIP (DOE-UCLA)P23142
IntAct (EBI)P23142
FunCoupENSG00000077942
BioGRIDFBLN1
STRING (EMBL)FBLN1
ZODIACFBLN1
Ontologies - Pathways
QuickGOP23142
Ontology : AmiGOnegative regulation of protein phosphorylation  fibronectin binding  extracellular matrix structural constituent  calcium ion binding  extracellular region  extracellular region  fibrinogen complex  proteinaceous extracellular matrix  basement membrane  extracellular space  negative regulation of cell adhesion  integrin-mediated signaling pathway  embryo implantation  protein C-terminus binding  positive regulation of peptidase activity  viral process  peptidase activator activity  extracellular matrix organization  extracellular matrix  protein complex binding  identical protein binding  fibrinogen binding  extracellular exosome  negative regulation of ERK1 and ERK2 cascade  elastic fiber  blood coagulation, fibrin clot formation  negative regulation of substrate adhesion-dependent cell spreading  negative regulation of cell motility  negative regulation of stem cell proliferation  
Ontology : EGO-EBInegative regulation of protein phosphorylation  fibronectin binding  extracellular matrix structural constituent  calcium ion binding  extracellular region  extracellular region  fibrinogen complex  proteinaceous extracellular matrix  basement membrane  extracellular space  negative regulation of cell adhesion  integrin-mediated signaling pathway  embryo implantation  protein C-terminus binding  positive regulation of peptidase activity  viral process  peptidase activator activity  extracellular matrix organization  extracellular matrix  protein complex binding  identical protein binding  fibrinogen binding  extracellular exosome  negative regulation of ERK1 and ERK2 cascade  elastic fiber  blood coagulation, fibrin clot formation  negative regulation of substrate adhesion-dependent cell spreading  negative regulation of cell motility  negative regulation of stem cell proliferation  
REACTOMEP23142 [protein]
REACTOME PathwaysR-HSA-2129379 [pathway]   
NDEx NetworkFBLN1
Atlas of Cancer Signalling NetworkFBLN1
Wikipedia pathwaysFBLN1
Orthology - Evolution
OrthoDB2192
GeneTree (enSembl)ENSG00000077942
Phylogenetic Trees/Animal Genes : TreeFamFBLN1
HOVERGENP23142
HOGENOMP23142
Homologs : HomoloGeneFBLN1
Homology/Alignments : Family Browser (UCSC)FBLN1
Gene fusions - Rearrangements
Fusion : MitelmanATXN10/FBLN1 [22q13.31/22q13.31]  [t(22;22)(q13;q13)]  
Fusion : MitelmanHACE1/FBLN1 [6q16.3/22q13.31]  [t(6;22)(q16;q13)]  
Fusion : MitelmanPLA2G2A/FBLN1 [1p36.13/22q13.31]  [t(1;22)(p36;q13)]  
Fusion: TCGAATXN10 22q13.31 FBLN1 22q13.31 OV
Fusion: TCGAHACE1 6q16.3 FBLN1 22q13.31 BRCA
Fusion: TCGAPLA2G2A 1p36.13 FBLN1 22q13.31 PRAD
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerFBLN1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)FBLN1
dbVarFBLN1
ClinVarFBLN1
1000_GenomesFBLN1 
Exome Variant ServerFBLN1
ExAC (Exome Aggregation Consortium)FBLN1 (select the gene name)
Genetic variants : HAPMAP2192
Genomic Variants (DGV)FBLN1 [DGVbeta]
DECIPHERFBLN1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisFBLN1 
Mutations
ICGC Data PortalFBLN1 
TCGA Data PortalFBLN1 
Broad Tumor PortalFBLN1
OASIS PortalFBLN1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICFBLN1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDFBLN1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch FBLN1
DgiDB (Drug Gene Interaction Database)FBLN1
DoCM (Curated mutations)FBLN1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)FBLN1 (select a term)
intoGenFBLN1
NCG5 (London)FBLN1
Cancer3DFBLN1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM135820    608180   
Orphanet21044    22922   
MedgenFBLN1
Genetic Testing Registry FBLN1
NextProtP23142 [Medical]
TSGene2192
GENETestsFBLN1
Target ValidationFBLN1
Huge Navigator FBLN1 [HugePedia]
snp3D : Map Gene to Disease2192
BioCentury BCIQFBLN1
ClinGenFBLN1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD2192
Chemical/Pharm GKB GenePA28013
Clinical trialFBLN1
Miscellaneous
canSAR (ICR)FBLN1 (select the gene name)
Probes
Litterature
PubMed93 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineFBLN1
EVEXFBLN1
GoPubMedFBLN1
iHOPFBLN1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Mon Sep 18 17:02:52 CEST 2017
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