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FBLN5 (fibulin 5)

Written2013-05Miao Wang, Rolf A Brekken
Hamon Center for Therapeutic Oncology Research, University of Texas Southwestern Medical Center, 6000 Harry Hines Blvd, Dallas, TX 75390-8593, USA

(Note : for Links provided by Atlas : click)


HGNC Alias symbEVEC
HGNC Alias nameembryonic vascular EGF-like repeat-containing protein
 developmental arteries and neural crest EGF-like
LocusID (NCBI) 10516
Atlas_Id 46779
Location 14q32.12  [Link to chromosome band 14q32]
Location_base_pair Starts at 91869411 and ends at 91947702 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping FBLN5.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
CATSPERB (14q32.12)::FBLN5 (14q32.12)DST (6p12.1)::FBLN5 (14q32.12)EML1 (14q32.2)::FBLN5 (14q32.12)
MARK3 (14q32.32)::FBLN5 (14q32.12)PPP4R3A (14q32.12)::FBLN5 (14q32.12)TC2N (14q32.12)::FBLN5 (14q32.12)
Note Fibulin-5 is a matricellular glycoprotein, belonging to fibulin family which has 7 members (Yanagisawa et al., 2009). Compared with other fibulins, it has a unique arginine-glycine-aspartic acid (RGD) domain in the N-terminal region that mediates binding to integrins (Nakamura et al., 1999). Fibulin-5 is produced and secreted by endothelial cells, fibroblasts and vascular smooth muscle cells. The expression of Fibulin-5 is down-regulated in adult tissue but reactivated upon injury and various disease conditions (Yanagisawa et al., 2009). Fibulin-5 is essential for elastic fiber organization as shown by generation of Fibulin-5 knockout (Fbln5-/-) mice (Nakamura et al., 2002; Yanagisawa et al., 2002) and biochemical analysis (Hirai et al., 2007; Zheng et al., 2007). However, a mouse model with point mutation (D to E) (Fbln5RGE/RGE) in the RGD domain has exhibited intact elastic fibers (Budatha et al., 2011), indicating that Fibulin-5-Integrin interaction is not required for elastic fiber assembly. Fibulin-5 has also been implicated in various pathological conditions including cancer, cutis laxa and age-related macular degeneration.


Description According to Ensembl Genome Browser, human Fbln5 gene locates on Chromosome 14q between region 92335756 and 92414331. This gene has 9 splicing variants transcriptionally. The only one with known protein function has 11 exons and 1347 nucleotides.


  Figure 1: The protein sequence of human Fibulin-5 (source database: UniProt).
Description Fibulin-5 is a secreted protein belonging to the fibulin family. It contains 448 amino acids with an approximate 66-Kda molecular weight. It is mainly produced and secreted by endothelial cells, smooth muscle cells and fibroblasts (Yanagisawa et al., 2009). It has six calcium-binding epidermal growth factor (cb EGF)-like domains, the first one of which contains a RGD motif responsible for cell surface integrin binding.
  Schematic drawing of Fibulin-5 protein. It contains an evolutionally conserved RGD sequence in the first CB-EGF-like (Calcium Binding-Epidermal Growth Factor-like) motif and a fibulin module in the C-terminus of the protein.
Expression The expression of Fibulin-5 is most prominent in embryonic vasculature and neural crest cells and down-regulated in most adult organs (Nakamura et al., 1999). Fibulin-5 mRNA is detected mainly in heart, ovary and colon of adult human tissue (Nakamura et al., 1999). However, Fibulin-5 expression can be reactivated upon tissue injury. It is reported that the expression of Fibulin-5 is elevated in human umbilical vein endothelial cells (HUVEC) by hypoxia in a HIF1α-dependent mechanism (Guadall et al., 2011). Transforming growth factors β (TGF-β) can also increase the expression of Fibulin-5 in human lung fibroblasts (Kuang et al., 2006).
Localisation Matricellular, secreted, extracellular matrix.
Function Fibulin-5 is essential for the assembly of elastic fibers. Biochemical analysis shows that Fibulin-5 preferentially binds to monomeric tropoelastin through N- and C-terminal elastin-binding regions (Zheng et al., 2007). Fbln5-/- mice exhibit severe elastic fibre disorganization throughout the whole body (Nakamura et al., 2002; Yanagisawa et al., 2002). Further studies have shown that Fibulin-5 regulates elastic fiber formation by increasing the efficacy of tropoelastin self-aggregation and cross-linking through direct binding to tropoelastin and lysyl oxidase like Loxl1, Loxl2 and Loxl4 (Yanagisawa et al., 2009). In addition, Fibulin-5 binds cell surface α4β1 and α5β1 integrins, but does not support receptor activation (Lomas et al., 2007). Additionally, Fibulin-5 competes with fibronectin for integrin binding. This competition serves to reduce fibronectin-mediated integrin-induced reactive oxygen species (ROS) generation (Schluterman et al., 2010).



Implicated in

Entity Bladder cancer
Note The expression of Fibulin-5 is downregulated in human bladder carcinoma samples (Hu et al., 2011). Increased proliferation and invasiveness were observed in a bladder cancer cell line with overexpression of Fibulin-5 (Hu et al., 2011).
Entity Breast cancer
Note The role of Fibulin-5 in breast cancer is still controversial. Oncomine database shows the reduction of Fibulin-5 mRNA in breast carcinomas, however, induction of Fibulin-5 expression is detected in breast cancer patient tissue by immunostaining (Lee et al., 2008). In addition, overexpression of Fibulin-5 can enhance tumor growth in an orthotopic mouse model of breast cancer (Lee et al., 2008). Meanwhile, overexpression of Fibulin-5 in breast cancer cells can reduce metastasis to liver and lung (Moller et al., 2011). The discrepancy between these studies could be due to cell line and mouse model differences. Fibulin-5 is also reported to participate in epithelial-mesenchymal-transition (EMT) in breast cancer cell lines in a MMP-dependent manner (Lee et al., 2008). However, the mechanism of Fibulin-5 regulation of MMP is unclear. For example, Fibulin-5 has been shown to inhibit and activate MMP9 activity, (Budatha et al., 2011; Lee et al., 2008; Moller et al., 2011).
Entity Lung cancer
Note Fibulin-5 expression is silenced in multiple lung cancer cell lines and human lung cancer samples by hypermethylation of the promoter region (Yue et al., 2009). Overexpression of Fibulin-5 reduces lung cancer invasion and metastasis through suppression of the MMP-7 expression and ERK phosphorylation (Yue et al., 2009).
Entity Ovarian cancer
Note The expression level of Fibulin-5 correlates inversely with the severity of disease (Wang et al., 2010). Expression of Fibulin-5 is also remarkably decreased in metastatic sites.
Entity Pancreatic cancer
Note Fibulin-5 is required for aggressive tumor growth and angiogenesis in a mouse model of pancreatic cancer (Schluterman et al., 2010). Tumor weight and blood vessel density in Fbln5-/- or Fbln5RGE/RGE mice are significantly reduced compared with wildtype mice in subcutaneous and orthotopic models. Increased level of ROS, DNA damage and apoptotic endothelial cells were detected in tumors grown in Fibulin-5 deficient mice. In vitro analysis identified that Fibulin-5 reduces ROS production in a fibronectin and integrin β1-dependent manner (Schluterman et al., 2010).
Entity Age-related macular degeneration (AMD)
Note DNA sequencing revealed 10 distinct heterozygous missense mutations in Fbln5 in 1-2% of AMD patients (Auer-Grumbach et al., 2011; Lotery et al., 2006; Stone et al., 2004). The underlying biochemical basis of two missense mutations, I169T and G267S was further studied by nuclear magnetic resonance (NMR) and chromophoric calcium chelation experiments. The results show that G267S substitution leads to protein misfolding and inhibition of secretion, but not the I169T substitution (Schneider et al., 2010).
Disease Age-related macular degeneration (AMD) is an eye disease affecting the macula and is the main reason for irreversible version loss in elderly people (Lotery et al., 2006).
Entity Charcot-Marie-Tooth disease (CMT)
Note Missense mutations of Fbln5 were detected in CMT neuropathy patients (Auer-Grumbach et al., 2011).
Disease Charcot-Marie-Tooth disease (CMT) is an autosomal dominantly inherited disorder of peripheral nervous system (Auer-Grumbach et al., 2011). It is characterized by lifelong disabilities because of muscle weakness and loss of touch sensation (Auer-Grumbach et al., 2011).
Entity Cutis laxa
Note Mutations in Fbln5 have been identified in hereditary and acquired forms of cutis laxa. Three homozygous mutations (C217R, S227P and R284X) in Fbln5 have been reported in autosomal recessive cutis laxa patients (Claus et al., 2008; Elahi et al., 2006; Loeys et al., 2002). In addition, a heterozygous in-frame tandem duplication of Fbln5 exon 5-8 has been discovered in a sporadic cutis laxa patient (Markova et al., 2003). Mutational analysis also shows that a cutis laxa patient has a heterozygous missense mutation (G202R) in Fbln5 and compound heterozygous mutation in elastin alleles (A55V and G773D) (Hu et al., 2006b). These findings further support that Fibulin-5 is essential for the formation and maturation of the tropoelastin self-aggregation process, which is required for elastic fiber assembly (Hu et al., 2006a).
Disease Cutis laxa is a connective tissue disorder characterized by loose and redundant skin and multiple internal organ abnormalities due to fragmentation and paucity of elastic fibers.
Entity Pelvic organ prolapse (POP)
Note Lower level expression of Fibulin-5 was identified in patients with POP (Soderberg et al., 2009; Takacs et al., 2009). It is reported that Fibulin-5 can prevent the development of POP by regulating elastic fiber homeostasis and inactivating MMP-9 in the vaginal wall (Budatha et al., 2011).
Disease Pelvic organ prolapse (POP) is a common disease for elder women characterized by loss of pelvic floor support leading to protrusion of pelvic organs like uterus, bladder and vagina.
Entity Thoracic aortic aneurysmal disease (TAD)
Note The expression of aortic Fibulin-5 is significantly decreased in patients with TAD. The low level of Fibulin-5 strongly correlates with disorganization of elastic fibers, which may contribute to aorta abnormality (Wang et al., 2005).
Disease Thoracic aortic aneurysmal disease (TAD) is an aortic disorder characterized by loss of elastin in the wall of aorta (Wang et al., 2005).


Fibulin-5 mutations link inherited neuropathies, age-related macular degeneration and hyperelastic skin.
Auer-Grumbach M, Weger M, Fink-Puches R, Papic L, Frohlich E, Auer-Grumbach P, El Shabrawi-Caelen L, Schabhuttl M, Windpassinger C, Senderek J, Budka H, Trajanoski S, Janecke AR, Haas A, Metze D, Pieber TR, Guelly C.
Brain. 2011 Jun;134(Pt 6):1839-52. doi: 10.1093/brain/awr076. Epub 2011 May 15.
PMID 21576112
Extracellular matrix proteases contribute to progression of pelvic organ prolapse in mice and humans.
Budatha M, Roshanravan S, Zheng Q, Weislander C, Chapman SL, Davis EC, Starcher B, Word RA, Yanagisawa H.
J Clin Invest. 2011 May;121(5):2048-59. doi: 10.1172/JCI45636. Epub 2011 Apr 25.
PMID 21519142
A p.C217R mutation in fibulin-5 from cutis laxa patients is associated with incomplete extracellular matrix formation in a skin equivalent model.
Claus S, Fischer J, Megarbane H, Megarbane A, Jobard F, Debret R, Peyrol S, Saker S, Devillers M, Sommer P, Damour O.
J Invest Dermatol. 2008 Jun;128(6):1442-50. doi: 10.1038/sj.jid.5701211. Epub 2008 Jan 10.
PMID 18185537
Homozygous missense mutation in fibulin-5 in an Iranian autosomal recessive cutis laxa pedigree and associated haplotype.
Elahi E, Kalhor R, Banihosseini SS, Torabi N, Pour-Jafari H, Houshmand M, Amini SS, Ramezani A, Loeys B.
J Invest Dermatol. 2006 Jul;126(7):1506-9. Epub 2006 May 11.
PMID 16691202
Fibulin-5 is up-regulated by hypoxia in endothelial cells through a hypoxia-inducible factor-1 (HIF-1α)-dependent mechanism.
Guadall A, Orriols M, Rodriguez-Calvo R, Calvayrac O, Crespo J, Aledo R, Martinez-Gonzalez J, Rodriguez C.
J Biol Chem. 2011 Mar 4;286(9):7093-103. doi: 10.1074/jbc.M110.162917. Epub 2010 Dec 30.
PMID 21193390
Fibulin-5/DANCE has an elastogenic organizer activity that is abrogated by proteolytic cleavage in vivo.
Hirai M, Ohbayashi T, Horiguchi M, Okawa K, Hagiwara A, Chien KR, Kita T, Nakamura T.
J Cell Biol. 2007 Mar 26;176(7):1061-71. Epub 2007 Mar 19.
PMID 17371835
Fibulin-5 mutations: mechanisms of impaired elastic fiber formation in recessive cutis laxa.
Hu Q, Loeys BL, Coucke PJ, De Paepe A, Mecham RP, Choi J, Davis EC, Urban Z.
Hum Mol Genet. 2006a Dec 1;15(23):3379-86. Epub 2006 Oct 11.
PMID 17035250
Inflammatory destruction of elastic fibers in acquired cutis laxa is associated with missense alleles in the elastin and fibulin-5 genes.
Hu Q, Reymond JL, Pinel N, Zabot MT, Urban Z.
J Invest Dermatol. 2006b Feb;126(2):283-90.
PMID 16374472
Fibulin-5 is down-regulated in urothelial carcinoma of bladder and inhibits growth and invasion of human bladder cancer cell line 5637.
Hu Z, Ai Q, Xu H, Ma X, Li HZ, Shi TP, Wang C, Gong DJ, Zhang X.
Urol Oncol. 2011 Jul-Aug;29(4):430-5. doi: 10.1016/j.urolonc.2009.06.004. Epub 2009 Sep 19.
PMID 19767220
Fibulin-5 gene expression in human lung fibroblasts is regulated by TGF-beta and phosphatidylinositol 3-kinase activity.
Kuang PP, Joyce-Brady M, Zhang XH, Jean JC, Goldstein RH.
Am J Physiol Cell Physiol. 2006 Dec;291(6):C1412-21. Epub 2006 Jul 12.
PMID 16837650
Fibulin-5 initiates epithelial-mesenchymal transition (EMT) and enhances EMT induced by TGF-beta in mammary epithelial cells via a MMP-dependent mechanism.
Lee YH, Albig AR, Regner M, Schiemann BJ, Schiemann WP.
Carcinogenesis. 2008 Dec;29(12):2243-51. doi: 10.1093/carcin/bgn199. Epub 2008 Aug 19.
PMID 18713838
Homozygosity for a missense mutation in fibulin-5 (FBLN5) results in a severe form of cutis laxa.
Loeys B, Van Maldergem L, Mortier G, Coucke P, Gerniers S, Naeyaert JM, De Paepe A.
Hum Mol Genet. 2002 Sep 1;11(18):2113-8.
PMID 12189163
Fibulin-5 binds human smooth-muscle cells through alpha5beta1 and alpha4beta1 integrins, but does not support receptor activation.
Lomas AC, Mellody KT, Freeman LJ, Bax DV, Shuttleworth CA, Kielty CM.
Biochem J. 2007 Aug 1;405(3):417-28.
PMID 17472576
Reduced secretion of fibulin 5 in age-related macular degeneration and cutis laxa.
Lotery AJ, Baas D, Ridley C, Jones RP, Klaver CC, Stone E, Nakamura T, Luff A, Griffiths H, Wang T, Bergen AA, Trump D.
Hum Mutat. 2006 Jun;27(6):568-74.
PMID 16652333
Genetic heterogeneity of cutis laxa: a heterozygous tandem duplication within the fibulin-5 (FBLN5) gene.
Markova D, Zou Y, Ringpfeil F, Sasaki T, Kostka G, Timpl R, Uitto J, Chu ML.
Am J Hum Genet. 2003 Apr;72(4):998-1004. Epub 2003 Feb 28.
PMID 12618961
Role of fibulin-5 in metastatic organ colonization.
Moller HD, Ralfkjaer U, Cremers N, Frankel M, Pedersen RT, Klingelhofer J, Yanagisawa H, Grigorian M, Guldberg P, Sleeman J, Lukanidin E, Ambartsumian N.
Mol Cancer Res. 2011 May;9(5):553-63. doi: 10.1158/1541-7786.MCR-11-0093. Epub 2011 Mar 31.
PMID 21454378
Fibulin-5/DANCE is essential for elastogenesis in vivo.
Nakamura T, Lozano PR, Ikeda Y, Iwanaga Y, Hinek A, Minamisawa S, Cheng CF, Kobuke K, Dalton N, Takada Y, Tashiro K, Ross Jr J, Honjo T, Chien KR.
Nature. 2002 Jan 10;415(6868):171-5.
PMID 11805835
Loss of fibulin-5 binding to beta1 integrins inhibits tumor growth by increasing the level of ROS.
Schluterman MK, Chapman SL, Korpanty G, Ozumi K, Fukai T, Yanagisawa H, Brekken RA.
Dis Model Mech. 2010 May-Jun;3(5-6):333-42. doi: 10.1242/dmm.003707. Epub 2010 Mar 2.
PMID 20197418
Biophysical characterisation of fibulin-5 proteins associated with disease.
Schneider R, Jensen SA, Whiteman P, McCullagh JS, Redfield C, Handford PA.
J Mol Biol. 2010 Aug 27;401(4):605-17. doi: 10.1016/j.jmb.2010.06.039. Epub 2010 Jun 25.
PMID 20599547
Gene expressions of small leucine-rich repeat proteoglycans and fibulin-5 are decreased in pelvic organ prolapse.
Soderberg MW, Bystrom B, Kalamajski S, Malmstrom A, Ekman-Ordeberg G.
Mol Hum Reprod. 2009 Apr;15(4):251-7. doi: 10.1093/molehr/gap011. Epub 2009 Feb 27.
PMID 19251763
Missense variations in the fibulin 5 gene and age-related macular degeneration.
Stone EM, Braun TA, Russell SR, Kuehn MH, Lotery AJ, Moore PA, Eastman CG, Casavant TL, Sheffield VC.
N Engl J Med. 2004 Jul 22;351(4):346-53.
PMID 15269314
Fibulin-5 expression is decreased in women with anterior vaginal wall prolapse.
Takacs P, Nassiri M, Viciana A, Candiotti K, Fornoni A, Medina CA.
Int Urogynecol J Pelvic Floor Dysfunct. 2009 Feb;20(2):207-11. doi: 10.1007/s00192-008-0757-x. Epub 2008 Nov 7.
PMID 18989607
[Expression of EVEC in ovarian carcinoma and its biological significance].
Wang Q, Li XG, Zhang Y, Cao LQ, Deng ZH, Chen Y.
Zhonghua Zhong Liu Za Zhi. 2010 Sep;32(9):676-80.
PMID 21122382
Decreased expression of fibulin-5 correlates with reduced elastin in thoracic aortic dissection.
Wang X, LeMaire SA, Chen L, Carter SA, Shen YH, Gan Y, Bartsch H, Wilks JA, Utama B, Ou H, Thompson RW, Coselli JS, Wang XL.
Surgery. 2005 Aug;138(2):352-9.
PMID 16153447
Fibulin-5 is an elastin-binding protein essential for elastic fibre development in vivo.
Yanagisawa H, Davis EC, Starcher BC, Ouchi T, Yanagisawa M, Richardson JA, Olson EN.
Nature. 2002 Jan 10;415(6868):168-71.
PMID 11805834
Fibulin-5 suppresses lung cancer invasion by inhibiting matrix metalloproteinase-7 expression.
Yue W, Sun Q, Landreneau R, Wu C, Siegfried JM, Yu J, Zhang L.
Cancer Res. 2009 Aug 1;69(15):6339-46. doi: 10.1158/0008-5472.CAN-09-0398. Epub 2009 Jul 7.
PMID 19584278
Molecular analysis of fibulin-5 function during de novo synthesis of elastic fibers.
Zheng Q, Davis EC, Richardson JA, Starcher BC, Li T, Gerard RD, Yanagisawa H.
Mol Cell Biol. 2007 Feb;27(3):1083-95. Epub 2006 Nov 27.
PMID 17130242


This paper should be referenced as such :
Wang, M ; Brekken, RA
FBLN5 (fibulin 5)
Atlas Genet Cytogenet Oncol Haematol. 2013;17(12):811-815.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)FBLN5   3602
LRG (Locus Reference Genomic)LRG_364
Entrez_Gene (NCBI)FBLN5    fibulin 5
GeneCards (Weizmann)FBLN5
Ensembl hg19 (Hinxton)ENSG00000140092 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000140092 [Gene_View]  ENSG00000140092 [Sequence]  chr14:91869411-91947702 [Contig_View]  FBLN5 [Vega]
ICGC DataPortalENSG00000140092
TCGA cBioPortalFBLN5
Genatlas (Paris)FBLN5
SOURCE (Princeton)FBLN5
Genetics Home Reference (NIH)FBLN5
Genomic and cartography
GoldenPath hg38 (UCSC)FBLN5  -     chr14:91869411-91947702 -  14q32.12   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)FBLN5  -     14q32.12   [Description]    (hg19-Feb_2009)
GoldenPathFBLN5 - 14q32.12 [CytoView hg19]  FBLN5 - 14q32.12 [CytoView hg38]
Genome Data Viewer NCBIFBLN5 [Mapview hg19]  
OMIM219100   604580   608895   614434   
Gene and transcription
Genbank (Entrez)AA812956 AF093118 AF112152 AJ133490 AK074540
RefSeq transcript (Entrez)NM_001384158 NM_001384159 NM_001384160 NM_001384161 NM_001384162 NM_006329
Consensus coding sequences : CCDS (NCBI)FBLN5
Gene ExpressionFBLN5 [ NCBI-GEO ]   FBLN5 [ EBI - ARRAY_EXPRESS ]   FBLN5 [ SEEK ]   FBLN5 [ MEM ]
Gene Expression Viewer (FireBrowse)FBLN5 [ Firebrowse - Broad ]
GenevisibleExpression of FBLN5 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)10516
GTEX Portal (Tissue expression)FBLN5
Human Protein AtlasENSG00000140092-FBLN5 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9UBX5   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9UBX5  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9UBX5
Domaine pattern : Prosite (Expaxy)ASX_HYDROXYL (PS00010)    EGF_2 (PS01186)    EGF_3 (PS50026)    EGF_CA (PS01187)   
Domains : Interpro (EBI)cEGF    EGF-like_Ca-bd_dom    EGF-like_dom    EGF-type_Asp/Asn_hydroxyl_site    EGF_Ca-bd_CS    Fibulin-5    Growth_fac_rcpt_cys_sf   
Domain families : Pfam (Sanger)cEGF (PF12662)    EGF_CA (PF07645)   
Domain families : Pfam (NCBI)pfam12662    pfam07645   
Domain families : Smart (EMBL)EGF (SM00181)  EGF_CA (SM00179)  
Conserved Domain (NCBI)FBLN5
AlphaFold pdb e-kbQ9UBX5   
Human Protein Atlas [tissue]ENSG00000140092-FBLN5 [tissue]
Protein Interaction databases
IntAct (EBI)Q9UBX5
Ontologies - Pathways
Ontology : AmiGOregulation of cell growth  integrin binding  calcium ion binding  protein binding  extracellular region  extracellular region  extracellular space  cell-matrix adhesion  protein C-terminus binding  extracellular matrix constituent conferring elasticity  extracellular matrix organization  extracellular matrix  protein localization to cell surface  protein homodimerization activity  secretion  elastic fiber assembly  elastic fiber assembly  elastic fiber assembly  collagen-containing extracellular matrix  collagen-containing extracellular matrix  collagen-containing extracellular matrix  extracellular exosome  elastic fiber  regulation of removal of superoxide radicals  
Ontology : EGO-EBIregulation of cell growth  integrin binding  calcium ion binding  protein binding  extracellular region  extracellular region  extracellular space  cell-matrix adhesion  protein C-terminus binding  extracellular matrix constituent conferring elasticity  extracellular matrix organization  extracellular matrix  protein localization to cell surface  protein homodimerization activity  secretion  elastic fiber assembly  elastic fiber assembly  elastic fiber assembly  collagen-containing extracellular matrix  collagen-containing extracellular matrix  collagen-containing extracellular matrix  extracellular exosome  elastic fiber  regulation of removal of superoxide radicals  
REACTOMEQ9UBX5 [protein]
REACTOME PathwaysR-HSA-2129379 [pathway]   
NDEx NetworkFBLN5
Atlas of Cancer Signalling NetworkFBLN5
Wikipedia pathwaysFBLN5
Orthology - Evolution
GeneTree (enSembl)ENSG00000140092
Phylogenetic Trees/Animal Genes : TreeFamFBLN5
Homologs : HomoloGeneFBLN5
Homology/Alignments : Family Browser (UCSC)FBLN5
Gene fusions - Rearrangements
Fusion : MitelmanCATSPERB::FBLN5 [14q32.12/14q32.12]  
Fusion : MitelmanDST::FBLN5 [6p12.1/14q32.12]  
Fusion : MitelmanEML1::FBLN5 [14q32.2/14q32.12]  
Fusion : MitelmanMARK3::FBLN5 [14q32.32/14q32.12]  
Fusion : MitelmanSMEK1::14q32.12 [FBLN5/t(14;14)(q32;q32)]  
Fusion : MitelmanTC2N::FBLN5 [14q32.12/14q32.12]  
Fusion : QuiverFBLN5
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerFBLN5 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)FBLN5
Exome Variant ServerFBLN5
GNOMAD BrowserENSG00000140092
Varsome BrowserFBLN5
ACMGFBLN5 variants
Genomic Variants (DGV)FBLN5 [DGVbeta]
DECIPHERFBLN5 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisFBLN5 
ICGC Data PortalFBLN5 
TCGA Data PortalFBLN5 
Broad Tumor PortalFBLN5
OASIS PortalFBLN5 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICFBLN5  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DFBLN5
Mutations and Diseases : HGMDFBLN5
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)FBLN5
DoCM (Curated mutations)FBLN5
CIViC (Clinical Interpretations of Variants in Cancer)FBLN5
NCG (London)FBLN5
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM219100    604580    608895    614434   
Orphanet20480    12024    12025   
Genetic Testing Registry FBLN5
NextProtQ9UBX5 [Medical]
Target ValidationFBLN5
Huge Navigator FBLN5 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDFBLN5
Pharm GKB GenePA28015
Clinical trialFBLN5
DataMed IndexFBLN5
PubMed123 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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