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FBLN1 (fibulin 1)

Written2012-05Lorenzo 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
This article is an update of :
2010-09Lorenzo 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

(Note : for Links provided by Atlas : click)


HGNC Alias symbFBLN
LocusID (NCBI) 2192
Atlas_Id 44462
Location 22q13.31  [Link to chromosome band 22q13]
Location_base_pair Starts at 45502883 and ends at 45558712 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping FBLN1.png]
Local_order Orientation: plus strand.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
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).


  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.


Note Name: Fibulin-1.
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).


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

Implicated in

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).


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).


Fibulin-1 and fibrinogen in human atherosclerotic lesions.
Argraves WS, Tanaka A, Smith EP, Twal WO, Argraves KM, Fan D, Haudenschild CC.
Histochem Cell Biol. 2009 Nov;132(5):559-65. Epub 2009 Aug 20.
PMID 19693531
Fibulin-1 is a marker for arterial extracellular matrix alterations in type 2 diabetes.
Cangemi C, Skov V, Poulsen MK, Funder J, Twal WO, Gall MA, Hjortdal V, Jespersen ML, Kruse TA, Aagard J, Parving HH, Knudsen S, Hoilund-Carlsen PF, Rossing P, Henriksen JE, Argraves WS, Rasmussen LM.
Clin Chem. 2011 Nov;57(11):1556-65. Epub 2011 Sep 16.
PMID 21926180
Fibulin 1 is downregulated through promoter hypermethylation in gastric cancer.
Cheng YY, Jin H, Liu X, Siu JM, Wong YP, Ng EK, Yu J, Leung WK, Sung JJ, Chan FK.
Br J Cancer. 2008 Dec 16;99(12):2083-7. Epub 2008 Nov 4.
PMID 18985039
Estrogens increase the expression of fibulin-1, an extracellular matrix protein secreted by human ovarian cancer cells.
Clinton GM, Rougeot C, Derancourt J, Roger P, Defrenne A, Godyna S, Argraves WS, Rochefort H.
Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):316-20.
PMID 8552629
Fibulin-1 is required for morphogenesis of neural crest-derived structures.
Cooley MA, Kern CB, Fresco VM, Wessels A, Thompson RP, McQuinn TC, Twal WO, Mjaatvedt CH, Drake CJ, Argraves WS.
Dev Biol. 2008 Jul 15;319(2):336-45. Epub 2008 May 3.
PMID 18538758
Serum opacity factor is a streptococcal receptor for the extracellular matrix protein fibulin-1.
Courtney HS, Li Y, Twal WO, Argraves WS.
J Biol Chem. 2009 May 8;284(19):12966-71. Epub 2009 Mar 10.
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.
PMID 11836357
Interaction of oncogenic papillomavirus E6 proteins with fibulin-1.
Du M, Fan X, Hong E, Chen JJ.
Biochem Biophys Res Commun. 2002 Aug 30;296(4):962-9.
PMID 12200142
Identification of breast cancer-restricted antigens by antibody screening of SKBR3 cDNA library using a preselected patient's serum.
Forti S, Scanlan MJ, Invernizzi A, Castiglioni F, Pupa S, Agresti R, Fontanelli R, Morelli D, Old LJ, Pupa SM, Menard S.
Breast Cancer Res Treat. 2002 Jun;73(3):245-56.
PMID 12160330
Elevated expression and altered processing of fibulin-1 protein in human breast cancer.
Greene LM, Twal WO, Duffy MJ, McDermott EW, Hill AD, O'Higgins NJ, McCann AH, Dervan PA, Argraves WS, Gallagher WM.
Br J Cancer. 2003 Mar 24;88(6):871-8.
PMID 12644824
Promoter hypermethylation of fibulin 1 gene is associated with tumor progression in hepatocellular carcinoma.
Kanda M, Nomoto S, Okamura Y, Hayashi M, Hishida M, Fujii T, Nishikawa Y, Sugimoto H, Takeda S, Nakao A.
Mol Carcinog. 2011 Aug;50(8):571-9. doi: 10.1002/mc.20735. Epub 2011 Jan 25.
PMID 21268132
Identification of stromal proteins overexpressed in nodular sclerosis Hodgkin lymphoma.
Kischel P, Waltregny D, Greffe Y, Mazzucchelli G, De Pauw E, de Leval L, Castronovo V.
Proteome Sci. 2011 Oct 5;9(1):63.
PMID 21975223
Microarray analysis identifies distinct gene expression profiles associated with histological subtype in human osteosarcoma.
Kubista B, Klinglmueller F, Bilban M, Pfeiffer M, Lass R, Giurea A, Funovics PT, Toma C, Dominkus M, Kotz R, Thalhammer T, Trieb K, Zettl T, Singer CF.
Int Orthop. 2011 Mar;35(3):401-11. Epub 2010 Mar 26.
PMID 20340016
Bernard-Soulier syndrome (hemorrhagiparous thrombocytic dystrophy).
Lanza F.
Orphanet J Rare Dis. 2006 Nov 16;1:46. (REVIEW)
PMID 17109744
Pathway analysis of differentially expressed genes in patients with acute aortic dissection.
Mohamed SA, Sievers HH, Hanke T, Richardt D, Schmidtke C, Charitos EI, Belge G, Bullerdiek J.
Biomark Insights. 2009 May 6;4:81-90.
PMID 19652764
Estrogen induction and overexpression of fibulin-1C mRNA in ovarian cancer cells.
Moll F, Katsaros D, Lazennec G, Hellio N, Roger P, Giacalone PL, Chalbos D, Maudelonde T, Rochefort H, Pujol P.
Oncogene. 2002 Feb 7;21(7):1097-107.
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
Quantitative proteomics analysis integrated with microarray data reveals that extracellular matrix proteins, catenins, and p53 binding protein 1 are important for chemotherapy response in ovarian cancers.
Pan S, Cheng L, White JT, Lu W, Utleg AG, Yan X, Urban ND, Drescher CW, Hood L, Lin B.
OMICS. 2009 Aug;13(4):345-54.
PMID 19422301
Complete exon-intron organization of the mouse fibulin-1 gene and its comparison with the human fibulin-1 gene.
Pan TC, Kostka G, Zhang RZ, Timpl R, Chu ML.
FEBS Lett. 1999 Feb 5;444(1):38-42.
PMID 10037144
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
Immunological and pathobiological roles of fibulin-1 in breast cancer.
Pupa SM, Argraves WS, Forti S, Casalini P, Berno V, Agresti R, Aiello P, Invernizzi A, Baldassari P, Twal WO, Mortarini R, Anichini A, Menard S.
Oncogene. 2004 Mar 18;23(12):2153-60.
PMID 14691454
Humoral immune response for early diagnosis of breast carcinoma.
Pupa SM, Forti S, Balsari A, Menard S.
Ann Oncol. 2002 Mar;13(3):483.
PMID 11996483
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.
Cancer Res. 2007 May 1;67(9):4271-7.
PMID 17483339
Suppression of anchorage-independent growth and matrigel invasion and delayed tumor formation by elevated expression of fibulin-1D in human fibrosarcoma-derived cell lines.
Qing J, Maher VM, Tran H, Argraves WS, Dunstan RW, McCormick JJ.
Oncogene. 1997 Oct;15(18):2159-68.
PMID 9393974
Expression and functional analysis of fibulin-1 (Fbln1) during normal and abnormal placental development of the mouse.
Singh U, Sun T, Larsson T, Elliott RW, Kostka G, Fundele RH.
Placenta. 2006 Sep-Oct;27(9-10):1014-21. Epub 2005 Dec 9.
PMID 16338003
Fibulins: a versatile family of extracellular matrix proteins.
Timpl R, Sasaki T, Kostka G, Chu ML.
Nat Rev Mol Cell Biol. 2003 Jun;4(6):479-89.
PMID 12778127
The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis.
Tran H, Tanaka A, Litvinovich SV, Medved LV, Haudenschild CC, Argraves WS.
J Biol Chem. 1995 Aug 18;270(33):19458-64.
PMID 7642629
Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility.
Twal WO, Czirok A, Hegedus B, Knaak C, Chintalapudi MR, Okagawa H, Sugi Y, Argraves WS.
J Cell Sci. 2001 Dec;114(Pt 24):4587-98.
PMID 11792823
Downregulation of several fibulin genes in prostate cancer.
Wlazlinski A, Engers R, Hoffmann MJ, Hader C, Jung V, Muller M, Schulz WA.
Prostate. 2007 Dec 1;67(16):1770-80.
PMID 17929269
Fibulins: multiple roles in matrix structures and tissue functions.
de Vega S, Iwamoto T, Yamada Y.
Cell Mol Life Sci. 2009 Jun;66(11-12):1890-902. (REVIEW)
PMID 19189051


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 ]
History of this paper:
Castagnoli, L ; Tagliabue, E ; Pupa, SM. FBLN1 (fibulin 1). Atlas Genet Cytogenet Oncol Haematol. 2011;15(5):450-454.

External links

HGNC (Hugo)FBLN1   3600
Entrez_Gene (NCBI)FBLN1    fibulin 1
AliasesFBLN; FIBL1
GeneCards (Weizmann)FBLN1
Ensembl hg19 (Hinxton)ENSG00000077942 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000077942 [Gene_View]  ENSG00000077942 [Sequence]  chr22:45502883-45558712 [Contig_View]  FBLN1 [Vega]
ICGC DataPortalENSG00000077942
TCGA cBioPortalFBLN1
Genatlas (Paris)FBLN1
SOURCE (Princeton)FBLN1
Genetics Home Reference (NIH)FBLN1
Genomic and cartography
GoldenPath hg38 (UCSC)FBLN1  -     chr22:45502883-45558712 +  22q13.31   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)FBLN1  -     22q13.31   [Description]    (hg19-Feb_2009)
GoldenPathFBLN1 - 22q13.31 [CytoView hg19]  FBLN1 - 22q13.31 [CytoView hg38]
Genome Data Viewer NCBIFBLN1 [Mapview hg19]  
OMIM135820   608180   
Gene and transcription
Genbank (Entrez)AF126110 AF217999 AI092723 AK075460 AK075566
RefSeq transcript (Entrez)NM_001996 NM_006485 NM_006486 NM_006487
Consensus coding sequences : CCDS (NCBI)FBLN1
Gene ExpressionFBLN1 [ NCBI-GEO ]   FBLN1 [ EBI - ARRAY_EXPRESS ]   FBLN1 [ SEEK ]   FBLN1 [ MEM ]
Gene Expression Viewer (FireBrowse)FBLN1 [ Firebrowse - Broad ]
GenevisibleExpression of FBLN1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2192
GTEX Portal (Tissue expression)FBLN1
Human Protein AtlasENSG00000077942-FBLN1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Conserved Domain (NCBI)FBLN1
Human Protein Atlas [tissue]ENSG00000077942-FBLN1 [tissue]
Protein Interaction databases
Ontologies - Pathways
PubMed122 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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