FSTL3 (follistatin-like 3 (secreted glycoprotein))

Written2009-01Michael Grusch
Medical University of Vienna, Department of Medicine I, Institute of Cancer Research, Borschkegasse 8a, A-1090 Vienna, Austria
Updated2012-09Michael Grusch
Medical University of Vienna, Department of Medicine I, Institute of Cancer Research, Borschkegasse 8a, A-1090 Vienna, Austria

(Note : for Links provided by Atlas : click)

1. Identity

General Information
Alias_symbol (synonym)FLRG
Other alias
LocusID (NCBI) 10272
Atlas_Id 111
Location 19p13.3  [Link to chromosome band 19p13]
Location_base_pair Starts at 676389 and ends at 683392 bp from pter ( according to hg19-Feb_2009)  [Mapping FSTL3.png]
Local_order RNF126 (ring finger protein 126) - FSTL3 - PRSSL1 (protease, serine-like 1).
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
CCND1 (11q13.3) / FSTL3 (19p13.3)FSTL3 (19p13.3) / BCL6 (3q27.3)FSTL3 (19p13.3) / CCND1 (11q13.3)
FSTL3 (19p13.3) / FSTL3 (19p13.3)FSTL3 (19p13.3) / SCARNA2 (1p13.3)MKL2 (16p13.12) / FSTL3 (19p13.3)
Note The term follistatin-related protein has been used to refer to either FSTL3 (FSRP) or FSTL1 (FRP), which may cause some confusion. A search in MEDLINE for FSTL3 will also retrieve several reports not mentioning FSTL3 but dealing with FRP/FSTL1 instead.


  Intron/exon structure of the FSTL3 gene and domain architecture of FSTL3 protein. 1,2,3,4,5: exon number; SP: signal peptide; NTD: N-terminal domain; FSD 1: follistatin domain 1; FSD 2: follistatin domain 2; AT: acidic tail.
Description The human FSTL3 gene is comprised of five exons spanning 7004 bp on chromosome 19p13 and gives rise to a main transcript of 2525 bp. The first exon encodes the signal peptide plus nine residues of the N-terminal domain, the second exon encodes the remainder of the N-terminal domain, the third and the fourth exon each code for a follistatin module and the fifth exon encodes the C-terminus rich in acidic amino acids (Schneyer et al., 2001; Sidis et al., 2002).
Transcription Transcription of FSTL3 mRNA was shown to be stimulated by TGF beta and activin A via Smad proteins (Bartholin et al., 2001; Bartholin et al., 2002), which seems to be part of a negative feedback loop as FSTL3 can antagonize activin A (see below). In a different study it was found that GDF9 - another TGF beta superfamily cytokine - can suppress both basal and activin A-induced FSTL3 (and follistatin) mRNA and protein levels in cultured human granulosa-lutein (hGL) cells from women undergoing in vitro fertilization (IVF) treatment (Shi et al., 2011). In addition NF-kappaB responsive elements have been identified in the FSTL3 promoter and are involved in the cooperative stimulation of FSTL3 transcription by TNF alpha and TGF beta (Bartholin et al., 2007). Upregulation of FSTL3 mRNA was observed as a response to hypoxia in human trophoblasts and a role for hypoxia inducible factor (HIF1 alpha) was suggested. In another study a combination of 17 beta estradiol and progesterone, but not either factor alone, stimulated FSTL3 expression in cultured human endometrial stromal cells (Wang et al., 2003). An analysis of the murine FSTL3 promoter identified phorbol 12-myristate 13-acetate (PMA) but not cAMP as transcriptional activators.

3. Protein

Description The FSTL3 protein precursor consists of 263 amino acids. Amino acids 1-26 form the signal peptide, which is reponsible for directing the protein to the secretory pathway but not present in the mature secreted protein. FSTL3 has been described to contain 2 follistatin (FS) domains (aa 97-168 and 169-244) (Schneyer et al., 2001) characterized by a conserved arrangement of 10 cysteine residues. The FS domains also have similarity with the Kazal domains found in multiple serine protease inhibitors. The FSTL3 protein contains two potential N-glycosilation sites on asparagines 73 and 215. Peptide N-glycosidase F digestion reduced the size of ectopically expressed FSTL3 from 33 to 27 kDa in Western analysis (Hayette et al., 1998).
Expression FSTL3 is expressed in a wide variety of tissues and organs with the highest expression in placenta and testis and low to absent expression in the hematopoietic system (Hayette et al., 1998; Tortoriello et al., 2001).
Localisation The signal peptide directs the nascent protein to the secretory pathway and FSTL3 has been detected in cell culture supernatants and in human serum (Hayette et al., 1998; Hill et al., 2002; Pryor-Koishi et al., 2007). In addition to its role as a secreted protein FSTL3 has also been found in the cell nucleus in a number of different cell lines, primary cells (Tortoriello et al., 2001) and tissue sections (Torres et al., 2007). Nuclear FSTL3 was glycosylated, albeit to a lower degree than secreted FSTL3, suggesting that it enters the nucleus after partial processing in the ER (Saito et al., 2005).
Function Similar to follistatin, secreted FSTL3 was shown to bind activin A and with lower affinity several other members of the TGF beta family including activin B, myostatin and BMP2, BMP6, and BMP7 (but excluding for instance TGF beta and BMP4) (Tsuchida et al., 2000; Tortoriello et al., 2001; Sidis et al., 2002; Hill et al., 2002; Schneyer et al., 2003). Affinity for BMPs, however, seems to be quite low and has been questioned by other studies (Sidis et al., 2006). FSTL3 bound ligands are unable to activate their cognate receptors and thus FSTL3 blocks signal transduction. Structural and biochemical data have implicated the N-terminal domain and the two FS domains in ligand binding and antagonism (Sidis et al., 2005; Stamler et al., 2008; Cash et al., 2012).
In contrast to follistatin, FSTL3 does not contain a heparin binding motif and does not bind cell surface heparan-sulfate proteoglycans (Sidis et al., 2002).
In addition to binding TGF beta family ligands, FSTL3 was demonstrated to interact with ADAM12 (a disintegrin and metalloprotease 12), an extracellular protein that has been implicated in insulin-like growth factor (IGF) and epidermal growth factor (EGF) receptor signaling (Bartholin et al., 2005), as well as with fibronectin type 1, which could indicate a role of FSTL3 in cell adhesion (Maguer-Satta et al., 2006).
Nuclear FSTL3 was shown to interact with AF10 (ALL-1 fused gene from chromosome 10) enhancing its homo-oligomerization and transcriptional activity (Forissier et al., 2007).
FSTL3 knock-out mice had increased pancreatic island number and size, enhanced insulin sensitivity and hepatic steatosis suggesting a role of FSTL3 in glucose and fat homeostasis (Mukherjee et al., 2007). Combined knockout of FSTL3 and follistatin, however, led to increased fat mass and insulin resistance despite elevated insulin production (Brown et al., 2011).
Homology FSTL3 has a similar domain architecture as follistatin, but harbours only two instead of three follistatin modules (Tortoriello et al., 2001). Follistatin modules are found in varying numbers in a wider set of secreted proteins including FSTL1, SPARC/osteonectin, or agrin (Ullman and Perkins, 1997). With respect to activin binding ability, functional homology among follistatin domain-containing proteins has only been demonstrated for FSTL3 and follistatin (Tsuchida et al., 2000). Between different species FSTL3 is clearly conserved (96% amino acid identity between mouse and rat and about 80% for either of these species compared to human), albeit to a lesser degree than follistatin, which has around 97% amino acid identity between human, mouse and rat.

4. Mutations

Somatic A t(11;19)(q13;p13) translocation has been described in a case of B-cell chronic lymphocytic leukemia. The chromosomal breakpoint occurred about 7 kbp upstream of FSTL3 leading to ectopic expression of the complete FSTL3 protein, likely as a consequence of altered upstream cis-regulatory sequences (Hayette et al., 1998). In the same study structural rearrangement of the FSTL3 locus has also been described in a case of non-Hodgkin lymphoma.
A deletion of about 1.2 Mb on chromosome 19p13.3 was identified in a patient with cleft palate, hearing impairment, congenital heart malformation, keloid scarring, immune dysregulation, and mild learning difficulties. The deleted area encompasses about 60 genes including FSTL3 (Archer et al., 2005).

5. Implicated in

Entity Malignant blood disorders
Disease Structural rearrangement of the FSTL3 locus has been described in malignant blood disorders (see above) and it has been suggested that deregulated expression of FSTL3 could contribute to leukemogenesis (Hayette et al., 1998).
Entity Breast carcinoma
Disease High expression of FSTL3 was observed in invasive breast carcinoma compared to normal luminal epithelial cells. SiRNA-mediated knock-down of FSTL3 expression in breast cancer cell lines lead to growth inhibition, smad2 phosphorylation and increased transcription of activin target genes (Razanajaona et al., 2007). These observations suggest that FSTL3 may contribute to tumorigenesis by antagonizing growth limiting activin effects. In agreement with this notion another study reported increased FSTL3 mRNA and protein levels in the epithelial compartment in infiltrating ductal carcinoma of the breast when compared to normal breast tissue (Bloise et al., 2009).
Entity Hepatocellular carcinoma
Disease FSTL3 expression levels were increased in hepatocytes in chemical hepatocarcinogenesis models in the rat but decreased in hepatocellular carcinoma (HCC) in humans (Grusch et al., 2006).
Entity Endometrial adenocarcinoma
Disease Downregulation of FSTL3 expression was found in human endometrial adenocarcinoma (Ciarmela et al., 2004).
Entity Endometriosis
Disease Ovarian endometriotic lesions showed a deranged expression of FSTL3 as well as follistatin. While follistatin expression was increased, FSTL3 mRNA and protein expression were lower in ovarian endometriosis than in healthy eutopic endometrium (Torres et al., 2007).
Entity Pre-eclampsia
Disease The mRNA and protein levels of FSTL3 were compared in placentas and maternal sera of women with uncomplicated pregnancy and those with pre-eclampsia. FSTL3 was upregulated in syncytiotrophoblast cells of pre-eclamptic placental tissue and in maternal serum. Its further evaluation as potential addition to existing diagnostic markers of pre-eclampsia was suggested (Pryor-Koishi et al., 2007).
Entity Heart disease
Disease FSTL3 (and FSTL1) were elevated in heart failure. FSTL3 expression correlated with markers of disease severity and returned to normal after recovery. The protein was localized to myocytes and endothelium and the expression profile of FSTL3 on microarrays revealed an association with the nuclear compartment and with genes involved in signal transduction and transcription (Lara-Pezzi et al., 2008). In a mouse model activin A and FSTL3 were upregulated in the herat by ischemic injury. While activin A protected myocytes from cell death, this effect was antagonized by FSTL3 (Oshima et al., 2009).

6. Bibliography

Distinct phenotype associated with a cryptic subtelomeric deletion of 19p13.3-pter.
Archer HL, Gupta S, Enoch S, Thompson P, Rowbottom A, Chua I, Warren S, Johnson D, Ledbetter DH, Lese-Martin C, Williams P, Pilz DT.
Am J Med Genet A. 2005 Jul 1;136(1):38-44. Review
PMID 15937949
Identification of NF-kappaB responsive elements in follistatin related gene (FLRG) promoter.
Bartholin L, Guindon S, Martel S, Corbo L, Rimokh R.
Gene. 2007 May 15;393(1-2):153-62. Epub 2007 Mar 1.
PMID 17395406
Differential expression of follistatin and FLRG in human breast proliferative disorders.
Bloise E, Couto HL, Massai L, Ciarmela P, Mencarelli M, Borges LE, Muscettola M, Grasso G, Amaral VF, Cassali GD, Petraglia F, Reis FM.
BMC Cancer. 2009 Sep 9;9:320.
PMID 19740438
Follistatin and follistatin like-3 differentially regulate adiposity and glucose homeostasis.
Brown ML, Bonomi L, Ungerleider N, Zina J, Kimura F, Mukherjee A, Sidis Y, Schneyer A.
Obesity (Silver Spring). 2011 Oct;19(10):1940-9. doi: 10.1038/oby.2011.97. Epub 2011 May 5.
PMID 21546932
Structure of myostatin follistatin-like 3: N-terminal domains of follistatin-type molecules exhibit alternate modes of binding.
Cash JN, Angerman EB, Kattamuri C, Nolan K, Zhao H, Sidis Y, Keutmann HT, Thompson TB.
J Biol Chem. 2012 Jan 6;287(2):1043-53. Epub 2011 Nov 3.
PMID 22052913
Follistatin-related gene expression, but not follistatin expression, is decreased in human endometrial adenocarcinoma.
Ciarmela P, Florio P, Sigurdardottir M, Toti P, Maguer-Satta V, Rimokh R, Altomare A, Tosi P, Petraglia F.
Eur J Endocrinol. 2004 Aug;151(2):251-7.
PMID 15296481
AF10-dependent transcription is enhanced by its interaction with FLRG.
Forissier S, Razanajaona D, Ay AS, Martel S, Bartholin L, Rimokh R.
Biol Cell. 2007 Oct;99(10):563-71.
PMID 17868029
Deregulation of the activin/follistatin system in hepatocarcinogenesis.
Grusch M, Drucker C, Peter-Vorosmarty B, Erlach N, Lackner A, Losert A, Macheiner D, Schneider WJ, Hermann M, Groome NP, Parzefall W, Berger W, Grasl-Kraupp B, Schulte-Hermann R.
J Hepatol. 2006 Nov;45(5):673-80. Epub 2006 Jul 28.
PMID 16935389
FLRG (follistatin-related gene), a new target of chromosomal rearrangement in malignant blood disorders.
Hayette S, Gadoux M, Martel S, Bertrand S, Tigaud I, Magaud JP, Rimokh R.
Oncogene. 1998 Jun 4;16(22):2949-54.
PMID 9671416
The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum.
Hill JJ, Davies MV, Pearson AA, Wang JH, Hewick RM, Wolfman NM, Qiu Y.
J Biol Chem. 2002 Oct 25;277(43):40735-41. Epub 2002 Aug 22.
PMID 12194980
Expression of follistatin-related genes is altered in heart failure.
Lara-Pezzi E, Felkin LE, Birks EJ, Sarathchandra P, Panse KD, George R, Hall JL, Yacoub MH, Rosenthal N, Barton PJ.
Endocrinology. 2008 Nov;149(11):5822-7. Epub 2008 Jul 10.
PMID 18617621
A novel role for fibronectin type I domain in the regulation of human hematopoietic cell adhesiveness through binding to follistatin domains of FLRG and follistatin.
Maguer-Satta V, Forissier S, Bartholin L, Martel S, Jeanpierre S, Bachelard E, Rimokh R.
Exp Cell Res. 2006 Feb 15;312(4):434-42. Epub 2005 Dec 5.
PMID 16336961
FSTL3 deletion reveals roles for TGF-beta family ligands in glucose and fat homeostasis in adults.
Mukherjee A, Sidis Y, Mahan A, Raher MJ, Xia Y, Rosen ED, Bloch KD, Thomas MK, Schneyer AL.
Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1348-53. Epub 2007 Jan 17.
PMID 17229845
Activin A and follistatin-like 3 determine the susceptibility of heart to ischemic injury.
Oshima Y, Ouchi N, Shimano M, Pimentel DR, Papanicolaou KN, Panse KD, Tsuchida K, Lara-Pezzi E, Lee SJ, Walsh K.
Circulation. 2009 Oct 20;120(16):1606-15. Epub 2009 Oct 5.
PMID 19805648
Overproduction of the follistatin-related gene protein in the placenta and maternal serum of women with pre-eclampsia.
Pryor-Koishi K, Nishizawa H, Kato T, Kogo H, Murakami T, Tsuchida K, Kurahashi H, Udagawa Y.
BJOG. 2007 Sep;114(9):1128-37. Epub 2007 Jul 6.
PMID 17617189
Silencing of FLRG, an antagonist of activin, inhibits human breast tumor cell growth.
Razanajaona D, Joguet S, Ay AS, Treilleux I, Goddard-Leon S, Bartholin L, Rimokh R.
Cancer Res. 2007 Aug 1;67(15):7223-9.
PMID 17671190
Differential biosynthesis and intracellular transport of follistatin isoforms and follistatin-like-3.
Saito S, Sidis Y, Mukherjee A, Xia Y, Schneyer A.
Endocrinology. 2005 Dec;146(12):5052-62. Epub 2005 Sep 8.
PMID 16150905
Differential binding and neutralization of activins A and B by follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG).
Schneyer A, Schoen A, Quigg A, Sidis Y.
Endocrinology. 2003 May;144(5):1671-4.
PMID 12697670
Growth differentiation factor 9 (GDF9) suppresses follistatin and follistatin-like 3 production in human granulosa-lutein cells.
Shi FT, Cheung AP, Huang HF, Leung PC.
PLoS One. 2011;6(8):e22866. Epub 2011 Aug 1.
PMID 21829661
Biological activity of follistatin isoforms and follistatin-like-3 is dependent on differential cell surface binding and specificity for activin, myostatin, and bone morphogenetic proteins.
Sidis Y, Mukherjee A, Keutmann H, Delbaere A, Sadatsuki M, Schneyer A.
Endocrinology. 2006 Jul;147(7):3586-97. Epub 2006 Apr 20.
PMID 16627583
Heparin and activin-binding determinants in follistatin and FSTL3.
Sidis Y, Schneyer AL, Keutmann HT.
Endocrinology. 2005 Jan;146(1):130-6. Epub 2004 Oct 7.
PMID 15471966
Follistatin-related protein and follistatin differentially neutralize endogenous vs. exogenous activin.
Sidis Y, Tortoriello DV, Holmes WE, Pan Y, Keutmann HT, Schneyer AL.
Endocrinology. 2002 May;143(5):1613-24.
PMID 11956142
The structure of FSTL3.activin A complex. Differential binding of N-terminal domains influences follistatin-type antagonist specificity.
Stamler R, Keutmann HT, Sidis Y, Kattamuri C, Schneyer A, Thompson TB.
J Biol Chem. 2008 Nov 21;283(47):32831-8. Epub 2008 Sep 2.
PMID 18768470
Deranged expression of follistatin and follistatin-like protein in women with ovarian endometriosis.
Torres PB, Florio P, Ferreira MC, Torricelli M, Reis FM, Petraglia F.
Fertil Steril. 2007 Jul;88(1):200-5. Epub 2007 Feb 12.
PMID 17296189
Human follistatin-related protein: a structural homologue of follistatin with nuclear localization.
Tortoriello DV, Sidis Y, Holtzman DA, Holmes WE, Schneyer AL.
Endocrinology. 2001 Aug;142(8):3426-34.
PMID 11459787
Identification and characterization of a novel follistatin-like protein as a binding protein for the TGF-beta family.
Tsuchida K, Arai KY, Kuramoto Y, Yamakawa N, Hasegawa Y, Sugino H.
J Biol Chem. 2000 Dec 29;275(52):40788-96.
PMID 11010968
The Factor I and follistatin domain families: the return of a prodigal son.
Ullman CG, Perkins SJ.
Biochem J. 1997 Sep 15;326 ( Pt 3):939-41.
PMID 9334166
Follistatin-related gene (FLRG) expression in human endometrium: sex steroid hormones regulate the expression of FLRG in cultured human endometrial stromal cells.
Wang HQ, Takebayashi K, Tsuchida K, Nishimura M, Noda Y.
J Clin Endocrinol Metab. 2003 Sep;88(9):4432-9.
PMID 12970321

7. Citation

This paper should be referenced as such :
Grusch, M
FSTL3 (follistatin-like 3 (secreted glycoprotein))
Atlas Genet Cytogenet Oncol Haematol. 2013;17(3):151-154.
Free journal version : [ pdf ]   [ DOI ]
On line version : https://atlasgeneticsoncology.usal.es/classic/Genes/FSTL3ID111ch19p13.html
History of this paper:
Grusch, M. FSTL3 (follistatin-like 3 (secreted glycoprotein)). Atlas Genet Cytogenet Oncol Haematol. 2009;13(12):935-938.

8. Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]

  t(11;19)(q13;p13) FSTL3/CCND1

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(16;19)(p13;p13) MKL2/FSTL3

9. External links

HGNC (Hugo)FSTL3   3973
Entrez_Gene (NCBI)FSTL3  10272  follistatin like 3
GeneCards (Weizmann)FSTL3
Ensembl hg19 (Hinxton)ENSG00000070404 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000070404 [Gene_View] &nbspENSG00000070404 [Sequence]  chr19:676389-683392 [Contig_View]  FSTL3 [Vega]
ICGC DataPortalENSG00000070404
TCGA cBioPortalFSTL3
Genatlas (Paris)FSTL3
SOURCE (Princeton)FSTL3
Genetics Home Reference (NIH)FSTL3
Genomic and cartography
GoldenPath hg38 (UCSC)FSTL3  -     chr19:676389-683392 +  19p13.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)FSTL3  -     19p13.3   [Description]    (hg19-Feb_2009)
EnsemblFSTL3 - 19p13.3 [CytoView hg19]  FSTL3 - 19p13.3 [CytoView hg38]
Mapping of homologs : NCBIFSTL3 [Mapview hg19]  FSTL3 [Mapview hg38]
Gene and transcription
Genbank (Entrez)AK291958 AK311521 AK311566 AK313341 AL050194
RefSeq transcript (Entrez)NM_005860
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)FSTL3
Cluster EST : UnigeneHs.529038 [ NCBI ]
CGAP (NCI)Hs.529038
Alternative Splicing GalleryENSG00000070404
Gene ExpressionFSTL3 [ NCBI-GEO ]   FSTL3 [ EBI - ARRAY_EXPRESS ]   FSTL3 [ SEEK ]   FSTL3 [ MEM ]
Gene Expression Viewer (FireBrowse)FSTL3 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets] &nbsp [Normal Tissue Atlas] &nbsp[carcinoma Classsification] &nbsp[NCI60]
GenevestigatorExpression in : [tissues] &nbsp[cell-lines] &nbsp[cancer] &nbsp[perturbations] &nbsp
BioGPS (Tissue expression)10272
GTEX Portal (Tissue expression)FSTL3
Human Protein AtlasENSG00000070404-FSTL3 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO95633   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtO95633  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO95633
Splice isoforms : SwissVarO95633
Domaine pattern : Prosite (Expaxy)KAZAL_2 (PS51465)    TB (PS51364)   
Domains : Interpro (EBI)Fol_N    Follistatin/Osteonectin_EGF    Kazal_dom    Kazal_dom_sf    TB_dom    TB_dom_sf   
Domain families : Pfam (Sanger)FOLN (PF09289)    Kazal_2 (PF07648)   
Domain families : Pfam (NCBI)pfam09289    pfam07648   
Domain families : Smart (EMBL)FOLN (SM00274)  KAZAL (SM00280)  
Conserved Domain (NCBI)FSTL3
DMDM Disease mutations10272
Blocks (Seattle)FSTL3
PDB (RSDB)2KCX    3B4V    3SEK   
PDB Europe2KCX    3B4V    3SEK   
PDB (PDBSum)2KCX    3B4V    3SEK   
PDB (IMB)2KCX    3B4V    3SEK   
Structural Biology KnowledgeBase2KCX    3B4V    3SEK   
SCOP (Structural Classification of Proteins)2KCX    3B4V    3SEK   
CATH (Classification of proteins structures)2KCX    3B4V    3SEK   
Human Protein Atlas [tissue]ENSG00000070404-FSTL3 [tissue]
Peptide AtlasO95633
IPIIPI00025155   IPI00955041   
Protein Interaction databases
IntAct (EBI)O95633
Ontologies - Pathways
Ontology : AmiGOossification  kidney development  fibronectin binding  hematopoietic progenitor cell differentiation  protein binding  extracellular region  extracellular space  nucleus  nucleoplasm  endoplasmic reticulum lumen  Golgi apparatus  regulation of transcription by RNA polymerase II  spermatogenesis  male gonad development  positive regulation of cell-cell adhesion  secretory granule  lung development  adrenal gland development  negative regulation of BMP signaling pathway  negative regulation of activin receptor signaling pathway  post-translational protein modification  cellular protein metabolic process  neuron projection terminus  negative regulation of osteoclast differentiation  positive regulation of transcription by RNA polymerase II  activin binding  cellular response to metal ion  negative regulation of transmembrane receptor protein serine/threonine kinase signaling pathway  
Ontology : EGO-EBIossification  kidney development  fibronectin binding  hematopoietic progenitor cell differentiation  protein binding  extracellular region  extracellular space  nucleus  nucleoplasm  endoplasmic reticulum lumen  Golgi apparatus  regulation of transcription by RNA polymerase II  spermatogenesis  male gonad development  positive regulation of cell-cell adhesion  secretory granule  lung development  adrenal gland development  negative regulation of BMP signaling pathway  negative regulation of activin receptor signaling pathway  post-translational protein modification  cellular protein metabolic process  neuron projection terminus  negative regulation of osteoclast differentiation  positive regulation of transcription by RNA polymerase II  activin binding  cellular response to metal ion  negative regulation of transmembrane receptor protein serine/threonine kinase signaling pathway  
REACTOMEO95633 [protein]
REACTOME PathwaysR-HSA-8957275 [pathway]   
NDEx NetworkFSTL3
Atlas of Cancer Signalling NetworkFSTL3
Wikipedia pathwaysFSTL3
Orthology - Evolution
GeneTree (enSembl)ENSG00000070404
Phylogenetic Trees/Animal Genes : TreeFamFSTL3
Homologs : HomoloGeneFSTL3
Homology/Alignments : Family Browser (UCSC)FSTL3
Gene fusions - Rearrangements
Fusion : MitelmanFSTL3/CCND1 [19p13.3/11q13.3] &nbsp
Fusion : MitelmanMKL2/FSTL3 [16p13.12/19p13.3] &nbsp[t(16;19)(p13;p13)]  
Fusion PortalMKL2 16p13.12 FSTL3 19p13.3 BRCA
Fusion : TICdbCCND1 [11q13.3]  -  FSTL3 [19p13.3]
Fusion : QuiverFSTL3
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerFSTL3 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)FSTL3
Exome Variant ServerFSTL3
ExAC (Exome Aggregation Consortium)ENSG00000070404
GNOMAD BrowserENSG00000070404
Varsome BrowserFSTL3
Genetic variants : HAPMAP10272
Genomic Variants (DGV)FSTL3 [DGVbeta]
DECIPHERFSTL3 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisFSTL3 
ICGC Data PortalFSTL3 
TCGA Data PortalFSTL3 
Broad Tumor PortalFSTL3
OASIS PortalFSTL3 [ Somatic mutations - Copy number]
Cancer Gene: CensusFSTL3 
Mutations and Diseases : HGMDFSTL3
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 FSTL3
DgiDB (Drug Gene Interaction Database)FSTL3
DoCM (Curated mutations)FSTL3 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)FSTL3 (select a term)
NCG5 (London)FSTL3
Cancer3DFSTL3(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry FSTL3
NextProtO95633 [Medical]
Target ValidationFSTL3
Huge Navigator FSTL3 [HugePedia]
snp3D : Map Gene to Disease10272
BioCentury BCIQFSTL3
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD10272
Chemical/Pharm GKB GenePA28390
Clinical trialFSTL3
canSAR (ICR)FSTL3 (select the gene name)
DataMed IndexFSTL3
PubMed50 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
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