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FST (follistatin)

Written2010-03Michael 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)

Identity

Alias_symbol (synonym)FS
Other alias
HGNC (Hugo) FST
LocusID (NCBI) 10468
Atlas_Id 44477
Location 5q11.2  [Link to chromosome band 5q11]
Location_base_pair Starts at 53480434 and ends at 53486474 bp from pter ( according to hg19-Feb_2009)  [Mapping FST.png]
Local_order RPS19P4 (ribosomal protein S19 pseudogene 4) - FST - NDUFS4 (NADH dehydrogenase (ubiquinone) Fe-S protein 4).
 
  Intron/exon structure of the FST gene and domain architecture of FST proteins. 1, 2, 3, 4, 5, 6A, 6B: exon number; SP: signal peptide; NTD: N-terminal domain; FSD: follistatin domain; AT: acidic tail.
Fusion genes
(updated 2017)		Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
FST (5q11.2) / FST (5q11.2)KDM4B (19p13.3) / FST (5q11.2)MORF4L2 (Xq22.2) / FST (5q11.2)

DNA/RNA

Description The human FST gene is comprised of six exons spanning 5329 bp on chromosome 5q11.2 and gives rise to two main transcripts of 1122 bp (transcript variant FST344) and 1386 bp (transcript variant FST317). The first exon encodes the signal peptide, the second exon the N-terminal domain and exons 3-5 each code for a follistatin module. Alternative splicing leads to usage of either exon 6A, which codes for an acidic region in FST344 or exon 6B, which contains two bases of the stop codon of FST317 (Shimasaki et al., 1988).
Transcription Transcription of FST mRNA was shown to be stimulated by TGF beta and activin A via Smad proteins (Bartholin et al., 2002), which seems to be part of a negative feedback loop as FST can antagonize activin A (see below). Other factors and pathways that have been demonstrated to stimulate follistatin gene transcription are gonadotropin-releasing hormone (GnRH) acting via cAMP and CREB (Winters et al., 2007), GLI2, a transcription factor activated by hedgehog signaling (Eichberger et al., 2008), dexamethasone (Hayashi et al., 2009), androgens and activators of wnt signaling (Willert et al., 2002; Yao et al., 2004; Singh et al., 2009). Repression of the follistatin promoter in response to peroxisome proliferator-activated receptor gamma was mediated via SP1 (Necela et al., 2008).

Protein

Description Mature secreted follistatin protein exists in three main forms consisting of 288, 303, and 315 amino acids (Sugino et al., 1993). The FST344 transcript gives rise to a protein precursor of 344 amino acids, which results in the mature 315 amino acid form after removal of the signal peptide. A fraction of follistatin 315 is further converted to the 303 amino acid form by proteolytic cleavage at the C-terminus. Signal peptide removal of FST317 leads to the mature 288 amino acid form of follistatin. All forms of follistatin contain three follistatin domains (FSD) characterized by a conserved arrangement of 10 cysteine residues. The N-terminal subdomains of the FSD have similarity with EGF-like modules, whereas the C-terminal regions resemble the Kazal domains found in multiple serine protease inhibitors. The follistatin protein contains two potential N-glycosilation sites on asparagines 124 and 288.
Localisation Follistatin is expressed in a wide variety of tissues and organs with the highest expression in the ovaries and testes (Phillips and de Kretser, 1998; Tortoriello et al., 2001). The signal peptide directs the nascent protein to the secretory pathway and follistatin has been detected in human serum and in cell culture supernatants of multiple cell lines (Phillips and de Kretser, 1998). Among the follistatin isoforms FST315 was secreted faster than FST288 (Schneyer et al., 2003) and due to the lack of binding to cell-surface heparin-sulfated proteoglycans, a larger fraction of FST315 enters the circulation (Schneyer et al., 1996).
Function Follistatin binds to several members of the TGF beta family and blocks the interaction of these cytokines with their cognate receptors. Follistatin was first identified as a factor that could inhibit the release of follicle-stimulating hormone from pituitary cells (Ueno et al., 1987). It binds activins A, B and AB with high affinity and was also reported to bind activin E but not activin C (Nakamura et al., 1990; Schneyer et al., 1994; Hashimoto et al., 2002; Wada et al., 2004). Follistatin-bound activin is unable to initiate signal transduction and consequently follistatin is a potent antagonist of physiological activin signals. Of the three follistatin domains present in all follistatin isoforms, (Shimasaki et al., 1988) the first two, but not the third, are necessary for activin A binding (Keutmann et al., 2004; Harrington et al., 2006). Aside from activins, follistatin also binds several bone morphogenetic proteins (BMP) including BMP2, BMP4, BMP6 and BMP7 (Iemura et al., 1998; Glister et al., 2004). In 2004 it was shown that follistatin binds myostatin (also known as growth and differentiation factor 8, GDF8) with high affinity and thereby is able to antagonize the inhibitory effect of myostatin on muscle growth (Amthor et al., 2004).
The functional significance of the interaction between follistatin and angiogenin, a pro-angiogenic factor unrelated to the TGF beta family, remains to be determined (Gao et al., 2007). The interaction of follistatin with heparin and heparan sulfates is isoform specific. Follistatin 288 binds to heparan sulfates, whereas this binding is blocked by the acidic tail of follistatin 315 (Sugino et al., 1993).
Knock-out mice for follistatin die within hours after birth and show multiple abnormalities of muscles, skin and skeleton (Matzuk et al., 1995). Evidence from many organs and tissues shows that counterbalancing of signals from TGF beta family members by follistatin is crucial for normal tissue development, architecture and function (de Kretser et al., 2004; McDowall et al., 2008; Kreidl et al., 2009; Antsiferova et al., 2009).
Due to the capability for efficient antagonization of signals from activin and myostatin, the therapeutic application of follistatin has been discussed in several clinical conditions involving elevated activin/myostatin activity. Potential areas of application include blocking increased activin expression in inflammation (Phillips et al., 2009) and fibrotic disorders (Aoki and Kojima, 2007) and inhibition of myostatin in muscle diseases (Rodino-Klapac et al., 2009).
Homology The follistatin module with its characteristic spacing of cysteines represents a conserved protein domain. Follistatin modules are found in varying numbers in a wider set of secreted proteins including FSTL1, SPARC/osteonectin, or agrin (Ullman and Perkins, 1997). Among these, follistatin-like 3 (FSTL3, FLRG) shares a similar overall domain architecture with follistatin, but harbors only two instead of three follistatin modules (Tortoriello et al., 2001). With respect to activin binding ability, functional homology among follistatin domain-containing proteins is only found between follistatin and FSTL3, whereas all other follistatin family proteins have not been demonstrated to bind proteins of the TGF beta family (Tsuchida et al., 2000). Follistatin is also highly conserved between species with around 97% amino acid identity in human, mouse and rat.

Implicated in

Note
  
Entity Malignancy
Note Overexpression of follistatin has been found in rat and mouse models of hepatocellular carcinoma (HCC) (Rossmanith et al., 2002; Fujiwara et al., 2008) as well as in tumor tissue and serum of HCC patients (Yuen et al., 2002; Grusch et al., 2006; Beale et al., 2008). However, follistatin had no benefit as surveillance biomarker for HCC development in patients with alcoholic and non-alcoholic liver disease (ALD and NAFLD) due to the already elevated levels in the underlying liver pathologies (Beale et al., 2008). Follistatin overexpression was also demonstrated in human melanoma cell lines (Stove et al., 2004) and has been suggested as candidate biomarker for lung cancer (Planque et al., 2009).
  
  
Entity Endometriosis
Note Follistatin was increased in serum of women with ovarian endometriosis and suggested as biomarker for endometrioma (Florio et al., 2009).
  
  
Entity Polycystic ovary syndrome
Note A genetic linkage analysis found evidence for linkage of follistatin with polycystic ovary syndrome (PCOS) (Urbanek et al., 1999). Another study reported that the follistatin gene is not a susceptibility locus for PCOS but a single nucleotide polymorphism of the gene may be involved in the hyperandrogenaemia of the disease (Jones et al., 2007).
  
  
Entity Liver failure
Note Serum levels of follistatin and activin A were increased in patients with acute liver failure and it was suggested that a decreased follistatin/activin A ratio in the blood may be an indicator for the severity of liver injury in hepatitis-related acute liver disease (Hughes and Evans, 2003; Lin et al., 2006).
  

Bibliography

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PMID 15136138
 
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Therapeutic potential of follistatin to promote tissue regeneration and prevent tissue fibrosis.
Aoki F, Kojima I.
Endocr J. 2007;54(6):849-54. Epub 2007 Oct 15. (REVIEW)
PMID 17938504
 
Transcription activation of FLRG and follistatin by activin A, through Smad proteins, participates in a negative feedback loop to modulate activin A function.
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PMID 11948405
 
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J Biol Chem. 2008 May 2;283(18):12426-37. Epub 2008 Mar 3.
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PMID 19549703
 
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Oncogene. 2008 Oct 9;27(46):6002-11. Epub 2008 Jun 23.
PMID 18574468
 
Identification and characterization of follistatin as a novel angiogenin-binding protein.
Gao X, Hu H, Zhu J, Xu Z.
FEBS Lett. 2007 Nov 27;581(28):5505-10. Epub 2007 Nov 6.
PMID 17991437
 
Bone morphogenetic protein (BMP) ligands and receptors in bovine ovarian follicle cells: actions of BMP-4, -6 and -7 on granulosa cells and differential modulation of Smad-1 phosphorylation by follistatin.
Glister C, Kemp CF, Knight PG.
Reproduction. 2004 Feb;127(2):239-54.
PMID 15056790
 
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.
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PMID 16935389
 
Structural basis for the inhibition of activin signalling by follistatin.
Harrington AE, Morris-Triggs SA, Ruotolo BT, Robinson CV, Ohnuma S, Hyvonen M.
EMBO J. 2006 Mar 8;25(5):1035-45. Epub 2006 Feb 16.
PMID 16482217
 
cDNA cloning and expression of human activin betaE subunit.
Hashimoto O, Tsuchida K, Ushiro Y, Hosoi Y, Hoshi N, Sugino H, Hasegawa Y.
Mol Cell Endocrinol. 2002 Aug 30;194(1-2):117-22.
PMID 12242034
 
BMP/Wnt antagonists are upregulated by dexamethasone in osteoblasts and reversed by alendronate and PTH: potential therapeutic targets for glucocorticoid-induced osteoporosis.
Hayashi K, Yamaguchi T, Yano S, Kanazawa I, Yamauchi M, Yamamoto M, Sugimoto T.
Biochem Biophys Res Commun. 2009 Feb 6;379(2):261-6. Epub 2008 Dec 25.
PMID 19101512
 
Activin A and follistatin in acute liver failure.
Hughes RD, Evans LW.
Eur J Gastroenterol Hepatol. 2003 Feb;15(2):127-31.
PMID 12560755
 
Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo.
Iemura S, Yamamoto TS, Takagi C, Uchiyama H, Natsume T, Shimasaki S, Sugino H, Ueno N.
Proc Natl Acad Sci U S A. 1998 Aug 4;95(16):9337-42.
PMID 9689081
 
Polymorphism of the follistatin gene in polycystic ovary syndrome.
Jones MR, Wilson SG, Mullin BH, Mead R, Watts GF, Stuckey BG.
Mol Hum Reprod. 2007 Apr;13(4):237-41. Epub 2007 Feb 6.
PMID 17284512
 
The role of follistatin domains in follistatin biological action.
Keutmann HT, Schneyer AL, Sidis Y.
Mol Endocrinol. 2004 Jan;18(1):228-40. Epub 2003 Oct 16.
PMID 14563935
 
Activins and follistatins: Emerging roles in liver physiology and cancer.
Kreidl E, Ozturk D, Metzner T, Berger W, Grusch M.
World J Hepatol Rev 2009 Oct 31; 1(1): 17-27. (REVIEW)
 
Ratio of circulating follistatin and activin A reflects the severity of acute liver injury and prognosis in patients with acute liver failure.
Lin SD, Kawakami T, Ushio A, Sato A, Sato S, Iwai M, Endo R, Takikawa Y, Suzuki K.
J Gastroenterol Hepatol. 2006 Feb;21(2):374-80.
PMID 16509861
 
Multiple defects and perinatal death in mice deficient in follistatin.
Matzuk MM, Lu N, Vogel H, Sellheyer K, Roop DR, Bradley A.
Nature. 1995 Mar 23;374(6520):360-3.
PMID 7885475
 
The role of activins and follistatins in skin and hair follicle development and function.
McDowall M, Edwards NM, Jahoda CA, Hynd PI.
Cytokine Growth Factor Rev. 2008 Oct-Dec;19(5-6):415-26. Epub 2008 Oct 14. (REVIEW)
PMID 18922734
 
Activin-binding protein from rat ovary is follistatin.
Nakamura T, Takio K, Eto Y, Shibai H, Titani K, Sugino H.
Science. 1990 Feb 16;247(4944):836-8.
PMID 2106159
 
Peroxisome proliferator-activated receptor gamma down-regulates follistatin in intestinal epithelial cells through SP1.
Necela BM, Su W, Thompson EA.
J Biol Chem. 2008 Oct 31;283(44):29784-94. Epub 2008 Sep 3.
PMID 18768463
 
Activin and related proteins in inflammation: not just interested bystanders.
Phillips DJ, de Kretser DM, Hedger MP.
Cytokine Growth Factor Rev. 2009 Apr;20(2):153-64. Epub 2009 Mar 3. (REVIEW)
PMID 19261538
 
Identification of five candidate lung cancer biomarkers by proteomics analysis of conditioned media of four lung cancer cell lines.
Planque C, Kulasingam V, Smith CR, Reckamp K, Goodglick L, Diamandis EP.
Mol Cell Proteomics. 2009 Dec;8(12):2746-58. Epub 2009 Sep 23.
PMID 19776420
 
Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease.
Rodino-Klapac LR, Haidet AM, Kota J, Handy C, Kaspar BK, Mendell JR.
Muscle Nerve. 2009 Mar;39(3):283-96. (REVIEW)
PMID 19208403
 
Follistatin overexpression in rodent liver tumors: a possible mechanism to overcome activin growth control.
Rossmanith W, Chabicovsky M, Grasl-Kraupp B, Peter B, Schausberger E, Schulte-Hermann R.
Mol Carcinog. 2002 Sep;35(1):1-5.
PMID 12203361
 
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
 
Follistatin-activin complexes in human serum and follicular fluid differ immunologically and biochemically.
Schneyer AL, Hall HA, Lambert-Messerlian G, Wang QF, Sluss P, Crowley WF Jr.
Endocrinology. 1996 Jan;137(1):240-7.
PMID 8536619
 
Primary structure of the human follistatin precursor and its genomic organization.
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Proc Natl Acad Sci U S A. 1988 Jun;85(12):4218-22.
PMID 3380788
 
Regulation of myogenic differentiation by androgens: cross talk between androgen receptor/ beta-catenin and follistatin/transforming growth factor-beta signaling pathways.
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Endocrinology. 2009 Mar;150(3):1259-68. Epub 2008 Oct 23.
PMID 18948405
 
Melanoma cells secrete follistatin, an antagonist of activin-mediated growth inhibition.
Stove C, Vanrobaeys F, Devreese B, Van Beeumen J, Mareel M, Bracke M.
Oncogene. 2004 Jul 8;23(31):5330-9.
PMID 15064726
 
Molecular heterogeneity of follistatin, an activin-binding protein. Higher affinity of the carboxyl-terminal truncated forms for heparan sulfate proteoglycans on the ovarian granulosa cell.
Sugino K, Kurosawa N, Nakamura T, Takio K, Shimasaki S, Ling N, Titani K, Sugino H.
J Biol Chem. 1993 Jul 25;268(21):15579-87.
PMID 8340384
 
Human follistatin-related protein: a structural homologue of follistatin with nuclear localization.
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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
 
Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone.
Ueno N, Ling N, Ying SY, Esch F, Shimasaki S, Guillemin R.
Proc Natl Acad Sci U S A. 1987 Dec;84(23):8282-6.
PMID 3120188
 
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
 
Thirty-seven candidate genes for polycystic ovary syndrome: strongest evidence for linkage is with follistatin.
Urbanek M, Legro RS, Driscoll DA, Azziz R, Ehrmann DA, Norman RJ, Strauss JF 3rd, Spielman RS, Dunaif A.
Proc Natl Acad Sci U S A. 1999 Jul 20;96(15):8573-8.
PMID 10411917
 
Assessment of the function of the betaC-subunit of activin in cultured hepatocytes.
Wada W, Maeshima A, Zhang YQ, Hasegawa Y, Kuwano H, Kojima I.
Am J Physiol Endocrinol Metab. 2004 Aug;287(2):E247-54. Epub 2004 Mar 23.
PMID 15039147
 
A transcriptional response to Wnt protein in human embryonic carcinoma cells.
Willert J, Epping M, Pollack JR, Brown PO, Nusse R.
BMC Dev Biol. 2002 Jul 2;2:8.
PMID 12095419
 
Transcriptional regulation of follistatin expression by GnRH in mouse gonadotroph cell lines: evidence for a role for cAMP signaling.
Winters SJ, Ghooray D, Fujii Y, Moore JP Jr, Nevitt JR, Kakar SS.
Mol Cell Endocrinol. 2007 Jun 15;271(1-2):45-54. Epub 2007 Apr 4.
PMID 17482756
 
Follistatin operates downstream of Wnt4 in mammalian ovary organogenesis.
Yao HH, Matzuk MM, Jorgez CJ, Menke DB, Page DC, Swain A, Capel B.
Dev Dyn. 2004 Jun;230(2):210-5.
PMID 15162500
 
Transforming growth factor-beta 1, activin and follistatin in patients with hepatocellular carcinoma and patients with alcoholic cirrhosis.
Yuen MF, Norris S, Evans LW, Langley PG, Hughes RD.
Scand J Gastroenterol. 2002 Feb;37(2):233-8.
PMID 11843063
 
The role of activin, follistatin and inhibin in testicular physiology.
de Kretser DM, Buzzard JJ, Okuma Y, O'Connor AE, Hayashi T, Lin SY, Morrison JR, Loveland KL, Hedger MP.
Mol Cell Endocrinol. 2004 Oct 15;225(1-2):57-64. (REVIEW)
PMID 15451568
 

Citation

This paper should be referenced as such :
Grusch, M
FST (follistatin)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(12):1132-1135.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/FSTID44477ch5q11.html

External links

Nomenclature
HGNC (Hugo)FST   3971
Cards
AtlasFSTID44477ch5q11
Entrez_Gene (NCBI)FST  10468  follistatin
AliasesFS
GeneCards (Weizmann)FST
Ensembl hg19 (Hinxton)ENSG00000134363 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000134363 [Gene_View]  ENSG00000134363 [Sequence]  chr5:53480434-53486474 [Contig_View]  FST [Vega]
ICGC DataPortalENSG00000134363
TCGA cBioPortalFST
AceView (NCBI)FST
Genatlas (Paris)FST
WikiGenes10468
SOURCE (Princeton)FST
Genetics Home Reference (NIH)FST
Genomic and cartography
GoldenPath hg38 (UCSC)FST  -     chr5:53480434-53486474 +  5q11.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)FST  -     5q11.2   [Description]    (hg19-Feb_2009)
EnsemblFST - 5q11.2 [CytoView hg19]  FST - 5q11.2 [CytoView hg38]
Mapping of homologs : NCBIFST [Mapview hg19]  FST [Mapview hg38]
OMIM136470   
Gene and transcription
Genbank (Entrez)AB451330 AB451474 BC004107 BQ941144 BQ949678
RefSeq transcript (Entrez)NM_006350 NM_013409
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)FST
Cluster EST : UnigeneHs.9914 [ NCBI ]
CGAP (NCI)Hs.9914
Alternative Splicing GalleryENSG00000134363
Gene ExpressionFST [ NCBI-GEO ]   FST [ EBI - ARRAY_EXPRESS ]   FST [ SEEK ]   FST [ MEM ]
Gene Expression Viewer (FireBrowse)FST [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)10468
GTEX Portal (Tissue expression)FST
Human Protein AtlasENSG00000134363-FST [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP19883   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP19883  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP19883
Splice isoforms : SwissVarP19883
PhosPhoSitePlusP19883
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)FST
DMDM Disease mutations10468
Blocks (Seattle)FST
PDB (SRS)2B0U    2P6A    3HH2    5JHW   
PDB (PDBSum)2B0U    2P6A    3HH2    5JHW   
PDB (IMB)2B0U    2P6A    3HH2    5JHW   
PDB (RSDB)2B0U    2P6A    3HH2    5JHW   
Structural Biology KnowledgeBase2B0U    2P6A    3HH2    5JHW   
SCOP (Structural Classification of Proteins)2B0U    2P6A    3HH2    5JHW   
CATH (Classification of proteins structures)2B0U    2P6A    3HH2    5JHW   
SuperfamilyP19883
Human Protein Atlas [tissue]ENSG00000134363-FST [tissue]
Peptide AtlasP19883
HPRD00641
IPIIPI00021081   IPI00217070   IPI00967838   IPI00964184   IPI00217071   
Protein Interaction databases
DIP (DOE-UCLA)P19883
IntAct (EBI)P19883
FunCoupENSG00000134363
BioGRIDFST
STRING (EMBL)FST
ZODIACFST
Ontologies - Pathways
QuickGOP19883
Ontology : AmiGOnegative regulation of transcription by RNA polymerase II  hematopoietic progenitor cell differentiation  protein binding  extracellular region  negative regulation of activin receptor signaling pathway  heparan sulfate proteoglycan binding  activin binding  positive regulation of hair follicle development  
Ontology : EGO-EBInegative regulation of transcription by RNA polymerase II  hematopoietic progenitor cell differentiation  protein binding  extracellular region  negative regulation of activin receptor signaling pathway  heparan sulfate proteoglycan binding  activin binding  positive regulation of hair follicle development  
Pathways : KEGGTGF-beta signaling pathway   
REACTOMEP19883 [protein]
REACTOME PathwaysR-HSA-2473224 [pathway]   
NDEx NetworkFST
Atlas of Cancer Signalling NetworkFST
Wikipedia pathwaysFST
Orthology - Evolution
OrthoDB10468
GeneTree (enSembl)ENSG00000134363
Phylogenetic Trees/Animal Genes : TreeFamFST
HOVERGENP19883
HOGENOMP19883
Homologs : HomoloGeneFST
Homology/Alignments : Family Browser (UCSC)FST
Gene fusions - Rearrangements
Fusion : QuiverFST
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerFST [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)FST
dbVarFST
ClinVarFST
1000_GenomesFST 
Exome Variant ServerFST
ExAC (Exome Aggregation Consortium)ENSG00000134363
GNOMAD BrowserENSG00000134363
Varsome BrowserFST
Genetic variants : HAPMAP10468
Genomic Variants (DGV)FST [DGVbeta]
DECIPHERFST [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisFST 
Mutations
ICGC Data PortalFST 
TCGA Data PortalFST 
Broad Tumor PortalFST
OASIS PortalFST [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICFST  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDFST
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 FST
DgiDB (Drug Gene Interaction Database)FST
DoCM (Curated mutations)FST (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)FST (select a term)
intoGenFST
NCG5 (London)FST
Cancer3DFST(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM136470   
Orphanet
DisGeNETFST
MedgenFST
Genetic Testing Registry FST
NextProtP19883 [Medical]
TSGene10468
GENETestsFST
Target ValidationFST
Huge Navigator FST [HugePedia]
snp3D : Map Gene to Disease10468
BioCentury BCIQFST
ClinGenFST
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD10468
Chemical/Pharm GKB GenePA28388
Clinical trialFST
Miscellaneous
canSAR (ICR)FST (select the gene name)
Probes
Litterature
PubMed116 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineFST
EVEXFST
GoPubMedFST
iHOPFST
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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