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TNFSF15 (tumor necrosis factor (ligand) superfamily, member 15)

Written2009-08Gui-Li Yang, Jian-Wei Qi, Zhi-Song Zhang, Lu-Yuan Li
Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213, USA (LYL); College of Pharmacy, College of Life Sciences, Nankai University, 94 Wei Jin Road, 300071 Tianjin, China (LYL, GLY, JWQ, ZSZ)

(Note : for Links provided by Atlas : click)

Identity

Alias_namestumor necrosis factor (ligand) superfamily
Alias_symbol (synonym)TL1
VEGI
TL1A
VEGI192A
MGC129934
MGC129935
Other alias
HGNC (Hugo) TNFSF15
LocusID (NCBI) 9966
Atlas_Id 42638
Location 9q32  [Link to chromosome band 9q32]
Location_base_pair Starts at 114784635 and ends at 114792530 bp from pter ( according to hg19-Feb_2009)  [Mapping TNFSF15.png]
Local_order TNFSF15 gene at 9q32, near the CD30L gene at 9q33.

DNA/RNA

 
  Boxes with roman numerals above represent exons and horizontal lines represent intronic sequence. The putative transcription start site is indicated by a double arrowhead. R denotes the 5' untranslated sequence unique to each respective transcript, and stippled boxe represents the common 3' untranslated region.
Description The human VEGI gene spans about 17 kb and consists of four exons.
Transcription The size of VEGI mRNA is approximately 6.5 kb. It is unusual for a human gene of 6.5 kb to contain only a small open reading frame of 522 nucleotides. Multiple VEGI transcripts generated by the use of cryptic splice sites and alternate exons.
Pseudogene Not known.

Protein

 
  Figure A. All three isoforms.
Figure B. A ribbon diagram of the TL1A trimer. (Jin et al. BBRC 364:1, 2007).
Description Hydrophobicity analysis of VEGI predicts a 13 amino acid hydrophobic region that follows the amino terminal segment of 12 amino acids, suggesting a structure characteristic of a type II transmembrane protein, with residues 26-174 constituting an extracellular domain analogous to domains found in other TNF family members.
VEGI isoforms exhibit a carboxyl terminal domain of 151 amino acid residues, which is encoded by part of the fourth exon, termed IVb. The initially characterized VEGI isoform, designated VEGI-174, is encoded by the fourth exon (parts IVa and IVb) alone, which includes both the putative transmembrane domain and the conserved extracellular domain. There are two additional endothelial-specific transcripts of 7.5 and 2.0 kb, which encode peptides of 251 (VEGI-251) and 192 (VEGI-192) residues, respectively. The VEGI-251 and -192 isoforms differ in their amino terminal regions, but share the conserved 151-amino acid residue carboxy terminal domain. VEGI-251 possesses a putative secretory signal peptide and its overexpression causes apoptosis of endothelial cells and inhibition of tumor growth.
 
  Amino acid sequence alignment of three VEGI isoforms. The putative hydrophobic regions of VEGI-251 and VEGI-174 are underlined. Asterisk denotes the start of shared sequences for all three isoforms.
Expression VEGI is specifically expressed in endothelial cells. Analysis of total RNA preparations from many cell lines and primary cell cultures by Northern blot analysis confirmed the specificity of VEGI expression, with only HUVEC and human venous endothelial cells demonstrating detectable levels of expression. Using multiple tissue Northern blots, the VEGI transcript was found in many adult human tissues, including placenta, lung, skeletal muscle, kidney, pancreas, spleen, prostate, small intestine, and colon, suggesting that the gene product may play a role in the function of a normal vasculature.The failure to detect the transcripts of this new gene in some of the human tissues probably is due to relatively small proportion of endothelial cells in these tissues. Using isoform-specific probes, we have determined that the distribution profiles of VEGI isoforms in human organs and tissues appear to be different. The 7.5 kb transcript encoding VEGI-251 was expressed at high levels in the placenta, kidney, lung and liver, whereas the 2 kb transcript corresponding to VEGI-174 was observed in liver, kidney, skeletal muscle and heart. VEGI-174 mRNA was more abundant in heart, skeletal muscle, pancreas, adrenal gland, and liver, while VEGI-251 was more abundant in fetal kidney and fetal lung. Overlapping expression of VEGI-251 and VEGI-174 mRNA was detected in prostate, salivary gland and placenta, whereas VEGI-192 mRNA was not readily detected by Northern blot. These expression patterns suggest the possibility of tissue or developmentally specific functions for VEGI isoforms. Alternatively, this expression pattern also supports the view that one VEGI isoform is the functional cytokine,while the others act in regulatory roles to modulate the activity of the active isoform. In this case, it is possible that the non-functional isoforms do not exist at the protein level. VEGI isoform expression has also been examined in cultured cells by RNase protection assay. All three known VEGI isoforms were detected in human endothelial cells, including coronary artery endothelial (HCAE), HUVE cells, and human microvascular endothelial (HMVE) cells. Very low levels are sometimes detected in adult bovine aortic endothelial (ABAE) cells. Little VEGI expression was detectable in human coronary artery smooth muscle (CASM) and mouse endothelioma bEND.3 cells. More than one isoform is detectable simultaneously, with VEGI-251 being the most abundant. The expression of this protein is inducible by TNF and IL-1 alpha, but not by gamma-interferon.
Localisation Endothelial cells and monocytes. However, VEGI was not expressed in either B or T cells.
Function VEGI is an endogenous inhibitor of angiogenesis produced largely by vascular endothelial cells and exerts a specific inhibitory activity on the proliferation of endothelial cells. VEGI enforces growth arrest of endothelial cells in G0 and early G1 phases of the cell cycle but induces apoptosis in proliferating endothelial cells. The MAPKs p38 and jun N-terminal kinase (JNK) are required for VEGI-mediated endothelial inhibition. Engineered overexpression of secreted VEGI by cancer cells or systemic administration of recombinant VEGI to tumor-bearing mice inhibits tumor growth in numerous tumor models. Recent studies show that VEGI helps modulate the immune system by activating T cells and stimulating dendritic cell maturation, suggesting that VEGI is directly involved in modulating the interaction between the endothelium and the immune system. Recombinant VEGI has an inhibitory activity on mouse bone marrow-derived EPCs in culture, preventing their differentiation toward endothelial cells.
Interaction of TL1A with DR3 promotes T cell expansion during an immune response (Migone et al., 2002).
Homology VEGI exhibits 20-30% sequence homology to human TNF-alpha, TNF-beta, and the Fas ligand, similar to that among other TNF family members.

Implicated in

Note
  
Entity Colon carcinoma
Note Local production of a secreted form of VEGI via gene transfer caused complete suppression of the growth of MC-38 murine colon cancers in syngeneic C57BL/6mice. Histological examination showed marked reduction of vascularization in MC-38 tumors that expressed soluble but not membrane-bound VEGI or were transfected with control vector. The conditioned media from soluble VEGI-expressing cells showed marked inhibitory effect on in vitro proliferation of adult bovine aortic endothelial cells.
  
  
Entity Breast cancer
Note The anticancer potential of VEGI was examined in a breast cancer xenograft tumor model in which the cancer cells were co-injected with Chinese hamster ovary cells overexpressing a secreted form of the protein. The co-injection resulted in potent inhibition of xenograft tumor growth. Our findings are consistent with the view that VEGI is an endothelial cell-specific negative regulator of angiogenesis.
  
  
Entity Mucosal vaccine adjuvant
Note Kayamuro et al., (2009) reported that TL1A induced the strongest immune response and augmented OVA-specific IgG and IgA responses in serum and mucosal compartments, respectively. The OVA-specific immune response of TL1A was characterized by high levels of serum IgG1 and increased production of IL-4 and IL-5 from splenocytes of immunized mice, suggesting that TL1A might induce Th2-type responses. These findings indicate that TL1A has the most potential as a mucosal adjuvant among the TNFS cytokines.
  
  
Entity Inflammatory bowel disease
Note Bamias et al., (2003) provided evidence that the novel cytokine TL1A may play an important role in a Th1-mediated disease such as Crohn's disease. Takedatsu et al., (2008) revealed that TL1A is an important modulator in the development of chronic mucosal inflammation by enhancing T(H)1 and T(H)17 effector functions. The central role of TL1A represents an attractive, novel therapeutic target for the treatment of Crohn's disease patients.
  
  
Entity Inflammatory arthritis
Note Bull et al., (2008) demonstrated that the DR3-TL1A pathway regulates joint destruction in two murine models of arthritis and represents a potential novel target for therapeutic intervention in inflammatory joint disease. Bamias et al., (2008) concluded that TL1A may serve as an inflammatory marker in rheumatoid arthritis. Interactions between TL1A and its receptors may be important in the pathogenesis of rheumatoid arthritis.
  
  
Entity Renal inflammation and injury
Note Al-Lamki et al., (2008) suggested that TL1A may contribute to renal inflammation and injury through DR3-mediated activation of NF-kappaB and caspase-3, respectively, but that an unidentified receptor may mediate the NF-kappaB-independent induction of TNFR2 in tubular epithelial cells.
  

Bibliography

TL1A both promotes and protects from renal inflammation and injury.
Al-Lamki RS, Wang J, Tolkovsky AM, Bradley JA, Griffin JL, Thiru S, Wang EC, Bolton E, Min W, Moore P, Pober JS, Bradley JR.
J Am Soc Nephrol. 2008 May;19(5):953-60. Epub 2008 Feb 20.
PMID 18287561
 
Endothelial progenitor cells for postnatal vasculogenesis.
Asahara T, Kawamoto A.
Am J Physiol Cell Physiol. 2004 Sep;287(3):C572-9. (REVIEW)
PMID 15308462
 
Expression, localization, and functional activity of TL1A, a novel Th1-polarizing cytokine in inflammatory bowel disease.
Bamias G, Martin C 3rd, Marini M, Hoang S, Mishina M, Ross WG, Sachedina MA, Friel CM, Mize J, Bickston SJ, Pizarro TT, Wei P, Cominelli F.
J Immunol. 2003 Nov 1;171(9):4868-74.
PMID 14568967
 
Role of TL1A and its receptor DR3 in two models of chronic murine ileitis.
Bamias G, Mishina M, Nyce M, Ross WG, Kollias G, Rivera-Nieves J, Pizarro TT, Cominelli F.
Proc Natl Acad Sci U S A. 2006 May 30;103(22):8441-6. Epub 2006 May 12.
PMID 16698931
 
Circulating levels of TNF-like cytokine 1A (TL1A) and its decoy receptor 3 (DcR3) in rheumatoid arthritis.
Bamias G, Siakavellas SI, Stamatelopoulos KS, Chryssochoou E, Papamichael C, Sfikakis PP.
Clin Immunol. 2008 Nov;129(2):249-55. Epub 2008 Aug 30.
PMID 18757243
 
The Death Receptor 3-TNF-like protein 1A pathway drives adverse bone pathology in inflammatory arthritis.
Bull MJ, Williams AS, Mecklenburgh Z, Calder CJ, Twohig JP, Elford C, Evans BA, Rowley TF, Slebioda TJ, Taraban VY, Al-Shamkhani A, Wang EC.
J Exp Med. 2008 Oct 27;205(11):2457-64. Epub 2008 Sep 29.
PMID 18824582
 
Preparation and characterization of a novel chimeric protein VEGI-CTT in Escherichia coli.
Cai J, Wei R, Cheng J.
J Biomed Biotechnol. 2008;2008:564969.
PMID 18769489
 
A novel secreted splice variant of vascular endothelial cell growth inhibitor.
Chew LJ, Pan H, Yu J, Tian S, Huang WQ, Zhang JY, Pang S, Li LY.
FASEB J. 2002 May;16(7):742-4. Epub 2002 Mar 26.
PMID 11923219
 
Endothelial progenitor cells control the angiogenic switch in mouse lung metastasis.
Gao D, Nolan DJ, Mellick AS, Bambino K, McDonnell K, Mittal V.
Science. 2008 Jan 11;319(5860):195-8.
PMID 18187653
 
VEGI-192, a new isoform of TNFSF15, specifically eliminates tumor vascular endothelial cells and suppresses tumor growth.
Hou W, Medynski D, Wu S, Lin X, Li LY.
Clin Cancer Res. 2005 Aug 1;11(15):5595-602.
PMID 16061878
 
Purification and crystallization of recombinant human TNF-like ligand TL1A.
Jin T, Kim S, Guo F, Howard A, Zhang YZ.
Cytokine. 2007 Nov;40(2):115-22. Epub 2007 Oct 1.
PMID 17905596
 
TNF superfamily member, TL1A, is a potential mucosal vaccine adjuvant.
Kayamuro H, Yoshioka Y, Abe Y, Katayama K, Yoshida T, Yamashita K, Yoshikawa T, Hiroi T, Itoh N, Kawai Y, Mayumi T, Kamada H, Tsunoda S, Tsutsumi Y.
Biochem Biophys Res Commun. 2009 Jul 3;384(3):296-300. Epub 2009 May 4.
PMID 19406102
 
Vascular endothelial growth inhibitor (VEGI), an endogenous negative regulator of angiogenesis.
Metheny-Barlow LJ, Li LY.
Semin Ophthalmol. 2006 Jan-Mar;21(1):49-58. (REVIEW)
PMID 16517446
 
TL1A is a TNF-like ligand for DR3 and TR6/DcR3 and functions as a T cell costimulator.
Migone TS, Zhang J, Luo X, Zhuang L, Chen C, Hu B, Hong JS, Perry JW, Chen SF, Zhou JX, Cho YH, Ullrich S, Kanakaraj P, Carrell J, Boyd E, Olsen HS, Hu G, Pukac L, Liu D, Ni J, Kim S, Gentz R, Feng P, Moore PA, Ruben SM, Wei P.
Immunity. 2002 Mar;16(3):479-92.
PMID 11911831
 
TL1A (TNFSF15) regulates the development of chronic colitis by modulating both T-helper 1 and T-helper 17 activation.
Takedatsu H, Michelsen KS, Wei B, Landers CJ, Thomas LS, Dhall D, Braun J, Targan SR.
Gastroenterology. 2008 Aug;135(2):552-67. Epub 2008 May 7.
PMID 18598698
 
Characterization of a novel TNF-like ligand and recently described TNF ligand and TNF receptor superfamily genes and their constitutive and inducible expression in hematopoietic and non-hematopoietic cells.
Tan KB, Harrop J, Reddy M, Young P, Terrett J, Emery J, Moore G, Truneh A.
Gene. 1997 Dec 19;204(1-2):35-46.
PMID 9434163
 
The endothelial cell-produced antiangiogenic cytokine vascular endothelial growth inhibitor induces dendritic cell maturation.
Tian F, Grimaldo S, Fujita M, Cutts J, Vujanovic NL, Li LY.
J Immunol. 2007 Sep 15;179(6):3742-51.
PMID 17785811
 
Inhibition of endothelial progenitor cell differentiation by VEGI.
Tian F, Liang PH, Li LY.
Blood. 2009 May 21;113(21):5352-60. Epub 2009 Mar 27.
PMID 19329781
 
Modulation of endothelial cell growth arrest and apoptosis by vascular endothelial growth inhibitor.
Yu J, Tian S, Metheny-Barlow L, Chew LJ, Hayes AJ, Pan H, Yu GL, Li LY.
Circ Res. 2001 Dec 7;89(12):1161-7.
PMID 11739281
 
TL1, a novel tumor necrosis factor-like cytokine, induces apoptosis in endothelial cells. Involvement of activation of stress protein kinases (stress-activated protein kinase and p38 mitogen-activated protein kinase) and caspase-3-like protease.
Yue TL, Ni J, Romanic AM, Gu JL, Keller P, Wang C, Kumar S, Yu GL, Hart TK, Wang X, Xia Z, DeWolf WE Jr, Feuerstein GZ.
J Biol Chem. 1999 Jan 15;274(3):1479-86.
PMID 9880523
 
VEGI, a novel cytokine of the tumor necrosis factor family, is an angiogenesis inhibitor that suppresses the growth of colon carcinomas in vivo.
Zhai Y, Ni J, Jiang GW, Lu J, Xing L, Lincoln C, Carter KC, Janat F, Kozak D, Xu S, Rojas L, Aggarwal BB, Ruben S, Li LY, Gentz R, Yu GL.
FASEB J. 1999 Jan;13(1):181-9.
PMID 9872942
 
Inhibition of angiogenesis and breast cancer xenograft tumor growth by VEGI, a novel cytokine of the TNF superfamily.
Zhai Y, Yu J, Iruela-Arispe L, Huang WQ, Wang Z, Hayes AJ, Lu J, Jiang G, Rojas L, Lippman ME, Ni J, Yu GL, Li LY.
Int J Cancer. 1999 Jul 2;82(1):131-6.
PMID 10360832
 
Structure and inhibitory effects on angiogenesis and tumor development of a new vascular endothelial growth inhibitor.
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Citation

This paper should be referenced as such :
Yang, GL ; Qi, JW ; Zhang, ZS ; Li, LY
TNFSF15 (tumor necrosis factor (ligand) superfamily, member 15)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(7):665-669.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/TNFSF15ID42638ch9q32.html


External links

Nomenclature
HGNC (Hugo)TNFSF15   11931
Cards
AtlasTNFSF15ID42638ch9q32
Entrez_Gene (NCBI)TNFSF15  9966  TNF superfamily member 15
AliasesTL1; TL1A; TNLG1B; VEGI; 
VEGI192A
GeneCards (Weizmann)TNFSF15
Ensembl hg19 (Hinxton)ENSG00000181634 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000181634 [Gene_View]  chr9:114784635-114792530 [Contig_View]  TNFSF15 [Vega]
ICGC DataPortalENSG00000181634
TCGA cBioPortalTNFSF15
AceView (NCBI)TNFSF15
Genatlas (Paris)TNFSF15
WikiGenes9966
SOURCE (Princeton)TNFSF15
Genetics Home Reference (NIH)TNFSF15
Genomic and cartography
GoldenPath hg38 (UCSC)TNFSF15  -     chr9:114784635-114792530 -  9q32   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)TNFSF15  -     9q32   [Description]    (hg19-Feb_2009)
EnsemblTNFSF15 - 9q32 [CytoView hg19]  TNFSF15 - 9q32 [CytoView hg38]
Mapping of homologs : NCBITNFSF15 [Mapview hg19]  TNFSF15 [Mapview hg38]
OMIM604052   
Gene and transcription
Genbank (Entrez)AF039390 AF520785 AK291642 AK313721 AW014795
RefSeq transcript (Entrez)NM_001204344 NM_005118
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)TNFSF15
Cluster EST : UnigeneHs.23349 [ NCBI ]
CGAP (NCI)Hs.23349
Alternative Splicing GalleryENSG00000181634
Gene ExpressionTNFSF15 [ NCBI-GEO ]   TNFSF15 [ EBI - ARRAY_EXPRESS ]   TNFSF15 [ SEEK ]   TNFSF15 [ MEM ]
Gene Expression Viewer (FireBrowse)TNFSF15 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)9966
GTEX Portal (Tissue expression)TNFSF15
Protein : pattern, domain, 3D structure
UniProt/SwissProtO95150   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtO95150  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO95150
Splice isoforms : SwissVarO95150
PhosPhoSitePlusO95150
Domaine pattern : Prosite (Expaxy)TNF_2 (PS50049)   
Domains : Interpro (EBI)TNF    TNF_dom    TNFSF15    Tumour_necrosis_fac-like_dom   
Domain families : Pfam (Sanger)TNF (PF00229)   
Domain families : Pfam (NCBI)pfam00229   
Domain families : Smart (EMBL)TNF (SM00207)  
Conserved Domain (NCBI)TNFSF15
DMDM Disease mutations9966
Blocks (Seattle)TNFSF15
PDB (SRS)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
PDB (PDBSum)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
PDB (IMB)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
PDB (RSDB)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
Structural Biology KnowledgeBase2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
SCOP (Structural Classification of Proteins)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
CATH (Classification of proteins structures)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
SuperfamilyO95150
Human Protein AtlasENSG00000181634
Peptide AtlasO95150
HPRD04956
IPIIPI00184879   IPI00478864   IPI00021380   
Protein Interaction databases
DIP (DOE-UCLA)O95150
IntAct (EBI)O95150
FunCoupENSG00000181634
BioGRIDTNFSF15
STRING (EMBL)TNFSF15
ZODIACTNFSF15
Ontologies - Pathways
QuickGOO95150
Ontology : AmiGOreceptor binding  cytokine activity  tumor necrosis factor receptor binding  extracellular space  intracellular  plasma membrane  plasma membrane  integral component of plasma membrane  apoptotic process  activation of cysteine-type endopeptidase activity involved in apoptotic process  immune response  signal transduction  activation of NF-kappaB-inducing kinase activity  integral component of membrane  tumor necrosis factor-mediated signaling pathway  cytokine metabolic process  
Ontology : EGO-EBIreceptor binding  cytokine activity  tumor necrosis factor receptor binding  extracellular space  intracellular  plasma membrane  plasma membrane  integral component of plasma membrane  apoptotic process  activation of cysteine-type endopeptidase activity involved in apoptotic process  immune response  signal transduction  activation of NF-kappaB-inducing kinase activity  integral component of membrane  tumor necrosis factor-mediated signaling pathway  cytokine metabolic process  
Pathways : KEGGCytokine-cytokine receptor interaction   
REACTOMEO95150 [protein]
REACTOME PathwaysR-HSA-5669034 [pathway]   
NDEx NetworkTNFSF15
Atlas of Cancer Signalling NetworkTNFSF15
Wikipedia pathwaysTNFSF15
Orthology - Evolution
OrthoDB9966
GeneTree (enSembl)ENSG00000181634
Phylogenetic Trees/Animal Genes : TreeFamTNFSF15
HOVERGENO95150
HOGENOMO95150
Homologs : HomoloGeneTNFSF15
Homology/Alignments : Family Browser (UCSC)TNFSF15
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTNFSF15 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TNFSF15
dbVarTNFSF15
ClinVarTNFSF15
1000_GenomesTNFSF15 
Exome Variant ServerTNFSF15
ExAC (Exome Aggregation Consortium)TNFSF15 (select the gene name)
Genetic variants : HAPMAP9966
Genomic Variants (DGV)TNFSF15 [DGVbeta]
DECIPHERTNFSF15 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisTNFSF15 
Mutations
ICGC Data PortalTNFSF15 
TCGA Data PortalTNFSF15 
Broad Tumor PortalTNFSF15
OASIS PortalTNFSF15 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICTNFSF15  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDTNFSF15
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 TNFSF15
DgiDB (Drug Gene Interaction Database)TNFSF15
DoCM (Curated mutations)TNFSF15 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)TNFSF15 (select a term)
intoGenTNFSF15
NCG5 (London)TNFSF15
Cancer3DTNFSF15(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM604052   
Orphanet874   
MedgenTNFSF15
Genetic Testing Registry TNFSF15
NextProtO95150 [Medical]
TSGene9966
GENETestsTNFSF15
Target ValidationTNFSF15
Huge Navigator TNFSF15 [HugePedia]
snp3D : Map Gene to Disease9966
BioCentury BCIQTNFSF15
ClinGenTNFSF15
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD9966
Chemical/Pharm GKB GenePA36623
Clinical trialTNFSF15
Miscellaneous
canSAR (ICR)TNFSF15 (select the gene name)
Probes
Litterature
PubMed120 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineTNFSF15
EVEXTNFSF15
GoPubMedTNFSF15
iHOPTNFSF15
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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