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CD248 (CD248 molecule, endosialin)

Written2008-12Renate Becker, Hellmut G Augustin
Department Vascular Oncology, Metastasis Research, German Cancer Research Center, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany

(Note : for Links provided by Atlas : click)


Alias (NCBI)2610111G01Rik
HGNC (Hugo) CD248
HGNC Alias symbTEM1
HGNC Alias nameendosialin
 tumor endothelial marker 1
HGNC Previous nameCD164L1
HGNC Previous nameCD164 sialomucin-like 1
 CD248 antigen, endosialin
 CD248 molecule, endosialin
LocusID (NCBI) 57124
Atlas_Id 968
Location 11q13.2  [Link to chromosome band 11q13]
Location_base_pair Starts at 66314494 and ends at 66317044 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping CD248.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
CD248 (11q13.2)::CD248 (11q13.2)CD248 (11q13.2)::NGFR (17q21.33)CD248 (11q13.2)::PPP1R7 (2q37.3)
Note The endosialin gene is localized on the minus strand.


  The endosialin gene is localized on the q arm of chromosome 11. The single-exon gene is transcribed from the minus strand (modified from Entrez Gene).
Description Endosialin was identified to be transcribed from a 2557 bp single-exon gene localized on chromosome 11q13 (Rettig et al., 1992; Christian et al., 2001), a region containing genes for a number of cell surface antigens (Rettig et al., 1992; Rettig and Old, 1989).
Transcription The 2580 bp mRNA of Endosialin consist of a 17 bp 5' UTR, an ORF of 2274 bp (AF279142), and a 289 bp 3' UTR (Christian et al., 2001).
Pseudogene No.


Note Although Endosialin was originally described as tumor endothelial marker (Rettig et al., 1992; Seaman et al., 2007; St Croix et al., 2000), it turned out that Endosialin is a marker for activated mesenchymal cells, including myofibroblasts, pericytes and smooth muscle cells (SMC) (MacFadyen et al., 2005; Christian et al., 2008).
  Structure of Endosialin and its homologues Thrombomodulin and C1qRp.
A: The extracellular domain of Endosialin consists of a signal sequence (orange triangle), a C-lectin like domain (dark green octagon), a Sushi/CCP/scr domain (grey circle), 3 EGF-like domains (red circles), and a negatively charged, O-glycosylated mucin-like domain (light green rectangle). The single transmembrane domain (blue cylinder) is followed by a short cytoplasmic tail (yellow cylinder).
B: The globular domains of Endosialin are homologue to thrombomodulin, containing 6 EGF repeats and the complement receptor C1qRp, demonstrating 5 EGF repeats.
Description Endosialin is a 757 amino acid (aa) type I C-type lectin-like transmembrane protein (Christian et al., 2001). The core protein has a molecular weight of 95 kDa (Rettig et al., 1992; Christian et al., 2001). The distinct extracellular domain (aa 1-685) consists of a signal leader peptide (aa 1-20) and 5 globular domains followed by a mucin-like region (Figure A) (Christian et al., 2001). The single hydrophobic transmembrane domain spans the aa 686-706, followed by a short intracellular domain of 50 aa (aa 707-757). The 5 globular domains are well defined as C-type lectin-like domain (aa 20-157), a Sushi/CCP/scr like domain (aa 176-230) and 3 EGF repeats (aa 235-271, aa 274-311, aa 316-350). The EGF repeats 2 and 3 are predicted to have a Ca2+ binding function. In contrast, in the C-terminal part (aa 360-757) specific binding sites or catalytic domains were not identified (Christian et al., 2001; Carson-Walter et al., 2001). The glycosylation and sialic acid modification of more than 30 possible O-glycosylation sites, but only N-glycosylation Asn-Xaa-(Ser/Thr) consensus sequence on Asn-628 results in a shift of the molecular weight from 95 kDa to 165 kDa (Rettig et al., 1992; Christian et al., 2001). Additionally, a 120 kDa asialo form of Endosialin was identified (Rettig et al., 1992; Christian et al., 2001). A ~150 kDa form of Endosialin was detectable in the LA1-5s cell supernatant (Rettig et al., 1992; Christian et al., 2001).
Expression Endosialin is expressed in the majority of human carcinomas, sarcomas and neuroectodermal tumors (Rettig et al., 1992; St Croix et al., 2000; Brady et al., 2004; Huber et al., 2006; Madden et al., 2004; Davies et al., 2004; Rmali et al., 2005; Christian et al., 2008) as well as during physiological processes, such as corpus luteum formation and wound healing (Carson-Walter et al., 2001; St Croix et al., 2000). In contrast, Endosialin is not or weakly expressed in the mesenchymal compartment of corresponding normal human tissues (MacFadyen et al., 2007; MacFadyen et al., 2005; Carson-Walter et al., 2001). Endosialin-positive cells in the tumors were identified as myofibroblasts, tumor vessel-associated pericytes and smooth muscle cells (MacFadyen et al., 2005; Huber et al., 2006; Christian et al., 2008; MacFadyen et al., 2007; Bagley et al., 2008a; Virgintino et al., 2007; Simonavicius et al., 2008), although Endosialin was described as tumor endothelial marker (Rettig et al., 1992; St Croix et al., 2000). In addition, recent publications identified Endosialin expressing CD45+ VE-cadherin+ CD146+ CD34+ CD31+ TEM1+ Tem7+ vascular leukocytes (VLC) (Conejo-Garcia et al., 2005), as well as Endosialin-positive VEGFR 2+ CD31+ CD45- VE-cadherin+ endothelial precursor cells (EPC) (Bagley et al., 2008b). During neovascularization of the human fetal telencephalon, Endosialin is expressed by vessel-associated pericytes (Virgintino et al., 2007).
In vitro, Endosialin is expressed by fibroblasts, pericytes, smooth muscle cells and preadipocytes (Christian et al., 2008). Some neuroblastoma cell lines including LA1-5s, IMR-32 and SMS-SAN express Endosialin (Rettig et al., 1992).
The mouse homologue of Endosialin is strongly and heterogeneously expressed in almost all tissues during embryonic development (Opavsky et al., 2001; Rupp et al., 2006; MacFadyen et al., 2007). The expression is decreased in new-born mice and almost undetectable in tissues of adult mice (Carson-Walter et al., 2001; MacFadyen et al., 2007; Lax et al., 2007; Rupp et al., 2006).
Localisation Endosialin is localized on the cell surface (Christian et al., 2001; Christian et al., 2008; MacFadyen et al., 2005). Some staining of the Golgi can also be observed, since Endosialin is a Typ-I transmembrane protein (MacFadyen et al., 2005).
Function A role of Endosialin in tumor progression and metastasis was demonstrated by experiments with Endosialin knock-out mice. In abdominal xenograft transplantations, tumor volume and the incidence of distant metastases were significantly reduced in knock-out mice compared to wild type mice, resulting in an increased survival rate of Endosialin-deficient mice (Nanda et al., 2006). Nevertheless, the molecular function of Endosialin is far from being understood. Recent publications demonstrated a role of Endosialin in the proliferation and migration of myofibroblasts (Christian et al., 2008). The tube-formation and migration of Endosialin expressing pericytes could be blocked by anti-Endosialin antibodies (Bagley et al., 2008a). Additionally, Endosialin overexpressing CHO cells demonstrated increased adhesion to fibronectin, migration though Matrigel and MMP-9 activity (Tomkowicz et al., 2007).
It is not clarified yet, how these functions of Endosialin result in tumor progression and metastasis. However, these findings indicate a role of Endosialin in early angiogenic stages (Bagley et al., 2008b) and vessel maturation, as well as a function of Endosialin in tumor stroma formation and reorganization of the tumor stroma including tumor blood vessels in tissues where areas of stable blood supply are in close proximity to regions of necrosis, hypoxia and excessive growth (Christian et al., 2001). Interestingly, recent findings described the induction of Endosialin expression by hypoxia, mediated by HIF-2a (Ohradanova et al., 2008).
Additionally, Endosialin functions as receptor for extracellular matrix components (Tomkowicz et al., 2007) and tumor cell expressed ligands like Mac-2 Binding Protein. The Endosialin-Mac-2 Binding Protein interaction results in a decreased adhesion between tumor cells and the surrounding myofibroblasts (Becker et al., 2008). However, this mechanism is not analyzed in detail.
Homology Whereas the C terminal part of human Endosialin (aa 361-757) showed no sequence homology to other proteins (Christian et al., 2001), the globular N-terminal extracellular part (aa 30-360) demonstrated 39% homology to thrombomodulin precursor protein and 33% homology to the complement receptor C1qRp (Figure B) (Christian et al., 2001). Although there is only moderate sequence identity, cysteine residues predicted to form disulfide bridges and a WIGL consensus motive found in endocytosis regulating proteins (Dean et al., 2000; Nepomuceno et al., 1997) localized in the C-type lectin-like domain are conserved in all three proteins.
Mouse Endosialin (mEn) shows 77.5% homology to human Endosialin (Opavsky et al., 2001; Carson-Walter et al., 2001). Like its human counterpart, mEn is a 765 aa type I transmembrane protein with a 17 aa signal peptide, a C-type lectin-like domain (aa 22-157), a Sushi domain (aa 164-230) and 3 EGF-like repeats (aa 234-272, aa 274-311 and aa 315-351), followed by a sialomucin-like region, a single membrane spanning domain (22 aa), and a 51 aa long cytoplasmatic tail. mEn is also transcribed from a single copy, intron-less gene, located on mouse chromosome 19, a region homologue to human chromosome region 11q. The 82 kDa core protein has multiple O- glycosylation sites in the extracellular domain but only one predicted N-glycosylation site on position aa 636, resulting in a glycosylated protein of 92 kDa. Whereas the mucine-like domain of mEn (aa 478-610) and human Endosialin are hardly conserved, the transmembrane domains are identical and only 4 aa are substituted in the cytoplasmatic tails (Carson-Walter et al., 2001; Opavsky et al., 2001). Additionally, possible phosphorylation and N-myristoylation sites as well as a PDZ binding sequence (Carson-Walter et al., 2001) were identified in the intracellular domain, indicating an evolutionary conserved function between mouse and human Endosialin.


Note In one publication, a single base pare substitution at bp 717 (aa 239) was detected (Brady et al., 2004). A resulting change in the function of Endosialin caused by this mutation has not been referred yet.

Implicated in

Entity Tumors
Disease Endosialin is poorly detectable in normal tissues. In contrast, it is highly expressed in human carcinomas, sarcomas and neuroectodermal tumors (Rettig et al., 1992; Christian et al., 2008).
Entity Brain tumors
Disease Endosialin expression was detected in 40% of analyzed benign meningioma (grade I) and less invasive grade II astrocytoma specimens, whereas Endosialin is undetectable in normal brain. In higher grade brain tumors Endosialin expression was detectable in 67% and 100% of grade III anaplastic astrocytoma and highly invasive glioblastoma multiforme specimens, respectively (Brady et al., 2004).
Prognosis Endosialin expression correlates with high tumor grade and aggressive histological behavior in human brain tumors (Brady et al., 2004; Simonavicius et al., 2008).
Entity Breast carcinomas
Disease Endosialin is significantly upregulated in breast carcinoma samples of patients with nodal involvement, as well as in specimens of patients with recurrent disease or death caused by breast cancer (Davies et al., 2004).
Entity Malignant melanoma
Disease Endosialin expression was detectable in benign melanocytic nevi, cutaneous melanoma metastases, lymph node metastases, basal cell carcinomas and squamous cell carcinomas. Whereas Endosialin expression is restricted to scattered fibroblasts in the normal human skin, the Endosialin expression pattern is heterogeneous (reactive fibroblasts and vessel-like structures) in the different stages of malignant melanoma progression (Huber et al., 2006; Christian et al., 2008).


Endosialin/TEM 1/CD248 is a pericyte marker of embryonic and tumor neovascularization.
Bagley RG, Honma N, Weber W, Boutin P, Rouleau C, Shankara S, Kataoka S, Ishida I, Roberts BL, Teicher BA.
Microvasc Res. 2008a Nov;76(3):180-8. Epub 2008 Aug 8.
PMID 18761022
Human endothelial precursor cells express tumor endothelial marker 1/endosialin/CD248.
Bagley RG, Rouleau C, St Martin T, Boutin P, Weber W, Ruzek M, Honma N, Nacht M, Shankara S, Kataoka S, Ishida I, Roberts BL, Teicher BA.
Mol Cancer Ther. 2008b Aug;7(8):2536-46.
PMID 18723498
Tumor stroma marker endosialin (Tem1) is a binding partner of metastasis-related protein Mac-2 BP/90K.
Becker R, Lenter MC, Vollkommer T, Boos AM, Pfaff D, Augustin HG, Christian S.
FASEB J. 2008 Aug;22(8):3059-67. Epub 2008 May 19.
PMID 18490383
Human endosialin (tumor endothelial marker 1) is abundantly expressed in highly malignant and invasive brain tumors.
Brady J, Neal J, Sadakar N, Gasque P.
J Neuropathol Exp Neurol. 2004 Dec;63(12):1274-83.
PMID 15624764
Cell surface tumor endothelial markers are conserved in mice and humans.
Carson-Walter EB, Watkins DN, Nanda A, Vogelstein B, Kinzler KW, St Croix B.
Cancer Res. 2001 Sep 15;61(18):6649-55.
PMID 11559528
Endosialin (Tem1) is a marker of tumor-associated myofibroblasts and tumor vessel-associated mural cells.
Christian S, Winkler R, Helfrich I, Boos AM, Besemfelder E, Schadendorf D, Augustin HG.
Am J Pathol. 2008 Feb;172(2):486-94. Epub 2008 Jan 10.
PMID 18187565
Vascular leukocytes contribute to tumor vascularization.
Conejo-Garcia JR, Buckanovich RJ, Benencia F, Courreges MC, Rubin SC, Carroll RG, Coukos G.
Blood. 2005 Jan 15;105(2):679-81. Epub 2004 Sep 9.
PMID 15358628
Levels of expression of endothelial markers specific to tumour-associated endothelial cells and their correlation with prognosis in patients with breast cancer.
Davies G, Cunnick GH, Mansel RE, Mason MD, Jiang WG.
Clin Exp Metastasis. 2004;21(1):31-7.
PMID 15065600
Molecular and cellular properties of the rat AA4 antigen, a C-type lectin-like receptor with structural homology to thrombomodulin.
Dean YD, McGreal EP, Akatsu H, Gasque P.
J Biol Chem. 2000 Nov 3;275(44):34382-92.
PMID 10934210
Expression of stromal cell markers in distinct compartments of human skin cancers.
Huber MA, Kraut N, Schweifer N, Dolznig H, Peter RU, Schubert RD, Scharffetter-Kochanek K, Pehamberger H, Garin-Chesa P.
J Cutan Pathol. 2006 Feb;33(2):145-55.
PMID 16420310
CD248/Endosialin is dynamically expressed on a subset of stromal cells during lymphoid tissue development, splenic remodeling and repair.
Lax S, Hou TZ, Jenkinson E, Salmon M, MacFadyen JR, Isacke CM, Anderson G, Cunningham AF, Buckley CD.
FEBS Lett. 2007 Jul 24;581(18):3550-6. Epub 2007 Jul 3.
PMID 17628549
Endosialin is expressed on stromal fibroblasts and CNS pericytes in mouse embryos and is downregulated during development.
MacFadyen J, Savage K, Wienke D, Isacke CM.
Gene Expr Patterns. 2007 Jan;7(3):363-9. Epub 2006 Jul 27.
PMID 16965941
Endosialin (TEM1, CD248) is a marker of stromal fibroblasts and is not selectively expressed on tumour endothelium.
MacFadyen JR, Haworth O, Roberston D, Hardie D, Webster MT, Morris HR, Panico M, Sutton-Smith M, Dell A, van der Geer P, Wienke D, Buckley CD, Isacke CM.
FEBS Lett. 2005 May 9;579(12):2569-75. Epub 2005 Apr 7.
PMID 15862292
Vascular gene expression in nonneoplastic and malignant brain.
Madden SL, Cook BP, Nacht M, Weber WD, Callahan MR, Jiang Y, Dufault MR, Zhang X, Zhang W, Walter-Yohrling J, Rouleau C, Akmaev VR, Wang CJ, Cao X, St Martin TB, Roberts BL, Teicher BA, Klinger KW, Stan RV, Lucey B, Carson-Walter EB, Laterra J, Walter KA.
Am J Pathol. 2004 Aug;165(2):601-8.
PMID 15277233
Tumor endothelial marker 1 (Tem1) functions in the growth and progression of abdominal tumors.
Nanda A, Karim B, Peng Z, Liu G, Qiu W, Gan C, Vogelstein B, St Croix B, Kinzler KW, Huso DL.
Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3351-6. Epub 2006 Feb 21.
PMID 16492758
cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro.
Nepomuceno RR, Henschen-Edman AH, Burgess WH, Tenner AJ.
Immunity. 1997 Feb;6(2):119-29.
PMID 9047234
Hypoxia upregulates expression of human endosialin gene via hypoxia-inducible factor 2.
Ohradanova A, Gradin K, Barathova M, Zatovicova M, Holotnakova T, Kopacek J, Parkkila S, Poellinger L, Pastorekova S, and Pastorek J.
Br. J. Cancer 2008; 99: 1348-1356
PMID 18813310
Molecular characterization of the mouse Tem1/endosialin gene regulated by cell density in vitro and expressed in normal tissues in vivo.
Opavsky R, Haviernik P, Jurkovicova D, Garin MT, Copeland NG, Gilbert DJ, Jenkins NA, Bies J, Garfield S, Pastorekova S, Oue A, Wolff L.
J Biol Chem. 2001 Oct 19;276(42):38795-807. Epub 2001 Aug 6.
PMID 11489895
Identification of endosialin, a cell surface glycoprotein of vascular endothelial cells in human cancer.
Rettig WJ, Garin-Chesa P, Healey JH, Su SL, Jaffe EA, Old LJ.
Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10832-6.
PMID 1438285
Immunogenetics of human cell surface differentiation.
Rettig WJ, Old LJ.
Annu Rev Immunol. 1989;7:481-511.
PMID 2653374
Prognostic values of tumor endothelial markers in patients with colorectal cancer.
Rmali KA, Puntis MC, Jiang WG.
World J Gastroenterol. 2005 Mar 7;11(9):1283-6.
PMID 15761964
Mouse endosialin, a C-type lectin-like cell surface receptor: expression during embryonic development and induction in experimental cancer neoangiogenesis.
Rupp C, Dolznig H, Puri C, Sommergruber W, Kerjaschki D, Rettig WJ, Garin-Chesa P.
Cancer Immun. 2006 Jul 31;6:10.
PMID 16875435
Genes that distinguish physiological and pathological angiogenesis.
Seaman S, Stevens J, Yang MY, Logsdon D, Graff-Cherry C, St Croix B.
Cancer Cell. 2007 Jun;11(6):539-54.
PMID 17560335
Endosialin (CD248) is a marker of tumor-associated pericytes in high-grade glioma.
Simonavicius N, Robertson D, Bax DA, Jones C, Huijbers IJ, Isacke CM.
Mod Pathol. 2008 Mar;21(3):308-15. Epub 2008 Jan 11.
PMID 18192970
Genes expressed in human tumor endothelium.
St Croix B, Rago C, Velculescu V, Traverso G, Romans KE, Montgomery E, Lal A, Riggins GJ, Lengauer C, Vogelstein B, Kinzler KW.
Science. 2000 Aug 18;289(5482):1197-202.
PMID 10947988
Interaction of endosialin/TEM1 with extracellular matrix proteins mediates cell adhesion and migration.
Tomkowicz B, Rybinski K, Foley B, Ebel W, Kline B, Routhier E, Sass P, Nicolaides NC, Grasso L, Zhou Y.
Proc Natl Acad Sci U S A. 2007 Nov 13;104(46):17965-70. Epub 2007 Nov 6.
PMID 17986615
An intimate interplay between precocious, migrating pericytes and endothelial cells governs human fetal brain angiogenesis.
Virgintino D, Girolamo F, Errede M, Capobianco C, Robertson D, Stallcup WB, Perris R, Roncali L.
Angiogenesis. 2007;10(1):35-45. Epub 2007 Jan 17.
PMID 17225955


This paper should be referenced as such :
Becker, R ; Augustin, HG
CD248 (CD248 molecule, endosialin)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(11):799-803.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)CD248   18219
Entrez_Gene (NCBI)CD248    CD248 molecule
AliasesCD164L1; TEM1
GeneCards (Weizmann)CD248
Ensembl hg19 (Hinxton)ENSG00000174807 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000174807 [Gene_View]  ENSG00000174807 [Sequence]  chr11:66314494-66317044 [Contig_View]  CD248 [Vega]
ICGC DataPortalENSG00000174807
TCGA cBioPortalCD248
AceView (NCBI)CD248
Genatlas (Paris)CD248
SOURCE (Princeton)CD248
Genetics Home Reference (NIH)CD248
Genomic and cartography
GoldenPath hg38 (UCSC)CD248  -     chr11:66314494-66317044 -  11q13.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)CD248  -     11q13.2   [Description]    (hg19-Feb_2009)
GoldenPathCD248 - 11q13.2 [CytoView hg19]  CD248 - 11q13.2 [CytoView hg38]
Genome Data Viewer NCBICD248 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF279142 AJ295846 AK027290 BC051340 BC098158
RefSeq transcript (Entrez)NM_020404
Consensus coding sequences : CCDS (NCBI)CD248
Gene ExpressionCD248 [ NCBI-GEO ]   CD248 [ EBI - ARRAY_EXPRESS ]   CD248 [ SEEK ]   CD248 [ MEM ]
Gene Expression Viewer (FireBrowse)CD248 [ Firebrowse - Broad ]
GenevisibleExpression of CD248 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)57124
GTEX Portal (Tissue expression)CD248
Human Protein AtlasENSG00000174807-CD248 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9HCU0   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9HCU0  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9HCU0
Domaine pattern : Prosite (Expaxy)C_TYPE_LECTIN_2 (PS50041)    EGF_2 (PS01186)    EGF_CA (PS01187)   
Domains : Interpro (EBI)C-type_lectin-like    C-type_lectin-like/link_sf    CTDL_fold    EGF-like_Ca-bd_dom    EGF-like_dom    EGF-type_Asp/Asn_hydroxyl_site    EGF_Ca-bd_CS    Growth_fac_rcpt_cys_sf   
Domain families : Pfam (Sanger)Lectin_C (PF00059)   
Domain families : Pfam (NCBI)pfam00059   
Domain families : Smart (EMBL)CLECT (SM00034)  EGF (SM00181)  EGF_CA (SM00179)  
Conserved Domain (NCBI)CD248
AlphaFold pdb e-kbQ9HCU0   
Human Protein Atlas [tissue]ENSG00000174807-CD248 [tissue]
Protein Interaction databases
IntAct (EBI)Q9HCU0
Ontologies - Pathways
Ontology : AmiGOmolecular_function  calcium ion binding  protein binding  cytoplasm  biological_process  positive regulation of cell population proliferation  external side of plasma membrane  integral component of membrane  cell migration  carbohydrate binding  extracellular matrix  lymph node development  extracellular matrix binding  anatomical structure regression  extracellular exosome  extracellular matrix protein binding  positive regulation of endothelial cell apoptotic process  
Ontology : EGO-EBImolecular_function  calcium ion binding  protein binding  cytoplasm  biological_process  positive regulation of cell population proliferation  external side of plasma membrane  integral component of membrane  cell migration  carbohydrate binding  extracellular matrix  lymph node development  extracellular matrix binding  anatomical structure regression  extracellular exosome  extracellular matrix protein binding  positive regulation of endothelial cell apoptotic process  
NDEx NetworkCD248
Atlas of Cancer Signalling NetworkCD248
Wikipedia pathwaysCD248
Orthology - Evolution
GeneTree (enSembl)ENSG00000174807
Phylogenetic Trees/Animal Genes : TreeFamCD248
Homologs : HomoloGeneCD248
Homology/Alignments : Family Browser (UCSC)CD248
Gene fusions - Rearrangements
Fusion : QuiverCD248
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerCD248 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)CD248
Exome Variant ServerCD248
GNOMAD BrowserENSG00000174807
Varsome BrowserCD248
ACMGCD248 variants
Genomic Variants (DGV)CD248 [DGVbeta]
DECIPHERCD248 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisCD248 
ICGC Data PortalCD248 
TCGA Data PortalCD248 
Broad Tumor PortalCD248
OASIS PortalCD248 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICCD248  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DCD248
Mutations and Diseases : HGMDCD248
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)CD248
DoCM (Curated mutations)CD248
CIViC (Clinical Interpretations of Variants in Cancer)CD248
NCG (London)CD248
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry CD248
NextProtQ9HCU0 [Medical]
Target ValidationCD248
Huge Navigator CD248 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDCD248
Pharm GKB GenePA134864533
Clinical trialCD248
canSAR (ICR)CD248
DataMed IndexCD248
PubMed47 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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