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ADAM10 (ADAM metallopeptidase domain 10)

Written2011-07Pascal Gelebart, Hanan Armanious, Raymond Lai
Department of Laboratory Medicine, Pathology, University of Alberta, Room 1466, 11560 University Avenue, T6G 1Z2-Edmonton, Alberta, Canada

(Note : for Links provided by Atlas : click)

Identity

Other namesAD10
CD156c
HsT18717
MADM
kuz
HGNC (Hugo) ADAM10
LocusID (NCBI) 102
Atlas_Id 44397
Location 15q21.3  [Link to chromosome band 15q21]
Location_base_pair Starts at 58887403 and ends at 59042177 bp from pter ( according to hg19-Feb_2009)  [Mapping ADAM10.png]
Fusion genes
(updated 2016)
ADAM10 (15q21.3) / ANKRD11 (16q24.3)ADAM10 (15q21.3) / FIZ1 (19q13.42)ADAM10 (15q21.3) / RER1 (1p36.32)
ADAM10 (15q21.3) / ZNF770 (15q14)CYBB (Xp11.4) / ADAM10 (15q21.3)

DNA/RNA

 
  Figure 1. Representation of the ADAM10 gene organization.
Description The gene spans a region of 15.36 kb and the coding part is divided into 16 exons.
Transcription Only one type of transcript has been described. The 2247-nucleotide transcript encodes a protein of 748 amino acid residues. The first and last exons are partially untranslated.
Pseudogene None described so far.

Protein

 
  Figure 2. Crystal structure of ADAM10 Disintegrin and cysteine-rich domain at 2.9 A resolution. Adapted from PDB (access number: 2AO7).
Description ADAM10 is a metalloproteinase composed of 748 residues.
 
  Figure 3. ADAM10 tissue expression profile. Adapted from GeneAtlas U113A.
Expression ADAM10 RNA has been reported to be present in wide range of human tissue (Yanai et al., 2005). Data obtained from GeneAtlas have shown that ADAM10 transcript is the most highly expressed in myeloid, NK cells and monocytes as well as cardiomyocytes and smooth muscle cells (figure 3). At the protein level, ADAM10 has been reported in epithelials tissue of the heart, liver and kidney (Hall and Erickson, 2003).
Localisation ADAM10 is localized at the plasma membrane. However, nuclear localization of ADAM10 has been reported in prostate cancer and in mantle cell lymphoma cells (Armanious et al., 2011).
 
  Figure 4. ADAM10 protein structure organization.
Function ADAM10 belongs to the family of metalloproteinases (Chantry et al., 1989; Chantry and Glynn, 1990; Edwards et al., 2008). ADAM10 protein is composed of multiple functional domains that include: a prodomain, a catalytic domain, a cysteine-rich domain, a transmembraneous domain, a cytoplasmic domain and a SH3 domain (Seals and Courtneidge, 2003; Edwards et al., 2008) (see figure 4). ADAM10 is synthesized as a pro-protein and therefore needs to be cleaved to be activated (Anders et al., 2001). Two proteins, the convertase 7 and the furin, have been implicated in the activation of ADAM10 (Anders et al., 2001). To date the major function of ADAM10 appears to be attributed to its enzymatic activity as a metalloproteinase. In fact, ADAM10 is involved in the intra-membrane proteolysis process, whereby it mediates ectodomain shedding of various membrane bound receptors, adhesion molecules, growth factors and cytokines like TNF-alpha (Rosendahl et al., 1997; Lunn et al., 1997; Hikita et al., 2009; Mezyk-Kopec et al., 2009), Notch (Hartmann et al., 2002; Gibb et al., 2010), E-cadherin (Maretzky et al., 2005), Ephrin (Janes et al., 2005), HER-2 (Liu et al., 2006), CD30 (Eichenauer et al., 2007), CD44 (Anderegg et al., 2009) and IL-6 receptor to name a few. The functional role of the SH3 domains of ADAM10 has never been studied. Moreover, the recent observation that ADAM10 can be found in the nucleus of some cells raises the possibility of new and uncovers function of ADAM10 (Arima et al., 2007).
ADAM10 seems to be detrimental for embryogenesis as the knockout mice for ADAM10 die at day 9.5 of embryogenesis (Hartmann et al., 2002). The mice present several developmental defects in the nervous central system as well in the cardiovascular system. This latest observation correlates well with the fact that ADAM10 transcript is highly expressed in cardiomyocyte.
In human, ADAM10 was recently been demonstrated to be a regulator of the lymphocyte development (Gibb et al., 2011).

Mutations

Note No mutation has been reported so far.

Implicated in

Note
Entity Various cancers
Note ADAM family members have been recently involved in malignant progression and development (Mochizuki and Okada, 2007; Rocks et al., 2008; Wagstaff et al., 2011; Duffy et al., 2009). ADAM10 has been shown to be constitutively active in a number of solid tumors, and this biochemical defect is implicated in the pathogenesis of many tumors. The following paragraphs will summarize what has been discovered about the function of ADAM10 in cancer.
  
Entity Brain tumors
Note ADAM10 protein has been reported to be highly expressed in the human central nervous system (Kärkkäinen et al., 2000). Recently, two different studies (Kohutek et al., 2009; Formolo et al., 2011) have uncovered the function of ADAM10 in the cell migration and invasiveness process of glioblastoma cells. In fact the authors have shown that ADAM10 by mediating the cleavage of N-cadherin was found to regulate the migratory properties of glioblastoma cells (Kohutek et al., 2009). On the other hand, the protein expression of ADAM10 was found to be higher in cell with strong invasiveness capability.
  
Entity Prostate cancer
Note Prostate cancer is one of the most frequent cancers in men. The cause of prostate cancer development is unknown but is likely to be arising from several factors. Development of prostate cancer is androgen-dependent in early stages of the disease but cell growth became androgen-independent. ADAM10 have been found to be expressed in all prostate tumor samples (Karan et al., 2003). Interestingly, McCulloch et al. have observed that ADAM10 expression was up-regulated by androgen stimulation. Those observations were confirmed in a study published by Arima et al. However, in this work they reveal that ADAM10 was predominantly localized in the nucleus of cancer cells and show that ADAM10 can co-immunoprecipitate with androgen receptor in the nucleus. Moreover, they also observed that nuclear expression of ADAM10 was correlating with several biological parameters like the Gleason score and prostate specific antigen expression. Inhibition of ADAM10 expression by a siRNA approach was able to induce a cell proliferation decrease of prostate cancer cells. This study suggests for the first time that ADAM10 may have some function in the nucleus by regulating androgen receptor function.
  
Entity Breast cancer
Note Expressions of different members of the ADAM family have been investigated in breast cancer. Despite that some ADAM family members present differential expression between non neoplastic and breast cancer tissue, no difference was observed for ADAM10 (Lendeckel et al., 2005). Nevertheless, Liu and co-workers have recently described than ADAM10 was the principal responsible for HER2 shedding in HER2 over-expressing breast cancer. The cleavage of HER2 liberates the extracellular domain of HER2 leaving a p95 fragment containing the transmembrane domain as well as the intracellular domain. This p95 fragment presents constitutive kinase activation and its expression correlates with a poor prognosis. The author demonstrated that in conjunction with low amount of HER2 inhibitor, ADAM10 inhibition was inducing a decrease in cell proliferation.
  
Entity Colon and gastric and oral carcinomas
Note Deregulation of ADAM10 in colon cancer development has been reported in several studies. Knösel et al. have reported that ADAM10 expression in colorectal cancer patient samples, detectable by immunohistochemistry was found to correlate with higher clinical stage.
Moreover, it has been demonstrated that xenografting of colorectal cancer cells with enforced expression of ADAM10 in nude mice induced formation of liver metastasis compared to the negative control cells, and this effect can be attributed to ADAM10-mediated cleavage and release of L1-CAM, a cell adhesion molecule (Gavert et al., 2007). Similarly to Knösel et al., ADAM10 expression was associated with gastric cancer progression and correlates with worst prognostic outcome (Wang et al., 2011). Using immunohistochemistry, it was also found that ADAM10 is over-expressed in squamous cell carcinomas of the oral cavity, as compared to the benign epithelial cells; knockdown of ADAM10 expression using siRNA in the cell lines derived from those tumors induces a significant decrease in cell growth (Ko et al., 2007).
  
Entity Melanoma, pancreatic cancer and adenoid cystic carcinoma
Note The expression of ADAM10 has been investigated in melanoma and Lee et al. have reported that ADAM10 is over-expressed in melanoma metastasis in comparison to primary melanoma cells. Similar findings were made in pancreatic cancer, where inhibition of ADAM10 expression in pancreatic carcinoma cell lines also resulted in a significant decrease in invasiveness and migration (Gaida et al., 2010).
  
Entity Hematologic malignancies
Note Recently, Armanious et al. have described for the first time the function of ADAM10 in non solid tumors. They have reported that ADAM10 is constitutively activated and over-expressed in different form of B-cell lymphoma like mantle cell lymphoma and diffuse large B-cell lymphoma. Moreover, the authors have described that inhibition of ADAM10 leads to a decrease of cell proliferation. On the other hand, stimulation of mantle cells with the recombinant active form of ADAM10 increases further their proliferation. Additionally, they also demonstrated, as reported previously in the literature, that ADAM10 was responsible for the release of active from of TNF-alpha that in turn was contributing to the activation of the NF-kappab pathways.
  

To be noted

To summarize, the function of ADAM protein family members emerge as an important player in the pathobiology of various form of cancers. Therefore, they represent today a new therapeutic target of choice for cancer therapy. In particular, ADAM10 is the object of intense drug development (Soundararajan et al., 2009; Crawford et al., 2009; Yavari et al., 1998; Moss et al., 2008).

Bibliography

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Constitutive activation of metalloproteinase ADAM10 in mantle cell lymphoma promotes cell growth and activates the TNFalpha/NFkappaB pathway.
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Expression of L1-CAM and ADAM10 in human colon cancer cells induces metastasis.
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PMID 17699774
 
ADAM10 is essential for Notch2-dependent marginal zone B cell development and CD23 cleavage in vivo.
Gibb DR, El Shikh M, Kang DJ, Rowe WJ, El Sayed R, Cichy J, Yagita H, Tew JG, Dempsey PJ, Crawford HC, Conrad DH.
J Exp Med. 2010 Mar 15;207(3):623-35. Epub 2010 Feb 15.
PMID 20156974
 
The emergence of ADAM10 as a regulator of lymphocyte development and autoimmunity.
Gibb DR, Saleem SJ, Chaimowitz NS, Mathews J, Conrad DH.
Mol Immunol. 2011 Jun;48(11):1319-27. Epub 2011 Jan 13. (REVIEW)
PMID 21236490
 
ADAM10 is expressed in human podocytes and found in urinary vesicles of patients with glomerular kidney diseases.
Gutwein P, Schramme A, Abdel-Bakky MS, Doberstein K, Hauser IA, Ludwig A, Altevogt P, Gauer S, Hillmann A, Weide T, Jespersen C, Eberhardt W, Pfeilschifter J.
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PMID 20070888
 
ADAM 10: an active metalloprotease expressed during avian epithelial morphogenesis.
Hall RJ, Erickson CA.
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PMID 12654298
 
The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts.
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Hum Mol Genet. 2002 Oct 1;11(21):2615-24.
PMID 12354787
 
Involvement of a disintegrin and metalloproteinase 10 and 17 in shedding of tumor necrosis factor-alpha.
Hikita A, Tanaka N, Yamane S, Ikeda Y, Furukawa H, Tohma S, Suzuki R, Tanaka S, Mitomi H, Fukui N.
Biochem Cell Biol. 2009 Aug;87(4):581-93.
PMID 19767822
 
Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans.
Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E, Blobel CP, Himanen JP, Lackmann M, Nikolov DB.
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PMID 16239146
 
Expression of ADAMs (a disintegrin and metalloproteases) and TIMP-3 (tissue inhibitor of metalloproteinase-3) in human prostatic adenocarcinomas.
Karan D, Lin FC, Bryan M, Ringel J, Moniaux N, Lin MF, Batra SK.
Int J Oncol. 2003 Nov;23(5):1365-71.
PMID 14532978
 
Metalloprotease-disintegrin (ADAM) genes are widely and differentially expressed in the adult CNS.
Karkkainen I, Rybnikova E, Pelto-Huikko M, Huovila AP.
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PMID 10860581
 
Immunoprofiles of 11 biomarkers using tissue microarrays identify prognostic subgroups in colorectal cancer.
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PMID 16207476
 
Increase of disintergin metalloprotease 10 (ADAM10) expression in oral squamous cell carcinoma.
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Cancer Lett. 2007 Jan 8;245(1-2):33-43. Epub 2005 Nov 23.
PMID 16309826
 
ADAM-10-mediated N-cadherin cleavage is protein kinase C-alpha dependent and promotes glioblastoma cell migration.
Kohutek ZA, diPierro CG, Redpath GT, Hussaini IM.
J Neurosci. 2009 Apr 8;29(14):4605-15.
PMID 19357285
 
Tissue inhibitor of metalloproteinases-1 promotes liver metastasis by induction of hepatocyte growth factor signaling.
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PMID 17875701
 
ADAM10 is upregulated in melanoma metastasis compared with primary melanoma.
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J Invest Dermatol. 2010 Mar;130(3):763-73. Epub 2009 Oct 29.
PMID 19865098
 
Increased expression of ADAM family members in human breast cancer and breast cancer cell lines.
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J Cancer Res Clin Oncol. 2005 Jan;131(1):41-8. Epub 2004 Sep 30.
PMID 15565459
 
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PMID 16627989
 
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FEBS Lett. 1997 Jan 6;400(3):333-5.
PMID 9009225
 
ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and beta-catenin translocation.
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Identification of ADAM10 as a major TNF sheddase in ADAM17-deficient fibroblasts.
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Cancer Sci. 2007 May;98(5):621-8. Epub 2007 Mar 9. (REVIEW)
PMID 17355265
 
ADAM10 as a target for anti-cancer therapy.
Moss ML, Stoeck A, Yan W, Dempsey PJ.
Curr Pharm Biotechnol. 2008 Feb;9(1):2-8. (REVIEW)
PMID 18289051
 
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PMID 17920749
 
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PMID 12514095
 
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PMID 19783906
 
The roles of ADAMTS metalloproteinases in tumorigenesis and metastasis.
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Front Biosci. 2011 Jan 1;16:1861-72. (REVIEW)
PMID 21196270
 
ADAM 10 is associated with gastric cancer progression and prognosis of patients.
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Inhibiting adenoid cystic carcinoma cells growth and metastasis by blocking the expression of ADAM 10 using RNA interference.
Xu Q, Liu X, Chen W, Zhang Z.
J Transl Med. 2010 Dec 20;8:136.
PMID 21171968
 
Genome-wide midrange transcription profiles reveal expression level relationships in human tissue specification.
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PMID 15388519
 
Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia.
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Hum Mol Genet. 1998 Jul;7(7):1161-7.
PMID 9618175
 

Citation

This paper should be referenced as such :
Gelebart, P ; Armanious, H ; Lai, R
ADAM10 (ADAM metallopeptidase domain 10)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(1):1-6.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/ADAM10ID44397ch15q21.html


External links

Nomenclature
HGNC (Hugo)ADAM10   188
Cards
AtlasADAM10ID44397ch15q21
Entrez_Gene (NCBI)ADAM10  102  ADAM metallopeptidase domain 10
AliasesAD10; AD18; CD156c; CDw156; 
HsT18717; MADM; RAK; kuz
GeneCards (Weizmann)ADAM10
Ensembl hg19 (Hinxton)ENSG00000137845 [Gene_View]  chr15:58887403-59042177 [Contig_View]  ADAM10 [Vega]
Ensembl hg38 (Hinxton)ENSG00000137845 [Gene_View]  chr15:58887403-59042177 [Contig_View]  ADAM10 [Vega]
ICGC DataPortalENSG00000137845
TCGA cBioPortalADAM10
AceView (NCBI)ADAM10
Genatlas (Paris)ADAM10
WikiGenes102
SOURCE (Princeton)ADAM10
Genomic and cartography
GoldenPath hg19 (UCSC)ADAM10  -     chr15:58887403-59042177 -  15q2   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)ADAM10  -     15q2   [Description]    (hg38-Dec_2013)
EnsemblADAM10 - 15q2 [CytoView hg19]  ADAM10 - 15q2 [CytoView hg38]
Mapping of homologs : NCBIADAM10 [Mapview hg19]  ADAM10 [Mapview hg38]
OMIM602192   615537   615590   
Gene and transcription
Genbank (Entrez)AA243020 AF009615 AK023460 AK300472 AY726599
RefSeq transcript (Entrez)NM_001110 NM_001320570
RefSeq genomic (Entrez)NC_000015 NC_018926 NG_033876 NT_010194 NW_004929398
Consensus coding sequences : CCDS (NCBI)ADAM10
Cluster EST : UnigeneHs.745136 [ NCBI ]
CGAP (NCI)Hs.745136
Alternative Splicing GalleryENSG00000137845
Gene ExpressionADAM10 [ NCBI-GEO ]   ADAM10 [ EBI - ARRAY_EXPRESS ]   ADAM10 [ SEEK ]   ADAM10 [ MEM ]
Gene Expression Viewer (FireBrowse)ADAM10 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)102
GTEX Portal (Tissue expression)ADAM10
Protein : pattern, domain, 3D structure
UniProt/SwissProtO14672 (Uniprot)
NextProtO14672  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO14672
Splice isoforms : SwissVarO14672 (Swissvar)
Catalytic activity : Enzyme3.4.24.81 [ Enzyme-Expasy ]   3.4.24.813.4.24.81 [ IntEnz-EBI ]   3.4.24.81 [ BRENDA ]   3.4.24.81 [ KEGG ]   
PhosPhoSitePlusO14672
Domaine pattern : Prosite (Expaxy)ADAM_MEPRO (PS50215)    DISINTEGRIN_2 (PS50214)    ZINC_PROTEASE (PS00142)   
Domains : Interpro (EBI)ADAM_10    Disintegrin_dom    MetalloPept_cat_dom    Peptidase_M12B    Peptidase_M12B_N   
Domain families : Pfam (Sanger)Disintegrin (PF00200)    Pep_M12B_propep (PF01562)   
Domain families : Pfam (NCBI)pfam00200    pfam01562   
Domain families : Smart (EMBL)DISIN (SM00050)  
DMDM Disease mutations102
Blocks (Seattle)ADAM10
PDB (SRS)1M1I   
PDB (PDBSum)1M1I   
PDB (IMB)1M1I   
PDB (RSDB)1M1I   
Structural Biology KnowledgeBase1M1I   
SCOP (Structural Classification of Proteins)1M1I   
CATH (Classification of proteins structures)1M1I   
SuperfamilyO14672
Human Protein AtlasENSG00000137845
Peptide AtlasO14672
HPRD03723
IPIIPI00013897   IPI00794448   IPI00791687   IPI00878134   
Protein Interaction databases
DIP (DOE-UCLA)O14672
IntAct (EBI)O14672
FunCoupENSG00000137845
BioGRIDADAM10
STRING (EMBL)ADAM10
ZODIACADAM10
Ontologies - Pathways
QuickGOO14672
Ontology : AmiGOin utero embryonic development  endopeptidase activity  metalloendopeptidase activity  metalloendopeptidase activity  metalloendopeptidase activity  receptor binding  integrin binding  protein binding  nucleus  cytoplasm  Golgi apparatus  Golgi-associated vesicle  trans-Golgi network  plasma membrane  focal adhesion  protein phosphorylation  membrane protein ectodomain proteolysis  membrane protein ectodomain proteolysis  negative regulation of cell adhesion  negative regulation of cell adhesion  Notch signaling pathway  Notch signaling pathway  Notch receptor processing  integrin-mediated signaling pathway  cell-cell signaling  metallopeptidase activity  metallopeptidase activity  metallopeptidase activity  zinc ion binding  positive regulation of cell proliferation  cell surface  positive regulation of T cell chemotaxis  postsynaptic density  membrane  integral component of membrane  protein processing  SH3 domain binding  protein kinase binding  extracellular matrix disassembly  positive regulation of cell growth  positive regulation of cell migration  response to tumor necrosis factor  monocyte activation  protein homodimerization activity  intracellular membrane-bounded organelle  ephrin receptor signaling pathway  PMA-inducible membrane protein ectodomain proteolysis  constitutive protein ectodomain proteolysis  extracellular exosome  perinuclear endoplasmic reticulum  tetraspanin-enriched microdomain  
Ontology : EGO-EBIin utero embryonic development  endopeptidase activity  metalloendopeptidase activity  metalloendopeptidase activity  metalloendopeptidase activity  receptor binding  integrin binding  protein binding  nucleus  cytoplasm  Golgi apparatus  Golgi-associated vesicle  trans-Golgi network  plasma membrane  focal adhesion  protein phosphorylation  membrane protein ectodomain proteolysis  membrane protein ectodomain proteolysis  negative regulation of cell adhesion  negative regulation of cell adhesion  Notch signaling pathway  Notch signaling pathway  Notch receptor processing  integrin-mediated signaling pathway  cell-cell signaling  metallopeptidase activity  metallopeptidase activity  metallopeptidase activity  zinc ion binding  positive regulation of cell proliferation  cell surface  positive regulation of T cell chemotaxis  postsynaptic density  membrane  integral component of membrane  protein processing  SH3 domain binding  protein kinase binding  extracellular matrix disassembly  positive regulation of cell growth  positive regulation of cell migration  response to tumor necrosis factor  monocyte activation  protein homodimerization activity  intracellular membrane-bounded organelle  ephrin receptor signaling pathway  PMA-inducible membrane protein ectodomain proteolysis  constitutive protein ectodomain proteolysis  extracellular exosome  perinuclear endoplasmic reticulum  tetraspanin-enriched microdomain  
Pathways : BIOCARTAGeneration of amyloid b-peptide by PS1 [Genes]   
Pathways : KEGGAlzheimer's disease    Epithelial cell signaling in Helicobacter pylori infection   
REACTOMEO14672 [protein]
REACTOME PathwaysR-HSA-1980150 Signaling by NOTCH4 [pathway]
REACTOME PathwaysR-HSA-2660826 Constitutive Signaling by NOTCH1 t(7 [pathway]
REACTOME Pathways9)(NOTCH1:M1580_K2555) Translocation Mutant [pathway]
REACTOME PathwaysR-HSA-177929 Signaling by EGFR [pathway]
REACTOME PathwaysR-HSA-2122948 Activated NOTCH1 Transmits Signal to the Nucleus [pathway]
REACTOME PathwaysR-HSA-3928665 EPH-ephrin mediated repulsion of cells [pathway]
REACTOME PathwaysR-HSA-2691232 Constitutive Signaling by NOTCH1 HD Domain Mutants [pathway]
REACTOME PathwaysR-HSA-1442490 Collagen degradation [pathway]
REACTOME PathwaysR-HSA-1980148 Signaling by NOTCH3 [pathway]
REACTOME PathwaysR-HSA-1474228 Degradation of the extracellular matrix [pathway]
REACTOME PathwaysR-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants [pathway]
REACTOME PathwaysR-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants [pathway]
REACTOME PathwaysR-HSA-2979096 NOTCH2 Activation and Transmission of Signal to the Nucleus [pathway]
NDEx NetworkADAM10
Atlas of Cancer Signalling NetworkADAM10
Wikipedia pathwaysADAM10
Orthology - Evolution
OrthoDB102
GeneTree (enSembl)ENSG00000137845
Phylogenetic Trees/Animal Genes : TreeFamADAM10
Homologs : HomoloGeneADAM10
Homology/Alignments : Family Browser (UCSC)ADAM10
Gene fusions - Rearrangements
Fusion : MitelmanADAM10/FIZ1 [15q21.3/19q13.42]  
Fusion : MitelmanADAM10/ZNF770 [15q21.3/15q14]  [t(15;15)(q14;q21)]  
Fusion: TCGAADAM10 15q21.3 FIZ1 19q13.42 BRCA
Fusion: TCGAADAM10 15q21.3 ZNF770 15q14 LGG
Polymorphisms : SNP, variants
NCBI Variation ViewerADAM10 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)ADAM10
dbVarADAM10
ClinVarADAM10
1000_GenomesADAM10 
Exome Variant ServerADAM10
ExAC (Exome Aggregation Consortium)ADAM10 (select the gene name)
Genetic variants : HAPMAP102
Genomic Variants (DGV)ADAM10 [DGVbeta]
Mutations
ICGC Data PortalADAM10 
TCGA Data PortalADAM10 
Broad Tumor PortalADAM10
OASIS PortalADAM10 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICADAM10 
intOGen PortalADAM10
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 ADAM10
DgiDB (Drug Gene Interaction Database)ADAM10
DoCM (Curated mutations)ADAM10 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)ADAM10 (select a term)
intoGenADAM10
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] 
Diseases
DECIPHER (Syndromes)15:58887403-59042177  ENSG00000137845
CONAN: Copy Number AnalysisADAM10 
Mutations and Diseases : HGMDADAM10
OMIM602192    615537    615590   
MedgenADAM10
Genetic Testing Registry ADAM10
NextProtO14672 [Medical]
TSGene102
GENETestsADAM10
Huge Navigator ADAM10 [HugePedia]
snp3D : Map Gene to Disease102
BioCentury BCIQADAM10
ClinGenADAM10
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD102
Chemical/Pharm GKB GenePA24505
Clinical trialADAM10
Miscellaneous
canSAR (ICR)ADAM10 (select the gene name)
Other databaseiHOP
Probes
Litterature
PubMed236 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineADAM10
EVEXADAM10
GoPubMedADAM10
iHOPADAM10
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Mon Sep 19 19:23:05 CEST 2016

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