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ADAMTS12 (ADAM Metallopeptidase With Thrombospondin Type 1 Motif, 12)

Written2013-07Santiago Cal, Alvaro J Obaya
Departamento de Bioquimica y Biologia Molecular, Instituto Universitario de Oncologia (IUOPA), Universidad de Oviedo, 33006, Asturias, Spain (SC); Biologia Funcional, Instituto Universitario de Oncologia (IUOPA), Universidad de Oviedo, 33006, Asturias, Spain (AJO)

(Note : for Links provided by Atlas : click)


Alias (NCBI)PRO4389
HGNC Previous namea disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 12
LocusID (NCBI) 81792
Atlas_Id 575
Location 5p13.3  [Link to chromosome band 5p13]
Location_base_pair Starts at 33523535 and ends at 33891990 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping ADAMTS12.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)
ADAMTS12 (5p13.3)::AKAP13 (15q25.3)ADAMTS12 (5p13.3)::C1QTNF3 (5p13.2)ADAMTS12 (5p13.3)::ZFR (5p13.3)
HSF1 (8q24.3)::ADAMTS12 (5p13.3)NECTIN2 (19q13.32)::ADAMTS12 (5p13.3)TMEM182 (2q12.1)::ADAMTS12 (5p13.3)
UQCC1 (20q11.22)::ADAMTS12 (5p13.3)WDR70 (5p13.2)::ADAMTS12 (5p13.3)


Description 24 exons, spans approximately 368.66 Kb of genomic DNA in the telomere-to-centromere orientation. The translation initiation codon is located to exon 1, and the stop codon to exon 24.
Transcription ADAMTS12 Human mRNA of 8.77 Kb as detected by northern-blot.


Description The open reading frame encodes a 1594 amino acid protein, with an estimated molecular weight of 178 kDa. ADAMTS-12 shares a structural multidomain complex architecture with the rest of members of the ADAMTS family. This organization includes a signal peptide, a prodomain involved in maintaining enzyme latency and a catalytic domain that contains the consensus sequence HEXXHGXXHD involved in the coordination of the zinc atom necessary for catalytic activity of the enzyme. This sequence ends in an Asp residue which distinguishes ADAMTSs from other metalloproteases such as MMPs. Following this catalytic region there are several other domains characterized as a disintegrin-like domain, a central thrombospondin-1 (TSP-1) motif, a cysteine-rich domain, a spacer region and a variable number of TSP-1 repeats, three in the case of ADAMTS-12. A structural hallmark of ADAMTS-12 is the presence of a second spacer region followed by four additional TSP-1 repeats (Figure 1) (Cal et al., 2001).
  Figure 1. Domain organization of ADAMTS-12. Pro: prodomain; TSP: thrombospondin type-1 domains.
Expression ADAMTS12 cDNA was originally cloned from a human fetal lung cDNA library and its expression was also detected in human fetal fibroblasts following treatment with TGF-β. By real-time polymerase chain reaction (PCR) assay ADAMTS12 expression can also be detected in cartilage, synovium, tendon, skeletal muscle and fat. ADAMTS12 was also found widely expressed in gastrointestinal, pancreatic and colon carcinomas but not in the paired normal tissues, suggesting that this enzyme could also participate in the development and/or progression of tumors from different origin (Cal et al., 2001; Liu et al., 2006; Moncada-Pazos et al., 2009).
Localisation Extracellular.
Function Several studies performed to characterized ADAMTS-12 function indicate its role as being a host-protective enzyme with antitumor properties (Llamazares et al., 2007; Moncada-Pazos et al., 2009; El-Hour et al., 2010; Wang et al., 2011). Additionally, ADAMTS-12 has a role in trophoblasts invasion during placental development which is independent of the proteolytic domain (Beristain et al., 2011). ADAMTS-12 also participates in other pathological processes such as inflammation, allergen-induced inflammation and hyperresponsiveness, and it is also involved in arthritic processes (Liu, 2009; Moncada-Pazos et al., 2012; Nah et al., 2012; Paulissen et al., 2012). Furthermore, different genomic approximations have described how other human pathologies like asthma, schizophrenia or predisposition to pediatric stroke are related to ADAMTS12 locus (Kurz et al., 2006; Arnin et al., 2012; Bespalova et al., 2012). However, besides its participation in pathological situations little is known about ADAMTS-12 partners and/or substrates in normal or pathogenic processes.
Homology The ADAMTS12 gene is conserved in chimpanzee (Refseq: XP_517836), macaque (Refseq: XM_001090049), dog (Refseq: XM_536508), cow (Refseq: NM_001192609), mouse (Refseq: NM_175501), rat (Refseq: NM_001106420), chicken (Refseq: XM_003642975), and zebrafish (Refseq: XM_001343335).
ADAMTS-12 belongs to the A Disintegrin And Metalloprotease Domains with ThromboSpondin motifs (ADAMTS) family, which consists of 19 secreted zinc metalloproteinases (Porter et al., 2005). All members of the family share the same structural domain design. ADAMTS-12 is closely related to ADAMTS-7 since both proteins display the C-terminal TSP residues separated by two spacer regions (spacer-1 and spacer-2). The rest of the members contain only one spacer region followed by a variable number of TSP domains.

Implicated in

Entity Various cancers
Note Different studies have highlighted the role of ADAMTS12 as a tumor-suppressor gene. ADAMTS-12 is able to alter the tumorigenic effects of hepatocyte growth factor (HGF) in Madin-Darby canine kidney (MDCK) cells (Llamazares et al., 2007). ADAMTS-12 also prevents the formation of tubules by bovine aortic endothelial cells in the presence of vascular endothelial growth factor (VEGF). Additionally, growth of subcutaneous tumors induced by the human lung tumor cell line A549 is compromised when ADAMTS12 is exogenously expressed. Analysis of the epigenetic status of ADAMTS12 promoter has reinforced the role of ADAMTS-12 as an in vivo tumor-suppressor enzyme. In fact, ADAMTS12 is epigenetically silenced in tumor cells from different sources such as colon cancer cell lines, breast cancer cell lines, cervix cancer cell lines or lymphoma cell lines (Moncada-Pazos et al., 2009). In particular, methylation levels of ADAMTS12 gene promoter were very high in a colon cancer sample panel that included both cancer cell lines and tumor samples, whereas it was found not or barely methylated in normal cells and tissues. However and similar to what has been found in gastrointestinal and pancreatic carcinomas, ADAMTS12 expression was higher in colon tumor samples cells than in normal tissues. This apparent contradiction resides in the fact that ADAMTS-12 is produced by the stromal cells surrounding neoplastic cells and not by the tumor cells themselves, which was confirmed using different approaches. For instance, immunofluorescence techniques allowed the localization of this protease in the proximity to alpha smooth muscle actin positive cells, which suggests that cancer-associated fibroblasts could be responsible for ADAMTS12 expression. By contrast, ADAMTS-12 staining resulted negative in the case of tumor cells. ADAMTS12 expression in fibroblasts was verified through the use of co-cultures of colon fibroblasts with colon cancer cells. Furthermore, this expression could be associated with a functional effect as colon cancer cells showed minor growth rates and an increase in apoptosis when co-cultured with colon fibroblasts in comparison to the colon tumor cell line cultured alone. Consequently, colon miofibroblast-ADAMTS12 expression could be part of a protective response aimed to compensate for the epigenetic silencing of this gene in tumor cells (Moncada-Pazos et al., 2009). Moreover, ADAMTS12 expression in colorectal cancer significantly correlated with the tumor histological grade, depth of tumor invasion, lymph node metastasis, and Duke's stage. In fact, patients with low or no ADAMTS12 expression in the tumor stroma had a significantly poor overall survival or disease-free survival (Wang et al., 2011). Phenotypic analysis of the Adamts12-deficient mouse has confirmed the role of this metalloprotease as a tumor-protective enzyme (El-Hour et al., 2010). This mouse develops normally and does not show any obvious phenotype. However, different models to analyze the angiogenesis process in vivo, including malignant keratinocyte transplantation, aortic ring assay and Matrigel plug, supported that this protease exhibits anti-angiogenic properties (El-Hour et al., 2010). Additionally, both intact ADAMTS-12 and a catalytically inactive form of ADAMTS-12 showed a similar ability to inhibit the spreading of endothelial cells. These data were in line with the previous results indicating that antitumor functions of ADAMTS-12 do not depend on its metalloprotease domain (Llamazares et al., 2007).
However, there are some data showing that ADAMTS-12 could also be a potential pro-tumor agent (Beristain et al., 2011). Thus, in placental cytotrophoblasts the expression of ADAMTS12 is able to exploit the same molecular machinery found in metastatic carcinoma cells. Comparing ADAMTS-family members-expression in highly versus poorly invasive cells during placental development, ADAMTS12 was preferentially expressed by the highly invasive cytotrophoblast cell line EVT. Furthermore, TGF-β or IL-1β, are also able to respectively induce or restrain ADAMTS12 expression in these cells as they also did in colon fibroblasts. Analyzing the domains involved in this process demonstrated how the metalloprotease domain does not fulfill a relevant role in this pro-invasive phenotype (Beristain et al., 2011).
In summary, there are several studies suggesting ADAMTS-12 as being involved in tumor progression. Nowadays, more data indicate this protein as a new member of the growing type of metalloproteases showing tumor-suppressor properties (Lopez-Otin and Matrisian, 2007). However, some data indicate a different role for this gene specifically regarding cellular invasion, which suggest that ADAMTS-12-function in tumor progression might depend on different interactions occurring within the extracellular microenvironment.
Entity Inflammation
Note Loss-of-function of Adamts-12 enhances mouse susceptibility to inflammatory processes (Moncada-Pazos et al., 2012). In this sense, it has been shown how Adamts12 deficiency is responsible for increase inflammation in mice that was not limited to a certain tissue as it was a common phenomenon affecting several organs. Different experimental conditions to induce colitis, endotoxic sepsis, pancreatitis or allergen-induced lung inflammation demonstrated that absence of ADAMTS-12 resulted in a more severe inflammation phenotype as well as a delayed recovery from these anomalies. These changes were accompanied by an increase in inflammatory markers and, at the same time, the clinical symptoms observed in Adamts12-deficient mice were also concomitant with neutrophilia or eosinophilia and mast cells recruitment in affected tissues (Moncada-Pazos et al., 2012; Paulissen et al., 2012). In vitro culture of human neutrophils indicated that the presence of ADAMTS-12 might be a player in inducing neutrophil clearance, a required step for the resolution of an inflammation process.
Entity Arthritis
Note ADAMTS-12 shows aggrecan-degrading activity, similarly to aggrecanases ADAMTS-4 and ADAMTS-5, and to other members of the family such as ADAMTS-1, ADAMTS-9, ADAMTS-15, ADAMTS-16 and ADAMTS-18 (Lin and Liu, 2010). Nevertheless, the ability of ADAMTS-12 to degrade aggrecan is reduced and it has only been reported to occur in vitro (Llamazares et al., 2007). Although barely detectable in adult tissues real-time polymerase chain reaction (PCR) assay revealed ADAMTS12 expression in cartilage, synovium, tendon, skeletal muscle and fat (Liu et al., 2006). In vitro experiments have also been used to demonstrate ADAMTS-12 proteolytic activity towards cartilage oligomeric matrix protein (COMP), other component of cartilage. This, together with ADAMTS-12 aggrecanolytic activity, may indicate a role of ADAMTS-12 in arthritic diseases (Liu et al., 2006). In this regard, profiling analysis demonstrated a significant upregulation of ADAMTS-12 in cartilage from patients with osteoarthritis when compared with normal cartilage (Kevorkian et al., 2004). Thus, ADAMTS-7 and ADAMTS-12, apart from the known aggrecanases ADAMTS-4 and -5, seem to be important players in the degradation of components of cartilaginous tissue during arthritic processes (Liu, 2009). In relation to potential endogenous inhibitors, it has been described that α2-macroglobulin and the granulin-epithelin precursor, a growth factor highly expressed in chondrocytes, can interact with ADAMTS-12, leading to an inhibition of its COMP-degrading activity (Luan et al., 2008; Guo et al., 2010).


A genome-wide association study identifies a gene network of ADAMTS genes in the predisposition to pediatric stroke.
Arning A, Hiersche M, Witten A, Kurlemann G, Kurnik K, Manner D, Stoll M, Nowak-Gottl U.
Blood. 2012 Dec 20;120(26):5231-6. doi: 10.1182/blood-2012-07-442038. Epub 2012 Sep 18.
PMID 22990015
Regulated expression of ADAMTS-12 in human trophoblastic cells: a role for ADAMTS-12 in epithelial cell invasion?
Beristain AG, Zhu H, Leung PC.
PLoS One. 2011 Apr 11;6(4):e18473. doi: 10.1371/journal.pone.0018473.
PMID 21494557
Genetic variations in the ADAMTS12 gene are associated with schizophrenia in Puerto Rican patients of Spanish descent.
Bespalova IN, Angelo GW, Ritter BP, Hunter J, Reyes-Rabanillo ML, Siever LJ, Silverman JM.
Neuromolecular Med. 2012 Mar;14(1):53-64. doi: 10.1007/s12017-012-8169-y. Epub 2012 Feb 10.
PMID 22322903
Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats.
Cal S, Arguelles JM, Fernandez PL, Lopez-Otin C.
J Biol Chem. 2001 May 25;276(21):17932-40. Epub 2001 Mar 2.
PMID 11279086
Higher sensitivity of Adamts12-deficient mice to tumor growth and angiogenesis.
El Hour M, Moncada-Pazos A, Blacher S, Masset A, Cal S, Berndt S, Detilleux J, Host L, Obaya AJ, Maillard C, Foidart JM, Ectors F, Noel A, Lopez-Otin C.
Oncogene. 2010 May 20;29(20):3025-32. doi: 10.1038/onc.2010.49. Epub 2010 Mar 8.
PMID 20208563
Granulin-epithelin precursor binds directly to ADAMTS-7 and ADAMTS-12 and inhibits their degradation of cartilage oligomeric matrix protein.
Guo F, Lai Y, Tian Q, Lin EA, Kong L, Liu C.
Arthritis Rheum. 2010 Jul;62(7):2023-36. doi: 10.1002/art.27491.
PMID 20506400
Expression profiling of metalloproteinases and their inhibitors in cartilage.
Kevorkian L, Young DA, Darrah C, Donell ST, Shepstone L, Porter S, Brockbank SM, Edwards DR, Parker AE, Clark IM.
Arthritis Rheum. 2004 Jan;50(1):131-41.
PMID 14730609
Fine mapping and positional candidate studies on chromosome 5p13 identify multiple asthma susceptibility loci.
Kurz T, Hoffjan S, Hayes MG, Schneider D, Nicolae R, Heinzmann A, Jerkic SP, Parry R, Cox NJ, Deichmann KA, Ober C.
J Allergy Clin Immunol. 2006 Aug;118(2):396-402. Epub 2006 Jun 9.
PMID 16890764
The role of ADAMTSs in arthritis.
Lin EA, Liu CJ.
Protein Cell. 2010 Jan;1(1):33-47. doi: 10.1007/s13238-010-0002-5. Epub 2010 Feb 7. (REVIEW)
PMID 21203996
ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein.
Liu CJ, Kong W, Xu K, Luan Y, Ilalov K, Sehgal B, Yu S, Howell RD, Di Cesare PE.
J Biol Chem. 2006 Jun 9;281(23):15800-8. Epub 2006 Apr 12.
PMID 16611630
The role of ADAMTS-7 and ADAMTS-12 in the pathogenesis of arthritis.
Liu CJ.
Nat Clin Pract Rheumatol. 2009 Jan;5(1):38-45. doi: 10.1038/ncprheum0961. (REVIEW)
PMID 19098927
The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway.
Llamazares M, Obaya AJ, Moncada-Pazos A, Heljasvaara R, Espada J, Lopez-Otin C, Cal S.
J Cell Sci. 2007 Oct 15;120(Pt 20):3544-52. Epub 2007 Sep 25.
PMID 17895370
Emerging roles of proteases in tumour suppression.
Lopez-Otin C, Matrisian LM.
Nat Rev Cancer. 2007 Oct;7(10):800-8. (REVIEW)
PMID 17851543
Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin.
Luan Y, Kong L, Howell DR, Ilalov K, Fajardo M, Bai XH, Di Cesare PE, Goldring MB, Abramson SB, Liu CJ.
Osteoarthritis Cartilage. 2008 Nov;16(11):1413-20. doi: 10.1016/j.joca.2008.03.017. Epub 2008 May 15.
PMID 18485748
ADAMTS-12 metalloprotease is necessary for normal inflammatory response.
Moncada-Pazos A, Obaya AJ, Llamazares M, Heljasvaara R, Suarez MF, Colado E, Noel A, Cal S, Lopez-Otin C.
J Biol Chem. 2012 Nov 16;287(47):39554-63. doi: 10.1074/jbc.M112.408625. Epub 2012 Sep 27.
PMID 23019333
Association of ADAMTS12 polymorphisms with rheumatoid arthritis.
Nah SS, Lee S, Joo J, Kim HK, Sohn DR, Kwon JT, Woo KM, Hong SJ, Kim HJ.
Mol Med Rep. 2012 Jul;6(1):227-31. doi: 10.3892/mmr.2012.867. Epub 2012 Apr 11.
PMID 22505177
Control of allergen-induced inflammation and hyperresponsiveness by the metalloproteinase ADAMTS-12.
Paulissen G, El Hour M, Rocks N, Gueders MM, Bureau F, Foidart JM, Lopez-Otin C, Noel A, Cataldo DD.
J Immunol. 2012 Oct 15;189(8):4135-43. doi: 10.4049/jimmunol.1103739. Epub 2012 Sep 7.
PMID 22962682
The ADAMTS metalloproteinases.
Porter S, Clark IM, Kevorkian L, Edwards DR.
Biochem J. 2005 Feb 15;386(Pt 1):15-27. (REVIEW)
PMID 15554875
Expression of ADAMTS12 in colorectal cancer-associated stroma prevents cancer development and is a good prognostic indicator of colorectal cancer.
Wang D, Zhu T, Zhang FB, He C.
Dig Dis Sci. 2011 Nov;56(11):3281-7. doi: 10.1007/s10620-011-1723-x. Epub 2011 May 11.
PMID 21559743


This paper should be referenced as such :
Cal, S ; Obaya, AJ
ADAMTS12 (ADAM Metallopeptidase With Thrombospondin Type 1 Motif, 12)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(2):78-81.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)ADAMTS12   14605
Entrez_Gene (NCBI)ADAMTS12    ADAM metallopeptidase with thrombospondin type 1 motif 12
GeneCards (Weizmann)ADAMTS12
Ensembl hg19 (Hinxton)ENSG00000151388 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000151388 [Gene_View]  ENSG00000151388 [Sequence]  chr5:33523535-33891990 [Contig_View]  ADAMTS12 [Vega]
ICGC DataPortalENSG00000151388
Genatlas (Paris)ADAMTS12
SOURCE (Princeton)ADAMTS12
Genetics Home Reference (NIH)ADAMTS12
Genomic and cartography
GoldenPath hg38 (UCSC)ADAMTS12  -     chr5:33523535-33891990 -  5p13.3-p13.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)ADAMTS12  -     5p13.3-p13.2   [Description]    (hg19-Feb_2009)
GoldenPathADAMTS12 - 5p13.3-p13.2 [CytoView hg19]  ADAMTS12 - 5p13.3-p13.2 [CytoView hg38]
Genome Data Viewer NCBIADAMTS12 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AJ250725 AK001058 AW938686 AY358745 BC058841
RefSeq transcript (Entrez)NM_001324511 NM_001324512 NM_030955
Consensus coding sequences : CCDS (NCBI)ADAMTS12
Gene ExpressionADAMTS12 [ NCBI-GEO ]   ADAMTS12 [ EBI - ARRAY_EXPRESS ]   ADAMTS12 [ SEEK ]   ADAMTS12 [ MEM ]
Gene Expression Viewer (FireBrowse)ADAMTS12 [ Firebrowse - Broad ]
GenevisibleExpression of ADAMTS12 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)81792
GTEX Portal (Tissue expression)ADAMTS12
Human Protein AtlasENSG00000151388-ADAMTS12 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP58397   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP58397  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP58397
Catalytic activity : Enzyme3.4.24.- [ Enzyme-Expasy ]   3.4.24.-3.4.24.- [ IntEnz-EBI ]   3.4.24.- [ BRENDA ]   3.4.24.- [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)ADAM_MEPRO (PS50215)    PLAC (PS50900)    TSP1 (PS50092)    ZINC_PROTEASE (PS00142)   
Domains : Interpro (EBI)ADAM_CR_2    ADAM_spacer1    ADAMTS/ADAMTS-like    MetalloPept_cat_dom_sf    Peptidase_M12B    Peptidase_M12B_N    PLAC    TSP1_rpt    TSP1_rpt_sf   
Domain families : Pfam (Sanger)ADAM_CR_2 (PF17771)    ADAM_spacer1 (PF05986)    Pep_M12B_propep (PF01562)    Reprolysin (PF01421)    TSP_1 (PF00090)   
Domain families : Pfam (NCBI)pfam17771    pfam05986    pfam01562    pfam01421    pfam00090   
Domain families : Smart (EMBL)TSP1 (SM00209)  
Conserved Domain (NCBI)ADAMTS12
AlphaFold pdb e-kbP58397   
Human Protein Atlas [tissue]ENSG00000151388-ADAMTS12 [tissue]
Protein Interaction databases
IntAct (EBI)P58397
Ontologies - Pathways
Ontology : AmiGOmetalloendopeptidase activity  metalloendopeptidase activity  protein binding  extracellular region  cell-matrix adhesion  cell migration  proteoglycan catabolic process  extracellular matrix organization  extracellular matrix  negative regulation of chondrocyte differentiation  metal ion binding  regulation of inflammatory response  proteolysis involved in cellular protein catabolic process  proteolysis involved in cellular protein catabolic process  cellular response to interleukin-1  cellular response to tumor necrosis factor  cellular response to BMP stimulus  regulation of endothelial tube morphogenesis  negative regulation of hepatocyte growth factor receptor signaling pathway  negative regulation of cellular response to vascular endothelial growth factor stimulus  negative regulation of cellular response to hepatocyte growth factor stimulus  
Ontology : EGO-EBImetalloendopeptidase activity  metalloendopeptidase activity  protein binding  extracellular region  cell-matrix adhesion  cell migration  proteoglycan catabolic process  extracellular matrix organization  extracellular matrix  negative regulation of chondrocyte differentiation  metal ion binding  regulation of inflammatory response  proteolysis involved in cellular protein catabolic process  proteolysis involved in cellular protein catabolic process  cellular response to interleukin-1  cellular response to tumor necrosis factor  cellular response to BMP stimulus  regulation of endothelial tube morphogenesis  negative regulation of hepatocyte growth factor receptor signaling pathway  negative regulation of cellular response to vascular endothelial growth factor stimulus  negative regulation of cellular response to hepatocyte growth factor stimulus  
REACTOMEP58397 [protein]
REACTOME PathwaysR-HSA-5173214 [pathway]   
NDEx NetworkADAMTS12
Atlas of Cancer Signalling NetworkADAMTS12
Wikipedia pathwaysADAMTS12
Orthology - Evolution
GeneTree (enSembl)ENSG00000151388
Phylogenetic Trees/Animal Genes : TreeFamADAMTS12
Homologs : HomoloGeneADAMTS12
Homology/Alignments : Family Browser (UCSC)ADAMTS12
Gene fusions - Rearrangements
Fusion : MitelmanADAMTS12::C1QTNF3 [5p13.3/5p13.2]  
Fusion : MitelmanADAMTS12::ZFR [5p13.3/5p13.3]  
Fusion : MitelmanHSF1::ADAMTS12 [8q24.3/5p13.3]  
Fusion : MitelmanTMEM182::ADAMTS12 [2q12.1/5p13.3]  
Fusion : MitelmanUQCC1::ADAMTS12 [20q11.22/5p13.3]  
Fusion : MitelmanWDR70::ADAMTS12 [5p13.2/5p13.3]  
Fusion : QuiverADAMTS12
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerADAMTS12 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)ADAMTS12
Exome Variant ServerADAMTS12
GNOMAD BrowserENSG00000151388
Varsome BrowserADAMTS12
ACMGADAMTS12 variants
Genomic Variants (DGV)ADAMTS12 [DGVbeta]
DECIPHERADAMTS12 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisADAMTS12 
ICGC Data PortalADAMTS12 
TCGA Data PortalADAMTS12 
Broad Tumor PortalADAMTS12
OASIS PortalADAMTS12 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICADAMTS12  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DADAMTS12
Mutations and Diseases : HGMDADAMTS12
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)ADAMTS12
DoCM (Curated mutations)ADAMTS12
CIViC (Clinical Interpretations of Variants in Cancer)ADAMTS12
NCG (London)ADAMTS12
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry ADAMTS12
NextProtP58397 [Medical]
Target ValidationADAMTS12
Huge Navigator ADAMTS12 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDADAMTS12
Pharm GKB GenePA24538
Clinical trialADAMTS12
DataMed IndexADAMTS12
PubMed34 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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