ADAM10 | ENSG00000137845 | NCBI 102

Details for: ADAM10

Gene ID: 102

Symbol: ADAM10

Ensembl ID: ENSG00000137845

Description: ADAM metallopeptidase domain 10

Associated with

Activated notch1 transmits signal to the nucleus
(R-HSA-2122948)
Amyloid fiber formation
(R-HSA-977225)
Axon guidance
(R-HSA-422475)
Collagen degradation
(R-HSA-1442490)
Constitutive signaling by notch1 hd+pest domain mutants
(R-HSA-2894862)
Constitutive signaling by notch1 hd domain mutants
(R-HSA-2691232)
Constitutive signaling by notch1 pest domain mutants
(R-HSA-2644606)
Constitutive signaling by notch1 t(7;9)(notch1:m1580_k2555) translocation mutant
(R-HSA-2660826)
Degradation of the extracellular matrix
(R-HSA-1474228)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Eph-ephrin mediated repulsion of cells
(R-HSA-3928665)
Eph-ephrin signaling
(R-HSA-2682334)
Extracellular matrix organization
(R-HSA-1474244)
Immune system
(R-HSA-168256)
Innate immune system
(R-HSA-168249)
Metabolism of proteins
(R-HSA-392499)
Nervous system development
(R-HSA-9675108)
Neutrophil degranulation
(R-HSA-6798695)
Notch2 activation and transmission of signal to the nucleus
(R-HSA-2979096)
Notch3 activation and transmission of signal to the nucleus
(R-HSA-9013507)
Notch4 activation and transmission of signal to the nucleus
(R-HSA-9013700)
Post-translational protein modification
(R-HSA-597592)
Post-translational protein phosphorylation
(R-HSA-8957275)
Regulation of insulin-like growth factor (igf) transport and uptake by insulin-like growth factor binding proteins (igfbps)
(R-HSA-381426)
Signaling by egfr
(R-HSA-177929)
Signaling by notch
(R-HSA-157118)
Signaling by notch1
(R-HSA-1980143)
Signaling by notch1 hd+pest domain mutants in cancer
(R-HSA-2894858)
Signaling by notch1 hd domain mutants in cancer
(R-HSA-2691230)
Signaling by notch1 in cancer
(R-HSA-2644603)
Signaling by notch1 pest domain mutants in cancer
(R-HSA-2644602)
Signaling by notch1 t(7;9)(notch1:m1580_k2555) translocation mutant
(R-HSA-2660825)
Signaling by notch2
(R-HSA-1980145)
Signaling by notch3
(R-HSA-9012852)
Signaling by notch4
(R-HSA-9013694)
Signaling by receptor tyrosine kinases
(R-HSA-9006934)
Signal transduction
(R-HSA-162582)
Adherens junction organization
(GO:0034332)
Amyloid precursor protein catabolic process
(GO:0042987)
Cell-cell signaling
(GO:0007267)
Cochlea development
(GO:0090102)
Constitutive protein ectodomain proteolysis
(GO:0051089)
Cytoplasm
(GO:0005737)
Endopeptidase activity
(GO:0004175)
Endoplasmic reticulum lumen
(GO:0005788)
Epidermal growth factor receptor ligand maturation
(GO:0038004)
Extracellular matrix disassembly
(GO:0022617)
Golgi-associated vesicle
(GO:0005798)
Golgi apparatus
(GO:0005794)
Golgi membrane
(GO:0000139)
Integrin-mediated signaling pathway
(GO:0007229)
Integrin binding
(GO:0005178)
In utero embryonic development
(GO:0001701)
Membrane protein ectodomain proteolysis
(GO:0006509)
Metal ion binding
(GO:0046872)
Metallodipeptidase activity
(GO:0070573)
Metalloendopeptidase activity
(GO:0004222)
Metalloendopeptidase activity involved in amyloid precursor protein catabolic process
(GO:1902945)
Metallopeptidase activity
(GO:0008237)
Molecular adaptor activity
(GO:0060090)
Monocyte activation
(GO:0042117)
Negative regulation of cell adhesion
(GO:0007162)
Negative regulation of gene expression
(GO:0010629)
Notch signaling pathway
(GO:0007219)
Nucleus
(GO:0005634)
Plasma membrane
(GO:0005886)
Pore complex assembly
(GO:0046931)
Positive regulation of cell growth
(GO:0030307)
Positive regulation of cell migration
(GO:0030335)
Positive regulation of cell population proliferation
(GO:0008284)
Positive regulation of t cell chemotaxis
(GO:0010820)
Postsynapse organization
(GO:0099173)
Protein binding
(GO:0005515)
Protein catabolic process at postsynapse
(GO:0140249)
Protein homodimerization activity
(GO:0042803)
Protein kinase binding
(GO:0019901)
Protein phosphorylation
(GO:0006468)
Protein processing
(GO:0016485)
Regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
(GO:0098696)
Regulation of notch signaling pathway
(GO:0008593)
Regulation of postsynapse organization
(GO:0099175)
Regulation of vasculature development
(GO:1901342)
Response to tumor necrosis factor
(GO:0034612)
Sh3 domain binding
(GO:0017124)
Signaling receptor binding
(GO:0005102)
Toxin transport
(GO:1901998)

Cells (max top 100)

(Marker Scores and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: anterior lens cell (CL0002223)
Fold Change: 3.1
Marker Score: 4,169
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 2.92
Marker Score: 3,532
Cell Name: epithelial cell of prostate (CL0002231)
Fold Change: 2.62
Marker Score: 1,822
Cell Name: central nervous system macrophage (CL0000878)
Fold Change: 2.5
Marker Score: 1,244
Cell Name: regular atrial cardiac myocyte (CL0002129)
Fold Change: 2.47
Marker Score: 8,766
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 2.44
Marker Score: 10,223
Cell Name: oligodendrocyte (CL0000128)
Fold Change: 2.37
Marker Score: 5,673
Cell Name: cerebral cortex endothelial cell (CL1001602)
Fold Change: 2.33
Marker Score: 1,393
Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
Fold Change: 2.31
Marker Score: 2,490
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 2.28
Marker Score: 1,331
Cell Name: pulmonary interstitial fibroblast (CL0002241)
Fold Change: 2.24
Marker Score: 1,793
Cell Name: sst GABAergic cortical interneuron (CL4023017)
Fold Change: 2.19
Marker Score: 43,517
Cell Name: renal principal cell (CL0005009)
Fold Change: 2.16
Marker Score: 1,664
Cell Name: basal epithelial cell of prostatic duct (CL0002236)
Fold Change: 2.13
Marker Score: 1,892
Cell Name: taste receptor cell (CL0000209)
Fold Change: 2.13
Marker Score: 1,840
Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
Fold Change: 2.1
Marker Score: 2,135
Cell Name: corneal epithelial cell (CL0000575)
Fold Change: 2.1
Marker Score: 2,315
Cell Name: vascular leptomeningeal cell (CL4023051)
Fold Change: 2.08
Marker Score: 2,397
Cell Name: early pro-B cell (CL0002046)
Fold Change: 2.08
Marker Score: 21,080
Cell Name: mature microglial cell (CL0002629)
Fold Change: 2.05
Marker Score: 742
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 2.05
Marker Score: 4,500
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 2.04
Marker Score: 596
Cell Name: sncg GABAergic cortical interneuron (CL4023015)
Fold Change: 2.03
Marker Score: 15,533
Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
Fold Change: 2
Marker Score: 29,960
Cell Name: astrocyte of the cerebral cortex (CL0002605)
Fold Change: 1.99
Marker Score: 42,560
Cell Name: germ cell (CL0000586)
Fold Change: 1.98
Marker Score: 3,464
Cell Name: regular ventricular cardiac myocyte (CL0002131)
Fold Change: 1.95
Marker Score: 43,629
Cell Name: A2 amacrine cell (CL0004219)
Fold Change: 1.93
Marker Score: 612
Cell Name: kidney interstitial fibroblast (CL1000692)
Fold Change: 1.92
Marker Score: 3,693
Cell Name: luminal cell of prostate epithelium (CL0002340)
Fold Change: 1.91
Marker Score: 1,113
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 1.9
Marker Score: 2,794
Cell Name: vip GABAergic cortical interneuron (CL4023016)
Fold Change: 1.89
Marker Score: 71,955
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.89
Marker Score: 116,300
Cell Name: parietal epithelial cell (CL1000452)
Fold Change: 1.89
Marker Score: 686
Cell Name: corneal endothelial cell (CL0000132)
Fold Change: 1.88
Marker Score: 1,094
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: 1.82
Marker Score: 17,282
Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
Fold Change: 1.81
Marker Score: 66,645
Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
Fold Change: 1.8
Marker Score: 16,923
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 1.78
Marker Score: 1,877
Cell Name: chandelier pvalb GABAergic cortical interneuron (CL4023036)
Fold Change: 1.76
Marker Score: 7,301
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: 1.74
Marker Score: 14,963
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: 1.7
Marker Score: 538
Cell Name: caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 1.7
Marker Score: 6,573
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 1.7
Marker Score: 94,894
Cell Name: mesangial cell (CL0000650)
Fold Change: 1.68
Marker Score: 2,027
Cell Name: cerebral cortex neuron (CL0010012)
Fold Change: 1.68
Marker Score: 4,784
Cell Name: lens fiber cell (CL0011004)
Fold Change: 1.67
Marker Score: 527
Cell Name: cholangiocyte (CL1000488)
Fold Change: 1.66
Marker Score: 622
Cell Name: kidney connecting tubule epithelial cell (CL1000768)
Fold Change: 1.62
Marker Score: 2,294
Cell Name: OFF retinal ganglion cell (CL4023033)
Fold Change: 1.61
Marker Score: 673
Cell Name: pyramidal neuron (CL0000598)
Fold Change: 1.59
Marker Score: 2,678
Cell Name: neuron (CL0000540)
Fold Change: 1.59
Marker Score: 6,488
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: 1.59
Marker Score: 541
Cell Name: squamous epithelial cell (CL0000076)
Fold Change: 1.55
Marker Score: 1,058
Cell Name: astrocyte (CL0000127)
Fold Change: 1.54
Marker Score: 1,334
Cell Name: cardiac neuron (CL0010022)
Fold Change: 1.53
Marker Score: 1,911
Cell Name: CD14-positive monocyte (CL0001054)
Fold Change: 1.52
Marker Score: 3,783
Cell Name: endothelial cell of lymphatic vessel (CL0002138)
Fold Change: 1.51
Marker Score: 941
Cell Name: microglial cell (CL0000129)
Fold Change: 1.51
Marker Score: 2,745
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 1.5
Marker Score: 1,704
Cell Name: blood cell (CL0000081)
Fold Change: 1.5
Marker Score: 17,419
Cell Name: endothelial cell (CL0000115)
Fold Change: 1.49
Marker Score: 1,337
Cell Name: luminal epithelial cell of mammary gland (CL0002326)
Fold Change: 1.48
Marker Score: 2,614
Cell Name: CD8-positive, alpha-beta cytokine secreting effector T cell (CL0000908)
Fold Change: 1.47
Marker Score: 636
Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
Fold Change: 1.47
Marker Score: 2,275
Cell Name: papillary tips cell (CL1000597)
Fold Change: 1.46
Marker Score: 294
Cell Name: choroid plexus epithelial cell (CL0000706)
Fold Change: 1.45
Marker Score: 1,332
Cell Name: kidney collecting duct principal cell (CL1001431)
Fold Change: 1.45
Marker Score: 3,648
Cell Name: melanocyte (CL0000148)
Fold Change: 1.45
Marker Score: 586
Cell Name: common dendritic progenitor (CL0001029)
Fold Change: 1.43
Marker Score: 495
Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
Fold Change: 1.43
Marker Score: 1,514
Cell Name: podocyte (CL0000653)
Fold Change: 1.42
Marker Score: 525
Cell Name: CD14-positive, CD16-positive monocyte (CL0002397)
Fold Change: 1.42
Marker Score: 2,766
Cell Name: renal interstitial pericyte (CL1001318)
Fold Change: 1.4
Marker Score: 1,335
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: 1.39
Marker Score: 1,448
Cell Name: lactocyte (CL0002325)
Fold Change: 1.38
Marker Score: 22,202
Cell Name: hepatocyte (CL0000182)
Fold Change: 1.38
Marker Score: 944
Cell Name: inhibitory interneuron (CL0000498)
Fold Change: 1.38
Marker Score: 6,363
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: 1.37
Marker Score: 679
Cell Name: basal cell (CL0000646)
Fold Change: 1.37
Marker Score: 1,766
Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
Fold Change: 1.36
Marker Score: 1,459
Cell Name: hematopoietic multipotent progenitor cell (CL0000837)
Fold Change: 1.36
Marker Score: 663
Cell Name: nasal mucosa goblet cell (CL0002480)
Fold Change: 1.36
Marker Score: 908
Cell Name: preosteoblast (CL0007010)
Fold Change: 1.35
Marker Score: 381
Cell Name: smooth muscle cell of prostate (CL1000487)
Fold Change: 1.34
Marker Score: 342
Cell Name: Unknown (CL0000548)
Fold Change: 1.33
Marker Score: 971
Cell Name: non-classical monocyte (CL0000875)
Fold Change: 1.32
Marker Score: 3,185
Cell Name: ON retinal ganglion cell (CL4023032)
Fold Change: 1.32
Marker Score: 360
Cell Name: alveolar macrophage (CL0000583)
Fold Change: 1.31
Marker Score: 33,673
Cell Name: Kupffer cell (CL0000091)
Fold Change: 1.31
Marker Score: 1,315
Cell Name: hematopoietic cell (CL0000988)
Fold Change: 1.31
Marker Score: 874
Cell Name: photoreceptor cell (CL0000210)
Fold Change: 1.31
Marker Score: 986
Cell Name: CD8-alpha-alpha-positive, alpha-beta intraepithelial T cell (CL0000915)
Fold Change: 1.31
Marker Score: 1,854
Cell Name: oligodendrocyte precursor cell (CL0002453)
Fold Change: 1.31
Marker Score: 1,619
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 1.31
Marker Score: 11,485
Cell Name: cell in vitro (CL0001034)
Fold Change: 1.31
Marker Score: 45,323
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: 1.3
Marker Score: 13,468
Cell Name: endothelial cell of uterus (CL0009095)
Fold Change: 1.3
Marker Score: 2,598
Cell Name: endothelial cell of vascular tree (CL0002139)
Fold Change: 1.3
Marker Score: 1,887
Cell Name: CD4-positive, alpha-beta cytotoxic T cell (CL0000934)
Fold Change: 1.3
Marker Score: 1,138

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Marker Score to the Marker Score Threshold, indicating how much the gene expression has changed compared to a baseline.
Marker Score: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

**Key Characteristics** ADAM10 is a type II transmembrane protein with a large ectodomain and a small cytoplasmic domain. The ectodomain of ADAM10 contains a metalloprotease domain, which is responsible for the shedding of proteins from the cell surface. ADAM10 is a member of the ADAM family, which is characterized by the presence of a disintegrin domain, a metalloprotease domain, and a cytoplasmic tail. ADAM10 is highly expressed in various tissues, including the central nervous system, epithelial cells, and immune cells. **Pathways and Functions** ADAM10 plays a critical role in various signaling pathways, including: 1. Notch signaling: ADAM10 is a key enzyme involved in the ectodomain shedding of Notch receptors, which is essential for regulating cell fate decisions, cell migration, and tissue development. 2. Cell signaling: ADAM10 sheds growth factors, receptors, and adhesion molecules, which regulates cellular signaling pathways, cell migration, and tissue development. 3. Cell adhesion: ADAM10 is involved in the shedding of adhesion molecules, which regulates cell-cell adhesion and tissue organization. 4. Protein processing: ADAM10 is involved in the processing of various proteins, including the amyloid precursor protein, which is implicated in Alzheimer's disease. **Clinical Significance** ADAM10 has been implicated in various diseases, including: 1. Cancer: ADAM10 is overexpressed in various types of cancer, including breast, lung, and colon cancer. ADAM10 promotes cancer progression by shedding growth factors and receptors that regulate cell growth and migration. 2. Alzheimer's disease: ADAM10 is involved in the processing of the amyloid precursor protein, which is implicated in Alzheimer's disease. ADAM10 shedding of the amyloid precursor protein may contribute to the formation of amyloid plaques. 3. Cardiovascular disorders: ADAM10 is involved in the regulation of blood pressure and cardiovascular function. ADAM10 shedding of endothelin-1, a potent vasoconstrictor, may contribute to the development of hypertension. 4. Neurodegenerative disorders: ADAM10 is involved in the regulation of neural development and function. ADAM10 shedding of Notch receptors may contribute to the development of neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease. In conclusion, ADAM10 is a critical enzyme involved in various cellular processes, including cell signaling, cell adhesion, and protein processing. ADAM10 has been implicated in various diseases, including cancer, Alzheimer's disease, and cardiovascular disorders. Further research is needed to fully understand the role of ADAM10 in human disease and to develop therapeutic strategies to target ADAM10 in the treatment of these diseases.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

CDw156

Genular Protein ID: 470821522

Symbol: ADA10_HUMAN

Name: CDw156

UniProtKB Accession Codes:

O14672 B4DU28 Q10742 Q92650

Database IDs:

Citations:

PubMed ID: 9305925

Title: Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases.

PubMed ID: 9305925

DOI: 10.1074/jbc.272.39.24588

PubMed ID: 8694785

Title: Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types.

PubMed ID: 8694785

DOI: 10.1042/bj3170045

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 9016778

Title: Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes.

PubMed ID: 9016778

DOI: 10.1006/bbrc.1996.5957

PubMed ID: 12475894

Title: ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles.

PubMed ID: 12475894

DOI: 10.1096/fj.02-0430fje

PubMed ID: 11477090

Title: The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein.

PubMed ID: 11477090

DOI: 10.1074/jbc.m105677200

PubMed ID: 11511685

Title: ADAM-10 protein is present in human articular cartilage primarily in the membrane-bound form and is upregulated in osteoarthritis and in response to IL-1alpha in bovine nasal cartilage.

PubMed ID: 11511685

DOI: 10.1177/002215540104900910

PubMed ID: 11786905

Title: Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells.

PubMed ID: 11786905

DOI: 10.1038/nm0102-41

PubMed ID: 16239146

Title: Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans.

PubMed ID: 16239146

DOI: 10.1016/j.cell.2005.08.014

PubMed ID: 16263699

Title: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.

PubMed ID: 16263699

DOI: 10.1074/mcp.m500324-mcp200

PubMed ID: 17557115

Title: The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells.

PubMed ID: 17557115

DOI: 10.1038/sj.cdd.4402175

PubMed ID: 19114711

Title: Substrate requirements for SPPL2b-dependent regulated intramembrane proteolysis.

PubMed ID: 19114711

DOI: 10.1074/jbc.m807485200

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 19349973

Title: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.

PubMed ID: 19349973

DOI: 10.1038/nbt.1532

PubMed ID: 20164177

Title: Nerve growth factor inhibits metalloproteinase-disintegrins and blocks ectodomain shedding of platelet glycoprotein VI.

PubMed ID: 20164177

DOI: 10.1074/jbc.m110.100479

PubMed ID: 20592283

Title: Junctional adhesion molecule-C is a soluble mediator of angiogenesis.

PubMed ID: 20592283

DOI: 10.4049/jimmunol.1000556

PubMed ID: 20624979

Title: Role of a disintegrin and metalloprotease 10 in Staphylococcus aureus alpha-hemolysin-mediated cellular injury.

PubMed ID: 20624979

DOI: 10.1073/pnas.1001815107

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21288900

Title: Ectodomain shedding and autocleavage of the cardiac membrane protease corin.

PubMed ID: 21288900

DOI: 10.1074/jbc.m110.185082

PubMed ID: 23676497

Title: Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease.

PubMed ID: 23676497

DOI: 10.1172/jci65401

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24990881

Title: TREM2 mutations implicated in neurodegeneration impair cell surface transport and phagocytosis.

PubMed ID: 24990881

DOI: 10.1126/scitranslmed.3009093

PubMed ID: 26091039

Title: A single kinase generates the majority of the secreted phosphoproteome.

PubMed ID: 26091039

DOI: 10.1016/j.cell.2015.05.028

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 26686862

Title: TspanC8 tetraspanins differentially regulate the cleavage of ADAM10 substrates, Notch activation and ADAM10 membrane compartmentalization.

PubMed ID: 26686862

DOI: 10.1007/s00018-015-2111-z

PubMed ID: 26876177

Title: Proteolytic Cleavage Governs Interleukin-11 Trans-signaling.

PubMed ID: 26876177

DOI: 10.1016/j.celrep.2016.01.053

PubMed ID: 26668317

Title: TspanC8 tetraspanins and A disintegrin and metalloprotease 10 (ADAM10) interact via their extracellular regions: evidence for distinct binding mechanisms for different TspanC8 proteins.

PubMed ID: 26668317

DOI: 10.1074/jbc.m115.703058

PubMed ID: 30463011

Title: A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to Promote alpha-Toxin Cytotoxicity.

PubMed ID: 30463011

DOI: 10.1016/j.celrep.2018.10.088

PubMed ID: 29430990

Title: The metalloprotease ADAM10 (a disintegrin and metalloprotease 10) undergoes rapid, postlysis autocatalytic degradation.

PubMed ID: 29430990

DOI: 10.1096/fj.201700823rr

PubMed ID: 30312582

Title: Astroprincin (FAM171A1, C10orf38): A Regulator of Human Cell Shape and Invasive Growth.

PubMed ID: 30312582

DOI: 10.1016/j.ajpath.2018.09.006

PubMed ID: 28600292

Title: ADAM10-Interacting Tetraspanins Tspan5 and Tspan17 Regulate VE-Cadherin Expression and Promote T Lymphocyte Transmigration.

PubMed ID: 28600292

DOI: 10.4049/jimmunol.1600713

PubMed ID: 31792032

Title: TspanC8 tetraspanins differentially regulate ADAM10 endocytosis and half-life.

PubMed ID: 31792032

DOI: 10.26508/lsa.201900444

PubMed ID: 34739841

Title: Crystal structure of the Tspan15 LEL domain reveals a conserved ADAM10 binding site.

PubMed ID: 34739841

DOI: 10.1016/j.str.2021.10.007

PubMed ID: 29224781

Title: Structural basis for regulated proteolysis by the alpha-secretase ADAM10.

PubMed ID: 29224781

DOI: 10.1016/j.cell.2017.11.014

PubMed ID: 37516108

Title: Structural basis for membrane-proximal proteolysis of substrates by ADAM10.

PubMed ID: 37516108

DOI: 10.1016/j.cell.2023.06.026

PubMed ID: 19608551

Title: Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate {alpha}-secretase activity.

PubMed ID: 19608551

DOI: 10.1093/hmg/ddp323

PubMed ID: 21618342

Title: Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and ADAM7 are often mutated in melanoma.

PubMed ID: 21618342

DOI: 10.1002/humu.21477

PubMed ID: 23666529

Title: Whole-exome sequencing identifies ADAM10 mutations as a cause of reticulate acropigmentation of Kitamura, a clinical entity distinct from Dowling-Degos disease.

PubMed ID: 23666529

DOI: 10.1093/hmg/ddt207

PubMed ID: 24055016

Title: ADAM10 missense mutations potentiate beta-amyloid accumulation by impairing prodomain chaperone function.

PubMed ID: 24055016

DOI: 10.1016/j.neuron.2013.08.035

Sequence Information:

Length: 748
Mass: 84142
Checksum: 0881E65B17022A71
Sequence:

MVLLRVLILL LSWAAGMGGQ YGNPLNKYIR HYEGLSYNVD SLHQKHQRAK RAVSHEDQFL 
RLDFHAHGRH FNLRMKRDTS LFSDEFKVET SNKVLDYDTS HIYTGHIYGE EGSFSHGSVI 
DGRFEGFIQT RGGTFYVEPA ERYIKDRTLP FHSVIYHEDD INYPHKYGPQ GGCADHSVFE 
RMRKYQMTGV EEVTQIPQEE HAANGPELLR KKRTTSAEKN TCQLYIQTDH LFFKYYGTRE 
AVIAQISSHV KAIDTIYQTT DFSGIRNISF MVKRIRINTT ADEKDPTNPF RFPNIGVEKF 
LELNSEQNHD DYCLAYVFTD RDFDDGVLGL AWVGAPSGSS GGICEKSKLY SDGKKKSLNT 
GIITVQNYGS HVPPKVSHIT FAHEVGHNFG SPHDSGTECT PGESKNLGQK ENGNYIMYAR 
ATSGDKLNNN KFSLCSIRNI SQVLEKKRNN CFVESGQPIC GNGMVEQGEE CDCGYSDQCK 
DECCFDANQP EGRKCKLKPG KQCSPSQGPC CTAQCAFKSK SEKCRDDSDC AREGICNGFT 
ALCPASDPKP NFTDCNRHTQ VCINGQCAGS ICEKYGLEEC TCASSDGKDD KELCHVCCMK 
KMDPSTCAST GSVQWSRHFS GRTITLQPGS PCNDFRGYCD VFMRCRLVDA DGPLARLKKA 
IFSPELYENI AEWIVAHWWA VLLMGIALIM LMAGFIKICS VHTPSSNPKL PPPKPLPGTL 
KRRRPPQPIQ QPQRQRPRES YQMGHMRR

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: ADAM10

Associated with

Cells (max top 100)

Other Information

Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases. PubMed ID: 9305925

Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. PubMed ID: 8694785

Analysis of the DNA sequence and duplication history of human chromosome 15. PubMed ID: 16572171

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes. PubMed ID: 9016778

ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles. PubMed ID: 12475894

The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. PubMed ID: 11477090

ADAM-10 protein is present in human articular cartilage primarily in the membrane-bound form and is upregulated in osteoarthritis and in response to IL-1alpha in bovine nasal cartilage. PubMed ID: 11511685

Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells. PubMed ID: 11786905

Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. PubMed ID: 16239146

Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. PubMed ID: 16263699

The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells. PubMed ID: 17557115

Substrate requirements for SPPL2b-dependent regulated intramembrane proteolysis. PubMed ID: 19114711

Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. PubMed ID: 19159218

Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. PubMed ID: 19349973

Nerve growth factor inhibits metalloproteinase-disintegrins and blocks ectodomain shedding of platelet glycoprotein VI. PubMed ID: 20164177

Junctional adhesion molecule-C is a soluble mediator of angiogenesis. PubMed ID: 20592283

Role of a disintegrin and metalloprotease 10 in Staphylococcus aureus alpha-hemolysin-mediated cellular injury. PubMed ID: 20624979

Initial characterization of the human central proteome. PubMed ID: 21269460

Ectodomain shedding and autocleavage of the cardiac membrane protease corin. PubMed ID: 21288900

Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease. PubMed ID: 23676497

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

TREM2 mutations implicated in neurodegeneration impair cell surface transport and phagocytosis. PubMed ID: 24990881

A single kinase generates the majority of the secreted phosphoproteome. PubMed ID: 26091039

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

TspanC8 tetraspanins differentially regulate the cleavage of ADAM10 substrates, Notch activation and ADAM10 membrane compartmentalization. PubMed ID: 26686862

Proteolytic Cleavage Governs Interleukin-11 Trans-signaling. PubMed ID: 26876177

TspanC8 tetraspanins and A disintegrin and metalloprotease 10 (ADAM10) interact via their extracellular regions: evidence for distinct binding mechanisms for different TspanC8 proteins. PubMed ID: 26668317

A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to Promote alpha-Toxin Cytotoxicity. PubMed ID: 30463011

The metalloprotease ADAM10 (a disintegrin and metalloprotease 10) undergoes rapid, postlysis autocatalytic degradation. PubMed ID: 29430990

Astroprincin (FAM171A1, C10orf38): A Regulator of Human Cell Shape and Invasive Growth. PubMed ID: 30312582

ADAM10-Interacting Tetraspanins Tspan5 and Tspan17 Regulate VE-Cadherin Expression and Promote T Lymphocyte Transmigration. PubMed ID: 28600292

TspanC8 tetraspanins differentially regulate ADAM10 endocytosis and half-life. PubMed ID: 31792032

Crystal structure of the Tspan15 LEL domain reveals a conserved ADAM10 binding site. PubMed ID: 34739841

Structural basis for regulated proteolysis by the alpha-secretase ADAM10. PubMed ID: 29224781

Structural basis for membrane-proximal proteolysis of substrates by ADAM10. PubMed ID: 37516108

Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate {alpha}-secretase activity. PubMed ID: 19608551

Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and ADAM7 are often mutated in melanoma. PubMed ID: 21618342

Whole-exome sequencing identifies ADAM10 mutations as a cause of reticulate acropigmentation of Kitamura, a clinical entity distinct from Dowling-Degos disease. PubMed ID: 23666529

ADAM10 missense mutations potentiate beta-amyloid accumulation by impairing prodomain chaperone function. PubMed ID: 24055016