Entity Details

Primary name ADA10_HUMAN
Entity type UniProt
Source Source Link

Details

AccessionO14672
EntryNameADA10_HUMAN
FullNameDisintegrin and metalloproteinase domain-containing protein 10
TaxID9606
Evidenceevidence at protein level
Length748
SequenceStatuscomplete
DateCreated2003-02-28
DateModified2021-06-02

Ontological Relatives

GenesADAM10

GO terms

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GOName
GO:0000139 Golgi membrane
GO:0001701 in utero embryonic development
GO:0004175 endopeptidase activity
GO:0004222 metalloendopeptidase activity
GO:0005102 signaling receptor binding
GO:0005178 integrin binding
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005788 endoplasmic reticulum lumen
GO:0005794 Golgi apparatus
GO:0005798 Golgi-associated vesicle
GO:0005802 trans-Golgi network
GO:0005886 plasma membrane
GO:0005912 adherens junction
GO:0005925 focal adhesion
GO:0006468 protein phosphorylation
GO:0006509 membrane protein ectodomain proteolysis
GO:0007162 negative regulation of cell adhesion
GO:0007219 Notch signaling pathway
GO:0007229 integrin-mediated signaling pathway
GO:0007267 cell-cell signaling
GO:0007283 spermatogenesis
GO:0008021 synaptic vesicle
GO:0008237 metallopeptidase activity
GO:0008284 positive regulation of cell population proliferation
GO:0008593 regulation of Notch signaling pathway
GO:0009986 cell surface
GO:0010629 negative regulation of gene expression
GO:0010820 positive regulation of T cell chemotaxis
GO:0014069 postsynaptic density
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0016485 protein processing
GO:0017124 SH3 domain binding
GO:0019901 protein kinase binding
GO:0022617 extracellular matrix disassembly
GO:0030136 clathrin-coated vesicle
GO:0030307 positive regulation of cell growth
GO:0030335 positive regulation of cell migration
GO:0030424 axon
GO:0034205 amyloid-beta formation
GO:0034332 adherens junction organization
GO:0034612 response to tumor necrosis factor
GO:0035333 Notch receptor processing, ligand-dependent
GO:0035579 specific granule membrane
GO:0042117 monocyte activation
GO:0042803 protein homodimerization activity
GO:0042987 amyloid precursor protein catabolic process
GO:0043025 neuronal cell body
GO:0043065 positive regulation of apoptotic process
GO:0043066 negative regulation of apoptotic process
GO:0043197 dendritic spine
GO:0043231 intracellular membrane-bounded organelle
GO:0043312 neutrophil degranulation
GO:0043687 post-translational protein modification
GO:0044267 cellular protein metabolic process
GO:0045211 postsynaptic membrane
GO:0046872 metal ion binding
GO:0046930 pore complex
GO:0046931 pore complex assembly
GO:0051089 constitutive protein ectodomain proteolysis
GO:0061001 regulation of dendritic spine morphogenesis
GO:0070062 extracellular exosome
GO:0070821 tertiary granule membrane
GO:0090102 cochlea development
GO:0097038 perinuclear endoplasmic reticulum
GO:0097060 synaptic membrane
GO:0097197 tetraspanin-enriched microdomain
GO:0097327 response to antineoplastic agent
GO:0098696 regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
GO:0098978 glutamatergic synapse
GO:0099173 postsynapse organization
GO:1901342 regulation of vasculature development
GO:1901998 toxin transport
GO:1902945 metalloendopeptidase activity involved in amyloid precursor protein catabolic process
GO:1990000 amyloid fibril formation

Subcellular Location

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Subcellular Location
Cell junction
Cell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus membrane

Domains

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DomainNameCategoryType
IPR001590 Peptidase M12B, ADAM/reprolysinDomainDomain
IPR001762 Disintegrin domainDomainDomain
IPR002870 Peptidase M12B, propeptideDomainDomain
IPR024079 Metallopeptidase, catalytic domain superfamilyFamilyHomologous superfamily
IPR027053 Disintegrin and metalloproteinase domain-containing protein 10FamilyFamily
IPR034025 ADAM10/ADAM17 catalytic domainDomainDomain
IPR036436 Disintegrin domain superfamilyFamilyHomologous superfamily

Diseases

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Disease IDSourceNameDescription
615537 OMIMReticulate acropigmentation of Kitamura (RAK)A rare cutaneous pigmentation disorder characterized by reticulate, slightly depressed, sharply demarcated brown macules without hypopigmentation, affecting the dorsa of the hands and feet and appearing in the first or second decade of life. The macules gradually darken and extend to the proximal regions of the extremities. The manifestations tend to progress until middle age, after which progression of the eruptions stops. The pigmentary augmentation is found on the flexor aspects of the wrists, neck, patella and olecranon. Other features include breaks in the epidermal ridges on the palms and fingers, palmoplantar pits, occasionally plantar keratoderma, and partial alopecia. The disease is caused by variants affecting the gene represented in this entry.
615590 OMIMAlzheimer disease 18 (AD18)A late-onset form of Alzheimer disease. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituents of these plaques are neurotoxic amyloid-beta protein 40 and amyloid-beta protein 42, that are produced by the proteolysis of the transmembrane APP protein. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products, such as C31, are also implicated in neuronal death. Disease susceptibility is associated with variants affecting the gene represented in this entry.

Drugs

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DrugNameSourceType
DB04991 XL784Drugbanksmall molecule

Interactions

72 interactions

InteractorPartnerSourcesPublicationsLink
ADA10_HUMANPDIA3_HUMANBioGRID, MINT17170699 details
ADA10_HUMANBACE1_HUMANUniProt30538620 details
ADA10_HUMANA4_HUMANIntAct, UniProt30538620 32814053 details
ADA10_HUMANSH3G1_HUMANUniProt25036101 details
ADA10_HUMANLCK_HUMANBioGRID, UniProt11741929 25036101 details
ADA10_HUMANZDHC6_HUMANUniProt25036101 details
ADA10_HUMANGRB2_HUMANBioGRID, UniProt11741929 25036101 details
ADA10_HUMANHCLS1_HUMANUniProt25036101 details
ADA10_HUMANDBNL_HUMANUniProt25036101 details
ADA10_HUMANOTOR_HUMANUniProt25036101 details
ADA10_HUMANDOCK4_HUMANUniProt25036101 details
ADA10_HUMANSH321_HUMANUniProt25036101 details
ADA10_HUMANRUSC1_HUMANUniProt25036101 details
ADA10_HUMANARH38_HUMANUniProt25036101 details
ADA10_HUMANPACN3_HUMANUniProt25036101 details
ADA10_HUMANGRAP2_HUMANUniProt25036101 details
ADA10_HUMANSRC_HUMANUniProt25036101 details
ADA10_HUMANABL1_HUMANUniProt25036101 details
ADA10_HUMANSNX18_HUMANUniProt25036101 details
ADA10_HUMANCRK_HUMANUniProt25036101 details
ADA10_HUMANARHGJ_HUMANUniProt25036101 details
ADA10_HUMANPEX13_HUMANUniProt25036101 details
ADA10_HUMANNGEF_HUMANUniProt25036101 details
ADA10_HUMANRHG32_HUMANUniProt25036101 details
ADA10_HUMANARHGG_HUMANUniProt25036101 details
ADA10_HUMANGAS7_HUMANUniProt25036101 details
ADA10_HUMANMYO1E_HUMANUniProt25036101 details
ADA10_HUMANARHG4_HUMANUniProt25036101 details
ADA10_HUMANVINEX_HUMANUniProt25036101 details
ADA10_HUMANRIM3A_HUMANUniProt25036101 details
ADA10_HUMANRHG33_HUMANUniProt25036101 details
ADA10_HUMANLASP1_HUMANUniProt25036101 details
ADA10_HUMANMYO7A_HUMANUniProt25036101 details
ADA10_HUMANDLG1_HUMANBioGRID, UniProt17301176 25036101 details
ADA10_HUMANSPTA1_HUMANUniProt25036101 details
ADA10_HUMANSPTN1_HUMANUniProt25036101 details
ADA10_HUMANSH319_HUMANHPRD, UniProt15280379 25036101 details
ADA10_HUMANRIMB2_HUMANUniProt25036101 details
ADA10_HUMANCSKP_HUMANUniProt25036101 details
ADA10_HUMANDOCK2_HUMANUniProt25036101 details
ADA10_HUMANANDR_HUMANIntAct17727679 details
ADA10_HUMANPHB_HUMANIntAct20195357 details
ADA10_HUMANCD9_HUMANMINT, UniProt23091066 23289620 26686862 details
ADA10_HUMANEPHA3_HUMANDIP, HPRD16239146 19823572 details
ADA10_HUMANTSN5_HUMANBioGRID, UniProt23091066 26686862 details
ADA10_HUMANTSN15_HUMANBioGRID, UniProt23091066 26686862 details
ADA10_HUMANCD81_HUMANIntAct, UniProt19587294 23091066 26686862 32900848 details
ADA10_HUMANTSN14_HUMANBioGRID, UniProt23091066 26686862 details
ADA10_HUMANTSN33_HUMANBioGRID, UniProt23091066 26686862 details
ADA10_HUMANTSN17_HUMANBioGRID, UniProt23091066 details
ADA10_HUMANTSN10_HUMANBioGRID, UniProt23091066 details
ADA10_HUMANTSN12_HUMANUniProt19587294 details
ADA10_HUMANFYN_HUMANUniProt25036101 details
ADA10_HUMANHCK_HUMANUniProt25036101 details
ADA10_HUMANYES_HUMANUniProt25036101 details
ADA10_HUMANGRAP_HUMANUniProt25036101 details
ADA10_HUMANPACN1_HUMANUniProt25036101 details
ADA10_HUMANPACN2_HUMANUniProt25036101 details
ADA10_HUMANNCK1_HUMANUniProt25036101 details
ADA10_HUMANITK_HUMANUniProt25036101 details
ADA10_HUMANNCF1_HUMANUniProt25036101 details
ADA10_HUMANPPIP1_HUMANUniProt25036101 details
ADA10_HUMANSNX9_HUMANUniProt25036101 details
ADA10_HUMANSNX33_HUMANUniProt25036101 details
ADA10_HUMANEFNA2_HUMANBioGRID, HPRD10958785 details
ADA10_HUMANMD2L1_HUMANBioGRID11741929 details
ADA10_HUMANPAXI_HUMANBioGRID23317503 details
ADA10_HUMANNOTC1_HUMANBioGRID28611181 details
ADA10_HUMANTGFA_HUMANHPRD12590602 details
ADA10_HUMANEFNA1_HUMANHPRD16239146 details
ADA10_HUMANUFO_HUMANHPRD16227584 7822279 details
ADA10_HUMANDLL1_HUMANHPRD12794186 details