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Protein

Disintegrin and metalloproteinase domain-containing protein 10

Gene

ADAM10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed:26686862, PubMed:11786905, PubMed:29224781). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146).By similarity10 Publications

Catalytic activityi

Endopeptidase of broad specificity.10 Publications

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Activity regulationi

Catalytically inactive when the propeptide is intact and associated with the mature enzyme (By similarity). The disintegrin and cysteine-rich regions modulate access of substrates to exerts an inhibitory effect on the cleavage of ADAM10 substrates (PubMed:29224781).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi173Zinc; in inhibited formBy similarity1
Metal bindingi383Zinc; via tele nitrogen; catalyticCombined sources2 Publications1
Active sitei3841 Publication1
Metal bindingi387Zinc; via tele nitrogen; catalyticCombined sources1 Publication1
Metal bindingi393Zinc; via tele nitrogen; catalyticCombined sources2 Publications1

GO - Molecular functioni

  • endopeptidase activity Source: UniProtKB
  • integrin binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: UniProtKB
  • metallopeptidase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • SH3 domain binding Source: UniProtKB-KW
  • signaling receptor binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processNotch signaling pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000137845-MONOMER
BRENDAi3.4.24.81 2681
ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-177929 Signaling by EGFR
R-HSA-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2660826 Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant
R-HSA-2691232 Constitutive Signaling by NOTCH1 HD Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-2979096 NOTCH2 Activation and Transmission of Signal to the Nucleus
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-6798695 Neutrophil degranulation
R-HSA-8957275 Post-translational protein phosphorylation
R-HSA-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus
R-HSA-9013700 NOTCH4 Activation and Transmission of Signal to the Nucleus
SignaLinkiO14672
SIGNORiO14672

Protein family/group databases

MEROPSiM12.210
TCDBi8.A.77.1.4 the sheddase (sheddase) family

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 10 (EC:3.4.24.817 Publications)
Short name:
ADAM 10
Alternative name(s):
CDw156
Kuzbanian protein homolog
Mammalian disintegrin-metalloprotease
CD_antigen: CD156c
Gene namesi
Name:ADAM10
Synonyms:KUZ, MADM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

EuPathDBiHostDB:ENSG00000137845.14
HGNCiHGNC:188 ADAM10
MIMi602192 gene
neXtProtiNX_O14672

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 672ExtracellularSequence analysisAdd BLAST653
Transmembranei673 – 693HelicalSequence analysisAdd BLAST21
Topological domaini694 – 748CytoplasmicSequence analysisAdd BLAST55

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Reticulate acropigmentation of Kitamura (RAK)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615537
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070907139P → S in RAK. 1 PublicationCorresponds to variant dbSNP:rs483352912EnsemblClinVar.1
Natural variantiVAR_070910524C → Y in RAK. 1 PublicationCorresponds to variant dbSNP:rs483352916EnsemblClinVar.1
Alzheimer disease 18 (AD18)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615590
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070908170Q → H in AD18; associated with disease susceptibility; significantly attenuates alpha-secretase activity of the enzyme; shifts APP processing toward beta-secretase-mediated cleavage resulting in enhanced amyloid-beta plaque load and reactive gliosis. 2 PublicationsCorresponds to variant dbSNP:rs61751103Ensembl.1
Natural variantiVAR_070909181R → G in AD18; associated with disease susceptibility; significantly attenuates alpha-secretase activity of the enzyme; shifts APP processing toward beta-secretase-mediated cleavage resulting in enhanced amyloid-beta plaque load and reactive gliosis. 2 PublicationsCorresponds to variant dbSNP:rs145518263EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi384E → A: Abrogates APP cleavage. Reduces Notch signaling. 1 Publication1

Keywords - Diseasei

Alzheimer disease, Amyloidosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi102
MalaCardsiADAM10
MIMi615537 phenotype
615590 phenotype
OpenTargetsiENSG00000137845
Orphaneti178307 Reticulate acropigmentation of Kitamura
PharmGKBiPA24505

Chemistry databases

ChEMBLiCHEMBL5028
DrugBankiDB04991 XL784
GuidetoPHARMACOLOGYi1658

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000002906620 – 213By similarityAdd BLAST194
ChainiPRO_0000029067214 – 748Disintegrin and metalloproteinase domain-containing protein 10Add BLAST535

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi222 ↔ 313Combined sources1 Publication
Glycosylationi267N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi278N-linked (GlcNAc...) asparagineCombined sources4 Publications1
Disulfide bondi344 ↔ 451Combined sources1 Publication
Disulfide bondi399 ↔ 435Combined sources1 Publication
Glycosylationi439N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi460 ↔ 495Combined sources1 Publication
Disulfide bondi471 ↔ 484Combined sources1 Publication
Disulfide bondi473 ↔ 479Combined sources1 Publication
Disulfide bondi483 ↔ 515Combined sources1 Publication
Disulfide bondi503 ↔ 511Combined sources1 Publication
Disulfide bondi510 ↔ 536Combined sources1 Publication
Disulfide bondi524 ↔ 543Combined sources1 Publication
Disulfide bondi530 ↔ 562Combined sources1 Publication
Glycosylationi551N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi555 ↔ 567Combined sources1 Publication
Disulfide bondi572 ↔ 598Combined sources1 Publication
Disulfide bondi580 ↔ 607Combined sources1 Publication
Disulfide bondi582 ↔ 597Combined sources1 Publication
Disulfide bondi594 ↔ 639Combined sources1 Publication
Disulfide bondi632 ↔ 645Combined sources1 Publication
Modified residuei719Phosphothreonine; by FAM20CCombined sources1 Publication1

Post-translational modificationi

The precursor is cleaved by furin and PCSK7.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei213 – 214Cleavage; by furin and PCSK7By similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

EPDiO14672
MaxQBiO14672
PaxDbiO14672
PeptideAtlasiO14672
PRIDEiO14672
ProteomicsDBi48162

PTM databases

GlyConnecti1178
iPTMnetiO14672
PhosphoSitePlusiO14672
SwissPalmiO14672

Miscellaneous databases

PMAP-CutDBiO14672

Expressioni

Tissue specificityi

Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver.2 Publications

Inductioni

In osteoarthritis affected-cartilage.

Gene expression databases

BgeeiENSG00000137845 Expressed in 242 organ(s), highest expression level in testis
CleanExiHS_ADAM10
ExpressionAtlasiO14672 baseline and differential
GenevisibleiO14672 HS

Organism-specific databases

HPAiCAB001709
HPA050670

Interactioni

Subunit structurei

Interacts with EPHA2 (By similarity). Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function, the cleavage occurs in trans, with ADAM10 and its substrate being on the membranes of opposing cells (PubMed:16239146). Interacts with NGF in a divalent cation-dependent manner (PubMed:20164177). Interacts with TSPAN14; the interaction promotes ADAM10 maturation and cell surface expression (PubMed:26668317, PubMed:26686862). Interacts with TSPAN5, TSPAN10, TSPAN15, TSPAN17 and TSPAN33; these interactions regulate ADAM10 substrate specificity (PubMed:26686862).By similarity3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi106616, 37 interactors
DIPiDIP-39889N
IntActiO14672, 11 interactors
MINTiO14672
STRINGi9606.ENSP00000260408

Chemistry databases

BindingDBiO14672

Structurei

Secondary structure

1748
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO14672
SMRiO14672
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini220 – 456Peptidase M12BPROSITE-ProRule annotationAdd BLAST237
Domaini457 – 551DisintegrinPROSITE-ProRule annotationAdd BLAST95

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi171 – 178Cysteine switchBy similarity8
Motifi708 – 715SH3-bindingSequence analysis8
Motifi722 – 728SH3-bindingSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi555 – 673Cys-richCuratedAdd BLAST119

Domaini

The propeptide keeps the metalloprotease in a latent form via a cysteine switch mechanism. This mechanism may be mediated by a highly conserved cysteine (Cys-173) in the propeptide, which interacts and neutralizes the zinc-coordinating HEXGHXXGXXHD catalytic core of the metalloprotease domain. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.By similarity
The Cys-rich region C-terminal to the disintegrin domain functions as a substrate-recognition module, it recognizes the EFNA5-EPHA3 complex but not the individual proteins (By similarity). Both Cys-rich and stalk region are necessary for interaction with TSPAN5, TSPAN10, TSPAN14, TSPAN17, TSPAN33 (PubMed:26668317). Stalk region is sufficient for interaction with TSPAN15 (By similarity).By similarity1 Publication

Keywords - Domaini

SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3658 Eukaryota
ENOG410XQWB LUCA
GeneTreeiENSGT00670000097974
HOGENOMiHOG000008148
HOVERGENiHBG050455
InParanoidiO14672
KOiK06704
OMAiEGFIQTH
OrthoDBiEOG091G01J4
PhylomeDBiO14672
TreeFamiTF352021

Family and domain databases

CDDicd04270 ZnMc_TACE_like, 1 hit
Gene3Di3.40.390.10, 1 hit
4.10.70.10, 1 hit
InterProiView protein in InterPro
IPR034025 ADAM10_ADAM17
IPR027053 ADAM_10
IPR001762 Disintegrin_dom
IPR036436 Disintegrin_dom_sf
IPR024079 MetalloPept_cat_dom_sf
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
PANTHERiPTHR11905:SF4 PTHR11905:SF4, 1 hit
PfamiView protein in Pfam
PF00200 Disintegrin, 1 hit
PF01562 Pep_M12B_propep, 1 hit
SMARTiView protein in SMART
SM00050 DISIN, 1 hit
SUPFAMiSSF57552 SSF57552, 1 hit
PROSITEiView protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50214 DISINTEGRIN_2, 1 hit
PS00142 ZINC_PROTEASE, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O14672-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MVLLRVLILL LSWAAGMGGQ YGNPLNKYIR HYEGLSYNVD SLHQKHQRAK
60 70 80 90 100
RAVSHEDQFL RLDFHAHGRH FNLRMKRDTS LFSDEFKVET SNKVLDYDTS
110 120 130 140 150
HIYTGHIYGE EGSFSHGSVI DGRFEGFIQT RGGTFYVEPA ERYIKDRTLP
160 170 180 190 200
FHSVIYHEDD INYPHKYGPQ GGCADHSVFE RMRKYQMTGV EEVTQIPQEE
210 220 230 240 250
HAANGPELLR KKRTTSAEKN TCQLYIQTDH LFFKYYGTRE AVIAQISSHV
260 270 280 290 300
KAIDTIYQTT DFSGIRNISF MVKRIRINTT ADEKDPTNPF RFPNIGVEKF
310 320 330 340 350
LELNSEQNHD DYCLAYVFTD RDFDDGVLGL AWVGAPSGSS GGICEKSKLY
360 370 380 390 400
SDGKKKSLNT GIITVQNYGS HVPPKVSHIT FAHEVGHNFG SPHDSGTECT
410 420 430 440 450
PGESKNLGQK ENGNYIMYAR ATSGDKLNNN KFSLCSIRNI SQVLEKKRNN
460 470 480 490 500
CFVESGQPIC GNGMVEQGEE CDCGYSDQCK DECCFDANQP EGRKCKLKPG
510 520 530 540 550
KQCSPSQGPC CTAQCAFKSK SEKCRDDSDC AREGICNGFT ALCPASDPKP
560 570 580 590 600
NFTDCNRHTQ VCINGQCAGS ICEKYGLEEC TCASSDGKDD KELCHVCCMK
610 620 630 640 650
KMDPSTCAST GSVQWSRHFS GRTITLQPGS PCNDFRGYCD VFMRCRLVDA
660 670 680 690 700
DGPLARLKKA IFSPELYENI AEWIVAHWWA VLLMGIALIM LMAGFIKICS
710 720 730 740
VHTPSSNPKL PPPKPLPGTL KRRRPPQPIQ QPQRQRPRES YQMGHMRR
Length:748
Mass (Da):84,142
Last modified:January 1, 1998 - v1
Checksum:i0881E65B17022A71
GO
Isoform 2 (identifier: O14672-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-319: Missing.

Note: No experimental confirmation available.
Show »
Length:447
Mass (Da):49,047
Checksum:iAAD95BF5D660C7D8
GO

Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YNC5H0YNC5_HUMAN
Disintegrin and metalloproteinase d...
ADAM10
148Annotation score:
C9J9B4C9J9B4_HUMAN
Disintegrin and metalloproteinase d...
ADAM10
125Annotation score:
H0YK87H0YK87_HUMAN
Disintegrin and metalloproteinase d...
ADAM10
115Annotation score:
B5MC71B5MC71_HUMAN
Disintegrin and metalloproteinase d...
ADAM10
71Annotation score:
H3BS53H3BS53_HUMAN
Disintegrin and metalloproteinase d...
ADAM10
58Annotation score:
H0YK32H0YK32_HUMAN
Disintegrin and metalloproteinase d...
ADAM10
38Annotation score:
A0A087WYG1A0A087WYG1_HUMAN
Disintegrin and metalloproteinase d...
ADAM10
59Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti162N → SERLKLRLRKLMSLELWTSC CLPCALLLHSWKKAVNSHCL YFKDFWGFSEIY in CAA88463 (PubMed:8694785).Curated1
Sequence conflicti212K → R in CAA88463 (PubMed:8694785).Curated1
Sequence conflicti296G → S in CAA88463 (PubMed:8694785).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070907139P → S in RAK. 1 PublicationCorresponds to variant dbSNP:rs483352912EnsemblClinVar.1
Natural variantiVAR_070908170Q → H in AD18; associated with disease susceptibility; significantly attenuates alpha-secretase activity of the enzyme; shifts APP processing toward beta-secretase-mediated cleavage resulting in enhanced amyloid-beta plaque load and reactive gliosis. 2 PublicationsCorresponds to variant dbSNP:rs61751103Ensembl.1
Natural variantiVAR_066309176H → Y in a cutaneous metastatic melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs267604273Ensembl.1
Natural variantiVAR_070909181R → G in AD18; associated with disease susceptibility; significantly attenuates alpha-secretase activity of the enzyme; shifts APP processing toward beta-secretase-mediated cleavage resulting in enhanced amyloid-beta plaque load and reactive gliosis. 2 PublicationsCorresponds to variant dbSNP:rs145518263EnsemblClinVar.1
Natural variantiVAR_070910524C → Y in RAK. 1 PublicationCorresponds to variant dbSNP:rs483352916EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05640119 – 319Missing in isoform 2. 1 PublicationAdd BLAST301

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009615 mRNA Translation: AAC51766.1
AK300472 mRNA Translation: BAG62190.1
AC018904 Genomic DNA No translation available.
AC091046 Genomic DNA No translation available.
Z48579 mRNA Translation: CAA88463.1
CCDSiCCDS10167.1 [O14672-1]
RefSeqiNP_001101.1, NM_001110.3 [O14672-1]
UniGeneiHs.172028
Hs.578508
Hs.745136

Genome annotation databases

EnsembliENST00000260408; ENSP00000260408; ENSG00000137845 [O14672-1]
GeneIDi102
KEGGihsa:102
UCSCiuc002afd.3 human [O14672-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009615 mRNA Translation: AAC51766.1
AK300472 mRNA Translation: BAG62190.1
AC018904 Genomic DNA No translation available.
AC091046 Genomic DNA No translation available.
Z48579 mRNA Translation: CAA88463.1
CCDSiCCDS10167.1 [O14672-1]
RefSeqiNP_001101.1, NM_001110.3 [O14672-1]
UniGeneiHs.172028
Hs.578508
Hs.745136

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M1Imodel-A207-453[»]
6BDZX-ray3.10A220-654[»]
6BE6X-ray2.80A/B/C/D214-654[»]
ProteinModelPortaliO14672
SMRiO14672
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106616, 37 interactors
DIPiDIP-39889N
IntActiO14672, 11 interactors
MINTiO14672
STRINGi9606.ENSP00000260408

Chemistry databases

BindingDBiO14672
ChEMBLiCHEMBL5028
DrugBankiDB04991 XL784
GuidetoPHARMACOLOGYi1658

Protein family/group databases

MEROPSiM12.210
TCDBi8.A.77.1.4 the sheddase (sheddase) family

PTM databases

GlyConnecti1178
iPTMnetiO14672
PhosphoSitePlusiO14672
SwissPalmiO14672

Proteomic databases

EPDiO14672
MaxQBiO14672
PaxDbiO14672
PeptideAtlasiO14672
PRIDEiO14672
ProteomicsDBi48162

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260408; ENSP00000260408; ENSG00000137845 [O14672-1]
GeneIDi102
KEGGihsa:102
UCSCiuc002afd.3 human [O14672-1]

Organism-specific databases

CTDi102
DisGeNETi102
EuPathDBiHostDB:ENSG00000137845.14
GeneCardsiADAM10
HGNCiHGNC:188 ADAM10
HPAiCAB001709
HPA050670
MalaCardsiADAM10
MIMi602192 gene
615537 phenotype
615590 phenotype
neXtProtiNX_O14672
OpenTargetsiENSG00000137845
Orphaneti178307 Reticulate acropigmentation of Kitamura
PharmGKBiPA24505
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3658 Eukaryota
ENOG410XQWB LUCA
GeneTreeiENSGT00670000097974
HOGENOMiHOG000008148
HOVERGENiHBG050455
InParanoidiO14672
KOiK06704
OMAiEGFIQTH
OrthoDBiEOG091G01J4
PhylomeDBiO14672
TreeFamiTF352021

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000137845-MONOMER
BRENDAi3.4.24.81 2681
ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-177929 Signaling by EGFR
R-HSA-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2660826 Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant
R-HSA-2691232 Constitutive Signaling by NOTCH1 HD Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-2979096 NOTCH2 Activation and Transmission of Signal to the Nucleus
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-6798695 Neutrophil degranulation
R-HSA-8957275 Post-translational protein phosphorylation
R-HSA-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus
R-HSA-9013700 NOTCH4 Activation and Transmission of Signal to the Nucleus
SignaLinkiO14672
SIGNORiO14672

Miscellaneous databases

ChiTaRSiADAM10 human
GeneWikiiADAM10
GenomeRNAii102
PMAP-CutDBiO14672
PROiPR:O14672
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137845 Expressed in 242 organ(s), highest expression level in testis
CleanExiHS_ADAM10
ExpressionAtlasiO14672 baseline and differential
GenevisibleiO14672 HS

Family and domain databases

CDDicd04270 ZnMc_TACE_like, 1 hit
Gene3Di3.40.390.10, 1 hit
4.10.70.10, 1 hit
InterProiView protein in InterPro
IPR034025 ADAM10_ADAM17
IPR027053 ADAM_10
IPR001762 Disintegrin_dom
IPR036436 Disintegrin_dom_sf
IPR024079 MetalloPept_cat_dom_sf
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
PANTHERiPTHR11905:SF4 PTHR11905:SF4, 1 hit
PfamiView protein in Pfam
PF00200 Disintegrin, 1 hit
PF01562 Pep_M12B_propep, 1 hit
SMARTiView protein in SMART
SM00050 DISIN, 1 hit
SUPFAMiSSF57552 SSF57552, 1 hit
PROSITEiView protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50214 DISINTEGRIN_2, 1 hit
PS00142 ZINC_PROTEASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiADA10_HUMAN
AccessioniPrimary (citable) accession number: O14672
Secondary accession number(s): B4DU28, Q10742, Q92650
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: January 1, 1998
Last modified: November 7, 2018
This is version 190 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  6. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
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