3.4.24.81: ADAM10 endopeptidase
This is an abbreviated version!
For detailed information about ADAM10 endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.81
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3.4.24.81
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alzheimer
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adam17
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amyloid
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ectodomain
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sheddase
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alpha-secretase
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endothelial
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metalloproteases
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neuroprotective
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plaque
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amyloidogenic
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non-amyloidogenic
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tnf
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sh-sy5y
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synaptic
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secretase
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membrane-anchored
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tetraspanins
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gamma-secretase
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n-cadherin
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presenilins
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notch1
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intramembrane
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abeta
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cxcl16
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prpc
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prion
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amyloid-beta
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prodomains
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psen1
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beta-secretase
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sappalpha
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hb-egf
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beta-site
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trans-signaling
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amphiregulin
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fractalkine
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meprin
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disintegrin-like
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adam17-mediated
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app-cleaving
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betacellulin
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nicastrin
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timp-3
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molecular biology
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anti-amyloidogenic
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medicine
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srage
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notch-dependent
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ad-like
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juxtamembrane
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bace-1
- 3.4.24.81
- alzheimer
- adam17
-
amyloid
- ectodomain
- sheddase
- alpha-secretase
- endothelial
- metalloproteases
-
neuroprotective
- plaque
-
amyloidogenic
-
non-amyloidogenic
- tnf
-
sh-sy5y
- synaptic
-
secretase
-
membrane-anchored
- tetraspanins
- gamma-secretase
- n-cadherin
-
presenilins
- notch1
-
intramembrane
- abeta
- cxcl16
- prpc
- prion
- amyloid-beta
- prodomains
- psen1
- beta-secretase
-
sappalpha
- hb-egf
-
beta-site
-
trans-signaling
- amphiregulin
- fractalkine
- meprin
-
disintegrin-like
-
adam17-mediated
-
app-cleaving
- betacellulin
-
nicastrin
- timp-3
- molecular biology
-
anti-amyloidogenic
- medicine
-
srage
-
notch-dependent
-
ad-like
-
juxtamembrane
- bace-1
Reaction
endopeptidase of broad specificity =
Synonyms
a disintegrin and metalloprotease 10, a disintegrin and metalloproteinase 10, a disintegrin and metalloproteinase-10, a-disintegrin-and-metalloprotease 10, AD10, ADAM 10, ADAM-10, ADAM10, CD156c, CD23 metalloprotease, HsT18717, kuz, kuzbanian, Kuzbanian protein, MADM, mammalian disintegrin-metalloprotease, metalloproteinase 10, metalloproteinase ADAM10, metalloproteinase Kuzbanian, metalloproteinase MADM, metalloproteinase-disintegrin, myelin-associated disintegrin metalloproteinase, notch proteinase, transmembrane metzinkin-protease of the a disintegrin and metalloproteinase family-10
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.4.24.81 - ADAM10 endopeptidase
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glycoprotein
proteolytic modification
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contains high-mannose as well as complex-type N-glycans. Glycosylation sites: S269, T280, S441, T553
glycoprotein
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glycosylation sites in the catalytic and disintegrin domain contain high-mannose as well as complex type N-glycans
glycoprotein
the enzyme has four potential N-glycosylation sites (N267, N278, N439 and N551)
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the enzyme has an inactive form that is activated by cleavage
proteolytic modification
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ADAM10 itself is subject to ectodomain shedding via a mechanism which is inhibited by ADAM inhibitor (GW4023) and stimulated by phorbol ester treatment of cells. The treatment of cells with GW4023 causes a reciprocal accumulation of membrane-associated mature ADAM10 in both cell lysates and extracellular membrane vesicles. ADAM9 is, at least in part, responsible for the ectodomain shedding of ADAM10
proteolytic modification
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tetraspanin overexpression enhances ADAM10 prodomain maturation, whereas TSPAN12 ablation diminishes ADAM10 maturation. TSPAN12 serves as a robust partner for ADAM10 and promotes ADAM10 maturation, thereby facilitating ADAM10-dependent proteolysis of amyloid precursor protein
proteolytic modification
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the nascent protein itself is not functional and is produced as a zymogen. After cleavage of the signalling sequence, ADAM10 enters the secretory pathway to be processed and thereby activated by the proprotein convertases furin or PC7
proteolytic modification
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synthesized in an inactive form, which is proteolytically activated during its forward transport along the secretory pathway and at the plasma membrane
proteolytic modification
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the nascent protein itself is not functional and is produced as a zymogen. After cleavage of the signalling sequence, ADAM10 enters the secretory pathway to be processed and thereby activated by the proprotein convertases furin or PC7