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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Localization
Localization on EC 3.4.24.81 - ADAM10 endopeptidase
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predominant localization of the protein at the perinuclear region and at the cell surface where it appears as punctuated dots evenly distributed at the plasma membrane
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identification of an endoplasmic reticulum retention motif within the ADAM10 intracellular C-terminal tail. Sequential deletion/mutagenesis analyses shows that an arginine-rich (723RRR) sequence is responsible for the retention of ADAM10 in the endoplasmic reticulum and its inefficient surface trafficking. Mutating the second arginine to alanine is sufficient to allow endoplasmic reticulum exit and surface expression in both heterologous cells and hippocampal neurons
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the typical multidomain structure of ADAM10 as a type I integral transmembrane protein consists of a prodomain, a catalytical domain with a conserved zinc binding sequence, a cysteine-rich disintegrin-like domain, a transmembrane domain and a rather short cytoplasmic domain
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treatment of the glioblastoma cells with the PKC activator phorbol 12-myristate 13-acetate (PMA) leads to the translocation of ADAM10 to the cell membrane, the site at which N-cadherin is cleaved and this translocation is significantly reduced by the PKC-alpha inhibitor Gรถ6976 [12-(2-cyanoethyl)-6,7,12,13-tetrahydro-13-methyl-5-oxo-5H-indolo[2,3-a]pyrrolo[3,4-c]carbazole] or PKC-alpha short hairpin RNA