3.4.23.B24: signal peptide peptidase
This is an abbreviated version!
For detailed information about signal peptide peptidase, go to the full flat file.
Word Map on EC 3.4.23.B24
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3.4.23.B24
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aspartyl
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presenilins
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intramembrane-cleaving
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gamma-secretase
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sppl2a
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medicine
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gxgd-type
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spp-mediated
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bri2
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i-clips
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presenilin-like
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site-2
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pharmacology
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analysis
- 3.4.23.B24
-
aspartyl
-
presenilins
-
intramembrane-cleaving
- gamma-secretase
- sppl2a
- medicine
-
gxgd-type
-
spp-mediated
- bri2
- i-clips
-
presenilin-like
-
site-2
- pharmacology
- analysis
Reaction
intramembrane cleavage of signal peptides =
Synonyms
ANID_08681, aspartic intramembrane protease, Hm13, hSPP, minor histocompatibility antigen H13, PF3D7_1457000, PlSPP, signal peptide peptidase like 2a, signal peptide peptidase-like 2a, signal peptide peptidase-like 2B, signal peptide peptidase-like 2C, signal peptide peptidase-like 3, SPP, SPP-like 2A, SPP-like 2B, SPP-like 2C, SPP-like 3, SPP1, SppA, SPPL, SPPL2a, SPPL2b, SPPL2c, UMAG_02729
ECTree
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Subunits
Subunits on EC 3.4.23.B24 - signal peptide peptidase
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octamer
additional information
x * 65000, SDS-PAGE, fusion construct with green fluorescent protein
?
x * 26624, electrospray ionization mass spectrometry of protease resistant fragment Leu51-Gly295
?
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x * 26624, electrospray ionization mass spectrometry of protease resistant fragment Leu51-Gly295
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?
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x * 37000, recombinant FLAG-tagged enzyme, SDS-PAGE, x * 52000, about, sequence calculation
8 * 36000, SDS-PAGE. 8 * 28000, SDS-PAGE after limited digestion using thermolysin
octamer
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8 * 36000, SDS-PAGE. 8 * 28000, SDS-PAGE after limited digestion using thermolysin
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signal peptides have a common three-domain structure comprised by a short positive-charged n-region, a hydrophobic h-region of 7-15 residues, and a polar c-region including the site for signal peptidase cleavage
additional information
SPP/SPPL proteases either act as mono- or homodimers
additional information
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the monomeric form is the dominant species observed for the recombinant enzyme, with lesser amounts of dimer and trimer
additional information
SPP/SPPL proteases either act as mono- or homodimers
additional information
SPP/SPPL proteases either act as mono- or homodimers
additional information
SPP/SPPL proteases either act as mono- or homodimers
additional information
SPP/SPPL proteases either act as mono- or homodimers
additional information
-
the monomeric form is the dominant species observed for the recombinant enzyme, with lesser amounts of dimer and trimer
additional information
-
the monomeric form is the dominant species observed for the recombinant enzyme, with lesser amounts of dimer and trimer. The enzyme has multiple intracellular domains (ICDs)