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1-aminocyclopropane-1-carboxylic acid synthase 6 + H2O
?
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phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase 6 introduces negative charges to the C-terminus of ACS6, which reduces the turnover of 1-aminocyclopropane-1-carboxylic acid synthase 6 by the 26S proteasome degradation machinery
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-
?
4-hydroxy-3-nitrophenol-Leu-Leu-Asn-vinylsulfone + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
4-hydroxy-3-nitrophenyl-Leu-Leu-Lys-vinylsulfone + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
AAF-7-amido-4-methylcoumarin + H2O
?
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highest activity in testicle, kidney and brain
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?
ABZ-Val-Val-Ser-Arg-Ser-Leu-Gly-Tyr(3-NO2)-NH2 + H2O
?
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synthetic, internally quenched substrate
-
-
?
acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O
acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin
acetyl-Arg-hSer-Thr-Arg-7-amido-4-methylcoumarin + H2O
acetyl-Arg-hSer-Thr-Arg + 7-amino-4-methylcoumarin
-
substrate for trypsin-like activity
-
-
?
acetyl-betaAla-Met(sulfone)-Thr-Arg-7-amido-4-methylcoumarin + H2O
acetyl-betaAla-Met(sulfone)-Thr-Arg + 7-amino-4-methylcoumarin
-
substrate for trypsin-like activity
-
-
?
acetyl-DPSD-7-amido-4-methylcoumarin + H2O
?
-
cleaved by the beta1 subunit of the 20S proteasome
-
-
?
acetyl-EPFD-7-amido-4-carbamoylcoumarin + H2O
?
acetyl-GPLD-7-amido-4-methylcoumarin + H2O
acetyl-GPLD + 7-amino-4-methylcoumarin
acetyl-GPLE-7-amido-4-methylcoumarin + H2O
acetyl-GPLE + 7-amino-4-methylcoumarin
acetyl-GPLL-7-amido-4-methylcoumarin + H2O
acetyl-GPLL + 7-amino-4-methylcoumarin
acetyl-hArg-Pro-2-fluoro-Phe-Asp-7-amido-4-methylcoumarin + H2O
acetyl-hArg-Pro-2-fluoro-Phe-Asp + 7-amino-4-methylcoumarin
-
substrate for caspase-like activity
-
-
?
acetyl-hArg-Pro-Abu-Asp-7-amido-4-methylcoumarin + H2O
acetyl-hArg-Pro-Abu-Asp + 7-amino-4-methylcoumarin
-
substrate for caspase-like activity
-
-
?
acetyl-HHSL-7-amido-4-carbamoylcoumarin + H2O
?
-
-
-
?
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin + H2O
?
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin
acetyl-Phe-Thr(Bzl)-His(3-benzyloxymethyl)-Leu-7-amido-4-methylcoumarin + H2O
acetyl-Phe-Thr(Bzl)-His(3-benzyloxymethyl)-Leu + 7-amino-4-methylcoumarin
-
substrate for chymotrypsin-like activity
-
-
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
acetyl-YWTQ-7-amido-4-carbamoylcoumarin + H2O
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzoyl-LRR-4-methyl-7-amido-coumarin + H2O
benzoyl-LRR + 4-methyl-7-amino-coumarin
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzoyl-VGR-4-methyl-7-amido-coumarin + H2O
benzoyl-VGR + 4-methyl-7-amino-coumarin
-
trypsin-like proteasome activity
-
-
?
benzoyl-VGR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyl-Val-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Leu-4-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-ARR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-D-Ala-Leu-Arg-4-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-dALR-2-naphthylamide + H2O
?
-
-
-
?
benzyloxycarbonyl-FR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-GAPLG-p-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-GGF-4-aminobenzoate + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GGF-p-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-GGL-2-naphthylamide + H2O
?
-
-
-
?
benzyloxycarbonyl-GGL-4-nitroanilide + H2O
?
-
chymotrypsin-like activity
-
?
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-GGR-2-naphthylamide + H2O
?
-
trypsin-like activity
-
?
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin + H2O
?
benzyloxycarbonyl-Gly-Gly-Arg-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-4-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
benzyloxycarbonyl-Gly-Gly-Leu-p-nitroanilide + H2O
?
benzyloxycarbonyl-Gly-Pro-Ala-Gly-Gly-p-aminobenzoate + aminopeptidase-N + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Ala-Leu-Ala-p-aminobenzoate + aminopeptidase-N + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GPAFG-4-aminobenzoate + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GPAFG-p-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-GPAGG-4-aminobenzoate + H2O
?
-
highest activity in soleus and brain
-
?
benzyloxycarbonyl-GPAGG-4-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
benzyloxycarbonyl-GPALG-p-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-LAF-4-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-2-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
?
-
11% of the activity with succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
benzyloxycarbonyl-Leu-Leu-Leu-7-amido-4-methylcoumarin + H2O
?
-
36% of the activity with succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
benzyloxycarbonyl-LLE-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-LLE-beta-naphthylamide + H2O
?
-
caspase-like activity
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-RR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
beta-casein + H2O
?
-
-
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
Boc-Leu-Leu-Glu-4-methylcoumarin-7-amide + H2O
Boc-Leu-Leu-Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Bz-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Bz-DL-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Bz-VGR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
DBC2 protein + H2O
?
-
-
-
-
?
dihydrofolate reductase + H2O
?
ERM transcription factor + H2O
?
-
-
-
-
?
erythroid Krueppel-like factor + H2O
?
-
-
-
-
?
fructose-1,6-bisphosphatase + H2O
?
-
-
-
-
?
Glu-Gly-Gly-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
H-VLK-7-amido-4-methylcoumarin + H2O
?
-
very-low activity
-
?
hepatitis B virus X protein + H2O
?
-
-
-
-
?
IkappaBalpha + H2O
?
-
can be directly degraded by 20S proteasomes. Deletion constructs of IkappaBalpha allow us to the determine that N-terminal (DELTA1-70)and C-terminal regions (DELTA280-327, removing the PEST region) of IkappaBalpha are not required for IkappaBalpha degradation,while a further C-terminal deletion including part of the arm repeats (DELTAC2 245-327) almost completely suppress the degradation by 20S proteasome. Degradation of IkappaBalpha involves specific interactions with a C3 subunit of the proteasome
-
-
?
Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Leu-Arg-Arg + H2O
?
-
-
-
-
?
Leu-Leu-Glu + H2O
?
-
-
-
-
?
Leu-Leu-Val-Tyr + H2O
?
-
-
-
-
?
Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
MATalpha2 repressor + H2O
?
-
-
-
-
?
methyl-casein + H2O
?
-
-
-
-
?
morpholinoacetyl-homophenylalanyl-methylseryl-thienylalanyl-7-amido-4-carbamoylmethylcoumarin + H2O
morpholinoacetyl-homophenylalanine-methylserine-thienylalanine + 7-amino-4-carbamoylmethylcoumarin
N-Cbz-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
N-methoxysuccinyl-Glu-Val-Lys-Met-p-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
N-succinyl-LLVY-aminoluciferin + H2O
?
-
-
-
-
?
N-t-Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butyloxycarbonyl-LSTR-7-amido-4-methylcoumarin + H2O
?
-
highest activity in kidney
-
?
ovalbumin + H2O
?
-
-
-
-
?
oxidized insulin B chain + H2O
?
-
-
-
-
?
p27(KIP1) + H2O
?
-
-
-
-
?
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
PS1/gamma-secretase complex component + H2O
?
S-RNase + H2O
?
-
S-RNase is ubiquitinated and degraded by the 26S proteasome
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + Suc-Leu-Leu-Val-Tyr
-
-
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
succinyl-AAF-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
succinyl-Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin-7-amide + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
succinyl-Leu-Met-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
t-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
t-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumarin-7-amide
?
-
-
-
-
?
tert-butyloxycarbonyl-LRR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
-
65% of the activity with succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
?
Tyr-Leu-Leu-Leu-vinylsulfone + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
Tyr-Val-Ala-Asp-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
ubiquitinylated proteins
?
unstable green fluorescence protein + H2O
?
-
artificial substrate for the proteasome. The model proteasomal substrate is stabilized by the carboxyl-terminal half of S5a, S5aC
-
-
?
Z-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Z-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Glu + 7-amino-4-methylcoumarin
Z-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
Z-LLE-2-naphthylamide + H2O
Z-LLE + 2-naphthylamine
-
post-acidic proteasome activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
Z-LLE-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Z-LRR-aminoluciferin + H2O
?
-
-
-
-
?
Z-nLPnLD-aminoluciferin + H2O
?
-
-
-
-
?
additional information
?
-
acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O
acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Ala-Pro-norleucine-Leu-Leu-7-amido-4-methylcoumarin + H2O
acetyl-Ala-Pro-norleucine-Leu-Leu + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-EPFD-7-amido-4-carbamoylcoumarin + H2O
?
-
-
-
?
acetyl-EPFD-7-amido-4-carbamoylcoumarin + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
acetyl-GPLD-7-amido-4-methylcoumarin + H2O
acetyl-GPLD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-GPLD-7-amido-4-methylcoumarin + H2O
acetyl-GPLD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-GPLE-7-amido-4-methylcoumarin + H2O
acetyl-GPLE + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-GPLE-7-amido-4-methylcoumarin + H2O
acetyl-GPLE + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-GPLL-7-amido-4-methylcoumarin + H2O
acetyl-GPLL + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-GPLL-7-amido-4-methylcoumarin + H2O
acetyl-GPLL + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin + H2O
?
-
-
-
?
acetyl-norleucine-Arg-norleucine-Arg-7-amido-4-carbamoylcoumarin + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-norleucine-Leu-Pro-norleucine-Leu-YVAD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-YWTQ-7-amido-4-carbamoylcoumarin + H2O
?
-
-
-
?
acetyl-YWTQ-7-amido-4-carbamoylcoumarin + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzoyl-LRR-4-methyl-7-amido-coumarin + H2O
benzoyl-LRR + 4-methyl-7-amino-coumarin
-
trypsin-like proteasome activity
-
-
?
benzoyl-LRR-4-methyl-7-amido-coumarin + H2O
benzoyl-LRR + 4-methyl-7-amino-coumarin
-
trypsin-like proteasome activity with the specific fluorogenic substrate
-
-
?
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin + H2O
?
-
tryspin-like activity
-
-
?
benzyloxycarbonyl-GGR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-p-nitroanilide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
-
-
-
?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
-
-
-
-
?
benzyloxycarbonyl-GPALG-4-aminobenzoate + H2O
?
-
highest activity in testicle, brain and soleus
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-beta-naphthylamide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
-
-
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
-
-
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
-
peptidyl-glutamyl-peptide-hydrolyzing activity
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
-
highest activity in testicle
-
?
benzyloxycarbonyl-LLE-2-naphthylamide + H2O
?
-
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
for trypsin-like activity
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
for trypsin-like activity
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
trypsin-like activity
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
trypsin-like activity
-
-
?
Boc-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
trypsin-like activity
-
-
?
casein + H2O
?
-
-
-
?
dihydrofolate reductase + H2O
?
-
directly hydrolyzed by the 20S complex, without any previous ubiquitination. The degradation is increased under oxidative conditions. The folate metabolism may be impaired by an increased degradation of dihydrofolate reductase, mediated by the 20S proteasome
-
-
?
dihydrofolate reductase + H2O
?
-
directly hydrolyzed by the 20S complex, without any previous ubiquitination. The degradation is increased under oxidative conditions
-
-
?
Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
morpholinoacetyl-homophenylalanyl-methylseryl-thienylalanyl-7-amido-4-carbamoylmethylcoumarin + H2O
morpholinoacetyl-homophenylalanine-methylserine-thienylalanine + 7-amino-4-carbamoylmethylcoumarin
-
most optimal combination of substrate residues identified
-
-
?
morpholinoacetyl-homophenylalanyl-methylseryl-thienylalanyl-7-amido-4-carbamoylmethylcoumarin + H2O
morpholinoacetyl-homophenylalanine-methylserine-thienylalanine + 7-amino-4-carbamoylmethylcoumarin
-
most optimal combination of substrate residues identified
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
-
highest activity in testicle, liver and spleen
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
chymotrypsin-like proteasome activity
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
chymotrypsin-like proteasome activity with the specific fluorogenic substrate
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
chymotrypsin-like proteasome activity
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
chymotrypsin-like proteasome activity
-
-
?
PS1/gamma-secretase complex component + H2O
?
-
gamma-secretase components are PS1, nicastrin, Pen-2, and Aph-1. Degradation of the complex components involves the proteasome, but regulation of their activity involves the PI3K/Akt pathway, overview. PS1/gamma-secretase is involved in the activation of phosphatidylinositol-3 kinase/Akt pathway, and is responsible for the intramembranous cleavage of various type-I membrane proteins. PS1/gamma-secretase is also deeply involved in the production of amyloid beta protein
-
-
?
PS1/gamma-secretase complex component + H2O
?
-
gamma-secretase components are PS1, nicastrin, Pen-2, and Aph-1
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
for chymotrypsin-like activity
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
for chymotrypsin-like activity
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
chymotrypsin-like activity
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
substrate for chymotrypsin-like activity of the 20S proteasome
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
O96780, O96787, O96788, Q9BMX8, Q9GU36, Q9GU37, Q9NDA1, Q9NDA2, Q9NDA3, Q9NHC5, Q9NHC6, Q9U793, Q9U794, Q9XZG5 -
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
A0A286S218; A0A286S1Z7; A0A286S200
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
-
chymotrypsin-like proteasome activity
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
-
chymotrypsin-like proteasome activity
-
-
?
succinyl-LLVY-aminoluciferin + H2O
succinyl-LLVY + aminoluciferin
-
chymotrypsin-like proteasome activity
-
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
ubiquitinylated proteins
?
-
individual substrates unknown
-
-
?
Z-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Glu + 7-amino-4-methylcoumarin
-
for caspase-like activity
-
-
?
Z-Leu-Leu-Glu-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Glu + 7-amino-4-methylcoumarin
-
for caspase-like activity
-
-
?
Z-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
for calpain-like activity
-
-
?
Z-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Z-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
for calpain-like activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
-
peptidylglutamyl peptide hydrolase proteasome activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
-
post-acidic proteasome activity
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
-
post-acidic proteasome activity with the specific fluorogenic substrate
-
-
?
Z-LLE-4-methyl-7-amido-coumarin + H2O
Z-LLE + 4-methyl-7-amino-coumarin
-
post-acidic proteasome activity
-
-
?
additional information
?
-
-
several other proteins associate with the Arabidopsis thaliana proteasome, including the PBAC2 assembly chaperonin, the associated DSS1/Sem1/RPN15 protein, the deubiquitylating enzyme UBP16, and the alternative activator PA200, genetic analysis of PA200 in Arabidopsis, overview
-
-
?
additional information
?
-
-
several other proteins associate with the Arabidopsis thaliana proteasome, including the PBAC2 assembly chaperonin, the associated DSS1/Sem1/RPN15 protein, the deubiquitylating enzyme UBP16, and the alternative activator PA200, genetic analysis of PA200 in Arabidopsis, overview
-
-
?
additional information
?
-
-
the tobacco mosaic virus-induced RNP7 subunit may be involved in programmed cell death
-
-
?
additional information
?
-
-
the 20S proteasome of Trypanosoma brucei shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
-
proteasome status in KG1a and U937 cells, overview
-
-
?
additional information
?
-
-
three major proteolytic activities of the proteasome can be distinguished as trypsin-like, chymotrypsin-like, and peptidyl-glutamyl peptide hydrolase activities, which cleave peptide bonds on the carboxyl side of basic, hydrophobic, and acidic amino acid residues, respectively. The catalytic core of the 20S proteasome is a Thr residue, responsible for the catalytic cleavage of substrates through nucleophilic attack
-
-
?
additional information
?
-
-
proteasome complexes possess three main catalytic activities, which are trypsin-like, chymotrypsin-like, and caspase-like
-
-
?
additional information
?
-
-
substrate docking sites, e.g. S5a, contain ubiquitin-interacting motifs that selectively recruit ubiquinated proteins to the proteasome. Human S5a-ubiquitin-interacting motifs stabilize only a subset of proteasomal substrates. Proliferation of A549 lung cancer cells is inhibited by S5a-ubiquitin-interacting motifs. S5a-ubiquitin-interacting motifs result in an increase in the number of apoptotic G0 cells, presumably because of inhibition of a subset of proteasomal substrate proteins
-
-
?
additional information
?
-
-
the proteasome cannot efficiently degrade unassembled R239C GFAP, and the interaction of R239C GFAP with proteasomes actually inhibits proteasomal protease activity. Soluble wild-type GFAP, but not R239C GFAP, is partially degraded by the 20 S proteasome
-
-
?
additional information
?
-
-
proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites. Caspase-like sites cleave after aspartates better than after glutamates
-
?
additional information
?
-
-
proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and two caspase-like proteolytic sites
-
?
additional information
?
-
-
the chymotrypsin-like and trypsin-like activities, but not the peptidylglutamyl peptide hydrolyzing activity plays a key role in oocyte maturation
-
?
additional information
?
-
-
enzyme has a preference for aromatic residues at P1 such as Phe, Tyr, Trp, and His. Aliphatic side chains (propyl, butyl) are well tolerated in the P2 position. The S3 pocket accommodates bulky and hydrophobic residues
-
-
?
additional information
?
-
-
enzyme has a preference for aromatic residues at P1 such as Phe, Tyr, Trp, and His. Aliphatic side chains (propyl, butyl) are well tolerated in the P2 position. The S3 pocket accommodates bulky and hydrophobic residues
-
-
?
additional information
?
-
-
maximal chymotrypsin-like activity of the 20S proteasome, which contributes to the cytolytic mechanism of the natural killer cells, is associated with the conformational changes occuring in a cluster of highly conserved proteasome residues from the alpha-subunit that lead to the proteasome open conformation, allowing substrate access into the proteolytic chamber
-
-
?
additional information
?
-
-
the proteasome is a cylindrical, multicatalytic proteolytic machine with three peptidase activities, chymotryptic, tryptic and postglutamyl peptide hydrolytic
-
-
?
additional information
?
-
-
mass spectrometric analysis of proteasome interactions. Several proteasome-interacting proteins unique to synaptic 26S proteasomes, i.e. 14-3-3gamma, TAX1BP1, drebrin, SNAP-25, may modulate proteolysis in a synapse-specific manner. Three E3s, i.e. KCMF1, HUWE1, and UBE3A, and five DUBs, i.e. USP5, USP7, USP13, USP14, and UCH37, in association with synaptic proteasomes, which may help proteasomes function more efficiently, help determine specificity for certain types of conjugates, or insure the rapid elimination of ubiquitin chains released from the substrate
-
-
?
additional information
?
-
-
mass spectrometric analysis of proteasome interactions. Several proteasome-interacting proteins unique to synaptic 26S proteasomes, i.e. 14-3-3gamma, TAX1BP1, drebrin, SNAP-25, may modulate proteolysis in a synapse-specific manner. Three E3s, i.e. KCMF1, HUWE1, and UBE3A, and five DUBs, i.e. USP5, USP7, USP13, USP14, and UCH37, in association with synaptic proteasomes, which may help proteasomes function more efficiently, help determine specificity for certain types of conjugates, or insure the rapid elimination of ubiquitin chains released from the substrate
-
-
?
additional information
?
-
-
the purified proteasome, comprising 102 distinct proteins, shows high chymotrypsin-like activity, mass spectrometry and protein identifications, overview
-
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?
additional information
?
-
-
overall substrate preference for hydrophobic residues at the P1 to P4 positions in a substrate. This overall stringency is relaxed in the 11 S regulatory (PA26)-20 S proteasome complex, which shows both appreciable activities for cleavage after acidic amino acids and a broadened activity for cleavage after basic amino acids. The 20S proteasome shows appreciable activity for cleavage after P1-Gln that is minimally observed in the human counterpart
-
?