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Information on EC 3.4.19.12 - ubiquitinyl hydrolase 1 and Organism(s) Homo sapiens and UniProt Accession Q92560

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.12 ubiquitinyl hydrolase 1
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This record set is specific for:
Homo sapiens
UNIPROT: Q92560 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
uch-l1, uchl1, ataxin-3, deubiquitinating enzyme, pgp 9.5, usp22, pgp9.5, plpro, otub1, isopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BRCA1-associated protein-1
-
C-terminal ubiquitin hydrolase
-
AD-019
-
-
-
-
AMSH
-
-
associated molecule with the SH3-domain of STAM
-
-
C-terminal hydrolases UCHL3
-
-
Cezanne
-
-
CGI-70
-
-
-
-
de-ubiquitinating enzyme
-
-
deubiquinating isopeptidase T
-
-
deubiquitinating enzyme
-
esterase, ubiquitin thiol-
-
-
-
-
hydrolase, ubiquitin carboxyl-terminal
-
-
-
-
hydrolase, ubiquitin carboxyl-terminal (Aplysia californica gene Ap-uch)
-
-
-
-
isopeptidase
-
-
-
-
isopeptidase T
Neuron cytoplasmic protein 9.5
-
-
-
-
Otubain-1
-
Otubain-2
-
ovarian tumour 1
-
PGP 9.5
PGP9.5
PGP9.5.1
-
-
Ub isopeptidase
-
-
ubiquitin C terminal hydrolase 1
-
-
ubiquitin C-terminal hydrolase
ubiquitin C-terminal hydrolase (Aplysia californica gene Ap-uch)
-
-
-
-
ubiquitin C-terminal hydrolase 37
-
-
ubiquitin C-terminal hydrolase L1
ubiquitin C-terminal hydrolase L3
-
Ubiquitin C-terminal hydrolase UCH37
ubiquitin C-terminal hydrolase-1
-
-
ubiquitin C-terminal hydrolase-L1
ubiquitin C-terminal hydrolase-L3
-
-
ubiquitin C-terminal hydrorase-L1
-
ubiquitin carboxy terminal hydrolase-L1
-
ubiquitin carboxy terminal hydrolase-L3
-
ubiquitin carboxy-terminal hydrolase
ubiquitin carboxy-terminal hydrolase L1
ubiquitin carboxy-terminal hydrolase-L1
-
-
ubiquitin carboxy-terminal hydrolase-L3
-
-
ubiquitin carboxyhydrolase L3
-
-
ubiquitin carboxyl terminal esterase L1
-
ubiquitin carboxyl terminal hydrolase 1
-
-
ubiquitin carboxyl terminal hydrolase L1
-
ubiquitin carboxyl terminal hydrolase-L1
-
ubiquitin carboxyl-terminal hydrolase
-
-
-
-
ubiquitin carboxyl-terminal hydrolase 1
ubiquitin carboxyl-terminal hydrolase 44
-
-
ubiquitin carboxyl-terminal hydrolase isozyme L1
-
ubiquitin carboxyl-terminal hydrolase L1
ubiquitin carboxyl-terminal hydrolase-L1
-
ubiquitin carboxyl-terminal hydrolase-L5
-
ubiquitin carboxyterminal hydrolase L3
-
-
ubiquitin hydrolase
ubiquitin hydrolase UCH-L3
-
ubiquitin isopeptidase
-
-
Ubiquitin thiolesterase
-
-
-
-
Ubiquitin thiolesterase L1
-
-
-
-
Ubiquitin thiolesterase L3
-
-
-
-
Ubiquitin thiolesterase L4
-
-
-
-
Ubiquitin thiolesterase L5
-
-
-
-
ubiquitin-C-terminal hydrolase L1
-
ubiquitin-carboxyl-terminal hydrolase PGP-9.5
-
-
-
-
ubiquitin-specific protease 44
-
-
UCH L1
UCH-1
-
-
-
-
UCH-L1
UCH-L2
-
-
-
-
UCH-L3
UCH-L4
-
-
-
-
UCH-L5
UCH37
UCHL-1
-
-
UCHL-3
-
-
UCHL1
UCHL1/PGP 9.5
-
-
Uchl3
UCHL5N240
-
USP22
-
-
USP44
-
-
yeast ubiquitin hydrolase
-
-
-
-
YUH1
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal)
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
189642-63-5
-
86480-67-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
HCF-1 + H2O
?
show the reaction diagram
HCF-1 is the principal Bap1-interacting protein. It is K48- and K63-ubiquitinated. Endogenous HCF-1C is ubiquitinated at lysine-1807 and/or lysine-1808
-
-
?
Ac-ALRGG-7-amido-4-trifluoromethylcoumarin
?
show the reaction diagram
-
-
-
?
Ac-LRGG-7-amido-4-trifluoromethylcoumarin
?
show the reaction diagram
-
-
-
?
Ac-RLRGG-7-amido-4-trifluoromethylcoumarin
?
show the reaction diagram
-
-
-
?
activity-based haemagglutinin-tagged ubiquitin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-tubulin + H2O
?
show the reaction diagram
-
-
-
-
?
beta-tubulin + H2O
?
show the reaction diagram
-
-
-
-
?
branched di-ubiquitin + H2O
ubiquitin
show the reaction diagram
branched dimeric ubiquitin + H2O
ubiquitin
show the reaction diagram
-
-
-
-
?
branched polyubiquitin + H2O
ubiquitin
show the reaction diagram
isopeptide-linked ubiquitin chains
-
?
di-ubiquitin + H2O
ubiquitin
show the reaction diagram
-
recombinant linear substrate, expressed in Escherichia coli
-
-
?
head-to-tail dimeric ubiquitin + H2O
ubiquitin
show the reaction diagram
-
-
-
-
?
head-to-tail polyubiquitin + H2O
ubiquitin
show the reaction diagram
-
recombinant substrate from expression in Escherichia coli
-
-
?
hemagglutinin-tagged ubiquitin-vinyl methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
inhibitor of kappa B-alpha + H2O
?
show the reaction diagram
-
UCHL1 deubiquitinates, thereby resulting in nuclear factor-kappa B inactivation
-
-
?
K48-linked tetraubiquitin + H2O
K48-linked diubiquitin + diubiquitin
show the reaction diagram
-
-
-
-
?
K63-linked polyubiquitin + H2O
K63-linked polyubiquitin + ubiquitin
show the reaction diagram
-
-
-
-
?
monoubiquitin + H2O
?
show the reaction diagram
N2-L-Asp-ubiquitin + H2O
ubiquitin + L-Asp
show the reaction diagram
-
-
-
?
N2-Lys-ubiquitin + H2O
ubiquitin + Lys
show the reaction diagram
-
ubiquitin amide of the alpha amino group of lysine
-
?
N6-(N2-acetyl)Lys-ubiquitin + H2O
ubiquitin + N2-acetyl-Lys
show the reaction diagram
-
ubiquitin amide of the alpha amino group of lysine
-
?
N6-Lys-ubiquitin + H2O
ubiquitin + Lys
show the reaction diagram
Nalpha-(diubiquitin)-[L-Lys] + H2O
?
show the reaction diagram
-
K48 linked diubiquitin
-
-
?
Nalpha-ubiquitin-[MQIFVRPR] + H2O
ubiquitin + MQIFVRPR
show the reaction diagram
-
-
-
-
?
Nedd-8 + H2O
?
show the reaction diagram
-
-
-
?
NEDD8-protein + H2O
NEDD8 + protein
show the reaction diagram
enzyme shows dual specificity for ubiquitin-conjugates and NEDD8-conjugates
-
?
Nepsilon-(diubiquitin)-[Nalpha-actyl-L-Lys] + H2O
?
show the reaction diagram
-
K48 linked diubiquitin
-
-
?
polyubiquitin + H2O
ubiquitin
show the reaction diagram
Smad2 + H2O
?
show the reaction diagram
-
weaker association
-
-
?
Smad3 + H2O
?
show the reaction diagram
-
weaker association
-
-
?
Smad7 + H2O
?
show the reaction diagram
-
association with Smad7, which can act as an adaptor able to recruit UCH37 to the type I TGF-beta receptor and reverses Smurf-mediated ubiquitination
-
-
?
spermidine-ubiquitin + H2O
ubiquitin + spermidine
show the reaction diagram
-
-
-
-
?
type I TGF-beta receptor + H2O
?
show the reaction diagram
ubiquitin + H2O
?
show the reaction diagram
ubiquitin + H2O
monoubiquitin
show the reaction diagram
-
UCH-L1 removes and recycles ubiquitin molecules from degraded proteins
-
-
?
ubiquitin 7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
ubiquitin C-terminal amide + H2O
ubiquitin + NH3
show the reaction diagram
-
-
-
-
?
ubiquitin ethyl ester + H2O
ubiquitin + ethanol
show the reaction diagram
-
-
-
-
?
ubiquitin glycine methyl ester + H2O
ubiquitin + methanol
show the reaction diagram
-
-
-
-
?
ubiquitin thiol ester of dithiothreitol + H2O
ubiquitin + dithiothreitol
show the reaction diagram
-
-
-
-
?
ubiquitin-4-methylcoumarin 7-amide + H2O
ubiquitin + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
ubiquitin-4-methylcoumarine 7-amide + H2O
ubiquitin + 7-amino-4-methylcoumarine
show the reaction diagram
-
-
-
?
ubiquitin-7-amido-4-methylcoumarin + H2O
ubiquitin + 7-amino-4-methylcoumarin
show the reaction diagram
ubiquitin-alcohol + H2O
ubiquitin + alcohol
show the reaction diagram
-
-
-
ir
ubiquitin-AMC + H2O
?
show the reaction diagram
-
-
-
?
ubiquitin-B domain of staphylococcal protein-A + H2O
ubiquitin + B domain of staphylococcal protein-A
show the reaction diagram
and variants thereof, substrate is expressed as alpha-linked C-terminal fusion to ubiquitin
-
-
?
ubiquitin-beta1 domain of streptococcal protein G + H2O
ubiquitin + beta1 domain of streptococcal protein G
show the reaction diagram
and variants thereof, substrate is expressed as alpha-linked C-terminal fusion to ubiquitin
-
-
?
ubiquitin-carboxyl extension protein + H2O
ubiquitin + ubiquitin-carboxyl extension protein
show the reaction diagram
-
carboxyl extension protein of 52 amino acids
-
?
ubiquitin-CEP52 + H2O
ubiquitin + CEP52
show the reaction diagram
-
substrate of UCHL1/PGP 9.5, no activity with UCHL3
-
-
?
ubiquitin-CEP80 + H2O
ubiquitin + CEP80
show the reaction diagram
-
substrate of UCHL3 and UCHL1/PGP 9.5
-
-
?
ubiquitin-peptide + H2O
?
show the reaction diagram
ubiquitin-protein + H2O
ubiquitin + protein
show the reaction diagram
ubiquitin-rhodamine110-glycine + H2O
rhodamine110
show the reaction diagram
-
-
-
-
?
ubiquitinyl-7-amido-4-methylcoumarin + H2O
ubiquitin + 7-amino-4-methylcoumarin
show the reaction diagram
mechanistic studies
-
-
?
ubiquitinyl-peptide + H2O
ubiquitin + peptide
show the reaction diagram
ubiquitinyl-Smad2 + H2O
ubiquitin + Smad2
show the reaction diagram
the enzyme de-ubiquitinates both Smad2 and Smad3 and up-regulates their stability
-
-
?
ubiquitinyl-Smad3 + H2O
ubiquitin + Smad3
show the reaction diagram
the enzyme de-ubiquitinates both Smad2 and Smad3 and up-regulates their stability
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
polyubiquitin + H2O
ubiquitin
show the reaction diagram
type I TGF-beta receptor + H2O
?
show the reaction diagram
UCH37 deubiquitinates and stabilizes type I TGF-beta receptor. Overexpression of UCH37 upregulates TGF-beta-dependent transcription
-
-
?
ubiquitin-CEP52 + H2O
ubiquitin + CEP52
show the reaction diagram
-
substrate of UCHL1/PGP 9.5, no activity with UCHL3
-
-
?
ubiquitin-CEP80 + H2O
ubiquitin + CEP80
show the reaction diagram
-
substrate of UCHL3 and UCHL1/PGP 9.5
-
-
?
ubiquitin-peptide + H2O
?
show the reaction diagram
ubiquitin-protein + H2O
ubiquitin + protein
show the reaction diagram
important role in regulation of cell growth
-
?
ubiquitinyl-Smad2 + H2O
ubiquitin + Smad2
show the reaction diagram
the enzyme de-ubiquitinates both Smad2 and Smad3 and up-regulates their stability
-
-
?
ubiquitinyl-Smad3 + H2O
ubiquitin + Smad3
show the reaction diagram
the enzyme de-ubiquitinates both Smad2 and Smad3 and up-regulates their stability
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
0.2 mol per mol of protein, native isozyme ISOT-S
Ni2+
-
0.5 mol per mol of protein, native isozyme ISOT-S
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
siRNA
stabilization of HCF-1 through depletion of Bap1. Knockdown of Bap1 results in a modest increase in the steady-state levels of HCF-1, which presumably helps to promote the transition from G1 into S-phase
-
(3E)-1-(3,4-dichlorobenzyl)-4-methoxy-5-phenyl-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0061 mM
(3E)-1-(3,4-dichlorobenzyl)-5-iodo-1H-indole-2,3-dione 3-(O-acetyloxime)
(3E)-1-(3,4-dichlorobenzyl)-5-methoxy-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0029 mM
(3E)-1-{2-bromo-2-[3-(trifluoromethyl)phenyl]ethyl}-5-chloro-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0095 mM
(3E)-3-[(acetyloxy)imino]-1-(3,4-dichlorobenzyl)-2-oxoindoline-5-carbonitrile
-
IC50: 0.012 mM
(3E)-3-[(acetyloxy)imino]-1-(3,4-dichlorobenzyl)-2-oxoindoline-5-carboxamide
-
IC50: 0.0041 mM
(3E)-3-[(acetyloxy)imino]-1-(3,4-dichlorobenzyl)-2-oxoindoline-5-carboxylic acid
-
IC50: 0.05 mM
(3E)-5-(trifluoromethoxy)-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0034 mM
(3E)-5-(trifluoromethoxy)-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-oxime
-
IC50: 0.078 mM
(3E)-5-bromo-1-(3,4-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.00081 mM
(3E)-5-chloro-1-(2,3-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0027 mM
(3E)-5-chloro-1-(2,4-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0012 mM
(3E)-5-chloro-1-(2,5-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.00088 mM
(3E)-5-chloro-1-(2-chloro-5-fluorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0065 mM
(3E)-5-chloro-1-(2-naphthylmethyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.014 mM
(3E)-5-chloro-1-(2-phenylethyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.019 mM
(3E)-5-chloro-1-(3,4-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
(3E)-5-chloro-1-(3,5-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0013 mM
(3E)-5-chloro-1-(3-chloro-4-methoxybenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.021 mM
(3E)-5-chloro-1-(3-methoxybenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.013 mM
(3E)-5-chloro-1-(4-chlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.012 mM
(3E)-5-chloro-1-(4-methoxybenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.052 mM
(3E)-5-chloro-1-[2-(3,4-dichlorophenoxy)ethyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0062 mM
(3E)-5-chloro-1-[2-(3,4-dichlorophenyl)ethyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0013 mM
(3E)-5-chloro-1-[2-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.018 mM
(3E)-5-chloro-1-[2-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-oxime
-
IC50: 0.321 mM
(3E)-5-chloro-1-[3-(3,4-dichlorophenyl)propyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.016 mM
(3E)-5-chloro-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
(3E)-5-chloro-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-oxime
-
IC50: 0.114 mM
(3E)-5-chloro-1-[4-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.012 mM
(3E)-5-chloro-1-[4-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-oxime
-
IC50: 0.013 mM
(3E)-5-chloro-1-{1-[2-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0088 mM
(3E)-5-chloro-1-{1-[2-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-oxime
-
IC50: 0.045 mM
(3E)-5-chloro-1-{1-[3-(trichloromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0034 mM
(3E)-5-chloro-1-{1-[3-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-oxime
-
IC50: 0.022 mM
(3E)-5-chloro-1-{2-ethoxy-2-[3-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.095 mM
(3E)-5-chloro-1-{2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.019 mM
(3E)-5-chloro-1-{2-[3-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0041 mM
(3E)-5-chloro-1-{2-[3-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-oxime
-
IC50: 0.08 mM
(3E)-5-chloro-7-methyl-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.012 mM
(3E)-5-fluoro-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0061 mM
(3E)-5-fluoro-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-oxime
-
IC50: 0.043 mM
(3E)-6-chloro-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0058 mM
1-(1,3-benzodioxol-5-ylmethyl)-4-(4-([(4-chlorophenyl)thio]methyl)benzoyl) piperazine
slight inhibition of UCH-L1
1-(3',4'-dihydroxybenzyl)-1,2,3,4-tetrahydroisoquinoline
the enzyme is covalently modified by the endogenous parkinsonism inducing dopamine derivative. 1-(3',4'-dihydroxybenzyl)-1,2,3,4-tetrahydroisoquinoline binds UCH-L1 specifically at Cys152 in vitro. This increases the amount of insoluble UCH-L1 and reduces its hydrolase activity in SH-SY5Y cells
1-benzyl-3-hydroxy-4-(5-methyl-2-furoyl)-5-(3-pyridinyl)-1,5-dihydro-2H-pyrrol-2-one
-
is a competitive inhibitor of UCH-L3, significantly inhibits hydrolysis activity of UCH-L3 by 83.2%
15-deoxy-DELTA12,14-prostaglandin J2
-
modification of UCH-L1 by cyclopentenone prostaglandins causes unfolding and aggregation. A single thiol group on Cys152 reacts with the alpha,beta-unsaturated carbonyl center in the cyclopentenone ring of prostaglandins, resulting in a covalent adduct, spectral analysis, overview
2-([4-(2-furylmethyl)-5-(2-thienylmethyl)-4H-1,2,4-triazol-3-yl]thio)-N-(2-methoxydibenzo[b,d]furan-3-yl)acetamide
-
2-propenal
-
carbonyl modification with 0.1 mM
2-[(5-ethyl-5H-[1,2,4]triazino[5,6-b]indol-3-yl)thio]-N-(4-methyl-2-pyridinyl)acetamide
-
3,5-bis[(4-nitrophenyl)methylidene]-1-prop-2-enoylpiperidin-4-one
i.e. b-AP15, administration of the UCHL5 inhibitor reduces the expression of FN, type I collagen, Smad2/Smad3, and the deposition of collagen in lung tissues in a bleomycin-induced model of pulmonary fibrosis
3-hydroxy-5-(4-methoxyphenyl)-1-(1,3,4-thiadiazol-2-yl)-4-(2-thienylcarbonyl)-1,5-dihydro-2H-pyrrol-2-one
-
significantly inhibits hydrolysis activity of UCH-L3 by 76.5%
3-[4-methyl-5-(([3-(2-thienyl)-1,2,4-oxadiazol-5-yl]methyl)thio)-4H-1,2,4-triazol-3-yl]-1H-indole
-
inhibits hydrolysis activity by 16.2%
4-([benzyl(methyl)amino]sulfonyl)-N-[5-(benzylthio)-1,3,4-thiadiazol-2-yl]benzamide
-
4-hydroxy-2-hexenal
-
carbonyl modification in a dose-dependent manner
4-hydroxy-2-nonenal
-
carbonyl modification with 0.01-0.1 mM leads to decreased ubiquitin binding, and both increased insolubility and interactions with proteins over 30 kDa compared with the wild-type
5-(4-fluorophenyl)-3-hydroxy-4-(5-methyl-2-furoyl)-1-(3-pyridinylmethyl)-1,5-dihydro-2H-pyrrol-2-one
-
significantly inhibits hydrolysis activity of UCH-L3 by 76.8%
5-chloro-1-(3,4-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
-
IC50: 0.0018 mM
5-chloro-1-(3,4-dichlorobenzyl)-1H-indole-2,3-dione 3-oxime
-
IC50: 0.012 mM
8-[(1H-benzimidazol-2-ylmethyl)sulfanyl]-2,2-dimethyl-5-(morpholin-4-yl)-1,4-dihydro-2H-pyrano[4'',3'':4',5']pyrido[3',2':4,5]thieno[3,2-d]pyrimidine
-
aldehyde product of fatty acid peroxidation
-
benzyloxycarbonyl-Val-Ala-Glu(gamma-methoxy) fluoromethylketone
co-crystal structure reveals that the inhibitor binds in the active-site cleft, irreversibly modifying the active-site cysteine
dimethyl sulfoxide
-
catalytic activity decreases slightly with increasing dimethyl sulfoxide concentrations. At 2% (v/v) dimethyl sulfoxide, the proteolytic activity of UCH-L3 is reduced by ca. 5% in comparison to dimethyl sulfoxide-free conditions
dipicolinic acid
-
-
DTT
-
erythrocyte isozyme ISOT-S and ISOT-L, inhibition by chelating of Zn2+
EDTA
-
-
EGTA
-
-
epoxysuccinyl-leucylamido-(4-guanidino) butane
reduces UCH-L1 mRNA, protein level and activity. Caspase-mediated apoptosis in epoxysuccinyl-leucylamido-(4-guanidino) butane-treated fibroblasts is reversed by transfection with a UCH-L1 plasmid
iodoacetamide
isatin O-acyl oximes
-
reversible and competitive inhibition, inhibitory potency and features of the drivatives, specific inhibition of UCH-L1, poor inhibition of UCH-L3, IC50 values, overview
J series prostaglandins
-
inhibition of the enzyme is involved in disruption of the proteasome pathway and leads to apoptosis
-
LDN 57 444
UCH-L1 inhibition leads to a time and concentration-dependent formation of membrane protrusions, accompanied by redistribution of alpha-actinin-4 to the membrane. Expression level of alpha-actinin-4 remains stable, whereas the beta-catenin content increases. Inhibition of UCH-L1 does not induce apoptosis
N,N'-(oxydi-4,1-phenylene)dibenzenesulfonamide
slight inhibition of UCH-L1
N,N'-4,4'-biphenyldiylbis(4-ethylbenzenesulfonamide)
strong inhibition of UCH-L1
N-(2-[(6,7-dimethoxy-1-isoquinolinyl)methyl]-4,5-dimethoxyphenyl)-4-(2-oxo-1-pyrrolidinyl)benzenesulfonamide
slight inhibition of UCH-L1
N-(3,6-dichloro-2-pyridinyl)-N'-([(4,6-diphenyl-2-pyrimidinyl)amino]carbonyl)sulfamide
-
N-(4-([(4-ethoxyphenyl)amino]sulfonyl)phenyl)-2-naphthalenesulfonamide
slight inhibition of UCH-L1
N-(4-([(4-methylphenyl)amino]sulfonyl)phenyl)-2-phenyl-2-(phenylthio)acetamide
slight inhibition of UCH-L1
N-ethylmaleimide
UBPY
N-[2-(4-benzyl-1-piperazinyl)-2-oxoethyl]-N-(3-methylphenyl)benzenesulfonamide
slight inhibition of UCH-L1
nitrilo-triacetate
-
-
peptides
-
containing either of the cleavage site sequence found in ubiquitin polymers, but not unrelated peptides
RNAi
-
siRNA
-
ubiquitin
Ubiquitin aldehyde
inhibition mechanism
-
ubiquitin vinyl methyl ester
a ubiquitin-based suicide substrate, binding structure analysis with wild-type and mutant S18Y enzymes, overview
-
ubiquitin vinylmethyl ester
inhibitor forms a covalent adduct with the active site cysteine of the enzyme
-
ubiquitin vinylsulfone
irreversible inhibitor that covalently modifies the active-site cysteines of DUBs
-
ubiquitin-aldehyde
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
active-site thiol is very sensitive to oxidation and requires reductants
4-hydroxy-2-alkenal
-
modification of UCH-L1 promotes direct interactions between UCH-L1 and tubulin
4-hydroxy-2-nonenal
-
modification of UCH-L1 promotes direct interactions between UCH-L1 and tubulin
Adrm1
recruits Uch37 to the proteasome. Binds the carboxy-terminal tail of Uch37. Following binding, Adrm1 relieves Uch37 autoinhibition, accelerating the hydrolysis of ubiquitin-7-amido-4-methylcoumarin
-
DTT
-
active-site thiol is very sensitive to oxidation and requires reductants
ethyl 1-[N-(4-methylphenyl)-N-(methylsulfonyl)alanyl]-4-piperidinecarboxylate
-
Sodium citrate
TNFalpha
-
inducer
-
tumor necrosis factor-alpha
-
treatment of cultured vascular smooth muscle cells for 24 and 48 hours does not significantly alter UCHL1 mRNA levels, whereas long term treatment (96 hours) significantly increases UCHL1 mRNA levels. Treatment of aortic endothelial cells and aortic smooth muscle cells with tumor necrosis factor-alpha for 24 hours does not significantly alter UCHL1 mRNA levels
-
ubiquitin
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
branched dimeric ubiquitin
-
pH 7.2, 37°C
-
0.015
head-to-tail dimeric ubiquitin
-
pH 7.2, 37°C
-
0.000047 - 0.02149
ubiquitin 7-amido-4-methylcoumarin
-
0.0006
ubiquitin ethyl ester
-
isozyme L1
-
0.0000833 - 0.00014
ubiquitin-7-amido-4-methylcoumarin
-
0.000034
ubiquitin-rhodamine110-glycine
-
-
-
0.000035
ubiquitinyl-7-amido-4-methylcoumarin
pH 7.5, 25°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011 - 33.67
ubiquitin 7-amido-4-methylcoumarin
-
0.0794 - 0.196
ubiquitin-7-amido-4-methylcoumarin
-
4.72
ubiquitin-rhodamine110-glycine
-
-
-
0.001
ubiquitinyl-7-amido-4-methylcoumarin
pH 7.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000104 - 7410
ubiquitin 7-amido-4-methylcoumarin
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00014 - 0.00019
ubiquitin
0.000001
Ubiquitin aldehyde
below, pH 7.5, 25°C, inhibition kinectis
-
additional information
additional information
-
inhibition kinetics of isatin O-acyl oximes, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0061
(3E)-1-(3,4-dichlorobenzyl)-4-methoxy-5-phenyl-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0061 mM
0.00094 - 0.016
(3E)-1-(3,4-dichlorobenzyl)-5-iodo-1H-indole-2,3-dione 3-(O-acetyloxime)
0.0029
(3E)-1-(3,4-dichlorobenzyl)-5-methoxy-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0029 mM
0.0095
(3E)-1-{2-bromo-2-[3-(trifluoromethyl)phenyl]ethyl}-5-chloro-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0095 mM
0.012
(3E)-3-[(acetyloxy)imino]-1-(3,4-dichlorobenzyl)-2-oxoindoline-5-carbonitrile
Homo sapiens
-
IC50: 0.012 mM
0.0041
(3E)-3-[(acetyloxy)imino]-1-(3,4-dichlorobenzyl)-2-oxoindoline-5-carboxamide
Homo sapiens
-
IC50: 0.0041 mM
0.05
(3E)-3-[(acetyloxy)imino]-1-(3,4-dichlorobenzyl)-2-oxoindoline-5-carboxylic acid
Homo sapiens
-
IC50: 0.05 mM
0.0034
(3E)-5-(trifluoromethoxy)-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0034 mM
0.078
(3E)-5-(trifluoromethoxy)-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-oxime
Homo sapiens
-
IC50: 0.078 mM
0.00081
(3E)-5-bromo-1-(3,4-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.00081 mM
0.0027
(3E)-5-chloro-1-(2,3-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0027 mM
0.0012
(3E)-5-chloro-1-(2,4-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0012 mM
0.00088
(3E)-5-chloro-1-(2,5-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.00088 mM
0.0065
(3E)-5-chloro-1-(2-chloro-5-fluorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0065 mM
0.014
(3E)-5-chloro-1-(2-naphthylmethyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.014 mM
0.019
(3E)-5-chloro-1-(2-phenylethyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.019 mM
0.0018 - 0.017
(3E)-5-chloro-1-(3,4-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
0.0013
(3E)-5-chloro-1-(3,5-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0013 mM
0.021
(3E)-5-chloro-1-(3-chloro-4-methoxybenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.021 mM
0.013
(3E)-5-chloro-1-(3-methoxybenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.013 mM
0.012
(3E)-5-chloro-1-(4-chlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.012 mM
0.052
(3E)-5-chloro-1-(4-methoxybenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.052 mM
0.0062
(3E)-5-chloro-1-[2-(3,4-dichlorophenoxy)ethyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0062 mM
0.0013
(3E)-5-chloro-1-[2-(3,4-dichlorophenyl)ethyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0013 mM
0.018
(3E)-5-chloro-1-[2-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.018 mM
0.321
(3E)-5-chloro-1-[2-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-oxime
Homo sapiens
-
IC50: 0.321 mM
0.016
(3E)-5-chloro-1-[3-(3,4-dichlorophenyl)propyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.016 mM
0.006 - 0.036
(3E)-5-chloro-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
0.114
(3E)-5-chloro-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-oxime
Homo sapiens
-
IC50: 0.114 mM
0.012
(3E)-5-chloro-1-[4-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.012 mM
0.013
(3E)-5-chloro-1-[4-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-oxime
Homo sapiens
-
IC50: 0.013 mM
0.0088
(3E)-5-chloro-1-{1-[2-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0088 mM
0.045
(3E)-5-chloro-1-{1-[2-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-oxime
Homo sapiens
-
IC50: 0.045 mM
0.0034
(3E)-5-chloro-1-{1-[3-(trichloromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0034 mM
0.022
(3E)-5-chloro-1-{1-[3-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-oxime
Homo sapiens
-
IC50: 0.022 mM
0.095
(3E)-5-chloro-1-{2-ethoxy-2-[3-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.095 mM
0.019
(3E)-5-chloro-1-{2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.019 mM
0.0041
(3E)-5-chloro-1-{2-[3-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0041 mM
0.08
(3E)-5-chloro-1-{2-[3-(trifluoromethyl)phenyl]ethyl}-1H-indole-2,3-dione 3-oxime
Homo sapiens
-
IC50: 0.08 mM
0.012
(3E)-5-chloro-7-methyl-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.012 mM
0.0061
(3E)-5-fluoro-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0061 mM
0.043
(3E)-5-fluoro-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-oxime
Homo sapiens
-
IC50: 0.043 mM
0.0058
(3E)-6-chloro-1-[3-(trifluoromethyl)benzyl]-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0058 mM
0.103
1-benzyl-3-hydroxy-4-(5-methyl-2-furoyl)-5-(3-pyridinyl)-1,5-dihydro-2H-pyrrol-2-one
Homo sapiens
-
-
0.154
3-hydroxy-5-(4-methoxyphenyl)-1-(1,3,4-thiadiazol-2-yl)-4-(2-thienylcarbonyl)-1,5-dihydro-2H-pyrrol-2-one
Homo sapiens
-
-
0.123
5-(4-fluorophenyl)-3-hydroxy-4-(5-methyl-2-furoyl)-1-(3-pyridinylmethyl)-1,5-dihydro-2H-pyrrol-2-one
Homo sapiens
-
-
0.0018
5-chloro-1-(3,4-dichlorobenzyl)-1H-indole-2,3-dione 3-(O-acetyloxime)
Homo sapiens
-
IC50: 0.0018 mM
0.012
5-chloro-1-(3,4-dichlorobenzyl)-1H-indole-2,3-dione 3-oxime
Homo sapiens
-
IC50: 0.012 mM
0.015
N,N'-4,4'-biphenyldiylbis(4-ethylbenzenesulfonamide)
Homo sapiens
-
0.00074
ubiquitin
Homo sapiens
-
-
0.1
additional information
Homo sapiens
-
IC50 above 0.1 mM: (3E)-5-chloro-1-(pyridin-3-ylmethyl)-1H-indole-2,3-dione 3-(O-acetyloxime), (3E)-5-chloro-1-(pyridin-4-ylmethyl)-1H-indole-2,3-dione 3-(O-acetyloxime), 4-({(3E)-3-[(acetyloxy)imino]-5-chloro-2-oxo-2,3-dihydro-1H-indol-1-yl}methyl)benzoi
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.2 - 8.3
-
broad optimum
7.4
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
analysis of pH dependence of the reaction, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
mRNA and protein expression, expressed in endothelial cells in atherosclerotic lesions from human carotid arteries
Manually annotated by BRENDA team
-
mRNA and protein expression
Manually annotated by BRENDA team
the median concentration of UCHL1 in the blood plasma of boys with cryptorchidism, is 5folds higher than in boys with inguinal hernia, whose testicles are located in the scrotum. Significant difference between UCHL1 levels in boys with cryptorchidism up to 2 years old, and above 2 years old. Older boys, whose testicles since birth are located in the inguinal pouch or in the abdominal cavity, have higher concentration of UCHL1 in their blood plasma, than boys from younger group
Manually annotated by BRENDA team
UCH-L1 is highly expressed
Manually annotated by BRENDA team
human cervical carcinoma cell line
Manually annotated by BRENDA team
-
UCHL3 and UCH37 are upregulated in the majority of tumor tissues compared to the adjacent normal tissues. UCH-L1 activity is lower in a significant proportion of the tumors but to a less extent in advanced tumors
Manually annotated by BRENDA team
prefrontal. UCH L1 is 1.1-1.2fold decreased in alcoholics
Manually annotated by BRENDA team
-
in accordance with the relatively low UCH-L1 activity in tumor biopsies, UCH-L1 is detected only in one out of eight cervical carcinoma lines
Manually annotated by BRENDA team
low level
Manually annotated by BRENDA team
-
non-small cell lung cancer cell line
Manually annotated by BRENDA team
isoform UCH-L1 does not partition to the membrane in the cultured cell lines tested
Manually annotated by BRENDA team
UCHL1 expression is low, which is well correlated with its promoter methylation status
Manually annotated by BRENDA team
UCHL1 expression is low, which is well correlated with its promoter methylation status
Manually annotated by BRENDA team
-
a bronchial epithelial cell line, the cells show increased UCH-L1 expression, overview
Manually annotated by BRENDA team
-
only UCH-L3 is clearly identified in primary keratinocytes. UCH-L1 and UCH-L3 activity is upregulated following HPV E6/E7 immortalization of keratinocytes
Manually annotated by BRENDA team
-
different cell lines
Manually annotated by BRENDA team
-
a B lymphoblastoid cell line
Manually annotated by BRENDA team
-
present in patients with sporadic Parkinson´s disease
Manually annotated by BRENDA team
isoform UCH-L1 does not partition to the membrane in the cultured cell lines tested
Manually annotated by BRENDA team
present in cancerous cells originating from tissues that do not normally express UCH-L1, including pancreatic cancer, colorectal cancer and invasive breast cancer
Manually annotated by BRENDA team
UCHL1 expression is low, which is well correlated with its promoter methylation status
Manually annotated by BRENDA team
expresses UCH-L1 and expression correlates with the differentiation status. In the cortex of normal biopsies, UCH-L1 is predominantly expressed in distal tubules, macula densa, and nerve fibres. A subset of human glomerulopathies associated with podocyte foot process effacement (membranous nephropathy, SLE class V, FSGS) de novo express UCH-L1 in podocyte cell bodies, nuclei, and processes
Manually annotated by BRENDA team
expression analysis of UCHL! in the renal cell carcinoma system, profiling, overview
Manually annotated by BRENDA team
-
photoreceptor cells, bipolar cells, and amacrine cells are devoid of staining while the dendrites and axons of both the horizontal cells and the ganglion cells stain strongly
Manually annotated by BRENDA team
human prostate cell line
Manually annotated by BRENDA team
-
a bronchial epithelial cell line, the cells show increased UCH-L1 expression, overview
Manually annotated by BRENDA team
-
a neuroblastoma cell line
Manually annotated by BRENDA team
level of UCH-L1 mRNA is significantly reduced in fibroblasts of patients affected with lysosomal storage disorders
Manually annotated by BRENDA team
UCHL1 expression is low, which is well correlated with its promoter methylation status
Manually annotated by BRENDA team
-
spermatogonia in humans can be subdivided into three types, overview
Manually annotated by BRENDA team
-
UCHL-1 protein reduced in cases with Lewy body pathology
Manually annotated by BRENDA team
-
isozyme L3
Manually annotated by BRENDA team
human osteosarcoma cell line
Manually annotated by BRENDA team
-
UCH37 activity is up-regulated in cervical carcinoma biopsies as well as cell lines, while UCH-L1 activity is lower in cervical carcinomas
Manually annotated by BRENDA team
-
mRNA and protein expression, expressed in vascular smooth muscle cells in atherosclerotic lesions from human carotid arteries
Manually annotated by BRENDA team
human fibroblast cell line
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
only Bap1, no presence of HCF-1
Manually annotated by BRENDA team
HCF-1 and Bap1 are similarly distributed throughout the nucleoplasm. HCF-1 interacts with Bap1 through its beta-propeller domain
Manually annotated by BRENDA team
undifferentiated podocytes exhibit strong UCH-L1 expression at the cell membrane along leading edges
-
Manually annotated by BRENDA team
-
membrane associated form UCH-L1M, C-terminal farnesylation promotes the association of UCH-L1 with the membrane
Manually annotated by BRENDA team
-
associated to
Manually annotated by BRENDA team
-
the membrane-associated UCH-L1M form is associated with the plasma membrane of oocytes, C-terminal farnesylation promotes the association of UCH-L1 with the membrane
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BAP1_HUMAN
729
0
80362
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
analytical ultracentrifugation
130000
x * 130000, SDS-PAGE
25000
immunoblot analysis
25902
-
x * 25902, UCH-L1, mass spectrometry
28900
-
x * 28900, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
-
C-terminal farnesylation promotes the association of UCH-L1 with membranes. Inhibition of UCH-L1 farnesylation by farnesyltransferase inhibitor FTI-277
ubiquitination
-
monoubiquitination is a posttranslational modification of UCH-L1 that controls the function of UCH-L1. It may occur reversibly to a lysine residue near the active site, probably K157, of UCH-L1. This modification restricts enzyme activity by preventing binding to the ubiquitinated targets, and permanent mono-ubiquitination, as mimicked by a ubiquitin-UCH-L1 fusion, inhibits UCH-L1 in its capacity to increase free ubiquitin levels. However, the lifetime of this modification on UCH-L1 is regulated by auto-deubiquitination
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.4 A resolution, x-ray crystallography. Overall fold resembles that of other ubiquitin hydrolases, including UCHL3. Geometry of the catalytic residues in the active site of UCH-L1 is distorted in such a way that the hydrolytic activity appears to be impossible without substrate induced conformational rearrangements
hanging drop vapour diffusion method, 1.45 A resolution crystal structure of human UCH-L3 in complex with the inhibitor ubiquitin vinylmethyl ester
purified recombinant UCH37 catalytic domain, i.e. UCH37N, selenomethionine-substituted UCH37N, and of mutant C88A, sitting-drop vapor diffusion method, 14 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 1 mM DTT, 20°C, versus a reservoir solution containing 22% PEG 4000, 0.2 M MgCl2, 0.1 M Tris-HCl, pH 8.5, and 3.5% xylitol, microseeding, X-ray diffraction structure determination and analysis at 2.2 A resolution
purified recombinant wild-type and mutant GST-tagged enzymes, 35 mg/ml protein in 50 mM Tris-HCl, pH 7.4, 150 mM NaCl, 10 mM DTT, crystallization at room temperature, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular modeling, structure-function relationship
purified recombinant wild-type UCH-L1 and the Parkinson disease-associated variant of the enzyme, mutant S18Y, bound to a ubiquitin-based suicide substrate, ubiquitin vinyl methyl ester, hanging drop vapour diffusion method, 25 mg/ml enzyme-UbVMe complex in 50 mM Tris-HCl, pH 7.4, 150 mM NaCl, and 10 mM DTT, are mixed with 2.4 M ammonium sulfate and 0.1 M bicine, pH 9.0, 2 months, X-ray diffraction structure determination and analysis at 2.4-2.85 A resolution, molecular replacement
UCH-L3, crystal structure at 1.8 A resolution
-
X-ray structure of UCHL1 co-crystallized with a peptide-based fluoromethylketone inhibitor, benzyloxycarbonyl-Val-Ala-Glu(gamma-methoxy) fluoromethylketone (Z-VAE(OMe)-FMK (VAEFMK)), at 2.35 A resolution is reported
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C91A
catalytically inactive mutant, can still associate with the HCF-1 beta-propeller but cannot remove ubiquitin chains
C132A
-
site-directed mutagenesis, the mutant behaves similar to the wild-type enzyme
C132S
-
no effect on protein insolubility or interactions
C152A
-
site-directed mutagenesis, removal of the C152 thiol group by mutation renders the protein refractory to attack by 15-deoxy-DELTA12,14-prostaglandin J2
C152S
-
binds to monoubiquitin in both 4-hydroxy-2-nonenal-treated cells and untreated cells
C201A
-
site-directed mutagenesis, the mutant behaves similar to the wild-type enzyme
C209S
-
catalytically inactive, does not suppress NF-kappaB nuclear translocation and transcriptional activity by targeting the TNFR signaling pathway at the level of the IkappaB kinase complex or upstream from it. Does not suppress polyubiquitinated RIP1 and does not enhance the levels of monubiquinated or unmodified RIP1 as compared to the wild-type
C220A
-
site-directed mutagenesis, the mutant behaves similar to the wild-type enzyme
C220S
C335S
-
site-directed mutagenesis of active site Cys335, unaltered substrate binding
C37A
site-directed mutagenesis
C47A
-
site-directed mutagenesis, the mutant behaves similar to the wild-type enzyme
C786A
site-directed mutagenesis, no activity
C90A
-
site-directed mutagenesis, the mutant behaves similar to the wild-type enzyme
C90S/K157R
-
reduces monoubiquitination
C95A
enhances the interaction of ubiquitin dimers with UCH-L3
D176A
mutant shows an increased interaction with CDK4 compared to wild-type
D176N
-
site-directed mutagenesis, isozyme L1, 97.5% reduced activity compared to wild-type
D30A
-
site-directed mutagenesis, the mutant enzyme shows highly reduced hydrolase and ubiquitin binding activity
D33A
ubiquitin affinity deficient mutant, diminishes the interaction of ubiquitin dimers with UCH-L3
D348A
-
site-directed mutagenesis, inactive mutant, leads to accumulation of ubiquitin on endosomes and the concomitant stabilization of an ubiquinated form of the signal transducing adeptor molecule, STAM
DELTA148-190
deletion mutant containing amino acids 148-190 interacts with CDK4
DELTA148-223
deletion mutant containing amino acids 148-223 interacts with CDK4
DELTA160-190
deletion mutant containing amino acids 160-190 interacts with CDK4
DELTA160-223
deletion mutant containing amino acids 160-223 interacts with CDK4
DELTA188-223
deletion mutant containing amino acids 188-223 does not interact with CDK4
E174A
mutant shows an increased interaction with CDK4 compared to wild-type
E7A
point mutation in UCH-L1 is identified as the cause of early onset neurodegeneration in three siblings who appear normal at birth, but became blind at 5 years old and suffer progressive neurological dysfunction and cerebellar ataxia, and are unable to stand by the age of 30
F214A
the F214A mutant binds with approximately 60fold less affinity to ubiquitin compared to the wild-type UCH-L1, it shows highly reduced activity compared tot he wild-type enzyme
H161D
H161K
H161N
H161Q
H161Y
H165A
mutant shows an increased interaction with CDK4 compared to wild-type
H185A
-
displays increased interactions with tubulin
Q37R
-
site-directed mutagenesis, isozyme L1, unaltered activity
Q82A
kcat and Km can not be determined individually because, even at concentrations of ubiquitin 7-amido-4-methylcoumarin as high as 12 microM, the Michaelis-Menten plot is still rising linearly with substrate concentration, not reaching the plateau that is diagnostic of saturation
Q84A
Km (ubiquitin 7-amido-4-methylcoumarin) increased compared to wild-type, kcat (ubiquitin 7-amido-4-methylcoumarin) decreased
Q89A
Km (ubiquitin 7-amido-4-methylcoumarin) increased compared to wild-type, kcat (ubiquitin 7-amido-4-methylcoumarin) decreased
S18Y/I93M
-
increased insolubility
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
active-site thiol is very sensitive to oxidation and requires reductants
-
35003
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-60°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant Bap1-flag proteins immunopurified with alpha-flag beads
affinity purified
by anion exchange chromatography and gel filtration
-
by gel filtration
isozyme ISOT-S from erythrocytes
-
on Ni-NTA column
on Ni-NTA resin
-
partial, recombinant wild-type and mutant isozymes ISOT-S and ISOT-L from Escherichia coli
-
purification of GST-tagged UCH-L1 by gel filtration
-
recombinant
recombinant GST-tagged enzyme from Escherichia coli
-
recombinant GST-tagged UCH-L1 from Escherichia coli strain Rosetta BL21(DE3) by glutathione affinity chromatography
recombinant GST-tagged wild-type UCHL1 and mutant S18Y from Escherichia coli strain BL21(Rosetta) by glutathione affinity chromatography, cleavage of the tag, and gel filtration
recombinant His-tagged wild-type and mutants of isozyme L1 expressed in Escherichia coli DH5alphaPRO
recombinant N-terminally GST-tagged UCH37 catalytic domain from Escherichia coli BL21(RIPL) by glutathione affinity chromatography, proteolytic removal of the GST-tag, and gel filtration
recombinant truncated GST-fusion protein of UBPY
recombinant wild-type and mutant GST-tagged enzymes from Escherichia coli by glutathione affinity chromatography and gel filtration
recombinant wild-type and mutants of isozymes L1 and L3 from Escherichia coli BL21(DE3), to near homogeneity
-
UCH-L1, UCH-L3
-
UCH-L3 purified on Ni-NTA column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Flag-tagged wild-type or mutant Bap1 expressed in HEK-293 cells. HA-tagged Bap1 transiently expressed in HeLa cells
COS-7 cells co-transfected with plasmids encoding His-tagged UCH-L1 and FLAG-tagged ubiquitin
-
determination of the UCHL1 promoter DNA methylation status and the mechanisms for the heterogeneous UCHL1 expression pattern in renal epithelium and in renal cell carcinoma, overview. Semi-quantitative and real-time RT-PCR analysis
-
expressed in BAEC cells
-
expressed in COS-7 cells
expressed in Escherichia coli
-
expressiom of GFP-tagged wild-type UCH L1 and mutants in PC12 Tet-off cells and in CHO-AA8-Luc1 cells
-
expression in Escherichia coli as GST-tagged enzyme
-
expression of a catalytically active UCH-L1 in a UCH-L1 negative EBV transformed lymphoblastoid cell line
expression of GST-tagged UCH-L1 in Escherichia coli strain Rosetta BL21(DE3)
expression of GST-tagged wild-type and mutant enzymes in HEK-293 cells
expression of GST-tagged wild-type UCHL1 and mutant S18Y in Escherichia coli strain BL21(Rosetta)
expression of HA-tagged wild-type and mutant enzymes in HEK-293 cells
-
expression of His-tagged wild-type and mutant enzymes
-
expression of UCH-L1 in H1299 cells
-
expression vectors encoding HA epitope-tagged Cezanne (pHM6-Cezanne), GFP-tagged Cezanne (pEGFP-Cezanne) and enzymatically inactive forms mutated at the catalytic cysteine (pHM6-Cezanne C209S and pEGFP-Cezanne C209S). Expressed in HEK293 cells
-
FLAG-HA tagged UCH-3 expressed in HeLa cells
FLAG-tagged UCH-L1 overexpression in the SH-SY5Y human neuroblastoma cell line, which endogenously expresses UCH-L1 and alpha-synuclein, can be cytotoxic at high expression levels in these cells. Coexpression of wild-type UCH-L1, but not of the protective S18Y variant, in COS-7 cells increases levels of transfected alpha-synuclein by inhibiting its degradation, the amount of UCH-L1M in transfected cells correlates with the intracellular level of alpha-synuclein
-
gene rs5030732, genotyping
gene rs5030732, genotyping and UCHL1 polymorphisms, expression analysis, overview
-
gene uch-L1, DNA and amino acid sequence determination and analysis
gene usp21, DNA sequence determination and analysis, located on chromosome 1q21, expression in COS cells, overexpression in U2O2 cells
HEK-293 cells transiently transfected with FLAG (DYKDDDDK)-tagged UCH37 expression construct
-
human UCHL1 and bovine eNOS subcloned into D-TOPO and transferred into the mammalian expression vector pcDNA3.1 or pCAGGS, transfection of plasmid DNA in rat carotid artery
-
into the pcDNA3.1-TOPO vector and expressed in HCT-116 or EC-109 cells
isozyme L1: expression of wild-type and mutants in Escherichia coli DH5alphaPRO as His-tagged proteins
isozymes ISOT-S and ISOT-L, cloning from brain mRNA, expression of both isozyme wild-types and mutant isozyme ISOT-S C335S in Escherichia coli strain MC1061
-
overexpression of wild-type and mutant GST-tagged enzymes in Escherichia coli
overexpression of wild-type and mutant isozymes L1 and L3 in Escherichia coli BL21(DE3)
-
pcDNA3.1-UCH-L1 plasmid overexpressed in MCF7 and MCF7/Adr cells
plasmids containing wild-type UCH-L1 and mutants with or without FLAG tag transiently transfected into Neuro2a, SH-SY5Y or COS-7 cells. NIH-3T3 cells stably expressing human UCH-L1 with a FLAG-HA double tag at the N-terminus. PGEX UCH-L1 vectors transformed into Escherichia coli BL21
-
recombinant UCH37 catalytic domain as N-terminally GST-tagged protein is expressed in Escherichia coli BL21(RIPL)
stable expression of HA-tagged wild-type UCH-L1 in murine NIH-3T3 cells, expression of FLAG-tagged or GFP-tagged wild-type UCH-L1 and mutants D30A and C90S in murine neural progenitor NP cells, the expression level is lower in NP cells derived from gad, i.e. gracile axonal dystrophy, mice compared to NP cells from wild-type mice, overview
-
subcloned from pcDNA-UCH-L1 vector into pGEX-6P-1 vector. The resulting N-terminally fused GST-tagged protein expressed in Escherichia coli Rosetta strain
UBPY, DNA sequence determination and analysis, expression of gene fragment, residues 9-188, fused to GST in a bacterial expression system
UBPY, expression of wild-type enzyme and mutant D786A in NIH 3T3 cells
UCH-L1, UCH-L3
-
UCH-L3 subcloned into a pET28 expression vector bearing an N-terminal histidine tag. Full-length UCH-L3 expressed in Escherichia coli BL21(DE3) cells
Uch37N (amino acids 1-237) expressed from pET21a with a C-terminal 6× histidine tag in Escherichia coli BL21(DE3). HEK293 cells stably expressing Uch37 containing an amino-terminal 2 × HA epitope. Uch37 expressed as a carboxy- or amino-terminal fusion to the Gal4 activation domain or the Gal4 DNA-binding domain. GST-Uch37, GST-Uch37N (1-237), GST-Uch37C (238-329), wild-type 6× His-Flag-Uch37 and mutant C88A subcloned into pBacPAK8 with their respective epitope tags and expressed using the BacPAK baculovirus expression system, expressed in Sf21 insect cells. DNA encoding human Uch37FL, Uch37N (1-237), Adrm1, and the 19S complex subunits S1, S2, S3, S4, S5a, S5b, S6, S6’, S7, S8, S9, S10a, S10b, S11, S12, S13, S14, S15 and p55 subcloned into pGAD or pGBD yeast two-hybrid vectors and transformed into the YRG-2 yeast strain
UCHL1 gene, the gene and its proximal promoter with a classic TATA box 25 bp upstream of a G base determined to be the transcription start site from mRNA 5'-mapping analyses, gene ragulation, detailed overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2'-deoxy-5-azacytidine, DAC, induces UCHL1 expression in renal carcinoma cell lines linked to the demethylation degree of the UCHL1 promoter DNA. Restoration of UCHL1 expression in renal carcinoma cells by treatment with DAC, overview
-
aberrant expression of UCHL1/PGP 9.5 in Schwann cells after nerve transection and even in fibroblasts after skin wounds
-
expression of isoform UCHL1 is elevated in osteosarcoma
promoter hypermethylation represents a mechanism for the silencing of the UCHL1 gene expression in in renal carcinoma cells as a concept of an epigenetic control for the expression of UCHL1 during disease progression. Restoration of UCHL1 expression in renal carcinoma cells by treatment with DAC, overview
-
the enzyme expression is increased in lymph node metastasis associated with poor prognosis in colorectal cancer
-
ubiquitin C-terminal hydrolase UCH-L3 is upregulated in normal or non-metastatic prostate cancer cells and is downregulated in metastatic prostate cancer cell lines
UCHL1 is consistently up-regulated in smokers compared with nonsmokers
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of the apoenzyme with Zn2+ at pH 5.5 under nondenaturing conditions completely restores activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
the proportion of inclusion-bearing cells showing high levels of ubiquitin C-terminal hydrolase may provide a marker of the activity of a degenerative process
degradation
-
a natural dodecapeptide amide from UCH-L3 with the sequence DPDELRFNAIAL is capable of binding to monoubiquitin and may enable the design of peptides with different affinities towards K48- and K63-linked polyubiquitin
diagnostics
drug development
medicine
pharmacology
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wilkinson, K.D.
Ubiquitin C-terminal hydroase
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
660-663
1998
Bos taurus, Drosophila melanogaster, Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Johnston, S.C.; Larsen, C.N.; Cook, W.J.; Wilkinson, K.D.; Hill, C.P.
Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution
EMBO J.
16
3787-3796
1997
Homo sapiens
Manually annotated by BRENDA team
Lowe, J.; McDermott, H.; Landon, M.; Mayer, R.J.; Wilkinson, K.D.
Ubiquitin carboxyl-terminal hydrolase (PGP9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases
J. Pathol.
161
153-160
1990
Homo sapiens
Manually annotated by BRENDA team
Moskovitz, J.
Characterization of the 30-kDa enzyme from red blood cells that cleaves ubiquitin-protein conjugates
Biochem. Biophys. Res. Commun.
205
354-360
1994
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Pickart, C.M.; Rose, I.A.
Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides
J. Biol. Chem.
260
7903-7910
1985
Homo sapiens
Manually annotated by BRENDA team
Larsen, C.N.; Price, J.S.; Wilkinson, K.D.
Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues
Biochemistry
35
6735-6744
1996
Bos taurus, Homo sapiens, Mammalia, Rattus norvegicus
Manually annotated by BRENDA team
Larsen, C.N.; Krantz, B.A.; Wilkinson, K.D.
Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases
Biochemistry
37
3358-3368
1998
Homo sapiens
Manually annotated by BRENDA team
Falquet, L.; Paquet, N.; Frutiger, S.; Hughes, G.J.; Hoang-Van, K.; Jaton, J.C.
A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro
FEBS Lett.
359
73-77
1995
Homo sapiens
Manually annotated by BRENDA team
Naviglio, S.; Mattecucci, C.; Matoskova, B.; Nagase, T.; Nomura, N.; Di Fiore, P.P.; Draetta, G.F.
UBPY: a growth-regulated human ubiquitin isopeptidase
EMBO J.
17
3241-3250
1998
Homo sapiens (P40818), Homo sapiens
Manually annotated by BRENDA team
Gong, L.; Kamitani, T.; Millas, S.; Yeh, E.T.
Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins
J. Biol. Chem.
275
14212-14216
2000
Homo sapiens (Q9UK80), Homo sapiens
Manually annotated by BRENDA team
Mullally, J.E.; Moos, P.J.; Edes, K.; Fitzpatrick, F.A.
Cyclopentenone prostaglandins of the J series inhibit the ubiquitin isopeptidase activity of the proteasome pathway
J. Biol. Chem.
276
30366-30373
2001
Homo sapiens
Manually annotated by BRENDA team
Gabriel, J.M.; Lacombe, T.; Carobbio, S.; Paquet, N.; Bisig, R.; Cox, J.A.; Jaton, J.C.
Zinc is required for the catalytic activity of the human deubiquitinating isopeptidase T
Biochemistry
41
13755-13766
2002
Homo sapiens
Manually annotated by BRENDA team
Nishikawa, K.; Li, H.; Kawamura, R.; Osaka, H.; Wang, Y.L.; Hara, Y.; Hirokawa, T.; Manago, Y.; Amano, T.; Noda, M.; Aoki, S.; Wada, K.
Alterations of structure and hydrolase activity of parkinsonism-associated human ubiquitin carboxyl-terminal hydrolase L1 variants
Biochem. Biophys. Res. Commun.
304
176-183
2003
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Son, O.L.; Kim, H.T.; Ji, M.H.; Yoo, K.W.; Rhee, M.; Kim, C.H.
Cloning and expression analysis of a Parkinson's disease gene, uch-L1, and its promoter in zebrafish
Biochem. Biophys. Res. Commun.
312
601-607
2003
Danio rerio, Danio rerio (Q6YI49), Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Naito, S.; Mochizuki, H.; Yasuda, T.; Mizuno, Y.; Furusaka, M.; Ikeda, S.; Adachi, T.; Shimizu, H.M.; Suzuki, J.; Fujiwara, S.; Okada, T.; Nishikawa, K.; Aoki, S.; Wada, K.
Characterization of multimetric variants of ubiquitin carboxyl-terminal hydrolase L1 in water by small-angle neutron scattering
Biochem. Biophys. Res. Commun.
339
717-725
2006
Homo sapiens
Manually annotated by BRENDA team
Case, A.; Stein, R.L.
Mechanistic studies of ubiquitin C-terminal hydrolase L1
Biochemistry
45
2443-2452
2006
Homo sapiens, Homo sapiens (P09936)
Manually annotated by BRENDA team
Liu, Y.; Lashuel, H.A.; Choi, S.; Xing, X.; Case, A.; Ni, J.; Yeh, L.A.; Cuny, G.D.; Stein, R.L.; Lansbury, P.T., Jr.
Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line
Chem. Biol.
10
837-846
2003
Homo sapiens
Manually annotated by BRENDA team
Choi, J.; Levey, A.I.; Weintraub, S.T.; Rees, H.D.; Gearing, M.; Chin, L.S.; Li, L.
Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
J. Biol. Chem.
279
13256-13264
2004
Homo sapiens, Homo sapiens (P09936)
Manually annotated by BRENDA team
McCullough, J.; Clague, M.J.; Urbe, S.
AMSH is an endosome-associated ubiquitin isopeptidase
J. Cell Biol.
166
487-492
2004
Homo sapiens
Manually annotated by BRENDA team
Sakurai, M.; Ayukawa, K.; Setsuie, R.; Nishikawa, K.; Hara, Y.; Ohashi, H.; Nishimoto, M.; Abe, T.; Kudo, Y.; Sekiguchi, M.; Sato, Y.; Aoki, S.; Noda, M.; Wada, K.
Ubiquitin C-terminal hydrolase L1 regulates the morphology of neural progenitor cells and modulates their differentiation
J. Cell Sci.
119
162-171
2006
Homo sapiens, Mus musculus, Mus musculus (Q9R0P9)
Manually annotated by BRENDA team
Manago, Y.; Kanahori, Y.; Shimada, A.; Sato, A.; Amano, T.; Sato-Sano, Y.; Setsuie, R.; Sakurai, M.; Aoki, S.; Wang, Y.L.; Osaka, H.; Wada, K.; Noda, M.
Potentiation of ATP-induced currents due to the activation of P2X receptors by ubiquitin carboxy-terminal hydrolase L1
J. Neurochem.
92
1061-1072
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Barrachina, M.; Castano, E.; Dalfo, E.; Maes, T.; Buesa, C.; Ferrer, I.
Reduced ubiquitin C-terminal hydrolase-1 expression levels in dementia with Lewy bodies
Neurobiol. Dis.
22
265-273
2006
Homo sapiens
Manually annotated by BRENDA team
Das, C.; Hoang, Q.Q.; Kreinbring, C.A.; Luchansky, S.J.; Meray, R.K.; Ray, S.S.; Lansbury, P.T.; Ringe, D.; Petsko, G.A.
Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1
Proc. Natl. Acad. Sci. USA
103
4675-4680
2006
Homo sapiens (P15374), Homo sapiens
Manually annotated by BRENDA team
Solano, S.M.; Miller, D.W.; Augood, S.J.; Young, A.B.; Penney, J.B.
Expression of alpha-synuclein, parkin, and ubiquitin carboxy-terminal hydrolase L1 mRNA in human brain: genes associated with familial Parkinsons disease
Ann. Neurol.
47
201-210
2000
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Shen, H.; Sikorska, M.; Leblanc, J.; Walker, P.R.; Liu, Q.Y.
Oxidative stress regulated expression of ubiquitin carboxyl-terminal hydrolase-L1: role in cell survival
Apoptosis
11
1049-1059
2006
Homo sapiens, Homo sapiens (P09936)
Manually annotated by BRENDA team
Misaghi, S.; Galardy, P.J.; Meester, W.J.; Ovaa, H.; Ploegh, H.L.; Gaudet, R.
Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate
J. Biol. Chem.
280
1512-1520
2005
Homo sapiens (P15374), Homo sapiens
Manually annotated by BRENDA team
Alexander-Kaufman, K.; James, G.; Sheedy, D.; Harper, C.; Matsumoto, I.
Differential protein expression in the prefrontal white matter of human alcoholics: a proteomics study
Mol. Psychiatry
11
56-65
2006
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Facheris, M.; Strain, K.J.; Lesnick, T.G.; de Andrade, M.; Bower, J.H.; Ahlskog, J.E.; Cunningham, J.M.; Lincoln, S.; Farrer, M.J.; Rocca, W.A.; Maraganore, D.M.
UCHL1 is associated with Parkinsons disease: A case-unaffected sibling and case-unrelated control study
Neurosci. Lett.
381
131-134
2005
Homo sapiens (P09936)
Manually annotated by BRENDA team
Wicks, S.J.; Haros, K.; Maillard, M.; Song, L.; Cohen, R.E.; Dijke, P.T.; Chantry, A.
The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling
Oncogene
24
8080-8084
2005
Homo sapiens (Q9Y5K5), Homo sapiens
Manually annotated by BRENDA team
Hassiepen, U.; Eidhoff, U.; Meder, G.; Bulber, J.F.; Hein, A.; Bodendorf, U.; Lorthiois, E.; Martoglio, B.
A sensitive fluorescence intensity assay for deubiquitinating proteases using ubiquitin-rhodamine110-glycine as substrate
Anal. Biochem.
371
201-207
2007
Homo sapiens
Manually annotated by BRENDA team
Takami, Y.; Nakagami, H.; Morishita, R.; Katsuya, T.; Cui, T.X.; Ichikawa, T.; Saito, Y.; Hayashi, H.; Kikuchi, Y.; Nishikawa, T.; Baba, Y.; Yasuda, O.; Rakugi, H.; Ogihara, T.; Kaneda, Y.
Ubiquitin carboxyl-terminal hydrolase L1, a novel deubiquitinating enzyme in the vasculature, attenuates NF-kappaB activation
Arterioscler. Thromb. Vasc. Biol.
27
2184-2190
2007
Homo sapiens
Manually annotated by BRENDA team
Schweitzer, K.; Decker, E.; Zhu, L.; Miller, R.E.; Mirra, S.S.; Spina, S.; Ghetti, B.; Wang, M.; Murrell, J.
Aberrantly regulated proteins in frontotemporal dementia
Biochem. Biophys. Res. Commun.
348
465-472
2006
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Wicks, S.J.; Grocott, T.; Haros, K.; Maillard, M.; ten Dijke, P.; Chantry, A.
Reversible ubiquitination regulates the Smad/TGF-beta signalling pathway
Biochem. Soc. Trans.
34
761-763
2006
Homo sapiens
Manually annotated by BRENDA team
Hirayama, K.; Aoki, S.; Nishikawa, K.; Matsumoto, T.; Wada, K.
Identification of novel chemical inhibitors for ubiquitin C-terminal hydrolase-L3 by virtual screening
Bioorg. Med. Chem.
15
6810-6818
2007
Homo sapiens
Manually annotated by BRENDA team
Carolan, B.J.; Heguy, A.; Harvey, B.G.; Leopold, P.L.; Ferris, B.; Crystal, R.G.
Up-regulation of expression of the ubiquitin carboxyl-terminal hydrolase L1 gene in human airway epithelium of cigarette smokers
Cancer Res.
66
10729-10740
2006
Homo sapiens
Manually annotated by BRENDA team
Miyoshi, Y.; Nakayama, S.; Torikoshi, Y.; Tanaka, S.; Ishihara, H.; Taguchi, T.; Tamaki, Y.; Noguchi, S.
High expression of ubiquitin carboxy-terminal hydrolase-L1 and -L3 mRNA predicts early recurrence in patients with invasive breast cancer
Cancer Sci.
97
523-529
2006
Homo sapiens
Manually annotated by BRENDA team
Lansbury, P.T.
Improving synaptic function in a mouse model of AD
Cell
126
655-657
2006
Aplysia sp., Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Bifsha, P.; Landry, K.; Ashmarina, L.; Durand, S.; Seyrantepe, V.; Trudel, S.; Quiniou, C.; Chemtob, S.; Xu, Y.; Gravel, R.A.; Sladek, R.; Pshezhetsky, A.V.
Altered gene expression in cells from patients with lysosomal storage disorders suggests impairment of the ubiquitin pathway
Cell Death Differ.
14
511-523
2007
Mus musculus, Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Roth, G.; Freund, S.; Moehrle, B.; Woellner, K.; Bruenjes, J.; Gauglitz, G.; Wiesmueller, K.H.; Jung, G.
Ubiquitin binds to a short peptide segment of hydrolase UCH-L3: a study by FCS, RIfS, ITC and NMR
Chembiochem
8
323-331
2007
Homo sapiens
Manually annotated by BRENDA team
Gong, B.; Leznik, E.
The role of ubiquitin C-terminal hydrolase L1 in neurodegenerative disorders
Drug News Perspect.
20
365-370
2007
Homo sapiens
Manually annotated by BRENDA team
Kabuta, T.; Setsuie, R.; Mitsui, T.; Kinugawa, A.; Sakurai, M.; Aoki, S.; Uchida, K.; Wada, K.
Aberrant molecular properties shared by familial Parkinsons disease-associated mutant UCH-L1 and carbonyl-modified UCH-L1
Hum. Mol. Genet.
17
1482-1496
2008
Homo sapiens
Manually annotated by BRENDA team
Meray, R.K.; Lansbury, P.T.
Reversible monoubiquitination regulates the Parkinson disease-associated ubiquitin hydrolase UCH-L1
J. Biol. Chem.
282
10567-10575
2007
Homo sapiens
Manually annotated by BRENDA team
Toda, T.; Nakamura, M.; Morisawa, H.; Hirota, M.
Proteomic identification of oxidative-stress-reporting biomarkers differentially secreted from human neuroblastoma SH-SY5Y cells
J. Electrophor.
51
21-26
2007
Homo sapiens (P09936)
-
Manually annotated by BRENDA team
Rolen, U.; Kobzeva, V.; Gasparjan, N.; Ovaa, H.; Winberg, G.; Kisseljov, F.; Masucci, M.G.
Activity profiling of deubiquitinating enzymes in cervical carcinoma biopsies and cell lines
Mol. Carcinog.
45
260-269
2006
Homo sapiens
Manually annotated by BRENDA team
Yao, T.; Song, L.; Xu, W.; DeMartino, G.N.; Florens, L.; Swanson, S.K.; Washburn, M.P.; Conaway, R.C.; Conaway, J.W.; Cohen, R.E.
Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1
Nat. Cell Biol.
8
994-1002
2006
Bos taurus (Q9XSJ0), Homo sapiens (Q9Y5K5)
Manually annotated by BRENDA team
Raichur, A.; Vali, S.; Gorin, F.
Dynamic modeling of alpha-synuclein aggregation for the sporadic and genetic forms of Parkinsons disease
Neuroscience
142
859-870
2006
Homo sapiens
Manually annotated by BRENDA team
Carmine Belin, A.; Westerlund, M.; Bergman, O.; Nissbrandt, H.; Lind, C.; Sydow, O.; Galter, D.
S18Y in ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) associated with decreased risk of Parkinsons disease in Sweden
Parkinsonism Relat. Disord.
13
295-298
2007
Homo sapiens
Manually annotated by BRENDA team
Ha, M.K.; Soo Cho, J.; Baik, O.R.; Lee, K.H.; Koo, H.S.; Chung, K.Y.
Caenorhabditis elegans as a screening tool for the endothelial cell-derived putative aging-related proteins detected by proteomic analysis
Proteomics
6
3339-3351
2006
Caenorhabditis elegans, Homo sapiens (P09936), Caenorhabditis elegans N2
Manually annotated by BRENDA team
Drag, M.; Mikolajczyk, J.; Bekes, M.; Reyes-Turcu, F.E.; Ellman, J.A.; Wilkinson, K.D.; Salvesen, G.S.
Positional-scanning fluorigenic substrate libraries reveal unexpected specificity determinants of DUBs (deubiquitinating enzymes)
Biochem. J.
415
367-375
2008
Severe acute respiratory syndrome-related coronavirus, Homo sapiens (P15374), Homo sapiens (P45974), Homo sapiens (Q5VVQ6), Homo sapiens
Manually annotated by BRENDA team
Tanaka, T.; Kuramitsu, Y.; Fujimoto, M.; Naito, S.; Oka, M.; Nakamura, K.
Downregulation of two isoforms of ubiquitin carboxyl-terminal hydrolase isozyme L1 correlates with high metastatic potentials of human SN12C renal cell carcinoma cell clones
Electrophoresis
29
2651-2659
2008
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Yu, J.; Tao, Q.; Cheung, K.F.; Jin, H.; Poon, F.F.; Wang, X.; Li, H.; Cheng, Y.Y.; Roecken, C.; Ebert, M.P.; Chan, A.T.; Sung, J.J.
Epigenetic identification of ubiquitin carboxyl-terminal hydrolase L1 as a functional tumor suppressor and biomarker for hepatocellular carcinoma and other digestive tumors
Hepatology
48
508-518
2008
Homo sapiens (P09936)
Manually annotated by BRENDA team
Wang, W.J.; Li, Q.Q.; Xu, J.D.; Cao, X.X.; Li, H.X.; Tang, F.; Chen, Q.; Yang, J.M.; Xu, Z.D.; Liu, X.P.
Over-expression of ubiquitin carboxy terminal hydrolase-L1 induces apoptosis in breast cancer cells
Int. J. Oncol.
33
1037-1045
2008
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Enesa, K.; Zakkar, M.; Chaudhury, H.; Luong, l.e..A.; Rawlinson, L.; Mason, J.C.; Haskard, D.O.; Dean, J.L.; Evans, P.C.
NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling
J. Biol. Chem.
283
7036-7045
2008
Homo sapiens
Manually annotated by BRENDA team
Rolen, U.; Freda, E.; Xie, J.; Pfirmann, T.; Frisan, T.; Masucci, M.G.
The Ubiquitin C-terminal Hydrolase UCH-L1 regulates B-cell proliferation and integrin activation
J. Cell. Mol. Med.
13
1666-1678
2009
Homo sapiens, Homo sapiens (P09936)
Manually annotated by BRENDA team
Meyer-Schwesinger, C.; Meyer, T.N.; Muenster, S.; Klug, P.; Saleem, M.; Helmchen, U.; Stahl, R.A.
A new role for the neuronal ubiquitin C-terminal hydrolase-L1 (UCH-L1) in podocyte process formation and podocyte injury in human glomerulopathies
J. Pathol.
217
452-464
2009
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Misaghi, S.; Ottosen, S.; Izrael-Tomasevic, A.; Arnott, D.; Lamkanfi, M.; Lee, J.; Liu, J.; ORourke, K.; Dixit, V.M.; Wilson, A.C.
Association of C-terminal ubiquitin hydrolase BAP1 with cell cycle regulator HCF-1
Mol. Cell. Biol.
29
2181-2192
2009
Homo sapiens (Q92560)
Manually annotated by BRENDA team
Yao, T.; Song, L.; Jin, J.; Cai, Y.; Takahashi, H.; Swanson, S.K.; Washburn, M.P.; Florens, L.; Conaway, R.C.; Cohen, R.E.; Conaway, J.W.
Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex
Mol. Cell
31
909-917
2008
Homo sapiens (Q9Y5K5), Homo sapiens
Manually annotated by BRENDA team
Setsuie, R.; Sakurai, M.; Sakaguchi, Y.; Wada, K.
Ubiquitin dimers control the hydrolase activity of UCH-L3
Neurochem. Int.
54
314-321
2009
Homo sapiens (P09936), Homo sapiens (P15374), Mus musculus (Q9JKB1), Mus musculus (Q9R0P9)
Manually annotated by BRENDA team
Kim, H.J.; Kim, Y.M.; Lim, S.; Nam, Y.K.; Jeong, J.; Kim, H.J.; Lee, K.J.
Ubiquitin C-terminal hydrolase-L1 is a key regulator of tumor cell invasion and metastasis
Oncogene
28
117-127
2009
Homo sapiens (P09936)
Manually annotated by BRENDA team
Nishio, K.; Kim, S.W.; Kawai, K.; Mizushima, T.; Yamane, T.; Hamazaki, J.; Murata, S.; Tanaka, K.; Morimoto, Y.
Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5) catalytic domain
Biochem. Biophys. Res. Commun.
390
855-860
2009
Homo sapiens (Q9Y5K5)
Manually annotated by BRENDA team
Fang, Y.; Fu, D.; Shen, X.Z.
The potential role of ubiquitin C-terminal hydrolases in oncogenesis
Biochim. Biophys. Acta
1806
1-6
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Andersson, F.I.; Jackson, S.E.; Hsu, S.T.
Backbone assignments of the 26 kDa neuron-specific ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1)
Biomol. NMR Assign.
4
41-43
2009
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Weber, B.; Schaper, C.; Wang, Y.; Scholz, J.; Bein, B.
Interaction of the ubiquitin carboxyl terminal esterase L1 with alpha(2)-adrenergic receptors inhibits agonist-mediated p44/42 MAP kinase activation
Cell. Signal.
21
1513-1521
2009
Homo sapiens (P09936)
Manually annotated by BRENDA team
Li, L.; Tao, Q.; Jin, H.; van Hasselt, A.; Poon, F.F.; Wang, X.; Zeng, M.S.; Jia, W.H.; Zeng, Y.X.; Chan, A.T.; Cao, Y.
The tumor suppressor UCHL1 forms a complex with p53/MDM2/ARF to promote p53 signaling and is frequently silenced in nasopharyngeal carcinoma
Clin. Cancer Res.
16
2949-2958
2010
Homo sapiens
Manually annotated by BRENDA team
Wu, Y.R.; Chen, C.M.; Chen, Y.C.; Chao, C.Y.; Ro, L.S.; Fung, H.C.; Hsiao, Y.C.; Hu, F.J.; Lee-Chen, G.J.
Ubiquitin specific proteases USP24 and USP40 and ubiquitin thiolesterase UCHL1 polymorphisms have synergic effect on the risk of Parkinsons disease among Taiwanese
Clin. Chim. Acta
411
955-958
2010
Homo sapiens
Manually annotated by BRENDA team
Papa, L.; Akinyi, L.; Liu, M.C.; Pineda, J.A.; Tepas, J.J.; Oli, M.W.; Zheng, W.; Robinson, G.; Robicsek, S.A.; Gabrielli, A.; Heaton, S.C.; Hannay, H.J.; Demery, J.A.; Brophy, G.M.; Layon, J.; Robertson, C.S.; Hayes, R.L.; Wang, K.K.
Ubiquitin C-terminal hydrolase is a novel biomarker in humans for severe traumatic brain injury
Crit. Care Med.
38
138-144
2010
Homo sapiens
Manually annotated by BRENDA team
Henderson, M.J.; Vij, N.; Zeitlin, P.L.
Ubiquitin C-terminal hydrolase-L1 protects cystic fibrosis transmembrane conductance regulator from early stages of proteasomal degradation
J. Biol. Chem.
285
11314-11325
2010
Homo sapiens
Manually annotated by BRENDA team
Kang, X.; Sun, L.; Guo, K.; Shu, H.; Yao, J.; Qin, X.; Liu, Y.
Serum protein biomarkers screening in HCC patients with liver cirrhosis by ICAT-LC-MS/MS
J. Cancer Res. Clin. Oncol.
136
1151-1159
2010
Homo sapiens
Manually annotated by BRENDA team
Ma, Y.; Zhao, M.; Zhong, J.; Shi, L.; Luo, Q.; Liu, J.; Wang, J.; Yuan, X.; Huang, C.
Proteomic profiling of proteins associated with lymph node metastasis in colorectal cancer
J. Cell. Biochem.
110
1512-1519
2010
Homo sapiens
Manually annotated by BRENDA team
Lewis, S.B.; Wolper, R.; Chi, Y.Y.; Miralia, L.; Wang, Y.; Yang, C.; Shaw, G.
Identification and preliminary characterization of ubiquitin C terminal hydrolase 1 (UCHL1) as a biomarker of neuronal loss in aneurysmal subarachnoid hemorrhage
J. Neurosci. Res.
88
1475-1484
2010
Homo sapiens
Manually annotated by BRENDA team
Seliger, B.; Handke, D.; Schabel, E.; Bukur, J.; Lichtenfels, R.; Dammann, R.
Epigenetic control of the ubiquitin carboxyl terminal hydrolase 1 in renal cell carcinoma
J. Transl. Med.
7
90
2009
Homo sapiens
Manually annotated by BRENDA team
Iizuka, N.; Okamoto, K.; Matsushita, R.; Kimura, M.; Nagai, K.; Arito, M.; Kurokawa, M.S.; Masuko, K.; Suematsu, N.; Hirohata, S.; Kato, T.
Identification of autoantigens specific for systemic lupus erythematosus with central nervous system involvement
Lupus
19
717-726
2010
Homo sapiens
Manually annotated by BRENDA team
Zetterberg, M.; Sjoelander, A.; von Otter, M.; Palmer, M.S.; Landgren, S.; Minthon, L.; Wallin, A.; Andreasen, N.; Blennow, K.; Zetterberg, H.
Ubiquitin carboxy-terminal hydrolase L1 (UCHL1) S18Y polymorphism in Alzheimers disease
Mol. Neurodegener.
5
11
2010
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Mitsui, T.; Hirayama, K.; Aoki, S.; Nishikawa, K.; Uchida, K.; Matsumoto, T.; Kabuta, T.; Wada, K.
Identification of a novel chemical potentiator and inhibitors of UCH-L1 by in silico drug screening
Neurochem. Int.
56
679-686
2010
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Bheda, A.; Yue, W.; Gullapalli, A.; Whitehurst, C.; Liu, R.; Pagano, J.S.; Shackelford, J.
Positive reciprocal regulation of ubiquitin C-terminal hydrolase L1 and beta-catenin/TCF signaling
PLoS ONE
4
e5955
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Liu, Z.; Meray, R.K.; Grammatopoulos, T.N.; Fredenburg, R.A.; Cookson, M.R.; Liu, Y.; Logan, T.; Lansbury, P.T.
Membrane-associated farnesylated UCH-L1 promotes alpha-synuclein neurotoxicity and is a therapeutic target for Parkinsons disease
Proc. Natl. Acad. Sci. USA
106
4635-4640
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Koharudin, L.M.; Liu, H.; Di Maio, R.; Kodali, R.B.; Graham, S.H.; Gronenborn, A.M.
Cyclopentenone prostaglandin-induced unfolding and aggregation of the Parkinson disease-associated UCH-L1
Proc. Natl. Acad. Sci. USA
107
6835-6840
2010
Homo sapiens
Manually annotated by BRENDA team
Boudreaux, D.A.; Maiti, T.K.; Davies, C.W.; Das, C.
Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation
Proc. Natl. Acad. Sci. USA
107
9117-9122
2010
Homo sapiens (P09936)
Manually annotated by BRENDA team
Day, I.N.; Thompson, R.J.
UCHL1 (PGP 9.5): neuronal biomarker and ubiquitin system protein
Prog. Neurobiol.
90
327-362
2010
Bos taurus, Homo sapiens, Macaca fuscata, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Seliger, B.; Dressler, S.P.; Wang, E.; Kellner, R.; Recktenwald, C.V.; Lottspeich, F.; Marincola, F.M.; Baumgaertner, M.; Atkins, D.; Lichtenfels, R.
Combined analysis of transcriptome and proteome data as a tool for the identification of candidate biomarkers in renal cell carcinoma
Proteomics
9
1567-1581
2009
Homo sapiens (P09936)
Manually annotated by BRENDA team
Song, H.M.; Lee, J.E.; Kim, J.H.
Ubiquitin C-terminal hydrolase-L3 regulates EMT process and cancer metastasis in prostate cell lines
Biochem. Biophys. Res. Commun.
452
722-727
2014
Homo sapiens (P15374)
Manually annotated by BRENDA team
Navarro, M.F.; Carmody, L.; Romo-Fewell, O.; Lokensgard, M.E.; Love, J.J.
Characterizing substrate selectivity of ubiquitin C-terminal hydrolase-L3 using engineered alpha-linked ubiquitin substrates
Biochemistry
53
8031-8042
2014
Homo sapiens (P15374), Homo sapiens
Manually annotated by BRENDA team
Davies, C.W.; Chaney, J.; Korbel, G.; Ringe, D.; Petsko, G.A.; Ploegh, H.; Das, C.
The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE(OMe)-FMK)
Bioorg. Med. Chem. Lett.
22
3900-3904
2012
Homo sapiens (P09936)
Manually annotated by BRENDA team
Zheng, S.; Qiao, G.; Min, D.; Zhang, Z.; Lin, F.; Yang, Q.; Feng, T.; Tang, L.; Sun, Y.; Zhao, H.; Li, H.; Yu, W.; Yang, Y.; Shen, Z.; Yao, Y.
Heterogeneous expression and biological function of ubiquitin carboxy-terminal hydrolase-L1 in osteosarcoma
Cancer Lett.
359
36-46
2015
Homo sapiens (P09936)
Manually annotated by BRENDA team
Pang, L.; Wu, Y.; Dong, N.; Xu, D.H.; Wang, D.W.; Wang, Z.H.; Li, X.L.; Bian, M.; Zhao, H.J.; Liu, X.L.; Zhang, N.
Elevated serum ubiquitin C-terminal hydrolase-L1 levels in patients with carbon monoxide poisoning
Clin. Biochem.
47
72-76
2014
Homo sapiens
Manually annotated by BRENDA team
Chipumuro, E.; Henriksen, M.
The ubiquitin hydrolase USP22 contributes to 3'-end processing of JAK-STAT-inducible genes
FASEB J.
26
842-854
2012
Homo sapiens
Manually annotated by BRENDA team
Boudreaux, D.A.; Chaney, J.; Maiti, T.K.; Das, C.
Contribution of active site glutamine to rate enhancement in ubiquitin C-terminal hydrolases
FEBS J.
279
1106-1118
2012
Homo sapiens (P09936), Homo sapiens (P15374), Homo sapiens (Q9Y5K5)
Manually annotated by BRENDA team
Wulfaenger, J.; Biehl, K.; Tetzner, A.; Wild, P.; Ikenberg, K.; Meyer, S.; Seliger, B.
Heterogeneous expression and functional relevance of the ubiquitin carboxyl-terminal hydrolase L1 in melanoma
Int. J. Cancer
133
2522-2532
2013
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Kabuta, T.; Mitsui, T.; Takahashi, M.; Fujiwara, Y.; Kabuta, C.; Konya, C.; Tsuchiya, Y.; Hatanaka, Y.; Uchida, K.; Hohjoh, H.; Wada, K.
Ubiquitin C-terminal hydrolase L1 (UCH-L1) acts as a novel potentiator of cyclin-dependent kinases to enhance cell proliferation independently of its hydrolase activity
J. Biol. Chem.
288
12615-12626
2013
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Bishop, P.; Rubin, P.; Thomson, A.R.; Rocca, D.; Henley, J.M.
The ubiquitin C-terminal hydrolase L1 (UCH-L1) C terminus plays a key role in protein stability, but its farnesylation is not required for membrane association in primary neurons
J. Biol. Chem.
289
36140-36149
2014
Homo sapiens (P09936)
Manually annotated by BRENDA team
Diaz-Arrastia, R.; Wang, K.K.; Papa, L.; Sorani, M.D.; Yue, J.K.; Puccio, A.M.; McMahon, P.J.; Inoue, T.; Yuh, E.L.; Lingsma, H.F.; Maas, A.I.; Valadka, A.B.; Okonkwo, D.O.; Manley, G.T.; Manley, G.T.
Acute biomarkers of traumatic brain injury: relationship between plasma levels of ubiquitin C-terminal hydrolase-L1 and glial fibrillary acidic protein
J. Neurotrauma
31
19-25
2014
Homo sapiens
Manually annotated by BRENDA team
Song, I.K.; Kim, H.J.; Magesh, V.; Lee, K.J.
Ubiquitin C-terminal hydrolase-L1 plays a key role in angiogenesis by regulating hydrogen peroxide generated by NADPH oxidase 4
Biochem. Biophys. Res. Commun.
495
1567-1572
2018
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Bishop, P.; Rocca, D.; Henley, J.M.
Ubiquitin C-terminal hydrolase L1 (UCH-L1) structure, distribution and roles in brain function and dysfunction
Biochem. J.
473
2453-2462
2016
Homo sapiens (P09936), Mus musculus (Q9R0P9)
Manually annotated by BRENDA team
Kang, S.J.; Kim, J.S.; Park, S.M.
Ubiquitin C-terminal hydrolase L1 regulates lipid raft-dependent endocytosis
Exp. Neurobiol.
27
377-386
2018
Homo sapiens (P09936)
Manually annotated by BRENDA team
Wang, W.; Zou, L.; Zhou, D.; Zhou, Z.; Tang, F.; Xu, Z.; Liu, X.
Overexpression of ubiquitin carboxyl terminal hydrolase-L1 enhances multidrug resistance and invasion/metastasis in breast cancer by activating the MAPK/Erk signaling pathway
Mol. Carcinog.
55
1329-1342
2016
Homo sapiens (P09936)
Manually annotated by BRENDA team
Toliczenko-Bernatowicz, D.; Matuszczak, E.; Tylicka, M.; Szymanska, B.; Komarowska, M.; Gorodkiewicz, E.; Debek, W.; Hermanowicz, A.
Overexpression of ubiquitin carboxyl-terminal hydrolase 1 (UCHL1) in boys with cryptorchidism
PLoS ONE
13
e0191806
2018
Homo sapiens (P09936), Homo sapiens
Manually annotated by BRENDA team
Nan, L.; Jacko, A.M.; Tan, J.; Wang, D.; Zhao, J.; Kass, D.J.; Ma, H.; Zhao, Y.
Ubiquitin carboxyl-terminal hydrolase-L5 promotes TGFbeta-1 signaling by de-ubiquitinating and stabilizing Smad2/Smad3 in pulmonary fibrosis
Sci. Rep.
6
33116
2016
Homo sapiens (Q9Y5K5), Homo sapiens
Manually annotated by BRENDA team
Sivakumar, D.; Stein, M.
Binding of SARS-CoV covalent non-covalent inhibitors to the SARS-CoV-2 papain-like protease and ovarian tumor domain deubiquitinases
Biomolecules
11
802
2021
Homo sapiens (Q96DC9), Homo sapiens (Q96FW1)
Manually annotated by BRENDA team