Any feedback?
Information on EC 3.4.19.12 - ubiquitinyl hydrolase 1 and Organism(s) Rattus norvegicus and UniProt Accession Q00981
for references in articles please use BRENDA:EC3.4.19.12Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.19.12 ubiquitinyl hydrolase 1Specify your search results
Word Map
- 3.4.19.12
- nerve
- proteasome
- neurodegenerative
- fiber
-
innervation
-
deubiquitinase
-
polyglutamine
- ataxia
- parkinsonism
- spinocerebellar
-
ubiquitin-proteasome
-
polyubiquitinated
- glial
- sars-cov-2
- coronavirus
- covid-19
- calcitonin
- neurofilament
-
fibrillary
-
neuropeptide
-
neuron-specific
-
traumatic
-
gene-related
- cyld
- parkin
-
polyq
-
synaptophysin
-
ubiquitin-like
- polyproteins
- usp7
-
ubiquitin-dependent
- alpha-synuclein
-
deubiquitylating
- npy
-
myenteric
- 3clpro
-
monoubiquitination
- nedd8
-
cd45ro
- isg15
-
intraepidermal
-
k48-linked
- spermatogonial
-
mono-ubiquitinated
-
ubiquitin-binding
-
3c-like
- mers-cov
- medicine
-
isopeptide
- degradation
- synthesis
- diagnostics
-
anti-sars-cov-2
- molecular biology
- analysis
- concussion
- pharmacology
- drug development
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AD-019
-
-
-
-
CGI-70
-
-
-
-
esterase, ubiquitin thiol-
-
-
-
-
hydrolase, ubiquitin carboxyl-terminal
-
-
-
-
hydrolase, ubiquitin carboxyl-terminal (Aplysia californica gene Ap-uch)
-
-
-
-
isopeptidase
-
-
-
-
isopeptidase T
-
-
-
-
Neuron cytoplasmic protein 9.5
-
-
-
-
PGP 9.5
PGP9.5
-
-
-
-
ubiquitin C-terminal hydrolase
-
-
-
-
ubiquitin C-terminal hydrolase (Aplysia californica gene Ap-uch)
-
-
-
-
Ubiquitin C-terminal hydrolase UCH37
-
-
-
-
ubiquitin carboxy-terminal hydrolase
-
-
-
-
ubiquitin carboxyl-terminal hydrolase
Ubiquitin thiolesterase
-
-
-
-
Ubiquitin thiolesterase L1
-
-
-
-
Ubiquitin thiolesterase L3
-
-
-
-
Ubiquitin thiolesterase L4
-
-
-
-
Ubiquitin thiolesterase L5
-
-
-
-
ubiquitin-carboxyl-terminal hydrolase PGP-9.5
-
-
-
-
UCH-1
-
-
-
-
UCH-L1
UCH-L2
-
-
-
-
UCH-L3
-
-
-
-
UCH-L4
-
-
-
-
UCH-L5
-
-
-
-
yeast ubiquitin hydrolase
-
-
-
-
YUH1
-
-
-
-
additional information
PGP 9.5
-
-
-
-
ubiquitin carboxyl-terminal hydrolase
-
-
-
-
UCH-L1
-
-
-
-
additional information
-
peptidase classification: clan CA, family C12, Merops ID: C12.001
additional information
-
UCH-L1 belongs to a family of de-ubiquitinating enzymes, comprising of UCH-L1-5
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
189642-63-5
-
86480-67-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ubiquitinyl-peptide + H2O
ubiquitin + peptide
-
catalyses the hydrolysis of an ester or amide bond involving the C-terminal Gly76 of ubiquitin
-
-
?
additional information
?
-
-
de novo synthesis of isozyme UCH-L1 in rostral ventrolateral medulla is crucial to survival during mevinphos intoxication, the enzyme is involved in synthesis of ubiquitin which is required for protein targeting in degradation in the ubiquitin-proteasome pathway in neurons, UCH-L1 plays a neuroprotective role
-
-
?
additional information
?
-
de novo synthesis of isozyme UCH-L1 in rostral ventrolateral medulla is crucial to survival during mevinphos intoxication, the enzyme is involved in synthesis of ubiquitin which is required for protein targeting in degradation in the ubiquitin-proteasome pathway in neurons, UCH-L1 plays a neuroprotective role
-
-
?
additional information
?
-
-
overexpression of UCH L1 potentiates ATP-induced currents due to the activation of P2X receptors that are widely distributed in the brain and involved in various biological activities including neurosecretion. UCH-L1 may play an important role in synaptic activity
-
-
?
additional information
?
-
-
UCHL1 can act as a ubiquitin hydrolase, and generate free ubiquitin species from precursor ubiquitin polypeptides. Synaptic activation of UCH-L1 is correlated with an increase in the levels of free monomeric ubiquitin
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
de novo synthesis of isozyme UCH-L1 in rostral ventrolateral medulla is crucial to survival during mevinphos intoxication, the enzyme is involved in synthesis of ubiquitin which is required for protein targeting in degradation in the ubiquitin-proteasome pathway in neurons, UCH-L1 plays a neuroprotective role
-
-
?
additional information
?
-
de novo synthesis of isozyme UCH-L1 in rostral ventrolateral medulla is crucial to survival during mevinphos intoxication, the enzyme is involved in synthesis of ubiquitin which is required for protein targeting in degradation in the ubiquitin-proteasome pathway in neurons, UCH-L1 plays a neuroprotective role
-
-
?
additional information
?
-
-
overexpression of UCH L1 potentiates ATP-induced currents due to the activation of P2X receptors that are widely distributed in the brain and involved in various biological activities including neurosecretion. UCH-L1 may play an important role in synaptic activity
-
-
?
additional information
?
-
-
UCHL1 can act as a ubiquitin hydrolase, and generate free ubiquitin species from precursor ubiquitin polypeptides. Synaptic activation of UCH-L1 is correlated with an increase in the levels of free monomeric ubiquitin
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
LDN-57444
-
i.e. 3-(O-acetyloxime), 5-chloro-1-[(2,5-dichlorophenyl)methyl]-1H-indole-2,3-dione
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
active-site thiol is very sensitive to oxidation and requires reductants
DTT
-
active-site thiol is very sensitive to oxidation and requires reductants
additional information
-
UCH-L1 activity is regulated by synaptic activity. Stimulation of synaptic activity by NMDA/glycine significantly up-regulates UCH-L1 activity in cultured neurons. NMDA-induced up-regulation of UCH-L1 activity is efficiently blocked by pre-treatment of neurons with the NMDA receptor antagonist D-2-amino-5-phosphonopentanoic acid
-
additional information
-
UCH-L1 is significantly elevated in cerebrospinal fluid following controlled cortical impact and middle cerebral artery occlusion, as a model of ischemic stroke, in rats, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
vascular smooth muscle cells. UCH-L1 is up-regulated in injured arteries
de novo synthesis of UCH-L1, leading to an enhanced dissassembly of ubiquitin-protein conjugates in the rostral ventrolateral medulla, is essential to maintenance of the pro-life phase of mevinphos intoxication via prevention of cardiovascular depression, leading to neuroprotection
-
UCH-L1 is significantly elevated in cerebrospinal fluid following controlled cortical impact and middle cerebral artery occlusion, as a model of ischemic stroke, in rats, overview
-
parietal epithelial cells of Bowman's capsules and some tubular epithelia in the kidney
-
parietal epithelial cells of Bowman's capsules and some tubular epithelia in the kidney
rostral ventrolateral, expression analysis of isozyme UCH-L1 during mevinphos intoxication, overview
-
the olfactory receptor neurones (replaceable) appear to be strongly immunoreactive as do the principal neurones (mitral and mitral/tufted cells), while in the olfactory bulb the replaceable periglomerular and granule cells appear to be non-reactive, distribution in cellular compartments, overview
-
cell culture, expression of UCH-L1 and the regulation of this expression in podocytes, overview
-
UCHL1/PGP 9.5, 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
additional information
-
high content of UCHL1, distribution in neuron types and cellular compartments, overview
additional information
-
tissue distribution and immunohistochemic analysis, overview
additional information
-
UCH-L1 expression in podocytes is significantly higher in acute proliferative glomerulonephritis, lupus nephritis, membranous glomerulonephritis, and IgA nephropathy than that in focal segmental glomerulosclerosis, minimal change disease, minor abnormality and normal kidney tissues, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
USP19 stabilizes the ubiquitin ligase KPC1 and, like KPC1, it is localized in the cytosol
additional information
-
UCHL1 expression is detected in both soma and dendrites of hippocampal neurons. UCH-L1 is distributed in a micropunctate fashion, localized to dendritic spines of neurons, and partially co-localized with PSD-95, overview
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
UCH-L1 is up-regulated in injured arteries, via posttranscriptional regulation, and local gene delivery of UCH-L1 inhibited vascular lesion formation with suppression of inflammatory responses in vasculature. ERK activation also contributes to the growth inhibitory effect of UCH-L1 in TNFalpha-inflamed vascular smooth muscle cells
physiological function
UCH-L1 appears to be a multi-functional protein and exerts cell type and/or tissue specific actions
malfunction
-
altered UCH-L1 activity leads to deleterious effects on synapse structure and function. Inhibition of UCH-L1 activity affects synaptic protein clusters
physiological function
physiological function
-
UCH-L1 is one of the major de-ubiquitinating enzymes in the brain which controls ubiquitin homeostasis. UCH-L1 function is required for synaptic plasticity and is itself regulated by synaptic activity. UCH-L1 activity is required for NMDA-induced up-regulation of free monomeric ubiquitin. UCH-L1 can also bind to ubiquitin and act as a ubiquitin stabilizer to prevent its degradation by lysosomes. UCH-L1 regulates spine morphology and density
physiological function
-
UCHL1/PGP 9.5 is important in the ubiquitin system, detailed overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UCHL1_RAT
223
0
24838
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C545A
catalytically inactive USP19 mutant, destabilizes ubiquitin ligase KPC1
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
peroxiredoxin II specifically binds to the near-native intermediates (early-unfolding intermediates) of ubiquitin C-terminal hydrolase-L1 to maintain its native state and activity against various stresses rather than preventing deleterious protein aggregation through quaternary structural changes
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Flag-USP19 transfected into FR3T3 cells. 293VSV cells transfected with pLXSN plasmid encoding N-terminally Flag3-tagged USP19
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
TNFalpha up-regulates UCH-L1via a translational regulation to inhibit ERK activity, thereby providing a negative feedback to control its growth promoting signaling in vascular smooth muscle cells
UCH-L1 expression is significantly decreased in middle cerebral artery occlusion, MCAO, rats
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
UCH-L1 is a biomarker for ischemic and traumatic brain injury in rats
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
-
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
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
Chang, C.; Chang, A.Y.W.; Chan, S.H.H.
De novo synthesis of ubiquitin carboxyl-terminal hydrolase isozyme L1 in rostral ventrolateral medulla is crucial to survival during mevinphos intoxication
Shock
22
575-581
2004
Rattus norvegicus, Rattus norvegicus (Q00981)
Lu, Y.; Adegoke, O.A.; Nepveu, A.; Nakayama, K.I.; Bedard, N.; Cheng, D.; Peng, J.; Wing, S.S.
USP19 deubiquitinating enzyme supports cell proliferation by stabilizing KPC1, a ubiquitin ligase for p27Kip1
Mol. Cell. Biol.
29
547-558
2009
Mus musculus (Q3UJD6), Rattus norvegicus (Q6J1Y9)
Ichikawa, T.; Li, J.; Dong, X.; Potts, J.D.; Tang, D.Q.; Li, D.S.; Cui, T.
Ubiquitin carboxyl terminal hydrolase L1 negatively regulates TNFalpha-mediated vascular smooth muscle cell proliferation via suppressing ERK activation
Biochem. Biophys. Res. Commun.
391
852-856
2010
Rattus norvegicus (Q00981)
Liu, M.C.; Akinyi, L.; Scharf, D.; Mo, J.; Larner, S.F.; Muller, U.; Oli, M.W.; Zheng, W.; Kobeissy, F.; Papa, L.; Lu, X.C.; Dave, J.R.; Tortella, F.C.; Hayes, R.L.; Wang, K.K.
Ubiquitin C-terminal hydrolase-L1 as a biomarker for ischemic and traumatic brain injury in rats
Eur. J. Neurosci.
31
722-732
2010
Rattus norvegicus
Cartier, A.E.; Djakovic, S.N.; Salehi, A.; Wilson, S.M.; Masliah, E.; Patrick, G.N.
Regulation of synaptic structure by ubiquitin C-terminal hydrolase L1
J. Neurosci.
29
7857-7868
2009
Rattus norvegicus
Liu, Y.; Wu, J.; Wu, H.; Wang, T.; Gan, H.; Zhang, X.; Liu, Y.; Li, R.; Zhao, Z.; Chen, Q.; Guo, M.; Zhang, Z.
UCH-L1 expression of podocytes in diseased glomeruli and in vitro
J. Pathol.
217
642-653
2009
Rattus norvegicus
Koh, P.O.
Proteomic analysis of focal cerebral ischemic injury in male rats
J. Vet. Med. Sci.
72
181-185
2010
Rattus norvegicus
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
Lee, S.P.; Park, C.M.; Kim, K.S.; Kim, E.; Jeong, M.; Shin, J.Y.; Yun, C.H.; Kim, K.; Chock, P.B.; Chae, H.Z.
Structural and biochemical analyses reveal ubiquitin C-terminal hydrolase-L1 as a specific client of the peroxiredoxin II chaperone
Arch. Biochem. Biophys.
640
61-74
2018
Rattus norvegicus (Q00981)
EXTERNAL LINKS (specific for EC-Number 3.4.19.12)
Transporter Classification Database (TCDB): 3.A.31.1.1, 3.A.16.1.2
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
