Search by BoMiProt ID - Bomi10225


Primary Information

BoMiProt ID Bomi10225
Protein Name Ubiquitin carboxyl-terminal hydrolase isozyme L1/UCH-L1/Neuron cytoplasmic protein 9.5/PGP 9.5/Ubiquitin thioesterase L1
Organism Bos taurus
Uniprot IdP23356
Milk FractionWhey
Ref Sequence Id NP_001039637.1
Aminoacid Length 252
Molecular Weight 28335
Fasta Sequence https://www.uniprot.org/uniprot/P23356.fasta
Gene Name UCHL1
Gene Id 514394
Protein Existence Status reviewed

Secondary Information

Protein Function deubiquitinating enzyme,plays a role in maintenance of muscle oxidative metabolism.is largely expressed in neuron, comprising almost 1–5% of total brain protein and its absence in mice due to intragenic deletions produces neurodegenerative phenotypes.
Biochemical Properties Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin
PTMs Phosphorylation on Ser,Prenylation,Glycosylation,Lipidation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P23356|UCHL1_BOVIN Ubiquitin carboxyl-terminal hydrolase isozyme L1 OS=Bos taurus OX=9913 GN=UCHL1 PE=1 SV=2 MQLKPMEINPEMLNKVLTRLGVAGQWRFEDVLGLEEESLGSVPAPACALLLLFPLTAQRC FKLGREAASRFHHPDYPGRLFILLVSQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCG TIGLIHAVANNQDKLEFEDGSVLKQFLSETEKLS*154PEDRAKCFEKNEAIQAAHDAVAQEGQ CRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGTSSEDSLLQDAAKVCREFTEREQGE VRFSAVALCKAA
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs UCHL1 undergoes S-nitrosylation.The preferential nitrosylation in the Cys 90, Cys 152 and Cys 220 has been observed which alters the catalytic activity and structural stability.S-nitrosylation of UCHL1 disrupts its deubiquitinase activity and structural fold which eventually produces amorphous protein aggregates.UCH-L1 is post-translationally modified by monoubiquitin in cells, at lysine residues near the active site. This modification restricts enzyme activity by preventing binding to ubiquitinated targets.UCH-L1 catalyzes its own deubiquitination in an intramolecular manner, thereby regulating the lifetime of this modification.
Bibliography Meray RK, Lansbury PT Jr. Reversible monoubiquitination regulates the Parkinson disease-associated ubiquitin hydrolase UCH-L1. J Biol Chem. 2007 Apr 6;282(14):10567-75. doi: 10.1074/jbc.M611153200. Epub 2007 Jan 26. PMID: 17259170.