Primary Information |
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| BoMiProt ID | Bomi10225 |
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| Protein Name | Ubiquitin carboxyl-terminal hydrolase isozyme L1/UCH-L1/Neuron cytoplasmic protein 9.5/PGP 9.5/Ubiquitin thioesterase L1 |
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| Organism | Bos taurus |
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| Uniprot ID | P23356 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001039637.1 |
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| Aminoacid Length | 252 |
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| Molecular Weight | 28335 |
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| FASTA Sequence |
Download |
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| Gene Name | UCHL1 |
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| Gene ID | 514394 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| 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. |
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| Biochemical Properties | Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin |
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| PTMs | Phosphorylation on Ser,Prenylation,Glycosylation,Lipidation |
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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
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| 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. |
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| 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. |
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