Literature summary for 3.4.19.12 extracted from

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 (2014), J. Biol. Chem., 289, 36140-36149.

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Protein Variants

Protein Variants	Comment	Organism
additional information	C-terminal deletion of the final four Rrsidues of isoform UCH-L1 (CKAA) leads to increased membrane association and decreased solubility. Deletion disrupts the protein secondary structure, leads to abrogation of substrate binding, increased cell death, and an abnormal intracellular distribution	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
additional information	isoform UCHL1 is differently processed in neurons compared with clonal cell lines and farnesylation does not account for the membrane association in neurons	Homo sapiens	-	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P09936	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
HEK-293T cell	isoform UCH-L1 does not partition to the membrane in the cultured cell lines tested	Homo sapiens	-
Neuro-2a cell	isoform UCH-L1 does not partition to the membrane in the cultured cell lines tested	Homo sapiens	-
neuron	isoform UCHL1 is differently processed in neurons compared with clonal cell lines. In primary cultured neurons, a proportion of UCH-L1M does partition to the membrane, but this does not require farnesylation	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
UCH-L1	-	Homo sapiens

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Release 2023.1 (January 2023)