Literature summary for 3.1.3.67 extracted from

Chen, Z.; Dempsey, D.R.; Thomas, S.N.; Hayward, D.; Bolduc, D.M.; Cole, P.A.
Molecular features of phosphatase and tensin homolog (PTEN) regulation by C-terminal phosphorylation (2016), J. Biol. Chem., 291, 14160-14169 .

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Cloned(Commentary)

Cloned (Comment)	Organism
fusion of a C-terminal truncated PTEN (amino acids 1-378) to Mycobacterium xenopi GyrA intein, and chitin-binding domain	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P60484	cf. EC 3.1.3.16, EC 3.1.3.48, EC 3.1.3.67	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	insertion of stoichiometric and site-specific phospho-Ser/Thr residues in the C-terminal tail of PTEN. No single phospho-modification of the Ser/Thr C-terminal cluster is dominant and each is partially additive in antagonizing catalysis. Conformational closure is influenced by the aggregate effect of multiple phospho-sites rather than dominated by a single phosphorylation site	Homo sapiens

Subunits

Subunits	Comment	Organism
More	the PTEN C-tail and a segment in the N-terminal region of the catalytic domain directly interact	Homo sapiens

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Release 2023.1 (January 2023)