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Ser/Thr and Tyr dual-specificity phosphatases are a group of enzymes with both Ser/Thr (EC 3.1.3.16) and tyrosine-specific protein phosphatase (EC 3.1.3.48) activity able to remove the serine/threonine or the tyrosine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under ...
Protein tyrosine phosphatase type IVA 2 is an enzyme that in humans is encoded by the PTP4A2 gene. [5] [6] [7] The protein encoded by this gene belongs to a small class of the protein tyrosine phosphatase (PTP) family. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes.
Tyrosine-protein phosphatase non-receptor type 1 also known as protein-tyrosine phosphatase 1B (PTP1B) is an enzyme that is the founding member of the protein tyrosine phosphatase (PTP) family. In humans it is encoded by the PTPN1 gene . [ 5 ]
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation.
The protein encoded by this gene is a member of the receptor tyrosine phosphatases (RTP), a family of protein tyrosine phosphatases.RTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation.
Receptor-type tyrosine-protein phosphatase S, also known as R-PTP-S, R-PTP-sigma, or PTPσ, is an enzyme that in humans is encoded by the PTPRS gene. [ 5 ] [ 6 ] [ 7 ] Function
Protein tyrosine phosphatase type IVA 1 is an enzyme that in humans is encoded by the PTP4A1 gene. [ 4 ] [ 5 ] The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs), which contains a PTP domain and a characteristic C-terminal prenylation motif.
Four alternatively spliced transcript variants, which encode distinct proteins, have been reported. [7]Examination of mouse full-length cDNA sequences for alternatively spliced phosphatase genes identified two novel forms of PTPRU predicted to result in two PCP-2 splice variants: a tethered variant of PCP-2, expressing an intact extracellular and transmembrane domain, and a PCP-2 variant that ...