Protein tyrosine phosphatase
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Protein tyrosine phosphatases (PTPs) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins.
Contents |
Functions
Together with tyrosine kinases, PTPs regulate the phosphorylation state of many important signalling molecules, such as the MAP kinase family.
PTPs are increasingly viewed as integral components of signal transduction cascades, despite little studied and ill-understood compared to Tyrosine Kinases.
PTPs have been implicated in regulation of many cellular processes, including, but not limited to:
- Cell growth
- Cellular differentiation
- Mitotic cycles
- Oncogenic transformation
Genes
- receptor type: PTPRA, PTPRB, PTPRC, PTPRD, PTPRE, PTPRF, PTPRG, PTPRH, PTPRJ, PTPRK, PTPRM, PTPRN, PTPRN2, PTPRO, PTPRQ, PTPRR, PTPRS, PTPRT, PTPRU, PTPRZ1, PTPRZ2
- non-receptor type: PTPN1, PTPN2, PTPN3, PTPN4, PTPN5, PTPN6, PTPN7, PTPN9, PTPN11, PTPN12, PTPN13, PTPN14, PTPN18, PTPN20A, PTPN20B, PTPN20C, PTPN21, PTPN22, PTPN23
- type IVA: PTP4A1, PTP4A2, PTP4A3
- mitochondrial: PTPMT1
See also
External links
- PTP Summary and Relevant Publications at Monash University
- MeSH Protein-Tyrosine-Phosphatase
- EC 3.1.3.48
References
- Alberts, Bruce; Alexander Johnson Julian Lewis Martin Raff Keith Roberts Peter Walter (2002). Molecular Biology of the Cell Fourth Edition. NYC, NY: Farland Science. ISBN 0-8153-3218-1. pp 886-887.
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