Protein tyrosine phosphatase

Protein tyrosine phosphatases (EC 3.1.3.48, systematic name protein-tyrosine-phosphate phosphohydrolase) are a group of

PTPs have been implicated in regulation of many cellular processes, including, but not limited to:

• Cell growth
• Cellular differentiation
• Mitotic cycles
• Oncogenic transformation
• Receptor endocytosis^[5]

PTP activity can be found in four protein families.[6]^[7]

Links to all 107 members of the protein tyrosine phosphatase family can be found in the template at the bottom of this article.

Class I

The class I PTPs, are the largest group of PTPs with 99 members, which can be further subdivided into

• 38 classical PTPs
  • 21 receptor tyrosine phosphatases
  • 17 nonreceptor-type PTPs
• 61 VH-1-like or dual-specific phosphatases (DSPs)
  • 11 MAPK phosphatases (MPKs)
  • 3 Slingshots
  • 3 PRLs
  • 4 CDC14s
  • 19 atypical DSPs
  • 5 phosphatase and tensin homologs (PTENs)
  • 16 myotubularins

Dual-specificity phosphatases (dTyr and dSer/dThr) dual-specificity protein-tyrosine phosphatases. 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 the action of a kinase. Dual-specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle.

Cdc25 phosphatases (dTyr and/or dThr)

The Class III PTPs contains three members, CDC25 A, B, and C

Class IV

These are members of the

• Receptor-like, which are
  immunoglobulin-like domains, MAM domains, or carbonic anhydrase
  -like domains in their extracellular region. In general, the cytoplasmic region contains two copies of the PTPase domain. The first seems to have enzymatic activity, whereas the second is inactive.
• Non-receptor (intracellular) PTPases[22]

Common elements

All PTPases, other than those of the EYA family, carry the highly conserved active site

Functional diversity between PTPases is endowed by regulatory domains and subunits.

Low-molecular-weight phosphotyrosine protein phosphatase SCOP2 1phr / SCOPe / SUPFAM CDD cd00115 Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB 1bvh​, 1c0e​, 1d1p​, 1d1q​, 1d2a​, 1dg9​, 1jf8​, 1jfv​, 1jl3​, 1ljl​

Protein-tyrosine phosphatase SCOP2 1ypt / SCOPe / SUPFAM CDD cd00047 Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB 1a5y​, 1aax​, 1bzc​, 1bzh​, 1bzj​, 1c83​, 1c84​, 1c85​, 1c86​, 1c87​

Dual-specificity phosphatase, catalytic domain SCOP2 1vhr / SCOPe / SUPFAM CDD cd14498 Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB 1d5r​, 1i9s​, 1i9t​, 1j4x​, 1m3g​, 1mkp​, 1ohc​, 1ohd​, 1ohe​, 2c46​

Protein-tyrosine phosphatase, SIW14-like Structure of a putative phosphoprotein phosphatase from Arabidopsis thaliana.[27] Identifiers Symbol Y_phosphatase2 Pfam PF03162 Pfam clan CL0031 InterPro IPR004861 CDD cd14528 Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB 1xri​, 2q47​

Protein-tyrosine phosphatase-like, PTPLA Identifiers Symbol PTPLA Pfam PF04387 InterPro IPR007482 Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Expression pattern

Individual PTPs may be