Type |
Details |
Score |
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
323
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
104
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
281
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
323
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Chao Y |
Year: |
2006 |
Journal: |
Mol Cell |
Title: |
Structure and mechanism of the phosphotyrosyl phosphatase activator. |
Volume: |
23 |
Issue: |
4 |
Pages: |
535-46 |
|
•
•
•
•
•
|
Publication |
First Author: |
Leulliot N |
Year: |
2006 |
Journal: |
Mol Cell |
Title: |
Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity. |
Volume: |
23 |
Issue: |
3 |
Pages: |
413-24 |
|
•
•
•
•
•
|
Publication |
First Author: |
Magnusdottir A |
Year: |
2006 |
Journal: |
J Biol Chem |
Title: |
The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions. |
Volume: |
281 |
Issue: |
32 |
Pages: |
22434-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jordens J |
Year: |
2006 |
Journal: |
J Biol Chem |
Title: |
The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/trans-isomerase. |
Volume: |
281 |
Issue: |
10 |
Pages: |
6349-57 |
|
•
•
•
•
•
|
Publication |
First Author: |
Janssens V |
Year: |
2001 |
Journal: |
Biochem J |
Title: |
Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. |
Volume: |
353 |
Issue: |
Pt 3 |
Pages: |
417-39 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
829
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
794
 |
Fragment?: |
false |
|
•
•
•
•
•
|
DO Term |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Homologous_superfamily |
Description: |
Phosphotyrosyl phosphatase activator (PTPA, also known as protein phosphatase 2A activator) proteins stimulate the phosphotyrosyl phosphatase (PTPase) activity of the dimeric form of protein phosphatase 2A (PP2A). PTPase activity in PP2A (in vitro) is relatively low when compared to the better recognised phosphoserine/ threonine protein phosphorylase activity. It also reactivates the serine/threonine phosphatase activity of an inactive form of PP2A. The specific biological role of PTPA is unknown. PTPA has been suggested to play a role in the insertion of metals to the PP2A catalytic subunit (PP2Ac) active site, to act as a chaperone, and more recently, to have peptidyl prolyl cis/trans isomerase activity that specifically targets human PP2Ac [, , , , , ]. Together, PTPA and PP2A constitute an ATPase and it has been suggested that PTPA alters the relative specificity of PP2A from phosphoserine/phosphothreonine substrates to phosphotyrosine substrates in an ATP-hydrolysis-dependent manner. Basal expression of PTPA depends on the activity of a ubiquitous transcription factor, Yin Yang 1 (YY1). The tumour suppressor protein p53 can inhibit PTPA expression through an unknown mechanism that negatively controls YY1 [].PTPA is an α-helical protein which consists of three distinct domains: the core, the linker and the lid. This superfamily consists of the lid domain of PTPA, located usually at the C-terminal. |
|
•
•
•
•
•
|
Publication |
First Author: |
Ponniah S |
Year: |
1999 |
Journal: |
Curr Biol |
Title: |
Targeted disruption of the tyrosine phosphatase PTPalpha leads to constitutive downregulation of the kinases Src and Fyn. |
Volume: |
9 |
Issue: |
10 |
Pages: |
535-8 |
|
•
•
•
•
•
|