EC Number   |
General Information |
Reference |
|---|
   3.1.3.16 | evolution |
analysis of mechanisms controlling the phosphorylation of these proteins and focus on the role of altered dephosphorylation via local type-1, type-2A and type-2B phosphatases (PP1, PP2A, and PP2B, also known as calcineurin, respectively) |
751351 |
| 3.1.3.16 | evolution |
analysis of mechanisms controlling the phosphorylation of these proteins and focus on the role of altered dephosphorylation via local type-1, type-2A and type-2B phosphatases (PP1, PP2A, and PP2B, also known as calcineurin, respectively). Three different CnA isoforms (CnAalpha/PPP3CA, CnAbeta/PPP3CB, and CnAgamma/PPP3CC) have been identified, of which CnAalpha and CnAbeta are ubiquitously expressed. CnB is expressed by two genes (CnBalpha/PPP3R1 and CnBbeta/PPP3R2) |
751351 |
| 3.1.3.16 | evolution |
clustering analyses of PP2As in sweet potato, overview |
752314 |
| 3.1.3.16 | evolution |
compared to kinetoplastid-specific phospho-protein phosphatase (PPP) in the sequence of locus Tb927.6.640 reveals two changes in the conserved PPP signature motif GDXXDRG: the second aspartate is replaced by asparagine and arginine is replaced by lysine. These changes are characteristic for an ApaH-like phosphatase (Alph), a subgroup of the PPP family that is closely related to the bacterial enzyme ApaH. Tb927.6.640 is referred to as TbALPH1. There are two further ApaH-like phosphatases in the Trypanosoma brucei genome: Tb927.4.4330 (TbALPH2) and Tb927.8.8040 (TbALPH3), but neither was identified as stress granule component or as involved in mRNA binding |
-, 758194 |
| 3.1.3.16 | evolution |
enzyme DhSIT4 is a member of PPP6 class of serine threonine phosphatases from the halotolerant yeast Debaryomyces hansenii |
-, 750691 |
| 3.1.3.16 | evolution |
enzyme PphC belongs to the eukaryote-like Ser/Thr phosphatases (eSTPs) in Escherichia coli, that have extensive sequence and structural homology to eukaryotic Ser/Thr protein phosphatase 2C (PP2C) phosphatases. But YegK is an atypical PP2C-like phosphatase. Unlike other bacterial PP2C homologues, YegK contains only six of the eight absolutely conserved residues that are involved in metal binding, coordination, and catalysis, instead of eleven. In particular, the amino acid sequence alignment clearly shows that YegK lacks the conserved glycine residue in motif VI and the aspartic acid residue in motif VIII |
-, 750974 |
| 3.1.3.16 | evolution |
group A Streptococcus (GAS) Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. GAS lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). SP-PTP falls into the category of low-molecular weight PTPases (LMW PTPases) |
751599 |
| 3.1.3.16 | evolution |
the enzyme belongs to the protein phosphatase 2C (PP2C) subfamily. Comparison of PrpC with typical PP2C phosphatases, overview |
-, 751129 |
| 3.1.3.16 | evolution |
the enzyme is a member of the PTP superfamily, but VHR is a dual-specific enzyme (a DSP) |
749953 |
| 3.1.3.16 | malfunction |
a decrease in alpha-isoform of PP2A catalytic subunit accelerates osteoblast differentiation through the expression of bone-related genes |
730105 |
