Protein Phosphatase

A protein phosphatase is an enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. The kiwifruit genome contains 177 predicted protein phosphatase genes.

Potential protein kinases and phosphatases were predicted and annotated from http://ekpd.biocuckoo.org/advance.php

aDSP CDC14 FCP Kelch MDP1 MKP NRPTP PP1
PP2A PP2C PP4 PP5 PP6 PP7 PTEN PTPLA

CDC14 phosphatase belongs to a family of highly conserved DUSP phosphatase. All CDC14 family members share a conserved N-terminal core domain, in which two subdomain contribute to critical function, one is involved in substrate specificity and another subdomain act as the phosphatase catalytic domain. The C-terminal domain of CDC14 family is variable which might be involved in subcellular localization. CDC14 family is a key regulator in cell cycle and they are characterized by controlling exit from mitosis. CDC14 is well understood in budding yeast Saccharomyces cerevisiae and studies show that ScCDC14 plays an important role in DNA replication, mitotic exit and cytokinesis. In Saccharomyces pombe CDC14-Like phosphatase, also known as Clp1, participates in G2−M transition and cytokinesis. In mammals, human CDC14B is important in regulating centriole duplication, cell cycle progression, mitotic exit, DNA damage and DNA repair.

Protein name Gene name Description Pathway Interaction
Protein name Gene name Description Pathway Interaction
Ach12g157211.2Ach12g157211Defense mechanisms2