Protein Kinase

A protein kinase is a kinase enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation). Phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins. The kiwifruit genome contains more than 1000 predicted protein kinase genes and they constitute about 2.5 % of all kiwifruit genes. Kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction.

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

AGC AGC/Akt AGC/MAST AGC/NDR AGC/PDK1 AGC/PKA AGC/RSK Atypical/ABC1 Atypical/PDHK
Atypical/PIKK Atypical/RIO CAMK CAMK/CAMK1 CAMK/CAMKL CK1 CK1/CK1 CMGC CMGC/CDK
CMGC/CLK CMGC/DYRK CMGC/GSK CMGC/MAPK CMGC/RCK CMGC/SRPK Others Others/Aur Others/Bud32
Others/NAK Others/NEK Others/PEK Others/TLK Others/TTK Others/ULK Others/VPS15 Others/WEE Others/WNK
STE STE/STE11 STE/STE20 STE/STE7 TK TK/Fer TKL TKL/IRAK TKL/MLK

In molecular biology, the ACT domain is a protein domain that is found in a variety of proteins involved in metabolism. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. The ACT domain is named after three of the proteins that contain it: aspartate kinase, chorismate mutase and TyrA. The archetypical ACT domain is the C-terminal regulatory domain of 3-phosphoglycerate dehydrogenase (3PGDH), which folds with a ferredoxin-like topology. A pair of ACT domains form an eight-stranded antiparallel sheet with two molecules of allosteric inhibitor serine bound in the interface. Biochemical exploration of a few other proteins containing ACT domains supports the suggestions that these domains contain the archetypical ACT structure.

Protein name Gene name Description Pathway Interaction
Protein name Gene name Description Pathway Interaction