Unknown

Dataset Information

0

Kinases on Double Duty: A Review of UniProtKB Annotated Bifunctionality within the Kinome.


ABSTRACT: Phosphorylation facilitates the regulation of all fundamental biological processes, which has triggered extensive research of protein kinases and their roles in human health and disease. In addition to their phosphotransferase activity, certain kinases have evolved to adopt additional catalytic functions, while others have completely lost all catalytic activity. We searched the Universal Protein Resource Knowledgebase (UniProtKB) database for bifunctional protein kinases and focused on kinases that are critical for bacterial and human cellular homeostasis. These kinases engage in diverse functional roles, ranging from environmental sensing and metabolic regulation to immune-host defense and cell cycle control. Herein, we describe their dual catalytic activities and how they contribute to disease pathogenesis.

SUBMITTER: Rangwala AM 

PROVIDER: S-EPMC9138534 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Kinases on Double Duty: A Review of UniProtKB Annotated Bifunctionality within the Kinome.

Rangwala Aziz M AM   Mingione Victoria R VR   Georghiou George G   Seeliger Markus A MA  

Biomolecules 20220511 5


Phosphorylation facilitates the regulation of all fundamental biological processes, which has triggered extensive research of protein kinases and their roles in human health and disease. In addition to their phosphotransferase activity, certain kinases have evolved to adopt additional catalytic functions, while others have completely lost all catalytic activity. We searched the Universal Protein Resource Knowledgebase (UniProtKB) database for bifunctional protein kinases and focused on kinases t  ...[more]

Similar Datasets

| S-EPMC5290486 | biostudies-literature
| S-EPMC5176325 | biostudies-literature
| S-EPMC2572974 | biostudies-literature
| S-EPMC11243673 | biostudies-literature
| S-EPMC511041 | biostudies-literature
| S-EPMC5961802 | biostudies-literature
| S-EPMC1420674 | biostudies-literature
2021-07-05 | GSE179336 | GEO
| S-EPMC6634314 | biostudies-literature
| S-EPMC11484317 | biostudies-literature