A protein kinase is an enzyme that catalyzes phosphorylation of a protein. In receptor tyrosine kinase signaling, ATP supplies the transferred phosphate group.
A kinase family in Hippo signalling. Phosphorylation of YAP can limit its nuclear transcriptional activity.
Plant sucrose non-fermenting-1-related protein kinase 2 family. Several members mediate abscisic acid responses, including OST1 in guard cells.
The Arabidopsis kinase also called SnRK2.6, important for ABA-dependent control of guard cell transport. Its activity is restrained by selected protein phosphatase 2C enzymes.
The plant symbiotic kinase CCaMK integrates calcium binding and calmodulin-dependent regulation. Its activation can connect nuclear calcium signaling to symbiotic developmental programs.
A plant kinase recruited and regulated by a calcineurin B-like protein. The separate sensor and kinase provide a modular route from calcium signaling to regulation of transport and other targets.
A kinase with an intrinsic calcium-sensing regulatory region. Calcium binding can relieve autoinhibition and couple calcium signaling to substrate phosphorylation.
A polarity-associated kinase. In fly male germline stem cells, it contributes to the centrosome orientation checkpoint and regulation of cyclin A localization.
A budding-yeast kinase with roles in morphogenesis and cell-cycle regulation, including activation of Kin4.
A budding-yeast kinase contributing to the spindle position checkpoint through regulation of the Bub2-Bfa1 complex. Its activation and location are both relevant.
The budding-yeast Polo-like kinase, with multiple mitotic functions including regulation of the Bub2-Bfa1 complex.
A kinase regulated by cyclic guanosine monophosphate, implicated in several physiological and behavioural processes.
An oncogenic fusion protein with deregulated tyrosine-kinase activity, classically associated with chronic myeloid leukaemia. Its signalling can be inhibited by drugs including imatinib.
A protein kinase participating in distinct regulatory complexes, including mTORC1. Total mTOR abundance and phosphorylation of a specified site are separate measurements.
A family of signaling protein kinases downstream of Ras and upstream of MEK in a major growth-regulatory cascade.
An energy-responsive protein kinase regulated by adenine nucleotide status and upstream inputs. It helps adjust cellular demand and supply when energetic conditions change.
A Janus kinase involved in cytokine-receptor signalling, including interferon-gamma responses in relevant cells.
A Janus kinase participating in cytokine-receptor signalling, including interferon responses relevant to tumour–immune interactions.
A checkpoint kinase that helps couple DNA replication stress and damage responses to cell-cycle progression.
A kinase participating in eukaryotic responses to replication stress and certain DNA lesions, including signalling to Chk1.
A kinase complex that promotes eukaryotic replication initiation through phosphorylation of the MCM complex and related regulatory events.
A kinase involved in mitotic chromosome-attachment error correction and later coordination of cytokinesis, including responses to chromatin bridges.
A kinase activated and regulated through association with a cyclin. Changing activity helps impose the order of replication, mitosis and mitotic exit.
A protein kinase regulated downstream of mTORC1, linking nutrient signaling to growth and translational control.
A stress-responsive protein kinase linking amino acid starvation and starved-ribosome signals to eIF2 phosphorylation.
A protein kinase whose substrates include regulatory proteins involved in cell migration and local biological translation.
Autophosphorylation is phosphorylation of a protein kinase by its own catalytic activity or that of another member of the same protein kinase assembly. Distinguish modification within one chain from trans-autophosphorylation between partners.
In trans-autophosphorylation, one protein kinase chain phosphorylates another partner chain. “Auto” therefore does not require the modified site and catalytic active site to be on the same chain. The insulin receptor provides an activation-loop example; EGFR shows why autophosphorylation and catalytic activation need not be the same event.
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