Polo-like kinase 1, catalytic domain (IPR033702)

Short name: PLK1_cat

Overlapping homologous superfamilies

Domain relationships


Serine/Threonine Kinases (STKs) catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Polo-like kinases (PLKs) are serine/threonine kinases that play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes [PMID: 21654194].

PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase [PMID: 17172872, PMID: 16849530, PMID: 15838519]. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations [PMID: 21153517]. PLK1 is overexpressed in many human cancers and is associated with poor prognosis [PMID: 22447658, PMID: 21601650, PMID: 20107874].

This entry represents the N-terminal catalytic kinase domain of PLK1.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.