Primary Information |
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| BoMiProt ID | Bomi9049 |
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| Protein Name | Serine/threonine-protein kinase PLK1/Polo-like kinase 1/PLK-1 |
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| Organism | Bos taurus |
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| Uniprot ID | Q2TA25 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001033262.1 |
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| Aminoacid Length | 602 |
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| Molecular Weight | 68000 |
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| FASTA Sequence |
Download |
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| Gene Name | PLK1 |
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| Gene ID | 538238 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | Serine/threonine-protein kinase. regulates the activity of the histone kinases Aurora B and Haspin to define centromere identity, of MPS1 to initiate spindle checkpoint signaling, and of BUB1 and its pseudokinase paralog BUBR1 to coordinate spindle checkpoint activation and inactivation. .regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. |
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| Biochemical Properties | PLK1 is composed of 3 main domains, the serine/threonine kinase domain (KD), the inter domain linker (IDL), and the polo-box domain (PBD).T210 is localized in the activation loop starting at amino acid D194 of the DFG motif (Asp194, Phe195, Gly196). W414 and L490 are involved in substrate recognition via the PBD. H538 and K540 are important for specific binding to phosphorylated substrates (phospho-pincer region). |
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| PTMs | Phosphorylation,Ubl conjugation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q2TA25|PLK1_BOVIN Serine/threonine-protein kinase PLK1 OS=Bos taurus OX=9913 GN=PLK1 PE=2 SV=2
MSAAAT*6AGKLGRAPADPGKAPGVAAPGASTAAPPAKEIPEVLVDPRSRRRYLRGRFLGKG
GFAKCFEISDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIS*101IHRSLAHQHVVGFHGFFED
NDFVFVVLELCRRRS*135LLELHKRRKALTEPEARYYLRQIVLGCQYLHGNRVIHRDLKLGNL
FLNEDLEVKIGDFGLATKVEYDGERKKT*208LCGT*212PNYIAPEVLSKKGHSFEVDVWSIGCIMY
TLLVGKPPFETSCLKETYLRIKNNEYS*267IPKHINPVASSLIKKMLQPDPTARPTIHELLND
EFFTSGYIPARLPITCLTIPPRFSIAPSSLDPS*333NRKPLTVLNKGMENPMPERPREKEEPV
VREASEPVDCHLS*373DMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYG
LGYQLCDNSVGVLFNDSTRLILYSDGDS*448LQYIERDGSESYLTVSSHPNSLIKKITLLKYF
RNYMSEHLLKAGANIT*496PREGDELARLPYLRTWFRTRSAIILHLSNGCVQINFFQDHTKLI
LCPLMAAVTYIDEKRDFRTYRLSLLEEYGCSKELASRLRYARAMVDKLLSSRSAANRLKA
SS |
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| Predicted Disorder Regions | 1-37, 346-396, 592-602 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Activated by phosphorylation of Thr-208 by AURKA.During G2/M transition,FoxM1 activity is enhanced by PLK1 phosphorylation, resulting in a positive feedback loop of increased expression of both PLK1 and Aurora B.The transcription factor Forkhead Box M1 (FoxM1) is important in regulating mitotic entry and subsequent execution of the mitotic program.in various cell types, or expression of a non-phosphorylatable FoxM1 results in decreased transcription of Aurora B. T210 is phosphorylated during G2 and mitosis whereas S137 is modified only during mitosis to activate PLK1. R337 and L340 are the 2 crucial residues of the D-box motif, and are essential for targeting PLK1 for degradation during late mitosis. K492 is mono-ubiquitylated by CUL3/KLHL22, allowing removal of PLK1 from the kinetochores and the metaphase to anaphase transition. |
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| Bibliography | 1.Schmucker S, Sumara I. Molecular dynamics of PLK1 during mitosis. Mol Cell Oncol. 2014 Oct 29;1(2):e954507. doi: 10.1080/23723548.2014.954507. PMID: 27308323; PMCID: PMC4905186. 2.Combes G, Alharbi I, Braga LG, Elowe S. Playing polo during mitosis: PLK1 takes the lead. Oncogene. 2017 Aug 24;36(34):4819-4827. doi: 10.1038/onc.2017.113. Epub 2017 Apr 24. PMID: 28436952. |
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