Polo-like kinase 1 (PLK1) is the founding human member of the Polo kinase family, a serine/threonine protein kinase composed of an N-terminal catalytic domain and a C-terminal tandem polo-box domain (PBD). The PBD binds Ser-[pThr/pSer]-Pro/X docking motifs, typically primed by CDK1, and thereby couples PLK1 catalysis to specific mitotic structures; PLK1 can also generate its own docking sites. PLK1 protein accumulates from S phase, peaks in G2/M and is activated in late G2 by Aurora A/BORA-dependent phosphorylation of Thr210; it is degraded by APC/C-CDH1 at mitotic exit. During the G2/M transition nuclear PLK1 phosphorylates and activates CDC25C, primes WEE1 for SCF(beta-TrCP)-mediated destruction, inhibits PKMYT1 and phosphorylates cyclin B1 and FOXM1, reinforcing the switch-like activation of CDK1-cyclin B. At centrosomes PLK1 drives pericentriolar material expansion and gamma-tubulin recruitment (via NEDD1, KIZ, NINL and pericentrin), promotes centrosome disjunction (via MST2/NEK2A and NEK9/EG5) and coordinates Aurora A localization through BORA turnover, all required for bipolar spindle assembly. At kinetochores, where it docks on BUB1, CENP-U and SGO1-dependent receptors, PLK1 promotes kinetochore-microtubule attachment, chromosome congression and spindle-checkpoint regulation; it also phosphorylates the cohesin subunit STAG2 to remove arm cohesin in prophase and phosphorylates EMI1 and APC/C to allow APC/C activation at the metaphase/anaphase transition. In anaphase PLK1 relocates to the spindle midzone by docking on PRC1 and KIF20A, phosphorylates the centralspindlin subunit RACGAP1 to recruit the RhoGEF ECT2, and thereby triggers RhoA-dependent cleavage-furrow formation; it persists at the midbody through abscission. Beyond these core mitotic roles, PLK1 promotes recovery from the G2 DNA damage checkpoint (by targeting CLASPIN, WEE1, 53BP1, CHK2 and MRE11), phosphorylates RAD51, POLQ and RHNO1 to modulate DNA double-strand break repair, antagonizes p53/p73, and has secondary roles in Golgi fragmentation, primary cilium disassembly and meiotic synaptonemal complex disassembly. PLK1 is essential for proliferation, is over-expressed in many cancers and is the target of clinical ATP-competitive inhibitors.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000070 mitotic sister chromatid segregation | IMP PMID:23455478 Ubiquitylation-dependent localization of PLK1 in mitosis. | ACCEPT | Summary: PLK1 is a core mitotic kinase whose dynamic localization to kinetochores, centrosomes and the spindle midzone is required for chromosome alignment and faithful segregation; a non-ubiquitylatable PLK1-K492R mutant that cannot be removed from kinetochores by CUL3-KLHL22 causes chromosome alignment defects and SAC activation. Reason: Kinetochore-localized PLK1 promotes stable kinetochore-microtubule attachment and sister chromatid segregation (via BUB1/BUBR1, CENP-U and cohesin-related substrates); the IMP evidence from the PLK1-K492R mutant directly implicates PLK1 dynamics in segregation fidelity. Core mitotic function. Supporting Evidence: PMID:23455478 Polo-like kinase 1 (PLK1) critically regulates mitosis through its dynamic localization to kinetochores, centrosomes and the midzone. PMID:23455478 Expression of a non-ubiquitylatable PLK1-K492R mutant phenocopies inactivation of CUL3-KLHL22. |
| GO:0000070 mitotic sister chromatid segregation | TAS Reactome:R-HSA-2500257 | ACCEPT | Summary: Reactome 'Resolution of Sister Chromatid Cohesion': PLK1 phosphorylates the cohesin subunit STAG2/SA2 to drive prophase-pathway removal of arm cohesin, a prerequisite for sister chromatid segregation. Reason: Pathway-level assertion consistent with PLK1's direct role in cohesin removal and chromosome segregation. Core mitotic function. |
| GO:0000086 G2/M transition of mitotic cell cycle | IDA PMID:19160488 Plk1-dependent phosphorylation of FoxM1 regulates a transcri... | ACCEPT | Summary: PLK1 binds CDK1-primed FOXM1 and phosphorylates it at G2/M, activating a transcriptional programme (including PLK1 itself) required for mitotic entry and progression. Reason: Direct phosphorylation of FOXM1 is one of several PLK1 outputs at the G2/M transition (alongside CDC25C activation and WEE1/PKMYT1 inactivation). G2/M transition is a core function of PLK1. Supporting Evidence: PMID:19160488 Formation of the Plk1-FoxM1 complex allows for direct phosphorylation of FoxM1 by Plk1 at G2/M and the subsequent activation of FoxM1 activity, which is required for expression of key mitotic regulators, including Plk1 itself. |
| GO:0000086 G2/M transition of mitotic cell cycle | TAS Reactome:R-HSA-69275 | ACCEPT | Summary: Reactome 'G2/M Transition': PLK1 activates CDC25C, primes WEE1 for SCF(beta-TrCP) degradation and inactivates PKMYT1, forming a feed-forward loop that drives CDK1-cyclin B activation. Reason: Well-established core function of PLK1 documented since the original Roshak et al. and Watanabe et al. studies. Supporting Evidence: PMID:11202906 The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase. |
| GO:0000122 negative regulation of transcription by RNA polymerase II | IMP PMID:18174154 Inhibitory role of Plk1 in the regulation of p73-dependent a... | MARK AS OVER ANNOTATED | Summary: PLK1 phosphorylates p73/TP73 at Thr-27 and blocks p73-mediated transcriptional activation in reporter assays; PLK1 knockdown increases p73-dependent apoptosis. Reason: The molecular event is phosphorylation of a transcription factor; the reduction in Pol II-dependent transcription of p73 targets is a downstream readout, and PLK1 is not a transcriptional regulator. Peripheral to the mitotic core function and one of many PLK1 substrates whose downstream consequences should not each become a process annotation. Supporting Evidence: PMID:18174154 Luciferase reporter assay and reverse transcription-PCR analysis revealed that Plk1 is able to block the p73-mediated transcriptional activation. |
| GO:0000278 mitotic cell cycle | IDA PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote check... | ACCEPT | Summary: Aurora A/Bora phosphorylates PLK1 Thr210 in G2, activating PLK1 to promote mitotic entry and checkpoint recovery. Reason: Correct but generic; PLK1 is an essential mitotic kinase. More specific child terms (G2/M transition, spindle organization, cytokinesis) are also annotated. Supporting Evidence: PMID:18615013 Polo-like kinase-1 (PLK1) is an essential mitotic kinase regulating multiple aspects of the cell division process. |
| GO:0000278 mitotic cell cycle | IMP PMID:18477460 Myosin phosphatase-targeting subunit 1 regulates mitosis by ... | ACCEPT | Summary: PLK1 depletion blocks gamma-tubulin recruitment and centrosome maturation, causing mitotic arrest; co-depletion of MYPT1 restores PLK1 Thr210 phosphorylation and rescues the arrest. Reason: Generic but correct parent term for PLK1's essential mitotic role. Supporting Evidence: PMID:18477460 Depletion of PLK1 by small interfering RNAs is known to result in loss of gamma-tubulin recruitment to the centrosomes, blocking centrosome maturation and leading to mitotic arrest. |
| GO:0000278 mitotic cell cycle | TAS PMID:9177283 Malignant transformation of mammalian cells initiated by con... | ACCEPT | Summary: Early study showing that microinjected PLK mRNA drives quiescent cells into mitosis and that constitutive PLK expression transforms NIH 3T3 cells. Reason: Generic term, supported by the sufficiency of PLK1 to drive mitotic entry; the transformation phenotype is a consequence of deregulated mitotic kinase activity rather than a separate function. Supporting Evidence: PMID:9177283 microinjection of Plk mRNA is sufficient to drive quiescent cells into mitosis |
| GO:0000280 nuclear division | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA-derived 'nuclear division'; PLK1 drives multiple steps of mitotic nuclear division. Reason: Broad but correct electronic inference; the experimental and IBA annotations to mitotic spindle organization and sister chromatid segregation are more informative. |
| GO:0000281 mitotic cytokinesis | IDA PMID:19468302 Plk1 self-organization and priming phosphorylation of HsCYK-... | ACCEPT | Summary: PLK1 self-targets to the spindle midzone and phosphorylates the centralspindlin subunit RACGAP1/HsCYK-4 at Ser157, creating an ECT2 BRCT docking site that triggers RhoA activation and cleavage furrow formation. Reason: Cytokinesis initiation via RACGAP1 phosphorylation and ECT2 recruitment is a core, mechanistically resolved PLK1 function. Supporting Evidence: PMID:19468302 the self-organized delivery of Polo-like kinase 1 (Plk1) to the midzone and its local phosphorylation of a MT-bound substrate are critical for generating this furrow-inducing signal. |
| GO:0000281 mitotic cytokinesis | TAS Reactome:R-HSA-68884 | ACCEPT | Summary: Reactome 'Mitotic Telophase/Cytokinesis': PLK1 phosphorylates KIF20A/MKLP2, KIF23/MKLP1, PRC1 and RACGAP1 at the central spindle. Reason: Consistent with extensive experimental evidence for PLK1 in cytokinesis. Core function. |
| GO:0000287 magnesium ion binding | IMP PMID:17461553 Structure of the catalytic domain of human polo-like kinase ... | ACCEPT | Summary: Crystal structures of the PLK1 kinase domain with AMPPNP show the canonical Mg-ATP binding site of a protein kinase. Reason: Magnesium is the obligatory cofactor for the phosphotransfer reaction; the annotation is a generic but accurate description of the kinase active site rather than a distinct function. Supporting Evidence: PMID:17461553 We determined the crystal structures of the T210V mutant of the kinase domain of human Plk1 complexed with the nonhydrolyzable ATP analogue adenylylimidodiphosphate (AMPPNP) |
| GO:0000775 chromosome, centromeric region | IEA GO_REF:0000107 | ACCEPT | Summary: Centromeric region localization inferred from mouse; consistent with human PLK1 at kinetochores/centromeres from prometaphase via BUB1, SGO1 and CENP-U docking. Reason: Ensembl Compara transfer from mouse Plk1 (Q07832). Fully consistent with the human IDA kinetochore annotations. |
| GO:0000776 kinetochore | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference that Polo kinases act at kinetochores, supported by fly polo, mouse Plk1, pombe plo1 and human PLK1 itself. Reason: Kinetochore localization is deeply conserved in the Polo family and experimentally established for human PLK1; the target's own IDA annotations are among the descendant evidence. |
| GO:0000776 kinetochore | IDA PMID:17617734 Shugoshin 1 plays a central role in kinetochore assembly and... | ACCEPT | Summary: PLK1 localizes to kinetochores from prometaphase, docking via its polo-box domain on CDK1-primed BUB1, CENP-U/PBIP1 and SGO1-dependent receptors. Reason: Kinetochore localization of PLK1 is robustly established by multiple independent studies. Core location. Supporting Evidence: PMID:17617734 RNAi assays show that depletion of Sgo1 did not affect AurB localization but diminished Plk1 kinetochore binding. |
| GO:0000776 kinetochore | IDA PMID:18477460 Myosin phosphatase-targeting subunit 1 regulates mitosis by ... | ACCEPT | Summary: PLK1 localizes to kinetochores from prometaphase, docking via its polo-box domain on CDK1-primed BUB1, CENP-U/PBIP1 and SGO1-dependent receptors. Abstract-only cache; localization data are in the full text and deferred to the curator. Reason: Kinetochore localization of PLK1 is robustly established by multiple independent studies. Core location. Supporting Evidence: PMID:18477460 Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1. |
| GO:0000776 kinetochore | IDA PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote check... | ACCEPT | Summary: PLK1 localizes to kinetochores from prometaphase, docking via its polo-box domain on CDK1-primed BUB1, CENP-U/PBIP1 and SGO1-dependent receptors. Abstract-only cache; deferred to the curator. Reason: Kinetochore localization of PLK1 is robustly established by multiple independent studies. Core location. Supporting Evidence: PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery. |
| GO:0000776 kinetochore | IDA PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kina... | ACCEPT | Summary: PLK1 localizes to kinetochores from prometaphase, docking via its polo-box domain on CDK1-primed BUB1, CENP-U/PBIP1 and SGO1-dependent receptors. Reason: Kinetochore localization of PLK1 is robustly established by multiple independent studies. Core location. Supporting Evidence: PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kinase 1, regulates chromosomal segregation |
| GO:0000776 kinetochore | IDA PMID:23455478 Ubiquitylation-dependent localization of PLK1 in mitosis. | ACCEPT | Summary: PLK1 localizes to kinetochores from prometaphase, docking via its polo-box domain on CDK1-primed BUB1, CENP-U/PBIP1 and SGO1-dependent receptors. Reason: Kinetochore localization of PLK1 is robustly established by multiple independent studies. Core location. Supporting Evidence: PMID:23455478 In the absence of KLHL22, PLK1 accumulates on kinetochores, resulting in activation of the spindle assembly checkpoint (SAC). |
| GO:0000776 kinetochore | IDA PMID:24157919 Bod1 regulates protein phosphatase 2A at mitotic kinetochore... | ACCEPT | Summary: PLK1 localizes to kinetochores from prometaphase, docking via its polo-box domain on CDK1-primed BUB1, CENP-U/PBIP1 and SGO1-dependent receptors. Reason: Kinetochore localization of PLK1 is robustly established by multiple independent studies. Core location. Supporting Evidence: PMID:24157919 Bod1 regulates protein phosphatase 2A at mitotic kinetochores. |
| GO:0000776 kinetochore | IDA PMID:25395579 Chromosome congression is promoted by CENP-Q- and CENP-E-dep... | ACCEPT | Summary: PLK1 localizes to kinetochores from prometaphase, docking via its polo-box domain on CDK1-primed BUB1, CENP-U/PBIP1 and SGO1-dependent receptors. Reason: Kinetochore localization of PLK1 is robustly established by multiple independent studies. Core location. Supporting Evidence: PMID:25395579 CENP-Q - a subunit of the CENP-O complex (comprising CENP-O, CENP-P, CENP-Q and CENP-U) that targets polo-like kinase (Plk1) to kinetochores |
| GO:0000776 kinetochore | IEA GO_REF:0000107 | ACCEPT | Summary: Kinetochore localization transferred from mouse Plk1. Reason: Ensembl Compara transfer from mouse Plk1 (Q07832). Matches extensive human IDA evidence. |
| GO:0000779 condensed chromosome, centromeric region | IEA GO_REF:0000107 | ACCEPT | Summary: Condensed chromosome, centromeric region; PLK1 occupies kinetochores/centromeres of condensed mitotic chromosomes. Reason: Ensembl Compara transfer from mouse Plk1 (Q07832). Consistent with experimental human kinetochore localization. |
| GO:0000785 chromatin | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Chromatin association inferred from mouse; human PLK1 co-purifies with MCM2-7 in a soluble chromatin fraction and phosphorylates chromatin-bound cohesin, condensin and KAT7/HBO1. Reason: Plausible and consistent with human data (PMID:15654075), but PLK1 acts on chromatin transiently as a mitotic kinase; the informative localizations are kinetochore, centrosome, spindle midzone and midbody. Supporting Evidence: PMID:15654075 The strongest interaction between endogenous Plk1 and Mcm7 was detected in a soluble chromatin |
| GO:0000795 synaptonemal complex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Synaptonemal complex localization transferred from mouse, where PLK1 (not PLK2-4) localizes to the SC at the meiotic G2/MI transition and phosphorylates SYCP1 and TEX12 to trigger SC disassembly. Reason: A genuine but meiosis-specific localization documented in mouse spermatocytes; not shown in human and peripheral to the somatic mitotic core function. Supporting Evidence: PMID:22854038 Only PLK1 (not PLK2-4) localizes to the SC during the G2/MI transition. |
| GO:0000922 spindle pole | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of spindle-pole localization across Polo kinases (fly, mouse, rat, budding and fission yeast, Dictyostelium, human). Reason: Spindle pole/SPB localization is the ancestral hallmark of the Polo family; established for human PLK1. |
| GO:0000922 spindle pole | IDA PMID:18331714 sSgo1, a major splice variant of Sgo1, functions in centriol... | ACCEPT | Summary: PLK1 localizes to spindle poles in mitosis where it regulates the sSgo1 splice variant that protects centriole cohesion. Reason: Spindle pole localization is well established. Supporting Evidence: PMID:18331714 sSgo1 interacts with Plk1 and its spindle pole localization is Plk1 dependent. |
| GO:0000922 spindle pole | IDA PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kina... | ACCEPT | Summary: PLK1 at spindle poles (Cdc6 study). Reason: Consistent with the extensive evidence for PLK1 at centrosomes/spindle poles from prophase to metaphase. |
| GO:0000922 spindle pole | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA-inferred spindle pole localization. Reason: Matches experimental evidence. |
| GO:0000940 outer kinetochore | IDA PMID:18195732 Cyclin B1 is localized to unattached kinetochores and contri... | ACCEPT | Summary: Outer kinetochore localization; PLK1 is recruited to the outer kinetochore via BUB1 and the CENP-O/P/Q/U complex and is enriched on unattached kinetochores. Reason: The cached abstract concerns cyclin B1 at unattached kinetochores and does not mention PLK1; the curator read the full text. The localization agrees with UniProt ('Localizes to the outer kinetochore') and with PMID:17617734/PMID:25395579, so the annotation is accepted. Supporting Evidence: PMID:18195732 Cyclin B1 is localized to unattached kinetochores and contributes to efficient microtubule attachment and proper chromosome alignment during mitosis. |
| GO:0001578 microtubule bundle formation | IDA PMID:12939256 Phosphorylation of mitotic kinesin-like protein 2 by polo-li... | MARK AS OVER ANNOTATED | Summary: PLK1 phosphorylates the central-spindle kinesin KIF20A/MKlp2, which is required for cytokinesis; central-spindle microtubule bundling itself is performed by PRC1 and KIF23/MKlp1. Reason: PLK1 regulates proteins of the central spindle but does not itself bundle microtubules; the paper's evidence concerns MKlp2 phosphorylation and cleavage-furrow ingression, and midzone regulation is better captured by regulation of mitotic spindle assembly (PMID:22621898) and regulation of cytokinesis. Supporting Evidence: PMID:12939256 We propose that phosphorylation of MKlp2 by Plk1 is necessary for the spatial restri |
| GO:0004672 protein kinase activity | IDA PMID:17146433 RGC32, a novel p53-inducible gene, is located on centrosomes... | MODIFY | Summary: Kinase-activity annotation from the RGC32/RGCC study (p53-inducible centrosomal protein phosphorylated by PLK1). Reason: PLK1 is a Ser/Thr-specific kinase; the specific child term is better supported. Proposed replacements: protein serine/threonine kinase activity Supporting Evidence: PMID:17146433 RGC32, a novel p53-inducible gene, is located on centrosomes during mitosis and results in G2/M arrest. |
| GO:0004672 protein kinase activity | IDA PMID:19596235 Mammalian BTBD12/SLX4 assembles a Holliday junction resolvas... | MODIFY | Summary: PLK1 associates with the SLX4 endonuclease scaffold complex. Reason: The abstract documents association, not a phosphorylation assay; nonetheless PLK1 is a Ser/Thr kinase and the specific term is more informative. Proposed replacements: protein serine/threonine kinase activity Supporting Evidence: PMID:19596235 the protein kinase PLK1 and the uncharacterized protein C20orf94 |
| GO:0004672 protein kinase activity | IDA PMID:22854038 Polo-like kinase is required for synaptonemal complex disass... | MODIFY | Summary: PLK1 (not PLK2-4) phosphorylates synaptonemal-complex central-element proteins SYCP1 and TEX12 in vitro (mouse spermatocyte study). Reason: Ser/Thr specificity is established; use the specific term. Proposed replacements: protein serine/threonine kinase activity Supporting Evidence: PMID:22854038 Phosphorylation assays in vitro demonstrated that PLK1, but not PLK2-4, phosphorylates central element proteins SYCP1 and TEX12. |
| GO:0004672 protein kinase activity | IEA GO_REF:0000120 | MODIFY | Summary: InterPro/Ensembl-derived generic protein kinase activity. Reason: Correct but redundant with the more specific IEA/IBA/IDA annotations to protein serine/threonine kinase activity; for consistency with the IDA rows the specific child term is preferred. Proposed replacements: protein serine/threonine kinase activity |
| GO:0004674 protein serine/threonine kinase activity | EXP PMID:18378770 Plk1- and beta-TrCP-dependent degradation of Bora controls m... | ACCEPT | Summary: PLK1 phosphorylates the BORA DSGxxT degron, promoting SCF(beta-TrCP)-mediated BORA destruction. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:18378770 Plk1 phosphorylates a conserved DSGxxT degron in Bora and promotes its interaction with beta-TrCP. |
| GO:0004674 protein serine/threonine kinase activity | EXP PMID:20577264 Polo-like kinase 1 phosphorylation of G2 and S-phase-express... | ACCEPT | Summary: PLK1 phosphorylates GTSE1 Ser435, promoting its nuclear localization during G2 checkpoint recovery. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:20577264 Plk1 phosphorylation of GTSE1 at Ser 435 promotes its nuclear localization |
| GO:0004674 protein serine/threonine kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of Ser/Thr kinase activity across the Polo family. Reason: Deeply conserved defining activity; human PLK1 has abundant direct evidence. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:12524548 Active cyclin B1-Cdk1 first appears on centrosomes in propha... | ACCEPT | Summary: PLK1 phosphorylates cyclin B1 (but not within its NES) on centrosomes in prophase. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:12524548 Plk1 phosphorylates cyclin B1, but not in the NES. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:12939256 Phosphorylation of mitotic kinesin-like protein 2 by polo-li... | ACCEPT | Summary: PLK1 phosphorylates KIF20A/MKlp2, creating a polo-box docking site. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:12939256 MKlp2 is a target for Plk1, and phosphorylated MKlp2 binds to the polo box domain of Plk1. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:15148369 Role of Polo-like kinase in the degradation of early mitotic... | ACCEPT | Summary: PLK1 phosphorylates the EMI1 DSGxxS degron, promoting its SCF(beta-TrCP)-dependent degradation. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:15148369 Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:16885022 SCFbetaTrCP-mediated degradation of Claspin regulates recove... | ACCEPT | Summary: PLK1 phosphorylates the CLASPIN degron required for beta-TrCP binding. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:16885022 Phosphorylation of Claspin is mediated by Plk1 and is essential for binding to betaTrCP. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:17351640 Choice of Plk1 docking partners during mitosis and cytokines... | ACCEPT | Summary: PLK1 phosphorylates PRC1 in anaphase, creating its own docking site. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:17351640 In anaphase, Plk1 creates its own docking site on PRC1 |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:18174154 Inhibitory role of Plk1 in the regulation of p73-dependent a... | ACCEPT | Summary: PLK1 phosphorylates p73/TP73 Thr27. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:18174154 in vitro kinase assay indicated that p73 is phosphorylated at Thr-27 by Plk1. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:18477460 Myosin phosphatase-targeting subunit 1 regulates mitosis by ... | ACCEPT | Summary: PLK1 phosphorylates substrates at centrosomes; its Thr210-phosphorylated active form is antagonized by MYPT1-PP1. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:18477460 MYPT1 depletion increases phosphorylation of PLK1 at its activating site (Thr210) in vivo |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:19160488 Plk1-dependent phosphorylation of FoxM1 regulates a transcri... | ACCEPT | Summary: PLK1 phosphorylates FOXM1 at G2/M after CDK1 priming. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:19160488 Formation of the Plk1-FoxM1 complex allows for direct phosphorylation of FoxM1 by Plk1 at G2/M |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:19468300 Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ec... | ACCEPT | Summary: PLK1 phosphorylates the RACGAP1/HsCyk-4 N terminus at the central spindle. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:19468300 Plk1 phosphorylates the noncatalytic N terminus of the RhoGAP HsCyk-4 at the central spindle |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:19468302 Plk1 self-organization and priming phosphorylation of HsCYK-... | ACCEPT | Summary: PLK1 phosphorylates RACGAP1/HsCYK-4 Ser157 at the midzone. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:19468302 Plk1 binds and directly phosphorylates the HsCYK-4 subunit of centralspindlin (also known as MgcRacGAP) at the midzone. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:20679239 Polo-like kinase 1 phosphorylation of p150Glued facilitates ... | ACCEPT | Summary: PLK1 phosphorylates DCTN1/p150Glued Ser179 at the prophase nuclear envelope. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:20679239 Plk1 phosphorylates p150(Glued) at Ser-179 |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:21857149 Phosphorylation of Ataxin-10 by polo-like kinase 1 is requir... | ACCEPT | Summary: PLK1 phosphorylates Ataxin-10 at S77 and T82, required for cytokinesis. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:21857149 Plk1 phosphorylates Ataxin-10 at S77 and T82 in vitro. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:22325354 Plk1 and CK2 act in concert to regulate Rad51 during DNA dou... | ACCEPT | Summary: PLK1 phosphorylates RAD51 Ser14. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:22325354 phosphorylates the essential Rad51 recombinase at serine 14 (S14) during the cell cycle and in response to DNA damage. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:23509069 MISP is a novel Plk1 substrate required for proper spindle o... | ACCEPT | Summary: PLK1 phosphorylates MISP, required for spindle orientation. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:23509069 MISP (C19orf21), as a substrate of Plk1 that is required for correct mitotic spindle positioning. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:28512243 Plk1 Phosphorylation of Mre11 Antagonizes the DNA Damage Res... | ACCEPT | Summary: PLK1 phosphorylates MRE11 Ser649. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:28512243 Plk1 phosphorylated Mre11, a component of the Mre11/Rad50/Nbs1 (MRN) complex, at serine 649 (S649) during DDR. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:37440612 RHINO directs MMEJ to repair DNA breaks in mitosis. | ACCEPT | Summary: PLK1 phosphorylates RHNO1/RHINO in mitosis. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:37440612 RHINO accumulates in M phase, undergoes Polo-like kinase 1 (PLK1) phosphorylation |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:37674080 PolΞΈ is phosphorylated by PLK1 to repair double-strand break... | ACCEPT | Summary: PLK1 phosphorylates POLQ/Pol-theta in mitosis. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:37674080 PolΞΈ is phosphorylated by PLK1 to repair double-strand breaks in mitosis. |
| GO:0004674 protein serine/threonine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: InterPro PLK1 catalytic-domain (IPR033702) mapping. Reason: Correct. |
| GO:0004674 protein serine/threonine kinase activity | IMP PMID:17461553 Structure of the catalytic domain of human polo-like kinase ... | ACCEPT | Summary: Kinase-domain crystal structure (T210V) with AMPPNP and an inhibitor; defines the catalytic machinery. Reason: Structural support for the defining activity. Supporting Evidence: PMID:17461553 Structure of the catalytic domain of human polo-like kinase 1. |
| GO:0004674 protein serine/threonine kinase activity | IMP PMID:19473992 Plk1-mediated phosphorylation of Topors regulates p53 stabil... | ACCEPT | Summary: PLK1 phosphorylates TOPORS Ser718 in vivo. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:19473992 We show that Plk1 phosphorylates Topors on Ser(718) in vivo. |
| GO:0004674 protein serine/threonine kinase activity | IMP PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kina... | ACCEPT | Summary: PLK1 phosphorylates CDC6 Thr37 in mitosis. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:21041660 Cdc6 is phosphorylated by Plk1 on T37. |
| GO:0004674 protein serine/threonine kinase activity | IMP PMID:23455478 Ubiquitylation-dependent localization of PLK1 in mitosis. | ACCEPT | Summary: PLK1 phosphorylates kinetochore substrates; its activity and PBD mediate recruitment to mitotic structures. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Direct kinase evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:23455478 The polo-box domain (PBD) and activity of PLK1 mediate its recruitment to mitotic structures |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-156673 | ACCEPT | Summary: Reactome reaction 'Regulation of KIF23 (MKLP1) by phosphorylation'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-156678 | ACCEPT | Summary: Reactome 'Activation of Cdc25C': PLK1 phosphorylates and activates CDC25C. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Founding PLK1 substrate (PMID:11202906); core G2/M function. Supporting Evidence: PMID:11202906 The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-156682 | ACCEPT | Summary: Reactome reaction 'PLK1 phosphorylates NUDC'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-156699 | ACCEPT | Summary: Reactome reaction 'Inactivation of Wee1 kinase'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. Supporting Evidence: PMID:15070733 the major M-phase kinases polo-like kinase 1 (Plk1) and Cdc2 are responsible for the phosphorylation of S53 and S123, respectively |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-156723 | ACCEPT | Summary: Reactome reaction 'Regulation of KIF20A (MKL2) by phosphorylation'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-162657 | ACCEPT | Summary: Reactome reaction 'Inactivation of Myt1 kinase'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-163010 | ACCEPT | Summary: Reactome reaction 'Down Regulation of Emi1 through Phosphorylation of Emi1'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-1638803 | ACCEPT | Summary: Reactome reaction 'Phosphorylation of cohesin by PLK1 at centromeres'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-174119 | ACCEPT | Summary: Reactome reaction 'Free APC/C phosphorylated by Plk1'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-174174 | ACCEPT | Summary: Reactome reaction 'Phosphorylation of the Emi1 DSGxxS degron by Plk1'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-2214351 | ACCEPT | Summary: Reactome reaction 'PLK1 phosphorylates GORASP1'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-2294580 | ACCEPT | Summary: Reactome reaction 'PLK1 hyperphosphorylates Condensin II complex'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-2466068 | ACCEPT | Summary: Reactome reaction 'Phosphorylation of cohesin by PLK1 at chromosomal arms'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-2562526 | ACCEPT | Summary: Reactome reaction 'PLK1 phosphorylates OPTN'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-2984226 | ACCEPT | Summary: Reactome reaction 'PLK1 phosphorylates NEK9'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-380272 | ACCEPT | Summary: Reactome 'Plk1-mediated phosphorylation of Nlp': PLK1 phosphorylates ninein-like protein (NINL), displacing it from maturing centrosomes. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-9851972 | ACCEPT | Summary: Reactome reaction 'PLK1 phosphorylates FIRRM at S43'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-9853369 | ACCEPT | Summary: Reactome reaction 'PLK1 phosphorylates FIRMM at S744'. Protein serine/threonine kinase activity is the defining molecular function of PLK1; the kinase domain (residues ~39-325) phosphorylates Ser/Thr on substrates docked via the C-terminal polo-box domain. Reason: Curated Reactome reaction in which PLK1 acts as the kinase; consistent with the experimental literature. |
| GO:0005515 protein binding | IPI PMID:12493754 Polo-like kinase 1 and Chk2 interact and co-localize to cent... | REMOVE | Summary: IPI with CHEK2, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:12493754 Chk2 coimmunoprecipitates with Polo-like kinase 1 |
| GO:0005515 protein binding | IPI PMID:12524548 Active cyclin B1-Cdk1 first appears on centrosomes in propha... | REMOVE | Summary: IPI with CCNB1 (cyclin B1), a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:12524548 Plk1 phosphorylates cyclin B1, but not in the NES. |
| GO:0005515 protein binding | IPI PMID:12939256 Phosphorylation of mitotic kinesin-like protein 2 by polo-li... | MODIFY | Summary: IPI with KIF20A/MKlp2: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on KIF20A/MKlp2. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:12939256 MKlp2 is a target for Plk1, and phosphorylated MKlp2 binds to the polo box domain of Plk1. |
| GO:0005515 protein binding | IPI PMID:15070733 M-phase kinases induce phospho-dependent ubiquitination of s... | REMOVE | Summary: IPI with WEE1, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:15070733 the major M-phase kinases polo-like kinase 1 (Plk1) and Cdc2 are responsible for the phosphorylation of S53 and S123, respectively |
| GO:0005515 protein binding | IPI PMID:15148369 Role of Polo-like kinase in the degradation of early mitotic... | REMOVE | Summary: IPI with FBXO5/EMI1, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:15148369 Role of Polo-like kinase in the degradation of early mitotic inhibitor 1 |
| GO:0005515 protein binding | IPI PMID:15654075 Interaction of chromatin-associated Plk1 and Mcm7. | REMOVE | Summary: IPI with MCM7; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:15654075 In a search for proteins that interact with the PBD of Plk1, we identified two of the minichromosome maintenance (MCM) proteins, Mcm2 and Mcm7. |
| GO:0005515 protein binding | IPI PMID:15654075 Interaction of chromatin-associated Plk1 and Mcm7. | REMOVE | Summary: IPI with MCM2; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:15654075 In a search for proteins that interact with the PBD of Plk1, we identified two of the minichromosome maintenance (MCM) proteins, Mcm2 and Mcm7. |
| GO:0005515 protein binding | IPI PMID:16439210 The evi5 oncogene regulates cyclin accumulation by stabilizi... | REMOVE | Summary: IPI with EVI5, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:16439210 Evi5 protein accumulates in early G1 following Plk1 destruction and is degraded in a Plk1- and ubiquitin-dependent manner in early mitosis. |
| GO:0005515 protein binding | IPI PMID:16753148 Polo-like kinase 1 regulates mitotic arrest after UV irradia... | REMOVE | Summary: IPI with TP53; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:16753148 Plk1 could bind to the sequence-specific DNA-binding domain of p53 |
| GO:0005515 protein binding | IPI PMID:16760428 Phosphorylation- and polo-box-dependent binding of Plk1 to B... | MODIFY | Summary: IPI with BUB1: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on BUB1. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:16760428 The Plk1-Bub1 interaction requires the polo-box domain (PBD) of Plk1 and is enhanced by cyclin-dependent kinase 1 (Cdk1)-mediated phosphorylation of Bub1 at T609. |
| GO:0005515 protein binding | IPI PMID:16760428 Phosphorylation- and polo-box-dependent binding of Plk1 to B... | REMOVE | Summary: IPI with BUB1B/BubR1; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:16760428 Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is required for the kinetochore localization of Plk1. |
| GO:0005515 protein binding | IPI PMID:16815967 Aberrant Wnt/beta-catenin signaling can induce chromosomal i... | REMOVE | Summary: IPI with AXIN2/conductin; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:16815967 Conductin is up-regulated during mitosis, localizes along the mitotic spindles |
| GO:0005515 protein binding | IPI PMID:16864798 MPS1-dependent mitotic BLM phosphorylation is important for ... | REMOVE | Summary: IPI with BLM; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:16864798 MPS1-dependent mitotic BLM phosphorylation is important for chromosome stability. |
| GO:0005515 protein binding | IPI PMID:16980960 The Plk1 target Kizuna stabilizes mitotic centrosomes to ens... | REMOVE | Summary: IPI with KIZ/Kizuna, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:16980960 we identify a novel centrosomal substrate of Plk1, Kizuna (Kiz) |
| GO:0005515 protein binding | IPI PMID:17146433 RGC32, a novel p53-inducible gene, is located on centrosomes... | REMOVE | Summary: IPI with RGCC/RGC32; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:17146433 RGC32, a novel p53-inducible gene, is located on centrosomes during mitosis and results in G2/M arrest. |
| GO:0005515 protein binding | IPI PMID:17307877 Molecular and structural basis of polo-like kinase 1 substra... | MODIFY | Summary: IPI with CDC25C: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on CDC25C. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:17307877 The crystal structures of the PBD in complex with Cdc25C and Cdc25C-P target peptides reveal that Trp-414 is fundamental in their recognition regardless of its phosphorylation status. |
| GO:0005515 protein binding | IPI PMID:17310276 TTDN1 is a Plk1-interacting protein involved in maintenance ... | MODIFY | Summary: IPI with MPLKIP/TTDN1: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on MPLKIP/TTDN1. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:17310276 Mutation of Thr120 of TTDN1 abolishes its interaction with Plk1, suggesting phosphorylation of Thr120 in the consensus Plk1-binding motif is required for its interaction with Plk1. |
| GO:0005515 protein binding | IPI PMID:17351640 Choice of Plk1 docking partners during mitosis and cytokines... | MODIFY | Summary: IPI with PRC1: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on PRC1. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:17351640 In anaphase, Plk1 creates its own docking site on PRC1, whereas in metaphase Cdk1 phosphorylates PRC1 adjacent to this docking site |
| GO:0005515 protein binding | IPI PMID:17495026 The tumor suppressor CYLD regulates entry into mitosis. | REMOVE | Summary: IPI with CYLD; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:17495026 We identified the protein kinase Plk1 as a potential target of CYLD in the regulation of mitotic entry, based on their physical interaction |
| GO:0005515 protein binding | IPI PMID:18174154 Inhibitory role of Plk1 in the regulation of p73-dependent a... | REMOVE | Summary: IPI with TP73, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:18174154 p73 binds to the kinase domain of Plk1 through its NH(2)-terminal region. |
| GO:0005515 protein binding | IPI PMID:18250300 Role for Plk1 phosphorylation of Hbo1 in regulation of repli... | MODIFY | Summary: IPI with KAT7/HBO1: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on KAT7/HBO1. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:18250300 During mitosis, Cdk1 phosphorylates Hbo1 on Thr-85/88, creating a docking site for Plk1 to be recruited. |
| GO:0005515 protein binding | IPI PMID:18329369 Final stages of cytokinesis and midbody ring formation are c... | REMOVE | Summary: IPI with BIRC6/BRUCE; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:18329369 BRUCE moves from the vesicular system to the midbody ring and serves as a platform for the membrane delivery machinery and mitotic regulators. |
| GO:0005515 protein binding | IPI PMID:18331714 sSgo1, a major splice variant of Sgo1, functions in centriol... | REMOVE | Summary: IPI with SGO1, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:18331714 sSgo1 interacts with Plk1 and its spindle pole localization is Plk1 dependent. |
| GO:0005515 protein binding | IPI PMID:18477460 Myosin phosphatase-targeting subunit 1 regulates mitosis by ... | MODIFY | Summary: IPI with PPP1R12A/MYPT1: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on PPP1R12A/MYPT1. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:18477460 MYPT1 is phosphorylated during mitosis by proline-directed kinases including cdc2, which generates the binding motif for the polo box domain of PLK1. |
| GO:0005515 protein binding | IPI PMID:18521620 Plk1 regulates mitotic Aurora A function through betaTrCP-de... | REMOVE | Summary: IPI with BORA, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:18521620 Following Cdk1-dependent recruitment, Plk1 triggers hBora destruction by phosphorylating a recognition site for SCF(Beta-TrCP). |
| GO:0005515 protein binding | IPI PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote check... | REMOVE | Summary: IPI with AURKA, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:18615013 aurora A can directly phosphorylate PLK1 on Thr 210 |
| GO:0005515 protein binding | IPI PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote check... | REMOVE | Summary: IPI with BORA, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:18615013 activity of aurora A towards PLK1 is greatly enhanced by Bora |
| GO:0005515 protein binding | IPI PMID:18794143 HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1... | REMOVE | Summary: IPI with HSF1, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:18794143 HSF1 was phosphorylated by Plk1 at Ser(216) of the DSGXXS motif |
| GO:0005515 protein binding | IPI PMID:19160488 Plk1-dependent phosphorylation of FoxM1 regulates a transcri... | MODIFY | Summary: IPI with FOXM1: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on FOXM1. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:19160488 The carboxy-terminal domain of FoxM1 binds Plk1, and phosphorylation of two key residues in this domain by Cdk1 is essential for Plk1-FoxM1 interaction. |
| GO:0005515 protein binding | IPI PMID:19468300 Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ec... | REMOVE | Summary: IPI with PRC1; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:19468300 Microtubules, as well as the microtubule-associated protein (MAP) Prc1, facilitate Plk1 phosphorylation of HsCyk-4. |
| GO:0005515 protein binding | IPI PMID:19468300 Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ec... | REMOVE | Summary: IPI with RACGAP1/HsCyk-4, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:19468300 Plk1 phosphorylates the noncatalytic N terminus of the RhoGAP HsCyk-4 at the central spindle |
| GO:0005515 protein binding | IPI PMID:19468302 Plk1 self-organization and priming phosphorylation of HsCYK-... | REMOVE | Summary: IPI with RACGAP1/HsCyk-4, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:19468302 Plk1 binds and directly phosphorylates the HsCYK-4 subunit of centralspindlin |
| GO:0005515 protein binding | IPI PMID:19473992 Plk1-mediated phosphorylation of Topors regulates p53 stabil... | REMOVE | Summary: IPI with TOPORS, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:19473992 We show that Plk1 phosphorylates Topors on Ser(718) in vivo. |
| GO:0005515 protein binding | IPI PMID:19596235 Mammalian BTBD12/SLX4 assembles a Holliday junction resolvas... | REMOVE | Summary: IPI with BORA; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:19596235 the protein kinase PLK1 and the uncharacterized protein C20orf94 |
| GO:0005515 protein binding | IPI PMID:19596235 Mammalian BTBD12/SLX4 assembles a Holliday junction resolvas... | REMOVE | Summary: IPI with SLX4; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:19596235 Human SLX4 forms a multiprotein complex with the ERCC4(XPF)-ERCC1, MUS81-EME1, and SLX1 endonucleases and also associates with MSH2/MSH3 mismatch repair complex, telomere binding complex TERF2(TRF2)-TERF2IP(RAP1), the protein kinase PLK1 |
| GO:0005515 protein binding | IPI PMID:19597481 Structural and functional analyses of minimal phosphopeptide... | MODIFY | Summary: IPI with CDC25C: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on CDC25C. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:19597481 we report the identification of minimal phosphopeptides that specifically interact with the PBD of human PLK1, but not those of the closely related PLK2 and PLK3. |
| GO:0005515 protein binding | IPI PMID:19597481 Structural and functional analyses of minimal phosphopeptide... | MODIFY | Summary: IPI with CENPU/PBIP1: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on CENPU/PBIP1. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:19597481 the C-terminal SpT dipeptide functions as a high-affinity anchor, whereas the N-terminal residues are crucial for providing specificity and affinity to the interaction. |
| GO:0005515 protein binding | IPI PMID:19833129 Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimula... | REMOVE | Summary: IPI with TP53; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:19833129 polo-like kinase-1 (PLK1), phosphorylates MDM2 at one of these residues, Ser260, and stimulates MDM2-mediated turnover of p53. |
| GO:0005515 protein binding | IPI PMID:19833129 Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimula... | REMOVE | Summary: IPI with mouse Mdm2, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:19833129 polo-like kinase-1 (PLK1), phosphorylates MDM2 at one of these residues, Ser260 |
| GO:0005515 protein binding | IPI PMID:19833129 Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimula... | REMOVE | Summary: IPI with MDM2, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:19833129 polo-like kinase-1 (PLK1), phosphorylates MDM2 at one of these residues, Ser260 |
| GO:0005515 protein binding | IPI PMID:20126263 A mitotic phosphorylation feedback network connects Cdk1, Pl... | REMOVE | Summary: IPI with CHEK2, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:20126263 Plk1 also phosphorylates the 53BP1-binding checkpoint kinase Chk2 to inactivate its FHA domain |
| GO:0005515 protein binding | IPI PMID:20126263 A mitotic phosphorylation feedback network connects Cdk1, Pl... | REMOVE | Summary: IPI with mouse Tp53bp1/53BP1, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:20126263 We show that Plk1 binds 53BP1 during mitosis and that this interaction is required for proper inactivation of the DNA damage checkpoint. |
| GO:0005515 protein binding | IPI PMID:20126263 A mitotic phosphorylation feedback network connects Cdk1, Pl... | REMOVE | Summary: IPI with TP53BP1/53BP1, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:20126263 We show that Plk1 binds 53BP1 during mitosis and that this interaction is required for proper inactivation of the DNA damage checkpoint. |
| GO:0005515 protein binding | IPI PMID:20360068 Systematic analysis of human protein complexes identifies ch... | REMOVE | Summary: IPI with ERCC6L/PICH from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:20360068 the MitoCheck consortium has analyzed about 100 human protein complexes |
| GO:0005515 protein binding | IPI PMID:20534861 Polo-like kinase 1 is involved in hepatitis C virus replicat... | REMOVE | Summary: IPI with HCV NS5A; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:20534861 Plk1 could be immunoprecipitated together with NS5A. |
| GO:0005515 protein binding | IPI PMID:20577264 Polo-like kinase 1 phosphorylation of G2 and S-phase-express... | REMOVE | Summary: IPI with GTSE1, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:20577264 Plk1 phosphorylation of GTSE1 at Ser 435 promotes its nuclear localization |
| GO:0005515 protein binding | IPI PMID:20679239 Polo-like kinase 1 phosphorylation of p150Glued facilitates ... | REMOVE | Summary: IPI with DCTN1/p150Glued, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:20679239 Plk1 interacts with and phosphoryates p150(Glued) during NEBD at prophase. |
| GO:0005515 protein binding | IPI PMID:20890306 Phosphorylation by polo-like kinase 1 induces the tumor-supp... | REMOVE | Summary: IPI with FADD, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:20890306 Plk1 phosphorylates FADD at Ser-194 in response to treatment with taxol. |
| GO:0005515 protein binding | IPI PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kina... | REMOVE | Summary: IPI with CDC6, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:21041660 Binding between Cdc6 and Plk1 occurs through the polo-box domain of Plk1, and Cdc6 is phosphorylated by Plk1 on T37. |
| GO:0005515 protein binding | IPI PMID:21642957 Nek9 is a Plk1-activated kinase that controls early centroso... | REMOVE | Summary: IPI with NEK9, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:21642957 We now identify Plk1 as Nek9 direct activator |
| GO:0005515 protein binding | IPI PMID:21880710 Phosphorylation of right open reading frame 2 (Rio2) protein... | REMOVE | Summary: IPI with RIOK2, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:21880710 Rio2 is a novel substrate of Plk1 |
| GO:0005515 protein binding | IPI PMID:21887822 Proteomic identification of Hsp70 as a new Plk1 substrate in... | REMOVE | Summary: IPI with EIF4B; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:21887822 we identified Hsp70, Rad 23B, and eukaryotic translation initiation factor 4B as potentially new substrates of polo-like kinase 1 (Plk1) |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: IPI with OFD1 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:21988832 establish a human liver protein interaction network (HLPN) composed of 3484 interactions among 2582 proteins |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: IPI with PHC2 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:21988832 establish a human liver protein interaction network (HLPN) composed of 3484 interactions among 2582 proteins |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: IPI with TANK from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:21988832 establish a human liver protein interaction network (HLPN) composed of 3484 interactions among 2582 proteins |
| GO:0005515 protein binding | IPI PMID:22609948 Identification of a novel Wnt5a-CK1Ι-Dvl2-Plk1-mediated prim... | MODIFY | Summary: IPI with DVL2: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on DVL2. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:22609948 Dvl2 is phosphorylated at S143 and T224 in a manner that requires both non-canonical Wnt5a ligand and casein kinase 1 epsilon (CK1Ι), and that this event is critical to interact with Plk1 |
| GO:0005515 protein binding | IPI PMID:22609948 Identification of a novel Wnt5a-CK1Ι-Dvl2-Plk1-mediated prim... | MODIFY | Summary: IPI with mouse Dvl2: the interaction is mediated by the PLK1 polo-box domain binding a phosphorylated (CDK1- or self-primed) docking motif on mouse Dvl2. Reason: Generic 'protein binding' is uninformative, but this paper demonstrates the defining molecular activity of the PLK1 polo-box domain: phospho-dependent recognition of a Ser-[pSer/pThr]-Pro/X docking motif. 'phosphoprotein binding' captures that evidence-backed function. Proposed replacements: phosphoprotein binding Supporting Evidence: PMID:22609948 Dvl2 is phosphorylated at S143 and T224 in a manner that requires both non-canonical Wnt5a ligand and casein kinase 1 epsilon (CK1Ι), and that this event is critical to interact with Plk1 |
| GO:0005515 protein binding | IPI PMID:22653443 Mutant p53 interactome identifies nardilysin as a p53R273H-s... | REMOVE | Summary: IPI with TP53 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:22653443 Here we analyze the p53R273H interactome using stable isotope labelling by amino acids in cell culture and quantitative mass spectrometry |
| GO:0005515 protein binding | IPI PMID:23036704 A novel big protein TPRBK possessing 25 units of TPR motif i... | REMOVE | Summary: IPI with AURKB; the reported interaction is incidental to PLK1 function or its functional significance is not established in the cited work. Reason: Generic 'protein binding' is uninformative and the paper does not support a more specific molecular function for PLK1. Removal does not imply the interaction is false. Supporting Evidence: PMID:23036704 A novel big protein TPRBK possessing 25 units of TPR motif is essential for the progress of mitosis and cytokinesis. |
| GO:0005515 protein binding | IPI PMID:23455478 Ubiquitylation-dependent localization of PLK1 in mitosis. | REMOVE | Summary: IPI with KLHL22, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:23455478 we identify PLK1 as a target of the cullin 3 (CUL3)-based E3 ubiquitin ligase, containing the BTB adaptor KLHL22 |
| GO:0005515 protein binding | IPI PMID:23509069 MISP is a novel Plk1 substrate required for proper spindle o... | REMOVE | Summary: IPI with MISP, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:23509069 MISP (C19orf21), as a substrate of Plk1 |
| GO:0005515 protein binding | IPI PMID:25503564 Degradation of Cep68 and PCNT cleavage mediate Cep215 remova... | REMOVE | Summary: IPI with CEP68, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:25503564 Cep68 degradation is initiated by PLK1 phosphorylation |
| GO:0005515 protein binding | IPI PMID:25852190 Integrative analysis of kinase networks in TRAIL-induced apo... | REMOVE | Summary: IPI with SLX4 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:25852190 Integrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapy. |
| GO:0005515 protein binding | IPI PMID:25986610 Phosphorylation of SAF-A/hnRNP-U Serine 59 by Polo-Like Kina... | REMOVE | Summary: IPI with HNRNPU/SAF-A, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:25986610 SAF-A is phosphorylated on serine 59 in mitosis, that phosphorylation requires polo-like kinase 1 (PLK1) rather than DNA-PKcs, that SAF-A interacts with PLK1 in nocodazole-treated cells |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: IPI with EVI5 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:26496610 we have generated a library of HeLa cell lines expressing 1,125 GFP-tagged proteins under near-endogenous control |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: IPI with ERCC6L/PICH from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:26496610 we have generated a library of HeLa cell lines expressing 1,125 GFP-tagged proteins under near-endogenous control |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: IPI with BIRC6/BRUCE from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:26496610 we have generated a library of HeLa cell lines expressing 1,125 GFP-tagged proteins under near-endogenous control |
| GO:0005515 protein binding | IPI PMID:26638075 A Dynamic Protein Interaction Landscape of the Human Centros... | REMOVE | Summary: IPI with OFD1 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:26638075 A Dynamic Protein Interaction Landscape of the Human Centrosome-Cilium Interface. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: IPI with MCM2 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:27173435 An organelle-specific protein landscape identifies novel diseases and molecular mechanisms. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: IPI with ERCC6L/PICH from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:28514442 Here we present BioPlex 2.0 (Biophysical Interactions of ORFeome-derived complexes) |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: IPI with BORA from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:28514442 Here we present BioPlex 2.0 (Biophysical Interactions of ORFeome-derived complexes) |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: IPI with Q5HYW2 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: IPI with C1orf198 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32707033 we present a comprehensive mass-spectrometry-based analysis of a human kinase interaction network covering more than 300 kinas |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: IPI with DVL2 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32707033 we present a comprehensive mass-spectrometry-based analysis of a human kinase interaction network covering more than 300 kinas |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: IPI with WEE1 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32707033 we present a comprehensive mass-spectrometry-based analysis of a human kinase interaction network covering more than 300 kinas |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: IPI with TP53BP1/53BP1 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32707033 we present a comprehensive mass-spectrometry-based analysis of a human kinase interaction network covering more than 300 kinas |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: IPI with BORA from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32707033 we present a comprehensive mass-spectrometry-based analysis of a human kinase interaction network covering more than 300 kinas |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: IPI with SLX4 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32707033 we present a comprehensive mass-spectrometry-based analysis of a human kinase interaction network covering more than 300 kinas |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with APP from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with PSEN1 isoform from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with CASP8 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with TGIF1 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: IPI with C1orf198 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins-half the proteome-in 293T cells |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: IPI with ERCC6L/PICH from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins-half the proteome-in 293T cells |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: IPI with BORA from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins-half the proteome-in 293T cells |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: IPI with TANK from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins-half the proteome-in 293T cells |
| GO:0005515 protein binding | IPI PMID:34260926 Feedback control of PLK1 by Apolo1 ensures accurate chromoso... | REMOVE | Summary: IPI with FIRRM/Apolo1, a PLK1 substrate or regulator characterized in this study. Reason: Generic 'protein binding' adds no functional information beyond the kinase-substrate (or activator-substrate) relationship already captured by the kinase-activity and process annotations. Removal does not imply the interaction is false. Supporting Evidence: PMID:34260926 Feedback control of PLK1 by Apolo1 ensures accurate chromosome segregation. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: IPI with ERCC6L/PICH from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:35271311 OpenCell: Endogenous tagging for the cartography of human cellular organization. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: IPI with BORA from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:35271311 OpenCell: Endogenous tagging for the cartography of human cellular organization. |
| GO:0005515 protein binding | IPI PMID:36931259 A central chaperone-like role for 14-3-3 proteins in human c... | REMOVE | Summary: IPI with YWHAE (14-3-3 epsilon) from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:36931259 A central chaperone-like role for 14-3-3 proteins in human cells. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: IPI with DVL2 from a high-throughput interactome or proteomic screen. Reason: Uninformative generic binding term from a proteome-scale screen; no PLK1-specific functional insight. Removal does not imply the interaction is false. Supporting Evidence: PMID:40205054 Multimodal cell maps as a foundation for structural and functional genomics. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro protein-kinase domain mapping; PLK1 binds ATP in its N-terminal catalytic domain. Reason: Intrinsic to kinase activity; supported by the AMPPNP-bound crystal structure (PMID:17461553). |
| GO:0005524 ATP binding | IMP PMID:17461553 Structure of the catalytic domain of human polo-like kinase ... | ACCEPT | Summary: AMPPNP-bound kinase domain structure defines the ATP-binding pocket of PLK1. Reason: Directly supported by the crystal structure with an ATP analogue. Supporting Evidence: PMID:17461553 complexed with the nonhydrolyzable ATP analogue adenylylimidodiphosphate (AMPPNP) |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of nuclear localization across Polo kinases. Reason: PLK1 accumulates in the nucleus in G2 (Bora-dependent NLS exposure) where it acts on CDC25C, WEE1, cyclin B1 and FOXM1 before nuclear envelope breakdown. |
| GO:0005634 nucleus | IDA PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote check... | ACCEPT | Summary: Nuclear PLK1 in G2 cells promotes mitotic entry after checkpoint arrest. Reason: Nuclear accumulation of PLK1 in G2 is well established. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location 'Nucleus'. Reason: Consistent. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-156673 | ACCEPT | Summary: Reactome places this PLK1 reaction (Regulation of KIF23 (MKLP1) by phosphorylation) in the nucleoplasm. Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-156699 | ACCEPT | Summary: Reactome places this PLK1 reaction (Inactivation of Wee1 kinase) in the nucleoplasm. Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-156723 | ACCEPT | Summary: Reactome places this PLK1 reaction (Regulation of KIF20A (MKL2) by phosphorylation) in the nucleoplasm. Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-162657 | ACCEPT | Summary: Reactome places this PLK1 reaction (Inactivation of Myt1 kinase) in the nucleoplasm. Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-163010 | ACCEPT | Summary: Reactome places this PLK1 reaction (Down Regulation of Emi1 through Phosphorylation of Emi1) in the nucleoplasm. Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-174119 | ACCEPT | Summary: Reactome places this PLK1 reaction (Free APC/C phosphorylated by Plk1) in the nucleoplasm. Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-174174 | ACCEPT | Summary: Reactome places this PLK1 reaction (Phosphorylation of the Emi1 DSGxxS degron by Plk1) in the nucleoplasm. Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2294580 | ACCEPT | Summary: Reactome places this PLK1 reaction (PLK1 hyperphosphorylates Condensin II complex) in the nucleoplasm. Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2294590 | ACCEPT | Summary: Reactome 'PLK1 binds phosphorylated condensin II complex' in the nucleoplasm. Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3002798 | ACCEPT | Summary: Reactome 'Cytosolic PLK1 translocates to the nucleus'. Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3002811 | ACCEPT | Summary: Reactome 'Myosin phosphatase dephosphorylates PLK1' (nucleoplasm). Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4088130 | ACCEPT | Summary: Reactome 'PLK1 binds FOXM1' (nucleoplasm). Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4088134 | ACCEPT | Summary: Reactome 'PLK1 phosphorylates FOXM1' (nucleoplasm). Reason: PLK1 enters the nucleus in G2 and acts on nuclear substrates (WEE1, CDC25C, PKMYT1 pathway, EMI1, FOXM1, condensin II); nucleoplasm is an appropriate compartment for these reactions. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of cytoplasmic localization. Reason: PLK1 is cytoplasmic in interphase and acts on cytoplasmic structures (centrosomes, spindle, midbody) in mitosis. |
| GO:0005813 centrosome | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of centrosome localization (fly polo, mouse Plk1, worm plk-1, human PLK1). Reason: Centrosome localization is conserved and experimentally established for human PLK1. |
| GO:0005813 centrosome | IDA GO_REF:0000054 | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. Localization of expressed fusion proteins in living cells. Reason: Centrosome localization is among the best-established features of PLK1. Core location. |
| GO:0005813 centrosome | IDA PMID:12524548 Active cyclin B1-Cdk1 first appears on centrosomes in propha... | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. Reason: Centrosome localization is among the best-established features of PLK1. Core location. Supporting Evidence: PMID:12524548 cyclin B1 is initially phosphorylated on centrosomes in prophase and that Plk1 phosphorylates cyclin B1 |
| GO:0005813 centrosome | IDA PMID:18477460 Myosin phosphatase-targeting subunit 1 regulates mitosis by ... | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. Reason: Centrosome localization is among the best-established features of PLK1. Core location. Supporting Evidence: PMID:18477460 Depletion of PLK1 by small interfering RNAs is known to result in loss of gamma-tubulin recruitment to the centrosomes |
| GO:0005813 centrosome | IDA PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote check... | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. Reason: Centrosome localization is among the best-established features of PLK1. Core location. Supporting Evidence: PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery. |
| GO:0005813 centrosome | IDA PMID:18940925 Hec1 overexpression hyperactivates the mitotic checkpoint an... | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. The cached abstract of this Hec1 paper does not mention PLK1; the localization is accepted on the strength of the wider literature. Reason: Centrosome localization is among the best-established features of PLK1. Core location. Supporting Evidence: PMID:18940925 Hec1 overexpression hyperactivates the mitotic checkpoint and induces tumor formation in vivo. |
| GO:0005813 centrosome | IDA PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kina... | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. Reason: Centrosome localization is among the best-established features of PLK1. Core location. Supporting Evidence: PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kinase 1 |
| GO:0005813 centrosome | IDA PMID:21399614 Novel asymmetrically localizing components of human centroso... | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. Proteomic/BAC-GFP definition of the centrosome proteome. Reason: Centrosome localization is among the best-established features of PLK1. Core location. Supporting Evidence: PMID:21399614 we distinguished 126 known and 40 candidate centrosomal proteins |
| GO:0005813 centrosome | IDA PMID:23455478 Ubiquitylation-dependent localization of PLK1 in mitosis. | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. Reason: Centrosome localization is among the best-established features of PLK1. Core location. Supporting Evidence: PMID:23455478 Polo-like kinase 1 (PLK1) critically regulates mitosis through its dynamic localization to kinetochores, centrosomes and the midzone. |
| GO:0005813 centrosome | IDA PMID:24157919 Bod1 regulates protein phosphatase 2A at mitotic kinetochore... | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. Reason: Centrosome localization is among the best-established features of PLK1. Core location. Supporting Evidence: PMID:24157919 Bod1 regulates protein phosphatase 2A at mitotic kinetochores. |
| GO:0005813 centrosome | IDA PMID:27579920 Interactions of Prototype Foamy Virus Capsids with Host Cell... | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. Foamy-virus capsid study; PLK localization at centrosomes is incidental to the paper's aim but consistent with all other evidence. Reason: Centrosome localization is among the best-established features of PLK1. Core location. Supporting Evidence: PMID:27579920 At the centrosome of non-dividing cells PFV capsids can remain intact |
| GO:0005813 centrosome | IDA PMID:8991084 Antibody microinjection reveals an essential role for human ... | ACCEPT | Summary: PLK1 localizes to centrosomes from G2 through mitosis, recruited by CEP192/pericentrin, where it drives pericentriolar material expansion, gamma-tubulin recruitment and centrosome maturation. Reason: Centrosome localization is among the best-established features of PLK1. Core location. Supporting Evidence: PMID:8991084 Antibody microinjection reveals an essential role for human polo-like kinase 1 (Plk1) in the functional maturation of mitotic centrosomes. |
| GO:0005813 centrosome | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location keyword 'centrosome'. Reason: Consistent with extensive experimental evidence. |
| GO:0005814 centriole | IEA GO_REF:0000107 | ACCEPT | Summary: Centriole localization transferred from mouse; PLK1 acts on centrioles to trigger CEP68 degradation and early-mitotic centriole disengagement. Reason: Ensembl Compara transfer from mouse Plk1 (Q07832). Consistent with PLK1's centrosomal localization and its documented role in centriole disengagement (PMID:25503564). Supporting Evidence: PMID:25503564 Cep68 degradation is initiated by PLK1 phosphorylation |
| GO:0005819 spindle | IDA PMID:12939256 Phosphorylation of mitotic kinesin-like protein 2 by polo-li... | ACCEPT | Summary: PLK1 binds microtubules directly and targets the central spindle via its polo-box domain. Reason: Spindle localization is directly demonstrated. Supporting Evidence: PMID:12939256 Plk1 also binds directly to microtubules and targets to the central spindle via its polo box domain |
| GO:0005819 spindle | IDA PMID:17351640 Choice of Plk1 docking partners during mitosis and cytokines... | ACCEPT | Summary: PLK1 docks on PRC1 at the anaphase spindle midzone. Reason: Directly shown; PRC1 is an anaphase-specific docking partner. Supporting Evidence: PMID:17351640 the microtubule-associated protein regulating cytokinesis (PRC1) is an anaphase-specific binding partner for Plk1 |
| GO:0005819 spindle | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location keyword 'spindle'. Reason: Consistent with experimental evidence. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-141409 | ACCEPT | Summary: Reactome assigns the reaction 'Mad1 binds kinetochore' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-141422 | ACCEPT | Summary: Reactome assigns the reaction 'MAD2 converted to an inhibitory state via interaction with Mad1' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-141431 | ACCEPT | Summary: Reactome assigns the reaction 'MAD2 associates with the Mad1 kinetochore complex' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-141439 | ACCEPT | Summary: Reactome assigns the reaction 'Release of activated MAD2 from kinetochores' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-156678 | ACCEPT | Summary: Reactome assigns the reaction 'Activation of Cdc25C' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-156682 | ACCEPT | Summary: Reactome assigns the reaction 'PLK1 phosphorylates NUDC' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1638803 | ACCEPT | Summary: Reactome assigns the reaction 'Phosphorylation of cohesin by PLK1 at centromeres' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1638821 | ACCEPT | Summary: Reactome assigns the reaction 'PP2A-B56 dephosphorylates centromeric cohesin' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-174088 | ACCEPT | Summary: Reactome assigns the reaction 'Association of cell cycle proteins with the APC/C:Cdh1 complex' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-174105 | ACCEPT | Summary: Reactome assigns the reaction 'Degradation of multiubiquitinated cell cycle proteins' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-174195 | ACCEPT | Summary: Reactome assigns the reaction 'Ubiquitination of cell cycle proteins targeted by the APC/C:Cdh1complex' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2214351 | ACCEPT | Summary: Reactome assigns the reaction 'PLK1 phosphorylates GORASP1' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2466068 | ACCEPT | Summary: Reactome assigns the reaction 'Phosphorylation of cohesin by PLK1 at chromosomal arms' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2467809 | ACCEPT | Summary: Reactome assigns the reaction 'ESPL1 (Separase) cleaves centromeric cohesin' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2467811 | ACCEPT | Summary: Reactome assigns the reaction 'Separation of sister chromatids' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2468287 | ACCEPT | Summary: Reactome assigns the reaction 'CDK1 phosphorylates CDCA5 (Sororin) at centromeres' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2484822 | ACCEPT | Summary: Reactome assigns the reaction 'Kinetochore assembly' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2562526 | ACCEPT | Summary: Reactome assigns the reaction 'PLK1 phosphorylates OPTN' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2574840 | ACCEPT | Summary: Reactome assigns the reaction 'AJUBA facilitates AURKA autophosphorylation' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2574845 | ACCEPT | Summary: Reactome assigns the reaction 'AJUBA binds centrosome-associated AURKA' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2984226 | ACCEPT | Summary: Reactome assigns the reaction 'PLK1 phosphorylates NEK9' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000310 | ACCEPT | Summary: Reactome assigns the reaction 'AURKA phosphorylates PLK1' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000319 | ACCEPT | Summary: Reactome assigns the reaction 'BORA binds PLK1 and AURKA' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000327 | ACCEPT | Summary: Reactome assigns the reaction 'PLK1 phosphorylates BORA' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3002798 | ACCEPT | Summary: Reactome assigns the reaction 'Cytosolic PLK1 translocates to the nucleus' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-375302 | ACCEPT | Summary: Reactome assigns the reaction 'Kinetochore capture of astral microtubules' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380272 | ACCEPT | Summary: Reactome assigns the reaction 'Plk1-mediated phosphorylation of Nlp' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380283 | ACCEPT | Summary: Reactome assigns the reaction 'Recruitment of additional gamma tubulin/ gamma TuRC to the centrosome' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380294 | ACCEPT | Summary: Reactome assigns the reaction 'Loss of C-Nap-1 from centrosomes' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380303 | ACCEPT | Summary: Reactome assigns the reaction 'Dissociation of Phospho-Nlp from the centrosome' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380311 | ACCEPT | Summary: Reactome assigns the reaction 'Recruitment of Plk1 to centrosomes' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380316 | ACCEPT | Summary: Reactome assigns the reaction 'Association of NuMA with microtubules' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380455 | ACCEPT | Summary: Reactome assigns the reaction 'Recruitment of CDK11p58 to the centrosomes' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380508 | ACCEPT | Summary: Reactome assigns the reaction 'Translocation of NuMA to the centrosomes' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4088305 | ACCEPT | Summary: Reactome assigns the reaction 'FOXM1 stimulates PLK1 transcription' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5617816 | ACCEPT | Summary: Reactome assigns the reaction 'RAB3IP stimulates nucleotide exchange on RAB8A' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626220 | ACCEPT | Summary: Reactome assigns the reaction 'C2CD3 binds the mother centriole' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626223 | ACCEPT | Summary: Reactome assigns the reaction 'C2CD3 and OFD1 recruit 5 distal appendage proteins to the centriole' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626227 | ACCEPT | Summary: Reactome assigns the reaction 'CP110 and CEP97 dissociate from the centriole' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626228 | ACCEPT | Summary: Reactome assigns the reaction 'The distal appendage proteins recruit TTBK2' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626681 | ACCEPT | Summary: Reactome assigns the reaction 'Recruitment of transition zone proteins' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626699 | ACCEPT | Summary: Reactome assigns the reaction 'MARK4 binds ODF2 in the centriole' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5638009 | ACCEPT | Summary: Reactome assigns the reaction 'CEP164 recruits RAB3IP-carrying Golgi-derived vesicles to the basal body' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5666129 | ACCEPT | Summary: Reactome assigns the reaction 'CDC42:GTP recruits DIAPH2-2 to kinetochores' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5666160 | ACCEPT | Summary: Reactome assigns the reaction 'AURKB phosphorylates DIAPH2-2 at kinetochores' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5666169 | ACCEPT | Summary: Reactome assigns the reaction 'Kinetochore capture of astral microtubules is positively regulated by CDC42:GTP:p-S196-DIAPH2-2' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8852317 | ACCEPT | Summary: Reactome assigns the reaction 'PLK1 phosphorylates GTSE1' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8852324 | ACCEPT | Summary: Reactome assigns the reaction 'GTSE1 binds PLK1' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853405 | ACCEPT | Summary: Reactome assigns the reaction 'TPX2 binds AURKA at centrosomes' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853419 | ACCEPT | Summary: Reactome assigns the reaction 'TPX2 promotes AURKA autophosphorylation' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9648114 | ACCEPT | Summary: Reactome assigns the reaction 'EML4 recruits NUDC to mitotic spindle' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9851946 | ACCEPT | Summary: Reactome assigns the reaction 'FIRRM binds PLK1' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9851972 | ACCEPT | Summary: Reactome assigns the reaction 'PLK1 phosphorylates FIRRM at S43' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9853369 | ACCEPT | Summary: Reactome assigns the reaction 'PLK1 phosphorylates FIRMM at S744' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9853385 | ACCEPT | Summary: Reactome assigns the reaction 'PPP1CC dephosphorylates PLK1' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9858636 | ACCEPT | Summary: Reactome assigns the reaction 'MITF-M-dependent PLK1 expression' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005829 cytosol | TAS Reactome:R-NUL-2423781 | ACCEPT | Summary: Reactome assigns the reaction 'PLK1 binds phosphorylated Gorasp1' to the cytosol; cytosolic PLK1 is the pool that acts on centrosomal, spindle, midzone and cytoplasmic substrates and is activated by AURKA/BORA before nuclear import. Reason: Generic compartment used by Reactome for cytoplasmic reactions; consistent with PLK1's cytoplasmic localization in interphase and during mitosis. Correct but uninformative relative to the centrosome, kinetochore, midzone and midbody annotations. |
| GO:0005876 spindle microtubule | IDA PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kina... | ACCEPT | Summary: Colocalization with spindle microtubules (with Cdc6 at the central spindle). Reason: Consistent with direct microtubule binding (PMID:12939256) and midzone localization. |
| GO:0006302 double-strand break repair | IDA PMID:22325354 Plk1 and CK2 act in concert to regulate Rad51 during DNA dou... | KEEP AS NON CORE | Summary: PLK1 phosphorylates RAD51 at Ser14, licensing CK2 phosphorylation of Thr13 and NBS1 binding, which facilitates RAD51 recruitment to DNA damage sites. Reason: A direct, mechanistically defined contribution to homologous-recombination repair, but a secondary role of a mitotic kinase; retained as non-core. Supporting Evidence: PMID:22325354 This mechanism facilitates Rad51 recruitment to damage sites, thus enhancing cellular resistance to genotoxic stresses. |
| GO:0006468 protein phosphorylation | IDA PMID:22701722 The centrosomal kinase Plk1 localizes to the transition zone... | ACCEPT | Summary: PLK1 localizes to the ciliary transition zone and phosphorylates nephrocystin-1 (NPHP1) in vitro. Reason: Generic process term that is trivially true for a protein kinase; retained (the ciliary context itself is peripheral). Supporting Evidence: PMID:22701722 demonstrated in vitro that Plk1 phosphorylates the nephrocystin N-terminus |
| GO:0007052 mitotic spindle organization | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference that Polo kinases organize the mitotic spindle; PLK1 promotes centrosome maturation (NEDD1, KIZ, pericentrin), centrosome separation (NEK9/EG5, MST2/NEK2A) and spindle bipolarity. Reason: Deeply conserved core function (monopolar spindles in polo, plo1 and PLK1 loss-of-function). Supporting Evidence: PMID:16980960 Polo-like kinase 1 (Plk1) is a highly conserved Ser/Thr kinase that has essential roles in the formation of a bipolar spindle with focused poles. |
| GO:0007052 mitotic spindle organization | TAS Reactome:R-HSA-9648025 | ACCEPT | Summary: Reactome 'EML4 and NUDC in mitotic spindle formation': PLK1 phosphorylates NUDC. Reason: Consistent with the core spindle-organization role. |
| GO:0007062 sister chromatid cohesion | TAS Reactome:R-HSA-1638803 | MODIFY | Summary: Reactome 'Phosphorylation of cohesin by PLK1 at centromeres': PLK1 phosphorylates STAG2/SA2 to promote cohesin release (prophase pathway); at centromeres this is counteracted by SGO1-PP2A. Reason: PLK1 phosphorylation of cohesin drives cohesin removal, i.e. it negatively regulates sister chromatid cohesion rather than establishing or maintaining it; 'sister chromatid cohesion' inverts the direction of PLK1's action. Proposed replacements: negative regulation of sister chromatid cohesion |
| GO:0007062 sister chromatid cohesion | TAS Reactome:R-HSA-2466068 | MODIFY | Summary: Reactome 'Phosphorylation of cohesin by PLK1 at chromosomal arms': PLK1-phosphorylated STAG2/SA2 cohesin is released from arms in prophase. Reason: As above: PLK1 dissolves arm cohesion; the appropriate term is negative regulation of sister chromatid cohesion. Proposed replacements: negative regulation of sister chromatid cohesion |
| GO:0007076 mitotic chromosome condensation | TAS Reactome:R-HSA-2299718 | ACCEPT | Summary: Reactome: PLK1 hyperphosphorylates the CDK1-primed condensin II complex during prophase chromosome condensation. Reason: Direct substrate relationship within the mitotic core function. |
| GO:0007077 mitotic nuclear membrane disassembly | TAS Reactome:R-HSA-2980766 | ACCEPT | Summary: Reactome 'Nuclear Envelope Breakdown': PLK1 phosphorylates DCTN1/p150Glued (and other targets) to promote NEBD. Reason: Supported by the IDA for positive regulation of mitotic nuclear envelope disassembly (PMID:20679239). |
| GO:0007091 metaphase/anaphase transition of mitotic cell cycle | TAS Reactome:R-HSA-68881 | ACCEPT | Summary: Reactome 'Mitotic Metaphase/Anaphase Transition': PLK1 phosphorylates EMI1 and APC/C to enable APC/C activation. Reason: Core function. |
| GO:0007094 mitotic spindle assembly checkpoint signaling | IMP PMID:23455478 Ubiquitylation-dependent localization of PLK1 in mitosis. | KEEP AS NON CORE | Summary: Failure to remove PLK1 from kinetochores (KLHL22 loss or PLK1-K492R) keeps the spindle assembly checkpoint active; PLK1 also cooperates with MPS1 at kinetochores. Reason: PLK1 contributes to SAC signaling (kinetochore MPS1/BUB1 pathway) and its timely removal is needed for SAC satisfaction; the IMP here reflects the latter. Retained as a genuine but non-core contribution. Supporting Evidence: PMID:23455478 CUL3-KLHL22-mediated ubiquitylation signals degradation-independent removal of PLK1 from kinetochores and SAC satisfaction, which are required for faithful mitosis. |
| GO:0007095 mitotic G2 DNA damage checkpoint signaling | IDA PMID:18662541 The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-respons... | MODIFY | Summary: In G2-damaged cells CDC14B activates APC/C-CDH1, which degrades PLK1; loss of PLK1 stabilizes CLASPIN and WEE1 and permits the G2 checkpoint. PLK1 is thus the antagonist that the checkpoint must remove, and it drives checkpoint recovery by phosphorylating CLASPIN and WEE1 for SCF(beta-TrCP) degradation. Reason: PLK1 does not execute G2 DNA-damage checkpoint signaling; it opposes and terminates it (PMID:18662541, PMID:16885022, PMID:20126263). 'involved_in mitotic G2 DNA damage checkpoint signaling' misrepresents the direction of its action. The better term is negative regulation of DNA damage checkpoint. Proposed replacements: negative regulation of DNA damage checkpoint Supporting Evidence: PMID:18662541 induces the activation of the ubiquitin ligase APC/C(Cdh1), with the consequent degradation of Plk1, a prominent mitotic kinase. This process induces the stabilization of Claspin, an activator of the DNA-damage checkpoint, and Wee1, an inhibitor of cell-cycle progression, and allows an efficient G2 checkpoint. PMID:16885022 Phosphorylation of Claspin is mediated by Plk1 and is essential for binding to betaTrCP. |
| GO:0007098 centrosome cycle | IMP PMID:18477460 Myosin phosphatase-targeting subunit 1 regulates mitosis by ... | ACCEPT | Summary: PLK1 is required for gamma-tubulin recruitment and centrosome maturation; MYPT1-PP1 antagonizes this by dephosphorylating PLK1 Thr210. Reason: Centrosome maturation/separation is a core PLK1 function; 'centrosome cycle' is the closest available process term (no dedicated 'centrosome maturation' term exists). Supporting Evidence: PMID:18477460 We found that codepletion of MYPT1 and PLK1 reinstates gamma-tubulin at the centrosomes, rescuing the mitotic arrest. |
| GO:0007098 centrosome cycle | IMP PMID:8991084 Antibody microinjection reveals an essential role for human ... | ACCEPT | Summary: Anti-PLK1 antibody microinjection blocks functional maturation of mitotic centrosomes and causes monoastral spindles. Reason: Founding evidence for PLK1's centrosome maturation role. Core function. Supporting Evidence: PMID:8991084 Antibody microinjection reveals an essential role for human polo-like kinase 1 (Plk1) in the functional maturation of mitotic centrosomes. |
| GO:0007346 regulation of mitotic cell cycle | IMP PMID:17495026 The tumor suppressor CYLD regulates entry into mitosis. | MODIFY | Summary: CYLD interacts with PLK1 and both are required for timely mitotic entry; PLK1 or CYLD depletion delays mitotic entry and CDC25C phosphorylation. Reason: 'regulation of mitotic cell cycle' is correct but too general. The phenotype and mechanism (PLK1-dependent CDC25C phosphorylation feeding CDK1-cyclin B activation) are specifically positive regulation of the G2/M transition. Proposed replacements: positive regulation of G2/M transition of mitotic cell cycle Supporting Evidence: PMID:17495026 cells depleted for CYLD or Plk1 delayed mitotic entry |
| GO:0008017 microtubule binding | IDA PMID:12939256 Phosphorylation of mitotic kinesin-like protein 2 by polo-li... | ACCEPT | Summary: PLK1 binds microtubules directly through its polo-box domain, contributing to its central-spindle targeting. Reason: Directly demonstrated; a supporting (non-core) molecular function. Supporting Evidence: PMID:12939256 Plk1 also binds directly to microtubules and targets to the central spindle via its polo box domain |
| GO:0010564 regulation of cell cycle process | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA 'regulation of cell cycle process'. Reason: Broad but correct. |
| GO:0010997 anaphase-promoting complex binding | IPI PMID:18662541 The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-respons... | MARK AS OVER ANNOTATED | Summary: PLK1 co-purifies with the APC/C activator CDH1/FZR1 in the context of APC/C-CDH1-mediated PLK1 degradation after DNA damage in G2. Reason: Here PLK1 is the substrate of APC/C-CDH1; binding reflects enzyme-substrate recognition and says nothing about a PLK1 function. PLK1 does phosphorylate APC/C subunits (Reactome R-HSA-174119), but that is captured under kinase activity, not by a binding term derived from its own degradation. Supporting Evidence: PMID:18662541 induces the activation of the ubiquitin ligase APC/C(Cdh1), with the consequent degradation of Plk1 |
| GO:0015630 microtubule cytoskeleton | IDA PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kina... | ACCEPT | Summary: Microtubule cytoskeleton localization. Reason: Generic parent of the spindle/midzone/centrosome localizations; correct. |
| GO:0019901 protein kinase binding | IPI PMID:12639966 Stk10, a new member of the polo-like kinase kinase family hi... | REMOVE | Summary: STK10/LOK, a Ste20-family kinase, phosphorylates PLK1 in vitro; the IPI records PLK1-STK10 interaction. Reason: 'protein kinase binding' here records PLK1 as a substrate of another kinase and adds no information about PLK1's own function; the generic binding annotation is uninformative (removal does not imply the interaction is false). Supporting Evidence: PMID:12639966 we investigated whether Stk10 might also play a role as a Plk1 activator. |
| GO:0019901 protein kinase binding | IPI PMID:18615013 Polo-like kinase-1 is activated by aurora A to promote check... | REMOVE | Summary: PLK1 binds AURKA (with BORA) which phosphorylates PLK1 Thr210 to activate it. Reason: PLK1 is the substrate of AURKA in this interaction; the binding term is uninformative about PLK1 function. The activation relationship is documented in UniProt and in the G2/M transition annotations. Supporting Evidence: PMID:18615013 aurora A can directly phosphorylate PLK1 on Thr 210, and that activity of aurora A towards PLK1 is greatly enhanced by Bora |
| GO:0030071 regulation of mitotic metaphase/anaphase transition | IDA PMID:23509069 MISP is a novel Plk1 substrate required for proper spindle o... | ACCEPT | Summary: MISP depletion impairs the metaphase-anaphase transition in a manner dependent on its phosphorylation by PLK1. Reason: PLK1 regulates the metaphase/anaphase transition via EMI1 degradation, APC/C phosphorylation and kinetochore substrates; MISP is one route. Supporting Evidence: PMID:23509069 MISP depletion led to an impaired metaphase-to-anaphase transition, which depended on phosphorylation by Plk1. |
| GO:0030071 regulation of mitotic metaphase/anaphase transition | IMP PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kina... | ACCEPT | Summary: PLK1 phosphorylates CDC6 Thr37, promoting CDC6-CDK1 binding, attenuation of CDK1 activity and separase release for anaphase. Reason: Consistent with PLK1's role at the metaphase/anaphase transition. Supporting Evidence: PMID:21041660 Plk1-mediated phosphorylation of Cdc6 promotes the interaction of Cdc6 and Cdk1, leading to the attenuation of Cdk1 activity, release of separase |
| GO:0030496 midbody | EXP PMID:30715179 Mutations in the microtubule-associated protein MAP11 (C7orf... | ACCEPT | Summary: MAP11 colocalizes with PLK1 at the midbody. Reason: Midbody localization of PLK1 in late cytokinesis is well established. Supporting Evidence: PMID:30715179 abscission at the midbody and is co-localized with PLK1 |
| GO:0030496 midbody | IDA PMID:19468300 Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ec... | ACCEPT | Summary: PLK1 at the midbody/central spindle during cytokinesis. Reason: Well established. |
| GO:0030496 midbody | IDA PMID:41361016 ANKLE1 processes chromatin bridges by cleaving mechanically ... | ACCEPT | Summary: ANKLE1 at the midbody is flanked by PLK1 and CEP55 staining. Reason: Consistent with midbody localization. Supporting Evidence: PMID:41361016 flanked by PLK1 and CEP55 staining |
| GO:0030496 midbody | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location 'Midbody'. Reason: Consistent. |
| GO:0030953 astral microtubule organization | IDA PMID:23509069 MISP is a novel Plk1 substrate required for proper spindle o... | KEEP AS NON CORE | Summary: PLK1 phosphorylates the cortical actin-associated protein MISP; MISP loss shortens astral microtubules and misorients the spindle. Reason: Spindle positioning via MISP (and via LRRK1/CDK5RAP2, PMID:26192437) is a documented but secondary output; retained as non-core. Supporting Evidence: PMID:23509069 Loss of MISP induced mitotic defects including spindle misorientation accompanied by shortened astral microtubules. |
| GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process | IMP PMID:19473992 Plk1-mediated phosphorylation of Topors regulates p53 stabil... | KEEP AS NON CORE | Summary: PLK1 phosphorylates TOPORS Ser718, suppressing TOPORS-mediated p53 sumoylation and enhancing p53 ubiquitination and degradation. Reason: Direct evidence, but the p53-antagonising role (also via MDM2 Ser260 and GTSE1) is a secondary function linked to checkpoint recovery and tumorigenesis rather than the mitotic core. Supporting Evidence: PMID:19473992 Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. |
| GO:0032465 regulation of cytokinesis | IDA PMID:17351640 Choice of Plk1 docking partners during mitosis and cytokines... | ACCEPT | Summary: PLK1 creates its own PRC1 docking site in anaphase; PRC1-PLK1 interaction is required for cytokinesis. Reason: Core cytokinesis function. Supporting Evidence: PMID:17351640 PRC1) is an anaphase-specific binding partner for Plk1, and that this interaction is required for cytokinesis. |
| GO:0032465 regulation of cytokinesis | IMP PMID:12939256 Phosphorylation of mitotic kinesin-like protein 2 by polo-li... | ACCEPT | Summary: An antibody blocking PLK1 phosphorylation of MKlp2 causes a cytokinesis defect. Reason: Core cytokinesis function. Supporting Evidence: PMID:12939256 An antibody to the neck region of MKlp2 that prevents phosphorylation of MKlp2 by Plk1 causes a cytokinesis defect when introduced into cells. |
| GO:0034451 centriolar satellite | IEA GO_REF:0000107 | UNDECIDED | Summary: Centriolar satellite localization transferred from a mouse Plk1 experimental annotation whose source publication is not among the cached references. Reason: PLK1 is a pericentriolar/centrosomal kinase, but a specific centriolar-satellite localization is not documented in any of the human references reviewed here and the mouse source paper could not be examined; left undecided rather than accepted or removed. |
| GO:0042802 identical protein binding | IPI PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kina... | REMOVE | Summary: Identical protein binding (PLK1 self-association) recorded from the Cdc6 substrate study. Reason: PLK1 can dimerize (BORA promotes dimerization), but 'identical protein binding' conveys no functional information and the cited paper is not about PLK1 oligomerization; removed as uninformative, without implying the interaction is false. |
| GO:0042802 identical protein binding | IPI PMID:23354166 Centrobin controls mother-daughter centriole asymmetry in Dr... | REMOVE | Summary: Identical protein binding (PLK1 self-association) recorded from the Drosophila Centrobin/POLO study. Reason: PLK1 can dimerize (BORA promotes dimerization), but 'identical protein binding' conveys no functional information and the cited paper is not about PLK1 oligomerization; removed as uninformative, without implying the interaction is false. |
| GO:0042802 identical protein binding | IPI PMID:26192437 PLK1-dependent activation of LRRK1 regulates spindle orienta... | REMOVE | Summary: Identical protein binding (PLK1 self-association) recorded from the LRRK1/CDK5RAP2 spindle-orientation study. Reason: PLK1 can dimerize (BORA promotes dimerization), but 'identical protein binding' conveys no functional information and the cited paper is not about PLK1 oligomerization; removed as uninformative, without implying the interaction is false. |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:18174154 Inhibitory role of Plk1 in the regulation of p73-dependent a... | MARK AS OVER ANNOTATED | Summary: PLK1 phosphorylates p73 Thr27 to inhibit its pro-apoptotic activity; PLK1 knockdown in p53-null cells increases sub-G1 cells. Reason: Suppression of p73-dependent apoptosis is a downstream consequence of one substrate phosphorylation; as for CDK1, treating apoptosis regulation as a PLK1 process function over-interprets substrate data. Kept flagged rather than removed since the mechanism is direct. Supporting Evidence: PMID:18174154 Plk1 (polo-like kinase 1) associates with p73, phosphorylates p73 at Thr-27, and thereby inhibits its pro-apoptotic activity. |
| GO:0045184 establishment of protein localization | IMP PMID:18331714 sSgo1, a major splice variant of Sgo1, functions in centriol... | MODIFY | Summary: Spindle-pole/centrosome localization of the sSgo1 splice variant depends on PLK1. Reason: 'establishment of protein localization' is uninformatively broad; the finding is PLK1-dependent localization of sSgo1 to centrosomes/spindle poles, best captured by protein localization to centrosome. Proposed replacements: protein localization to centrosome Supporting Evidence: PMID:18331714 sSgo1 interacts with Plk1 and its spindle pole localization is Plk1 dependent. |
| GO:0045842 positive regulation of mitotic metaphase/anaphase transition | IDA PMID:15148369 Role of Polo-like kinase in the degradation of early mitotic... | ACCEPT | Summary: PLK1 phosphorylates the EMI1 DSGxxS degron, enabling SCF(beta-TrCP)-mediated EMI1 degradation and hence APC/C activation at prometaphase. Reason: A direct, core mechanism by which PLK1 promotes the metaphase/anaphase transition. Supporting Evidence: PMID:15148369 The degradation of Emi1 in early mitosis is necessary for the activation of APC/C in late mitosis. |
| GO:0048313 Golgi inheritance | TAS Reactome:R-HSA-162658 | KEEP AS NON CORE | Summary: Reactome 'Golgi Cisternae Pericentriolar Stack Reorganization': PLK1 phosphorylates GORASP1/GRASP65 to promote mitotic Golgi fragmentation. Reason: A documented mitotic substrate relationship, but organelle inheritance is a peripheral output of the mitotic kinase. |
| GO:0051233 spindle midzone | IDA PMID:19468302 Plk1 self-organization and priming phosphorylation of HsCYK-... | ACCEPT | Summary: PLK1 delivers itself to the spindle midzone in anaphase (via PRC1/KIF20A docking) and phosphorylates RACGAP1 there. Reason: Midzone localization is core to PLK1's cytokinesis function. Supporting Evidence: PMID:19468302 Plk1 binds and directly phosphorylates the HsCYK-4 subunit of centralspindlin (also known as MgcRacGAP) at the midzone. |
| GO:0051233 spindle midzone | IDA PMID:21041660 Cell division cycle 6, a mitotic substrate of polo-like kina... | ACCEPT | Summary: PLK1 and Cdc6 colocalize at the central spindle in anaphase. Reason: Directly observed. Supporting Evidence: PMID:21041660 Cdc6 and Plk1 colocalize to the central spindle in anaphase. |
| GO:0051726 regulation of cell cycle | TAS Reactome:R-HSA-156678 | ACCEPT | Summary: Reactome 'Activation of Cdc25C' by PLK1. Reason: Generic term; correct. |
| GO:0051726 regulation of cell cycle | TAS Reactome:R-HSA-156699 | ACCEPT | Summary: Reactome 'Inactivation of Wee1 kinase' by PLK1 phosphorylation. Reason: Generic term; correct. |
| GO:0051726 regulation of cell cycle | TAS Reactome:R-HSA-162657 | ACCEPT | Summary: Reactome 'Inactivation of Myt1 kinase' by PLK1. Reason: Generic term; correct. |
| GO:0071168 protein localization to chromatin | IDA PMID:21111234 Sororin mediates sister chromatid cohesion by antagonizing W... | UNDECIDED | Summary: Annotation to 'protein localization to chromatin' from the Sororin/WAPL cohesion study; the cached record is abstract-only and does not mention PLK1. Reason: The full text (in which PLK1 presumably features in cohesin/Sororin phosphorylation experiments) is not available in the cache, so the specific claim cannot be evaluated; left undecided per the rule against overruling curators from incomplete evidence. |
| GO:0097431 mitotic spindle pole | IEA GO_REF:0000107 | ACCEPT | Summary: Mitotic spindle pole localization transferred from mouse. Reason: Ensembl Compara transfer from mouse Plk1 (Q07832). Consistent with human data. |
| GO:0097681 double-strand break repair via alternative nonhomologous end joining | IDA PMID:37440612 RHINO directs MMEJ to repair DNA breaks in mitosis. | KEEP AS NON CORE | Summary: PLK1 phosphorylates RHNO1/RHINO in mitosis, enabling its interaction with POLQ and recruitment of Pol-theta to DSBs for microhomology-mediated end joining. Reason: Genuine and direct role in mitotic MMEJ, but a specialised extension of the mitotic kinase function rather than a core activity. Supporting Evidence: PMID:37440612 RHINO accumulates in M phase, undergoes Polo-like kinase 1 (PLK1) phosphorylation, and interacts with polymerase ΞΈ (PolΞΈ), enabling its recruitment to DSBs for subsequent repair. |
| GO:0097681 double-strand break repair via alternative nonhomologous end joining | IDA PMID:37674080 PolΞΈ is phosphorylated by PLK1 to repair double-strand break... | KEEP AS NON CORE | Summary: PLK1 phosphorylates Pol-theta (POLQ) in mitosis, which is required for its recruitment to DSBs and mitotic MMEJ. Reason: Direct evidence, but a non-core DNA-repair role of the mitotic kinase. Supporting Evidence: PMID:37674080 PolΞΈ is phosphorylated by PLK1 to repair double-strand breaks in mitosis. |
| GO:0106310 protein serine kinase activity | EXP PMID:11202906 The human polo-like kinase, PLK, regulates cdc2/cyclin B thr... | ACCEPT | Summary: PLK1 phosphorylates and activates CDC25C on serine. Protein serine kinase activity is a child of Ser/Thr kinase activity and is directly supported. Reason: Direct serine-phosphorylation evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:11202906 The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase. |
| GO:0106310 protein serine kinase activity | EXP PMID:12207013 Phosphorylation of threonine 210 and the role of serine 137 ... | ACCEPT | Summary: Regulation of PLK1 kinase activity by Thr210 phosphorylation (and the Ser137 site); activating T210D/S137D mutants elevate activity toward substrates. Reason: Supports the catalytic activity and its activation-loop control. Supporting Evidence: PMID:12207013 Thr-210 is a major phosphorylation site in activated Plk from mitotic HeLa cells. |
| GO:0106310 protein serine kinase activity | EXP PMID:21880710 Phosphorylation of right open reading frame 2 (Rio2) protein... | ACCEPT | Summary: PLK1 phosphorylates RIOK2 at Ser335, Ser380 and Ser548, regulating metaphase-anaphase progression on serine. Protein serine kinase activity is a child of Ser/Thr kinase activity and is directly supported. Reason: Direct serine-phosphorylation evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:21880710 Rio2 is a novel substrate of Plk1 and can be phosphorylated by Plk1 at Ser-335, Ser-380, and Ser-548. |
| GO:0106310 protein serine kinase activity | EXP PMID:22325354 Plk1 and CK2 act in concert to regulate Rad51 during DNA dou... | ACCEPT | Summary: PLK1 phosphorylates RAD51 Ser14 on serine. Protein serine kinase activity is a child of Ser/Thr kinase activity and is directly supported. Reason: Direct serine-phosphorylation evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:22325354 phosphorylates the essential Rad51 recombinase at serine 14 (S14) |
| GO:0106310 protein serine kinase activity | EXP PMID:28512243 Plk1 Phosphorylation of Mre11 Antagonizes the DNA Damage Res... | ACCEPT | Summary: PLK1 phosphorylates MRE11 Ser649 on serine. Protein serine kinase activity is a child of Ser/Thr kinase activity and is directly supported. Reason: Direct serine-phosphorylation evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:28512243 Plk1 phosphorylated Mre11, a component of the Mre11/Rad50/Nbs1 (MRN) complex, at serine 649 (S649) during DDR. |
| GO:0106310 protein serine kinase activity | EXP PMID:37440612 RHINO directs MMEJ to repair DNA breaks in mitosis. | ACCEPT | Summary: PLK1 phosphorylates RHNO1/RHINO in mitosis on serine. Protein serine kinase activity is a child of Ser/Thr kinase activity and is directly supported. Reason: Direct serine-phosphorylation evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:37440612 RHINO accumulates in M phase, undergoes Polo-like kinase 1 (PLK1) phosphorylation |
| GO:0106310 protein serine kinase activity | EXP PMID:37674080 PolΞΈ is phosphorylated by PLK1 to repair double-strand break... | ACCEPT | Summary: PLK1 phosphorylates POLQ/Pol-theta in mitosis on serine. Protein serine kinase activity is a child of Ser/Thr kinase activity and is directly supported. Reason: Direct serine-phosphorylation evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:37674080 PolΞΈ is phosphorylated by PLK1 to repair double-strand breaks in mitosis. |
| GO:0106310 protein serine kinase activity | IDA PMID:21723128 Plk1 controls the Nek2A-PP1Ξ³ antagonism in centrosome disjun... | ACCEPT | Summary: PLK1 phosphorylates MST2/STK3, preventing PP1gamma binding and licensing NEK2A-driven centrosome disjunction on serine. Protein serine kinase activity is a child of Ser/Thr kinase activity and is directly supported. Reason: Direct serine-phosphorylation evidence toward a physiological substrate; core molecular function. Supporting Evidence: PMID:21723128 Plk1 regulates Mst2-Nek2A-induced centrosome disjunction by phosphorylating Mst2. |
| GO:0106310 protein serine kinase activity | IEA GO_REF:0000116 | ACCEPT | Summary: Rhea reaction RHEA:17989 (protein L-serine phosphorylation). Reason: Consistent with EC 2.7.11.21. |
| GO:1900182 positive regulation of protein localization to nucleus | TAS Reactome:R-HSA-8852317 | KEEP AS NON CORE | Summary: Reactome: PLK1 phosphorylates GTSE1 Ser435, promoting GTSE1 nuclear localization and p53 nuclear export during G2 checkpoint recovery. Reason: Direct but secondary (p53 axis during checkpoint recovery). Supporting Evidence: PMID:20577264 Plk1 phosphorylation of GTSE1 at Ser 435 promotes its nuclear localization |
| GO:1901673 regulation of mitotic spindle assembly | IDA PMID:22621898 Plk1 negatively regulates PRC1 to prevent premature midzone ... | ACCEPT | Summary: PLK1 phosphorylates PRC1 at Thr602 before anaphase to suppress premature midzone (antiparallel bundle) assembly; PLK1 inhibition causes midzones to form in metaphase. Reason: Direct, site-specific regulation of spindle microtubule organization by PLK1. Core spindle function. Supporting Evidence: PMID:22621898 We found that Plk1 negatively regulates PRC1 through phosphorylation of a single site, Thr-602, near the C-terminus of PRC1. |
| GO:1901990 regulation of mitotic cell cycle phase transition | TAS Reactome:R-HSA-176412 | ACCEPT | Summary: Reactome 'Phosphorylation of the APC/C': PLK1 (with CDK1) phosphorylates APC/C to promote CDC20 binding. Reason: Consistent with core mitotic-exit function. |
| GO:1903673 mitotic cleavage furrow formation | IDA PMID:19468300 Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ec... | ACCEPT | Summary: PLK1 phosphorylation of RACGAP1/HsCyk-4 creates the ECT2 BRCT docking epitope required for central-spindle ECT2 recruitment and furrow induction. Reason: Directly demonstrated; core cytokinesis function. Supporting Evidence: PMID:19468300 Failure to phosphorylate HsCyk-4 blocks Ect2 recruitment to the central spindle and the subsequent induction of furrowing. |
| GO:1904776 regulation of protein localization to cell cortex | IDA PMID:23509069 MISP is a novel Plk1 substrate required for proper spindle o... | MARK AS OVER ANNOTATED | Summary: PLK1-phosphorylated MISP regulates the cortical distribution of p150Glued/dynactin. Reason: Two steps removed from PLK1 (PLK1 -> MISP -> p150Glued cortical distribution); the regulatory claim belongs to MISP. The PLK1 contribution is adequately captured by astral microtubule organization. Supporting Evidence: PMID:23509069 MISP formed a complex with and regulated the cortical distribution of the +TIP binding protein p150(glued) |
| GO:1905559 positive regulation of mitotic nuclear envelope disassembly | IDA PMID:20679239 Polo-like kinase 1 phosphorylation of p150Glued facilitates ... | ACCEPT | Summary: PLK1 phosphorylates p150Glued/DCTN1 Ser179 at the nuclear envelope in prophase; the non-phosphorylatable mutant reduces NEBD and arrests cells in G2. Reason: Direct, site-specific evidence for PLK1 promoting NEBD as part of mitotic entry. Supporting Evidence: PMID:20679239 Plk1-mediated phosphorylation of p150(Glued) at Ser-179 positively regulates its accumulation at the nuclear envelope during prophase. |
| GO:1905784 regulation of anaphase-promoting complex-dependent catabolic process | TAS Reactome:R-HSA-176408 | ACCEPT | Summary: Reactome: PLK1 phosphorylates EMI1 and APC/C subunits, regulating APC/C-dependent degradation. Reason: Core function. |
| GO:2000042 negative regulation of double-strand break repair via homologous recombination | IDA PMID:28512243 Plk1 Phosphorylation of Mre11 Antagonizes the DNA Damage Res... | KEEP AS NON CORE | Summary: PLK1 phosphorylates MRE11 Ser649 (priming CK2 at Ser688), which inhibits MRN loading onto damaged DNA and thereby suppresses HR repair and terminates the checkpoint. Reason: Direct and specific, but part of PLK1's checkpoint-recovery/DDR-antagonising role rather than its core mitotic function. Supporting Evidence: PMID:28512243 Phosphorylation of Mre11 at S649/S688 inhibited loading of the MRN complex to damaged DNA, leading to both premature DNA damage checkpoint termination and inhibition of DNA repair. |
| GO:2000060 positive regulation of ubiquitin-dependent protein catabolic process | IDA PMID:16885022 SCFbetaTrCP-mediated degradation of Claspin regulates recove... | ACCEPT | Summary: PLK1 phosphorylates the CLASPIN DSGxxS degron, which is essential for beta-TrCP binding and SCF-mediated ubiquitylation during replication-checkpoint recovery. Reason: Phosphodegron priming for SCF(beta-TrCP) is a signature mechanism of PLK1 shared by WEE1, EMI1, BORA, CLASPIN, CEP68 and HSF1; this is how PLK1 executes several core functions, so the term is accepted. Supporting Evidence: PMID:16885022 In vitro ubiquitylation of Claspin requires betaTrCP, Plk1, and an intact DSGxxS degron. |
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Download this section (compressed HTML)Q: Which PLK1 outputs at kinetochores are executed by PLK1 itself versus by MPS1 or Aurora B acting downstream of PLK1-dependent priming, and does PLK1 belong under 'mitotic spindle assembly checkpoint signaling' as a participant or only as a regulator whose removal permits SAC satisfaction?
Q: GO lacks a 'centrosome maturation' (pericentriolar material expansion) term; PLK1's best-documented centrosomal function is currently annotated to the broader 'centrosome cycle'. Would a dedicated child term be warranted for PLK1, AURKA, CEP192 and pericentrin?
Q: Should the many individual substrate-derived process annotations (p73/apoptosis, MDM2/TOPORS/p53 turnover, GTSE1 nuclear localization, GORASP1/Golgi) be consolidated, given that each reflects one phosphorylation event downstream of the mitotic kinase rather than an independently evolved PLK1 function?
Experiment: Analog-sensitive PLK1 (as-PLK1) combined with stage-resolved mitotic phosphoproteomics to distinguish direct PLK1 substrates from CDK1-, MPS1- and Aurora-dependent secondary events at centrosomes, kinetochores and the midzone.
Experiment: Separation-of-function alleles (kinase-dead, PBD H538A/K540M, K492R) scored in isogenic cells for centrosome maturation, spindle bipolarity, chromosome congression, SAC silencing and furrow induction to map which functions require catalysis versus PBD docking.
Experiment: Endogenous degron-tagged PLK1 depleted acutely in G2-arrested (DNA-damaged) cells with time-lapse imaging of CLASPIN/WEE1 levels and mitotic entry, to quantify PLK1's contribution to checkpoint termination versus recovery.
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