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Center for Computational Systems Medicine
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Kinase Fusion Gene Summary

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Kinase Fusion Gene Sample Information

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Kinase Fusion ORF Analysis

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Kinase Fusion Amino Acid Sequences

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Multiple Sequence Alignment of All Fusion Protein Isoforms

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Kinase Fusion Protein Functional Features

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Kinase Fusion Protein Structures

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Comparison of Fusion Protein Isoforms

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Comparison of Fusion Protein Sequences/Structures with Known Sequences/Structures from PDB

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pLDDT Scores and Difference Analysis of pLDDT Scores Between the Active Sites (Best) and Non-Active Sites.

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Ramachandran Plot of Kinase Fusion Protein Structure

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Potential Active Site Information

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Virtual Screening Results

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Kinase-Substrate Information

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Related Drugs with This Kinase Fusion Protein

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Related Disease with This Kinase Fusion Protein

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Clinical Trials of the Found Drugs/Small Molecules

Kinase Fusion Gene:PLK1_PLK1

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: PLK1_PLK1
KinaseFusionDB ID: KFG4746
FusionGDB2.0 ID: KFG4746
HgeneTgene
Gene symbol

PLK1

PLK1

Gene ID

5347

5347

Gene namepolo like kinase 1polo like kinase 1
SynonymsPLK|STPK13PLK|STPK13
Cytomap

16p12.2

16p12.2

Type of geneprotein-codingprotein-coding
Descriptionserine/threonine-protein kinase PLK1PLK-1cell cycle regulated protein kinasepolo (Drosophia)-like kinaseserine/threonine-protein kinase 13serine/threonine-protein kinase PLK1PLK-1cell cycle regulated protein kinasepolo (Drosophia)-like kinaseserine/threonine-protein kinase 13
Modification date2024041120240411
UniProtAcc

P53350

P53350

Ensembl transtripts involved in fusion geneENST idsENST00000300093, ENST00000564202, 
ENST00000564202, ENST00000300093, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: PLK1 [Title/Abstract] AND PLK1 [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)PLK1(23695200)-PLK1(23700558), # samples:1
check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
HgenePLK1

GO:0000086

G2/M transition of mitotic cell cycle

19160488

HgenePLK1

GO:0000132

establishment of mitotic spindle orientation

23509069

HgenePLK1

GO:0000278

mitotic cell cycle

18615013

HgenePLK1

GO:0000281

mitotic cytokinesis

19468302

HgenePLK1

GO:0001578

microtubule bundle formation

12939256

HgenePLK1

GO:0006302

double-strand break repair

22325354

HgenePLK1

GO:0006468

protein phosphorylation

19468300|20679239|22701722|23509069

HgenePLK1

GO:0007095

mitotic G2 DNA damage checkpoint signaling

18662541

HgenePLK1

GO:0016567

protein ubiquitination

16885022

HgenePLK1

GO:0018105

peptidyl-serine phosphorylation

16885022

HgenePLK1

GO:0030071

regulation of mitotic metaphase/anaphase transition

23509069

HgenePLK1

GO:0031648

protein destabilization

16885022

HgenePLK1

GO:0032465

regulation of cytokinesis

17351640

HgenePLK1

GO:0045862

positive regulation of proteolysis

16885022

HgenePLK1

GO:0071168

protein localization to chromatin

21111234

HgenePLK1

GO:0097681

double-strand break repair via alternative nonhomologous end joining

37440612|37674080

HgenePLK1

GO:1901673

regulation of mitotic spindle assembly

22621898

HgenePLK1

GO:1904668

positive regulation of ubiquitin protein ligase activity

15148369

HgenePLK1

GO:1904776

regulation of protein localization to cell cortex

23509069

HgenePLK1

GO:2000042

negative regulation of double-strand break repair via homologous recombination

28512243

TgenePLK1

GO:0000086

G2/M transition of mitotic cell cycle

19160488

TgenePLK1

GO:0000132

establishment of mitotic spindle orientation

23509069

TgenePLK1

GO:0000278

mitotic cell cycle

18615013

TgenePLK1

GO:0000281

mitotic cytokinesis

19468302

TgenePLK1

GO:0001578

microtubule bundle formation

12939256

TgenePLK1

GO:0006302

double-strand break repair

22325354

TgenePLK1

GO:0006468

protein phosphorylation

19468300|20679239|22701722|23509069

TgenePLK1

GO:0007095

mitotic G2 DNA damage checkpoint signaling

18662541

TgenePLK1

GO:0016567

protein ubiquitination

16885022

TgenePLK1

GO:0018105

peptidyl-serine phosphorylation

16885022

TgenePLK1

GO:0030071

regulation of mitotic metaphase/anaphase transition

23509069

TgenePLK1

GO:0031648

protein destabilization

16885022

TgenePLK1

GO:0032465

regulation of cytokinesis

17351640

TgenePLK1

GO:0045862

positive regulation of proteolysis

16885022

TgenePLK1

GO:0071168

protein localization to chromatin

21111234

TgenePLK1

GO:0097681

double-strand break repair via alternative nonhomologous end joining

37440612|37674080

TgenePLK1

GO:1901673

regulation of mitotic spindle assembly

22621898

TgenePLK1

GO:1904668

positive regulation of ubiquitin protein ligase activity

15148369

TgenePLK1

GO:1904776

regulation of protein localization to cell cortex

23509069

TgenePLK1

GO:2000042

negative regulation of double-strand break repair via homologous recombination

28512243


check buttonKinase Fusion gene breakpoints across PLK1 (5'-gene)
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
all structure

check buttonKinase Fusion gene breakpoints across PLK1 (3'-gene)
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
all structure


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Kinase Fusion Gene Sample Information

check buttonKinase Fusion gene information.
check button Kinase Fusion gene information from four resources (ChiTars 5.0, ChimerDB 4.0, COSMIC, and CCLE)
* All genome coordinats were lifted-over on hg19.
* Click on the break point to see the gene structure around the break point region using the UCSC Genome Browser.
SourceSampleHgeneHchrHbpTgeneTchrTbp
ChiTaRS5.0BI033419PLK1chr16

23695200

PLK1chr16

23700558



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Kinase Fusion ORF Analysis


check buttonKinase Fusion information from ORFfinder translation from full-length transcript sequence from KinaseFusionDB.
HenstTenstHgeneHchrHbpTgeneTchrTbpSeq length
(transcript)
Seq length
(amino acids)

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Kinase Fusion Amino Acid Sequences


check button For individual full-length fusion transcript sequence from KinaseFusionDB, we ran ORFfinder and chose the longest ORF among the all predicted ones.
>Henst_Tenst_Hgene_Hchr_Hbp_Tgene_Tchr_Tbp_length(fusion AA)_AAseq

Multiple Sequence Alignment of All Fusion Protein Isoforms



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Kinase Fusion Protein Functional Features


check button Four levels of functional features of fusion genes
Go to FGviewer search page for the most frequent breakpoint (https://ccsmweb.uth.edu/FGviewer/chr16:23695200/chr16:23700558)
- FGviewer provides the online visualization of the retention search of the protein functional features across DNA, RNA, protein, and pathological levels.
- How to search
1. Put your fusion gene symbol.
2. Press the tab key until there will be shown the breakpoint information filled.
4. Go down and press 'Search' tab twice.
4. Go down to have the hyperlink of the search result.
5. Click the hyperlink.
6. See the FGviewer result for your fusion gene.
FGviewer

check buttonMain function of each fusion partner protein. (from UniProt)
HgeneTgene
PLK1

P53350

PLK1

P53350

FUNCTION: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis (PubMed:8991084, PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, PubMed:23509069). Polo-like kinase proteins act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains (PubMed:8991084, PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, PubMed:23509069). Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, POLQ, PRC1, RACGAP1/CYK4, RAD51, RHNO1, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU (PubMed:8991084, PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17218258, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:22325354, PubMed:19597481, PubMed:23455478, PubMed:23509069, PubMed:25986610, PubMed:26811421, PubMed:37674080, PubMed:37440612). Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL (PubMed:16980960, PubMed:19509060). NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation (PubMed:19509060). Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins (PubMed:12852856). Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1 (PubMed:12939256, PubMed:16247472, PubMed:17351640, PubMed:19468300, PubMed:19468302). Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains (PubMed:12939256, PubMed:17351640). Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation (PubMed:19468300, PubMed:19468302). Promotes the central spindle recruitment of ECT2 (PubMed:16247472). Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1 (PubMed:11202906, PubMed:12447691, PubMed:12524548, PubMed:19160488). Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1 (PubMed:11202906). Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase (PubMed:12447691, PubMed:12524548). Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity (PubMed:19160488). Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2 (PubMed:15469984, PubMed:15148369, PubMed:17376779, PubMed:18331714). PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation (PubMed:17617734). Required for kinetochore localization of BUB1B (PubMed:17376779). Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2 (By similarity). Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function (PubMed:18331714). Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome (PubMed:15469984, PubMed:15148369). Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53 (PubMed:19473992). Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA (PubMed:18521620). Contributes to the regulation of AURKA function (PubMed:18662541, PubMed:18615013). Also required for recovery after DNA damage checkpoint and entry into mitosis (PubMed:18662541, PubMed:18615013). Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning (PubMed:23509069). Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage (By similarity). Phosphorylates CEP68 and is required for its degradation (PubMed:25503564). Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope (PubMed:20679239). Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock (PubMed:15661742). Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression (PubMed:18794143). Regulates mitotic progression by phosphorylating RIOK2 (PubMed:21880710). Through the phosphorylation of DZIP1 regulates the localization during mitosis of the BBSome, a ciliary protein complex involved in cilium biogenesis (PubMed:27979967). Regulates DNA repair during mitosis by mediating phosphorylation of POLQ and RHNO1, thereby promoting POLQ recruitment to DNA damage sites (PubMed:37674080, PubMed:37440612). {ECO:0000250|UniProtKB:P70032, ECO:0000250|UniProtKB:Q5F2C3, ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:12524548, ECO:0000269|PubMed:12738781, ECO:0000269|PubMed:12852856, ECO:0000269|PubMed:12939256, ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:14734534, ECO:0000269|PubMed:15070733, ECO:0000269|PubMed:15148369, ECO:0000269|PubMed:15469984, ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:16247472, ECO:0000269|PubMed:16980960, ECO:0000269|PubMed:17081991, ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17351640, ECO:0000269|PubMed:17376779, ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:18174154, ECO:0000269|PubMed:18331714, ECO:0000269|PubMed:18418051, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18521620, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:18662541, ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:19509060, ECO:0000269|PubMed:19597481, ECO:0000269|PubMed:20679239, ECO:0000269|PubMed:21880710, ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:23509069, ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25986610, ECO:0000269|PubMed:26811421, ECO:0000269|PubMed:27979967, ECO:0000269|PubMed:37440612, ECO:0000269|PubMed:37674080, ECO:0000269|PubMed:8991084}.FUNCTION: Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis (PubMed:8991084, PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, PubMed:23509069). Polo-like kinase proteins act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains (PubMed:8991084, PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, PubMed:23509069). Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, POLQ, PRC1, RACGAP1/CYK4, RAD51, RHNO1, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU (PubMed:8991084, PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17218258, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:22325354, PubMed:19597481, PubMed:23455478, PubMed:23509069, PubMed:25986610, PubMed:26811421, PubMed:37674080, PubMed:37440612). Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL (PubMed:16980960, PubMed:19509060). NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation (PubMed:19509060). Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins (PubMed:12852856). Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1 (PubMed:12939256, PubMed:16247472, PubMed:17351640, PubMed:19468300, PubMed:19468302). Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains (PubMed:12939256, PubMed:17351640). Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation (PubMed:19468300, PubMed:19468302). Promotes the central spindle recruitment of ECT2 (PubMed:16247472). Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1 (PubMed:11202906, PubMed:12447691, PubMed:12524548, PubMed:19160488). Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1 (PubMed:11202906). Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase (PubMed:12447691, PubMed:12524548). Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity (PubMed:19160488). Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2 (PubMed:15469984, PubMed:15148369, PubMed:17376779, PubMed:18331714). PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation (PubMed:17617734). Required for kinetochore localization of BUB1B (PubMed:17376779). Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2 (By similarity). Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function (PubMed:18331714). Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome (PubMed:15469984, PubMed:15148369). Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53 (PubMed:19473992). Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA (PubMed:18521620). Contributes to the regulation of AURKA function (PubMed:18662541, PubMed:18615013). Also required for recovery after DNA damage checkpoint and entry into mitosis (PubMed:18662541, PubMed:18615013). Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning (PubMed:23509069). Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage (By similarity). Phosphorylates CEP68 and is required for its degradation (PubMed:25503564). Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope (PubMed:20679239). Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock (PubMed:15661742). Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression (PubMed:18794143). Regulates mitotic progression by phosphorylating RIOK2 (PubMed:21880710). Through the phosphorylation of DZIP1 regulates the localization during mitosis of the BBSome, a ciliary protein complex involved in cilium biogenesis (PubMed:27979967). Regulates DNA repair during mitosis by mediating phosphorylation of POLQ and RHNO1, thereby promoting POLQ recruitment to DNA damage sites (PubMed:37674080, PubMed:37440612). {ECO:0000250|UniProtKB:P70032, ECO:0000250|UniProtKB:Q5F2C3, ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:12524548, ECO:0000269|PubMed:12738781, ECO:0000269|PubMed:12852856, ECO:0000269|PubMed:12939256, ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:14734534, ECO:0000269|PubMed:15070733, ECO:0000269|PubMed:15148369, ECO:0000269|PubMed:15469984, ECO:0000269|PubMed:15661742, ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:16247472, ECO:0000269|PubMed:16980960, ECO:0000269|PubMed:17081991, ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17351640, ECO:0000269|PubMed:17376779, ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:18174154, ECO:0000269|PubMed:18331714, ECO:0000269|PubMed:18418051, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18521620, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:18662541, ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:19509060, ECO:0000269|PubMed:19597481, ECO:0000269|PubMed:20679239, ECO:0000269|PubMed:21880710, ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:23509069, ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25986610, ECO:0000269|PubMed:26811421, ECO:0000269|PubMed:27979967, ECO:0000269|PubMed:37440612, ECO:0000269|PubMed:37674080, ECO:0000269|PubMed:8991084}.

check buttonRetention analysis result of each fusion partner protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at

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* Minus value of BPloci means that the break pointn is located before the CDS.

check button - Retained domain in the 5'-partner of fusion protein (protein functional feature from UniProt).
PartnerHgeneeneHbpTgeneeneTbpENSTBPexonTotalExonProtein feature lociBPlociTotalLenFeatureNote


check button - Retained domain in the 3'-partner of fusion protein (protein functional feature from UniProt).
PartnerHgeneeneHbpTgeneeneTbpENSTBPexonTotalExonProtein feature lociBPlociTotalLenFeatureNote


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Kinase-Substrate Information of PLK1_PLK1


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
PLK1P53350humanDCTN1Q14203S179sASAGELsSSEPSTP
PLK1P53350humanCCNT1O60563S564KTYSLSSsFSSSSsT
PLK1P53350humanNINLQ9Y2I6S88RPSDEDssSLESAAS
PLK1P53350humanPTENP60484S380EPDHyRYsDttDsDP
PLK1P53350humanPINX1Q96BK5S226ATGKDVEsyLQPkAK
PLK1P53350humanCLASP2O75122S1092MKLtQEEsFSVWDEH
PLK1P53350humanANAPC1Q9H1A4T520GLPAPsLtMsNtMPR
PLK1P53350humanMAP9Q49MG5S289SDENKENsFsADHVT
PLK1P53350humanPCNTO95613T1221ALPELDRtLSECAEM
PLK1P53350humanCDC25CP30307S75PkRCLDLsNLSSGEI
PLK1P53350humanPRC1O43663T616TSGILNstNIQs___
PLK1P53350humanKIF2CQ99661S715MQLEEQAsRQIsSKK
PLK1P53350humanKMT2EQ8IZD2S861sPLLLNDsCSLPDLT
PLK1P53350humanMAD1L1Q9Y6D9T680SKMQLLEtEFSHTVGMAD
PLK1P53350humanMDC1Q14676S20EEEEtEQssESLRCN
PLK1P53350humanVCPP55072T76CIVLsDDtCSDEkIRCDC48_N
PLK1P53350humanCDC27P30260T209LtEtPQDtIELNRLN
PLK1P53350humanBORAQ6PGQ7S497SSNIQMDsGYNtQNC
PLK1P53350humanTNKSO95271T982SLIsPAStPSCLsAA
PLK1P53350humanKNL1Q8NG31-2T875DKNDMDItKSYTIEIMELT
PLK1P53350humanTTKP33981T46NKISADttDNsGTVN
PLK1P53350humanCENPQQ7L2Z9T123RLLQQCEtLKVPPKkCENP-Q
PLK1P53350humanPCNTO95613T1209TAPALEEtWSDVALP
PLK1P53350humanSTK38Q15208T407EIKSIDDtSNFDEFPPkinase_C
PLK1P53350humanPPP6R2O75170T10WKFDLNTtSHVDkLL
PLK1P53350humanSTK38Q15208T7_MAMtGstPCssMsN
PLK1P53350humanCDC20Q12834S170KtCRYIPsLPDrILD
PLK1P53350humanTOP2AP11388T1343FsDFDEKtDDEDFVP
PLK1P53350humanTTKP33981T33kFkNEDLtDELsLNK
PLK1P53350humanNEDD1Q8NHV4S637HSLLERysVNEGLVA
PLK1P53350humanTOP2AP11388S1525PIKyLEEsDEDDLF_
PLK1P53350humanCDC16Q13042S112EkYLkDEsGFkDPSS
PLK1P53350humanKIF2BQ8N4N8T125MIPQKNQtAsGDsLD
PLK1P53350humanHSPA1BP0DMV8S633GPkGGsGsGPtIEEV
PLK1P53350humanDVL2O14641T206MTSELEStSLGDsDEDishevelled
PLK1P53350humanCLASP2O75122S1053DQFPDDLsLDHsDLV
PLK1P53350humanPTPN1P18031S393sPAKGEPsLPEKDED
PLK1P53350humanMDM2Q00987S260sLDsEDYsLsEEGQE
PLK1P53350humanHNRNPUQ00839S59AMEPGNGsLDLGGDs
PLK1P53350humanTOPORSQ9NS56S718kDRDGYEsSYRRRTL
PLK1P53350humanCENPQQ7L2Z9S138MEDLtNVssLLNMERCENP-Q
PLK1P53350humanCTNNB1P35222S311LAYGNQEsKLIILAS
PLK1P53350humanTTKP33981T594RLYDYEItDQYIYMVPkinase
PLK1P53350humanKLF4O43474S234GkFVLkAsLsAPGSE
PLK1P53350humanCENPQQ7L2Z9T256sQMKsMstFIEEAYKCENP-Q
PLK1P53350humanTTKP33981S321SkPsGNDsCELRNLk
PLK1P53350humanBRCA1P38398S1164GEIKEDTsFAENDIk
PLK1P53350humanANAPC1Q9H1A4S377NIssHNQsPkRHSIS
PLK1P53350humanSTK3Q13188T384GtMKRNAtsPQVQRP
PLK1P53350humanLRRK1Q38SD2S1817GDSIADVsIMYSEEL
PLK1P53350humanTTKP33981S108DkYGQNEsFARIQVR
PLK1P53350humanCENPQQ7L2Z9S253HNssQMKsMstFIEECENP-Q
PLK1P53350humanANAPC7Q9UJX3S23HsNVRLLssLLLtMs
PLK1P53350humanTTKP33981T458CktPsSNtLDDyMsC
PLK1P53350humanCEP68Q76N32S332ADPVLQDsGVDLDSF
PLK1P53350humanPPP1R7Q15435S44sGIVADLsEQsLkDG
PLK1P53350humanTTKP33981T12DLsGRELtIDsIMNk
PLK1P53350humanNEDD1Q8NHV4S426VNKGsDEsIGkGDGF
PLK1P53350humanTTKP33981S333NLkSVQNsHFkEPLV
PLK1P53350humanMAD1L1Q9Y6D9S22RsLNNFIsQRVEGGs
PLK1P53350humanPPP1R7Q15435S27RRVEsEEsGDEEGKk
PLK1P53350humanCASP8Q14790S305IYQLMDHsNMDCFICPeptidase_C14
PLK1P53350humanUSP16Q9Y5T5S386HESFLDLsLPVLDDQUCH
PLK1P53350humanNCAPH2Q6IBW4S288EsRsPQQsAALPRRY
PLK1P53350humanPPP1R7Q15435S24EVDRRVEsEEsGDEE
PLK1P53350humanFOXM1Q08050S739SKILLDIsFPGLDED
PLK1P53350humanMAP2K1Q02750S222LIDsMANsFVGtRSYPkinase
PLK1P53350humanPCNTO95613S1235MSSVAEIsSHMREsF
PLK1P53350humanPRC1O43663S615ATSGILNstNIQs__
PLK1P53350humanCDC6Q99741T37SDAkLEPtNVQTVtC
PLK1P53350humanCENPQQ7L2Z9S249LDILHNssQMKsMstCENP-Q
PLK1P53350humanVIMP08670T336EVdALkGtNEsLERQFilament
PLK1P53350humanCCNB1P14635S126PILVDTAsPsPMETs
PLK1P53350humanRACGAP1Q9H0H5S164sFDKtDEsLDWDssL
PLK1P53350humanFOXM1Q08050-2S724SKILLDIsFPGLDED
PLK1P53350humanNCAPD3P42695S1419AIstPEKsISDVtFG
PLK1P53350humanTTKP33981S291CDVktDDsVVPCFMK
PLK1P53350humanPAX3/FOXO1AAC50053S503PRTSSNAsTISGRLs
PLK1P53350humanAXIN2Q9Y2T1S311SDALTDDsMSMTDSS
PLK1P53350humanRAD21O60216S175REIMREGsAFEDDDM
PLK1P53350humanMDC1Q14676T4____MEDtQAIDWDV
PLK1P53350humanTTKP33981T371LLAkLEEtkEyQEPE
PLK1P53350humanBRCA2P51587S205LATPPtLsstVLIVR
PLK1P53350humanBRF1Q92994S450GDGELDLsGIDDLEIBRF1
PLK1P53350humanTNKSO95271T930LAHGADPtMkNQEGQAnk_5
PLK1P53350humanYY1P25490T39PVETIETtVVGEEEE
PLK1P53350humanWDCPQ9H6R7S686RsDVFRDsFsHsPGA
PLK1P53350humanCDC25BP30305S465PLERDAEsFLLksPIRhodanese
PLK1P53350humanNUAK1O60285S480QREsGYYsSPERSES
PLK1P53350humanTP53BP1Q12888S1618LtkAADIsLDNLVEG
PLK1P53350humanVIMP08670S83GVRLLQDsVdFsLAdFilament_head
PLK1P53350humanCDC23Q9UJX2T562QLRNQGEtPttEVPA
PLK1P53350humanSUZ12Q15022S539RPKRTkAsMsEFLEs
PLK1P53350humanMAP2K1Q02750S218VsGQLIDsMANsFVGPkinase
PLK1P53350humanBRCA2P51587S193AEVDPDMsWSSSLAT
PLK1P53350humanSTK3Q13188S15KSKLKkLsEDsLTkQ
PLK1P53350humanCENPUQ71F23S77TFDPPLHstAIyADE
PLK1P53350humanCDC27P30260T430INDsLEItkLDssII
PLK1P53350humanCHEK2O96017T205VFVFFDLtVDDQsVY
PLK1P53350humanKIF2CQ99661S632EELSsQMssFNEAMT
PLK1P53350humanWEE1P30291S53GHstGEDsAFQEPDS
PLK1P53350humanVIMP08670S459GQVINEtsQHHDDLE
PLK1P53350humanKDM1AO60341S126EYREMDEsLANLsED
PLK1P53350humanCDC23Q9UJX2T565NQGEtPttEVPAPFF
PLK1P53350humanTTKP33981T676NQMQPDttsVVkDSQPkinase
PLK1P53350humanRIOK2Q9BVS4S548KSSLEAAsFWGE___
PLK1P53350humanRAPGEF2Q17RH5S794RECKNFNsMFAIISGRasGEF
PLK1P53350humanTP73O15350T27SSLEPDStyFDLPQS
PLK1P53350humanTSC1Q92574S579CQTSLETsIFTPsPCHamartin
PLK1P53350humanRUVBL1Q9Y265T239kEIIQDVtLHDLDVATIP49
PLK1P53350humanCEP55Q53EZ4S436PtAALNEsLVECPkC
PLK1P53350humanCDC25BP30305S375ARVLRsksLCHDEIEM-inducer_phosp
PLK1P53350humanSTK38Q15208T183TLLMKKDtLTEEETQPkinase
PLK1P53350humanRACGAP1Q9H0H5T260QPWNsDstLNSRQLE
PLK1P53350humanBCL2L1Q07817S62PSWHLADsPAVNGAT
PLK1P53350humanTERF1P54274S435KKLKLIssDsED___
PLK1P53350humanERCC6LQ2NKX8T1063VKQFDAstPkNDIsP
PLK1P53350humanNUDCQ9Y266S326QHPEMDFskAkFN__
PLK1P53350humanVIMP08670T327RRQVQsLtCEVdALkFilament
PLK1P53350humanSNCBQ16143S118LMEPEGEsYEDPPQESynuclein
PLK1P53350humanTNKSO95271T839DTQGRNStPLHLAAGAnk_4
PLK1P53350humanKIZQ2M2Z5T379WSTSSDLtISISEDD
PLK1P53350humanBRCA2P51587S206ATPPtLsstVLIVRN
PLK1P53350humanRAPGEF2Q17RH5S1164DERRQRHsVSIVETN
PLK1P53350humanRBBP8Q99708T693ETVDMDCtLVSETVL
PLK1P53350humanPINX1Q96BK5S110SDKKEKKsFSLEEKs
PLK1P53350humanSUZ12Q15022S546sMsEFLEsEDGEVEQVEFS-Box
PLK1P53350humanMAD1L1Q9Y6D9S29sQRVEGGsGLDISTS
PLK1P53350humanHSF1Q00613S419SALLDLFsPSVTVPDVert_HS_TF
PLK1P53350humanMAP2K2P36507S222VsGQLIDsMANsFVGPkinase
PLK1P53350humanNINLQ9Y2I6S87VRPSDEDssSLESAA
PLK1P53350humanCDC25BP30305S397RELIGDYskAFLLQt
PLK1P53350humanRAPGEF2Q17RH5S921KKWRSLGsLSQGSTN
PLK1P53350humanPPP1R7Q15435T277LENNNKLtMLDIASNLRR_9
PLK1P53350humanCLASP2O75122S1027NPyNysDsIsPFNKs
PLK1P53350humanCLIP1P30622S195LtKtAsEsIsNLsEA
PLK1P53350humanCDC27P30260S435EItkLDssIIsEGkI
PLK1P53350humanYAP1P46937T77NAVMNPktANVPQtV
PLK1P53350humanTEX14Q8IWB6S437QKAATVKsDIYSFSMPK_Tyr_Ser-Thr
PLK1P53350humanCCNB1P14635S147EDLCQAFsDVILAVN
PLK1P53350humanSNCAP37840S129NEAyEMPsEEGyQDySynuclein
PLK1P53350humanRACGAP1Q9H0H5S157GsILsDIsFDKtDEs
PLK1P53350humanCENPQQ7L2Z9S139EDLtNVssLLNMERACENP-Q
PLK1P53350humanFIRRMQ9NSG2S744ETKNKVVsFLEkTGF
PLK1P53350humanCDC25BP30305S353VQNkRRRsVtPPEEQM-inducer_phosp
PLK1P53350humanNOTCH1P46531S1791REPLGEDsVGLkPLK
PLK1P53350humanCDC25BP30305T127DPHMAEQtFEQAIQAM-inducer_phosp
PLK1P53350humanTTKP33981T210LSASTVLtAQEsFsG
PLK1P53350humanTTKP33981S214TVLtAQEsFsGsLGH
PLK1P53350humanCDC25BP30305T265LTPAEGDtEEDDGFVM-inducer_phosp
PLK1P53350humanKIF2CQ99661S633ELSsQMssFNEAMTQ
PLK1P53350humanIRS1P35568S24GYLRKPKsMHKRFFVPH
PLK1P53350humanCENPQQ7L2Z9S255ssQMKsMstFIEEAYCENP-Q
PLK1P53350humanPCNTO95613S1241IsSHMREsFLMsPES
PLK1P53350humanTTKP33981S362TLKNktEssLLAkLE
PLK1P53350humanRB1P06400S758SIIVFYNsVFMQRLK
PLK1P53350humanRBBP8Q99708S723EERKMNDsLEDMFDR
PLK1P53350humanSUZ12Q15022S541KRTkAsMsEFLEsED
PLK1P53350humanRIOK2Q9BVS4S335TKEGsEFsFsDGEVA
PLK1P53350humanMRE11P49959S688sKGVDFEssEDDDDD
PLK1P53350humanKIF2AO00139T554ANRVKELtVDPTAAG
PLK1P53350humanOPTNQ96CV9S177ssGssEDsFVEIRMA
PLK1P53350humanANAPC1Q9H1A4S373VQRFNIssHNQsPkR
PLK1P53350humanCLSPNQ9HAW4S30EADSPSDsGQGsYET
PLK1P53350humanTTKP33981S345PLVSDEKsSELIItD
PLK1P53350humanPIN1Q13526S65sHLLVkHsQSRRPssRotamase
PLK1P53350humanESPL1Q14674S1399KVNFsDDsDLEDPVS
PLK1P53350humanFBXO5Q9UKT4S149yEDsGYSsFSLQSGL
PLK1P53350humanANAPC7Q9UJX3S17MAAAGLHsNVRLLss
PLK1P53350humanRAP1GAPP47736S525AGQKtPDsGHVSQEP
PLK1P53350humanANAPC1Q9H1A4S547PLsKLLGsLDEVVLL
PLK1P53350humanANAPC1Q9H1A4S688FDFEGsLsPVIAPkkApc1_MidN
PLK1P53350humanCIP2AQ8TCG1S904NPETVNLsI______
PLK1P53350humanRAPGEF2Q17RH5T632AIREFAVtATPDQYSRA
PLK1P53350humanTNKSO95271S978VVSASLIsPAStPSC
PLK1P53350humanBIRC5O15392S20FLkDHRIstFkNWPFBIR
PLK1P53350humanIKBKBO14920S740sFtALDWsWLQTEEEIKKbetaNEMObind
PLK1P53350humanGTSE1Q9NYZ3S454RsIRRRDsCLNsKTK
PLK1P53350humanZMYM2Q9UBW7S303QkQPGVDsLsPVAsL
PLK1P53350humanCDC27P30260T205PEtVLtEtPQDtIEL
PLK1P53350humanPTPN1P18031S286KFIMGDSsVQDQWKE
PLK1P53350humanUSP16Q9Y5T5S330ILKAFGNsTEkLDEEUCH
PLK1P53350humanRAPGEF2Q17RH5S1010KPVKSETsPVAPRAG
PLK1P53350humanPLEKHG6Q3KR16T574HLVVTEDtDEDAPLV
PLK1P53350humanCENPQQ7L2Z9S248DLDILHNssQMKsMsCENP-Q
PLK1P53350humanTRIOBPQ9H2D6-5T457QAEEREHtLRRCQQE
PLK1P53350humanWDCPQ9H6R7S695sHsPGAVssLKVFTG
PLK1P53350humanKIF2BQ8N4N8S204HLDssKIsVLEPPQE
PLK1P53350humanPRKNO60260S378AyHEGECsAVFEASG
PLK1P53350humanRBBP8Q99708T731LEDMFDRtTHEEYES
PLK1P53350humanCTNNB1P35222S718QDDPsyRsFHsGGyG
PLK1P53350humanSUN1O94901-9S138RPPVLDEsWIREQTTMRP
PLK1P53350humanNOTCH1P46531S2439SFLSGEPsQADVQPL
PLK1P53350humanRIOK2Q9BVS4S380PEQIkEdsLsEEsAD
PLK1P53350humanNPM1P06748S4____MEDsMDMDMsP
PLK1P53350humanMDC1Q14676T847PERQTDVtGEEELTK
PLK1P53350humanAURKBQ96GD4T236RRktMCGtLDyLPPEPkinase
PLK1P53350humanSTK3Q13188T336TSVEsVGtMRATSTM
PLK1P53350humanFADDQ13158S194QNRsGAMsPMsWNsD
PLK1P53350humanCDC25BP30305S513RAVNDYPsLYYPEMYRhodanese
PLK1P53350humanUSP16Q9Y5T5S486SEYEAEMsLQGEVNIUCH
PLK1P53350humanKIF2BQ8N4N8S201YRRHLDssKIsVLEP
PLK1P53350humanBRF1Q92994T270RLTEFEDtPTSQLTITFIIB
PLK1P53350humanRACGAP1Q9H0H5S149RLstIDEsGsILsDI
PLK1P53350humanCDC25CP30307S198sDELMEFsLKDQEAKM-inducer_phosp
PLK1P53350humanGORASP1Q9BQQ3S189AAWGGEGsLGCGIGYGRASP55_65
PLK1P53350humanBRCA2P51587T207TPPtLsstVLIVRNE
PLK1P53350humanPLK1P53350T210YDGERKktLCGtPNyPkinase
PLK1P53350humanESPL1Q14674T1363AGPHVPFtVFEEVCP
PLK1P53350humanATXN10Q9UBB4T82ASsLQLItECFRCLR
PLK1P53350humanRACGAP1Q9H0H5S170EsLDWDssLVkTFKL
PLK1P53350humanCDC25BP30305S291AVPPGMEsLISAPLVM-inducer_phosp
PLK1P53350humanKAT7O95251S57sQssQDssPVRNLQs
PLK1P53350humanGTSE1Q9NYZ3S242LLLPRAAsVRGRsIP
PLK1P53350humanRESTQ13127S1030MsEGsDDsGLHGARP
PLK1P53350humanCLIP1P30622S1364DDLNNYDsDDQEKQS
PLK1P53350humanMTHFRP42898T549NVKGENItNAPELQP
PLK1P53350humanSTILQ15468S1108DRSTVGLsLIsPNNM
PLK1P53350humanANAPC4Q9UJX5S779kEEVLsEsEAENQQA
PLK1P53350humanTSC1Q92574S468GFLGDLAsEEDsIEKHamartin
PLK1P53350humanBUB1BO60566T1008LNANDEAtVSVLGEL
PLK1P53350humanANAPC1Q9H1A4T291kFsEQGGtPQNVATS
PLK1P53350humanCCNB1P14635S133sPsPMETsGCAPAEE
PLK1P53350humanTNKSO95271T1128VEEEMQStIREHRDGPARP
PLK1P53350humanCENPUQ71F23T78FDPPLHstAIyADEE
PLK1P53350humanPINX1Q96BK5S117sFSLEEKsKISKNRV
PLK1P53350humanNINLQ9Y2I6T161SDEEAEStKEAQNEL
PLK1P53350humanNEDD1Q8NHV4T382PRsINTDtLSkEtDs
PLK1P53350humanSTK3Q13188S18LKkLsEDsLTkQPEE
PLK1P53350humanNUDCQ9Y266S274kkINPENskLsDLDs
PLK1P53350humanIKBKBO14920S750QTEEEEHsCLEQAS_
PLK1P53350humanANAPC7Q9UJX3S30ssLLLtMsNNNPELF
PLK1P53350humanCEP192Q8TEP8T44GLPVAVStLARDRSS
PLK1P53350humanPKMYT1Q99640T495LLSLFEDtLDPT___
PLK1P53350humanFOXM1Q08050S730VLDTMNDsLSKILLD
PLK1P53350humanPINX1Q96BK5T141DLSSRSKtDLDCIFG
PLK1P53350humanWDR62O43379S897KPESLENsILDSLEP
PLK1P53350humanTTKP33981T564LEEADNQtLDSYRNEPkinase
PLK1P53350humanTOP2AP11388S1337LDsDEDFsDFDEKtD
PLK1P53350humanCDC25BP30305T404skAFLLQtVDGkHQD
PLK1P53350humanZMYM2Q9UBW7S309DsLsPVAsLPkQIFQ
PLK1P53350humanCTNNB1P35222S60EEEDVDTsQVLyEWE
PLK1P53350humanMYCP01106S77LLPtPPLsPsRRsGLMyc_N
PLK1P53350humanANAPC1Q9H1A4S355AALsrAHsPALGVHs
PLK1P53350humanTTKP33981S37EDLtDELsLNKISAD
PLK1P53350humanPARP10Q53GL7T601EVRELLAtLEGLDLD
PLK1P53350humanPRKDCP78527S3205tPLPEDNsMNVDQDGFAT
PLK1P53350humanPPP1R7Q15435S47VADLsEQsLkDGEEr
PLK1P53350humanHSPA1BP0DMV8S631AQGPkGGsGsGPtIE
PLK1P53350humanCHEK2O96017T68SsLEtVstQELYsIP
PLK1P53350humanFBXO5Q9UKT4S145TSRLyEDsGYSsFSL
PLK1P53350humanKIF2BQ8N4N8S200EYRRHLDssKIsVLE
PLK1P53350humanCDC27P30260S434LEItkLDssIIsEGk
PLK1P53350humanCHEK2O96017S164IAYIEDHsGNGTFVNFHA
PLK1P53350humanCENPQQ7L2Z9T135PKkMEDLtNVssLLNCENP-Q
PLK1P53350humanTTKP33981S363LKNktEssLLAkLEE
PLK1P53350humanSVILO95425S238sFSGRDssFtEVPRs
PLK1P53350humanCDC25BP30305S50PVRAAASsPVttLtQ
PLK1P53350humanCCNB1P14635S128LVDTAsPsPMETsGC
PLK1P53350humanBRCA2P51587T203SSLATPPtLsstVLI
PLK1P53350humanBUB1BO60566T792PRNSAELtVIKVsSQ
PLK1P53350humanCDCA5Q96FF9T151RsysRLEtLGsAStsSororin
PLK1P53350humanPPP6R2O75170S289GtEGLVDsFsQGLERSAPS
PLK1P53350humanPRKAA2P54646T172sDGEFLRtsCGsPNyPkinase
PLK1P53350humanPKMYT1Q99640S426CSLLLDSsLSSNWDD
PLK1P53350humanVIMP08670S339ALkGtNEsLERQMREFilament
PLK1P53350humanZMYM2Q9UBW7S305QPGVDsLsPVAsLPk
PLK1P53350humanRAD21O60216S454EPsRLQEsVMEAsRT
PLK1P53350humanRACGAP1Q9H0H5S214AVDQGNEsIVAKTTV
PLK1P53350humanATXN10Q9UBB4S77QVENLASsLQLItEC
PLK1P53350humanCDC25BP30305T167sPVLRNItNsQAPDGM-inducer_phosp
PLK1P53350humanRANP62826S135DRkVKAksIVFHRkkRas
PLK1P53350humanSUGT1Q9Y2Z0S331VkRAMNksFMEsGGtSGS
PLK1P53350humanKIF2CQ99661S621ALIPGNLsKEEEELS
PLK1P53350humanCDCA5Q96FF9T115VPAtPtStPVPNPEASororin
PLK1P53350humanBUB1BO60566T680IEDsREAtHSsGFSG
PLK1P53350humanHSF1Q00613S216IPLMLNDsGsAHSMP
PLK1P53350humanMAP2K2P36507S226LIDsMANsFVGtRSYPkinase
PLK1P53350humanPTENP60484T383HyRYsDttDsDPENE
PLK1P53350humanSTK3Q13188S385tMKRNAtsPQVQRPs
PLK1P53350humanSRIP30626T155YstNGKItFDDYIAC
PLK1P53350humanNUAK1O60285S476KKTQQREsGYYsSPE
PLK1P53350humanSTILQ15468S1116LIsPNNMsFAtkKYM
PLK1P53350humanCLASP2O75122S1034sIsPFNKsALKEAMF
PLK1P53350humanCDC27P30260T446EGkIStItPQIQAFN
PLK1P53350humanMRE11P49959S649EVIEVDEsDVEEDIF
PLK1P53350humanCLIP1P30622S312AsLKRsPsAssLsSM
PLK1P53350humanSTK3Q13188S316LEEEEENsDEDELDs
PLK1P53350humanBUB1BO60566S676LsPIIEDsREAtHSs
PLK1P53350humanANAPC1Q9H1A4T701kkARPsEtGsDDDWEApc1_MidN
PLK1P53350humanANAPC1Q9H1A4T530NtMPRPstPLDGVst
PLK1P53350humanPTENP60484T382DHyRYsDttDsDPEN
PLK1P53350humanBORAQ6PGQ7T501QMDsGYNtQNCGSNI
PLK1P53350humanCDC25BP30305T58PVttLtQtMHDLAGL
PLK1P53350humanTPT1P13693S46tEGNIDDsLIGGNAsTCTP
PLK1P53350humanCDC25BP30305S209PWkPTHPsSTHALAEM-inducer_phosp
PLK1P53350humanFIRRMQ9NSG2S43SQARGLSsQNLEIQT
PLK1P53350humanNEDD1Q8NHV4S397GkNQDFssFDDtGKs
PLK1P53350humanSMAD4Q13485T197ASTETyStPALLAPS
PLK1P53350humanRAD51Q06609S14LEANADtsVEEESFG
PLK1P53350humanMAD2L1BPQ15013S102kHFyRkPsPQAEEMLp31comet
PLK1P53350humanCHEK2O96017S210DLtVDDQsVYPKALR
PLK1P53350humanRSF1Q96T23S1359ENVGKVGsPLDysLV
PLK1P53350humanCDC27P30260S426TQPNINDsLEItkLD
PLK1P53350humanNEK9Q8TD19T210SEYsMAEtLVGtPYYPkinase
PLK1P53350humanIKBKBO14920S733TVREQDQsFtALDWsIKKbetaNEMObind
PLK1P53350humanNINLQ9Y2I6S686LEELHEKsQEVIWGL
PLK1P53350humanORC2Q13416S188SEYSASNsEDDEGVA
PLK1P53350humanVIMP08670S56srsLyAssPGGVyAtFilament_head
PLK1P53350humanBIRC5O15392T21LkDHRIstFkNWPFLBIR
PLK1P53350humanPINX1Q96BK5T317EDATLEEtLVKKKKK


check button Biological Network Integration of This Kinase and Substrates
(GeneMANIA website)

check button Enriched GO biological processes of the phosphorylation target genes of the kinase
KinaseGOIDGO termP.adjust
PLK1IDDescription0.00e+00
PLK1GO:0007059chromosome segregation4.81e-45
PLK1GO:0098813nuclear chromosome segregation1.58e-44
PLK1GO:0000819sister chromatid segregation1.09e-41
PLK1GO:0000280nuclear division4.20e-39
PLK1GO:0048285organelle fission1.83e-38
PLK1GO:0140014mitotic nuclear division7.18e-37
PLK1GO:0000070mitotic sister chromatid segregation7.74e-36
PLK1GO:1901987regulation of cell cycle phase transition1.10e-34
PLK1GO:0033044regulation of chromosome organization2.54e-34
PLK1GO:0044772mitotic cell cycle phase transition3.33e-34
PLK1GO:1901990regulation of mitotic cell cycle phase transition2.78e-31
PLK1GO:0051983regulation of chromosome segregation3.49e-31
PLK1GO:0010948negative regulation of cell cycle process2.52e-30
PLK1GO:0045786negative regulation of cell cycle7.35e-28
PLK1GO:0033045regulation of sister chromatid segregation2.04e-27
PLK1GO:0007051spindle organization3.61e-27
PLK1GO:1901988negative regulation of cell cycle phase transition3.82e-27
PLK1GO:0007091metaphase/anaphase transition of mitotic cell cycle6.24e-27
PLK1GO:0044784metaphase/anaphase transition of cell cycle1.32e-26
PLK1GO:0007052mitotic spindle organization5.15e-25
PLK1GO:1901991negative regulation of mitotic cell cycle phase transition8.98e-25
PLK1GO:0045930negative regulation of mitotic cell cycle1.17e-24
PLK1GO:1905818regulation of chromosome separation2.67e-24
PLK1GO:0051306mitotic sister chromatid separation3.15e-24
PLK1GO:0030071regulation of mitotic metaphase/anaphase transition4.07e-24
PLK1GO:1902850microtubule cytoskeleton organization involved in mitosis4.11e-24
PLK1GO:1902099regulation of metaphase/anaphase transition of cell cycle8.05e-24
PLK1GO:0051304chromosome separation1.68e-23
PLK1GO:0007088regulation of mitotic nuclear division4.60e-23
PLK1GO:0010965regulation of mitotic sister chromatid separation6.04e-23
PLK1GO:0000075cell cycle checkpoint signaling5.76e-21
PLK1GO:0051783regulation of nuclear division5.83e-21
PLK1GO:2001251negative regulation of chromosome organization1.59e-20
PLK1GO:0090068positive regulation of cell cycle process2.97e-20
PLK1GO:0010639negative regulation of organelle organization4.18e-20
PLK1GO:0045787positive regulation of cell cycle6.16e-20
PLK1GO:0007093mitotic cell cycle checkpoint signaling7.73e-20
PLK1GO:0051321meiotic cell cycle2.76e-19
PLK1GO:0051303establishment of chromosome localization7.43e-18
PLK1GO:0050000chromosome localization2.79e-17
PLK1GO:0033047regulation of mitotic sister chromatid segregation1.25e-16
PLK1GO:0045931positive regulation of mitotic cell cycle1.66e-16
PLK1GO:0051656establishment of organelle localization4.48e-16
PLK1GO:0051310metaphase chromosome alignment7.97e-16
PLK1GO:0033046negative regulation of sister chromatid segregation9.84e-16
PLK1GO:0033048negative regulation of mitotic sister chromatid segregation9.84e-16
PLK1GO:0045841negative regulation of mitotic metaphase/anaphase transition9.84e-16
PLK1GO:2000816negative regulation of mitotic sister chromatid separation9.84e-16
PLK1GO:1901989positive regulation of cell cycle phase transition9.92e-16

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Related Drugs to PLK1_PLK1


check button Drugs used for this fusion-positive patient.
(Manual curation of PubMed, 04-30-2022 + MyCancerGenome)
HgeneTgeneDrugSourcePMID

check button Distribution of the number of studies mentioning PLK1-PLK1 and kinase inhibitors the PubMed Abstract (04-01-2024)

Fusion gene - drug pair 1Fusion gene - drug pair 2PMIDPublication dateDOIStudy title

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Related Diseases to PLK1_PLK1


check button Diseases that have this fusion gene.
(Manual curation of PubMed, 04-30-2022 + MyCancerGenome)
HgeneTgeneDiseaseSourcePMID

check button Related diseases from the literature mentioned this fusion gene and drug.
(PubMed, 04-01-2024)
MeSH IDMeSH term

check button Diseases associated with fusion partners.
(DisGeNet 4.0)
PartnerGeneDisease IDDisease name# pubmedsSource


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Clinical Trials of the Found Drugs/Small Molecules


check button Statistics of the Clinical Trials of the Found Kinase Inibitors from clinicaltrials.gov (06-17-2024)

check button Clinical Trials from clinicaltrials.gov (06-17-2024)

Fusion GeneKinase InhibitorNCT IDStudy StatusPhasesDisease# EnrolmentDate