PLK1
entrez
5347
canonical
uniprot
P53350
canonical
ensembl
ENSG00000166851
resolver
ensp
ENSP00000300093
resolver
enst
ENST00000300093
resolver
genesymbol
PLK1
resolver
genesymbol_syn
PLK
resolver
hgnc
HGNC:9077
resolver
uniprot
Q15153
resolver
uniprot
Q99746
resolver
uniprot_entry
PLK1_HUMAN
resolver
uniprot_sec
Q15153
resolver
uniprot_sec
Q99746
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphorylation of Thr-210 by AURKA; phosphorylation by AURKA is enhanced by BORA (PubMed:17307877, PubMed:18615013). Once activated, activity is stimulated by binding target proteins (PubMed:17307877, PubMed:18615013). Binding of target proteins has no effect on the non-activated kinase (PubMed:17307877, PubMed:18615013). Several inhibitors targeting PLKs are currently in development and are under investigation in a growing number of clinical trials, such as BI 2536, an ATP-competitive PLK1 inhibitor or BI 6727, a dihydropteridinone that specifically inhibits the catalytic activity of PLK1 (PubMed:18005335). {ECO:0000269|PubMed:17307877, ECO:0000269|PubMed:18005335, ECO:0000269|PubMed:18615013}.
uniprot
proteins
amino_acid_sequence
MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERPREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in PLK1 are associated with some cancers, such as gastric, thyroid or B-cell lymphomas. Expression is cancer increased in tumor tissues with a poor prognosis, suggesting a role in malignant transformations and carcinogenesis.
uniprot
proteins
ec_number
2.7.11.21
uniprot
proteins
function
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: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, PubMed:28512243, PubMed:8991084). 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: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, PubMed:28512243, PubMed:8991084). Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, MRE11, PPP1R12A/MYPT1, POLQ, PRC1, RACGAP1/CYK4, RAD51, RHNO1, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU (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:19597481, PubMed:22325354, PubMed:23455478, PubMed:23509069, PubMed:25986610, PubMed:26811421, PubMed:28512243, PubMed:37440612, PubMed:37674080, PubMed:8991084). 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:15148369, PubMed:15469984, 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:15148369, PubMed:15469984). 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:18615013, PubMed:18662541). Also required for recovery after DNA damage checkpoint and entry into mitosis (PubMed:18615013, PubMed:18662541). 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:37440612, PubMed:37674080). Phosphorylates ATXN10 which may play a role in the regulation of cytokinesis and may stimulate the proteasome-mediated degradation of ATXN10 (PubMed:21857149). {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:21857149, 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}.
uniprot
proteins
mass_dalton
68255
uniprot
proteins
mutagenesis
MUTAGEN 67; /note="C->V: In analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with G-130."; /evidence="ECO:0000269|PubMed:19468302"; MUTAGEN 82; /note="K->M: Loss of kinase activity. No effect on S-phase progression."; /evidence="ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:18174154, ECO:0000269|PubMed:24018379"; MUTAGEN 82; /note="K->R: Loss of kinase activity. No effect on RIOK2-binding."; /evidence="ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:21880710"; MUTAGEN 130; /note="L->G: In analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with V-67."; /evidence="ECO:0000269|PubMed:19468302"; MUTAGEN 137; /note="S->A: No change in activity. Increases activity and restores recovery after DNA damage checkpoint; when associated with D-210."; /evidence="ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:18615013"; MUTAGEN 137; /note="S->D: Increases activity. Results in a block in G1/S."; /evidence="ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:18615013"; MUTAGEN 176; /note="D->N: Abolishes kinase activity."; /evidence="ECO:0000269|PubMed:18615013"; MUTAGEN 194; /note="D->A: Does not interfere with FRY-binding."; /evidence="ECO:0000269|PubMed:22753416"; MUTAGEN 210; /note="T->A: Abolishes activity. Abolishes checkpoint recovery."; /evidence="ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:17461553, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19160488"; MUTAGEN 210; /note="T->D: Increases activity and restores recovery after DNA damage checkpoint."; /evidence="ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:17461553, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19160488"; MUTAGEN 210; /note="T->V: Reduced catalytic activity, but no effect on affinity for ATP."; /evidence="ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:17461553, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19160488"; MUTAGEN 337; /note="R->A: Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-340."; /evidence="ECO:0000269|PubMed:14734534, ECO:0000269|PubMed:18662541"; MUTAGEN 340; /note="L->A: Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-337."; /evidence="ECO:0000269|PubMed:14734534, ECO:0000269|PubMed:18662541"; MUTAGEN 414; /note="W->F: Abolishes interaction with CDC25C and reduces centrosomal localization."; /evidence="ECO:0000269|PubMed:17307877"; MUTAGEN 414; /note="W->F: No effect on centrosomal localization, nor on S-phase progression; when asscociated with A-427. Loss of centrosomal localization and of S-phase progression; when associated with A- 415 and A-427."; /evidence="ECO:0000269|PubMed:24018379"; MUTAGEN 415; /note="V->A: Loss of centrosomal localization and of S-phase progression; when associated with A- 414 and A-427."; /evidence="ECO:0000269|PubMed:24018379"; MUTAGEN 427; /note="L->A: No effect on centrosomal localization, nor on S-phase progression; when associated with A-414. Loss of centrosomal localization and of S-phase progression; when associated with A- 414 and A-415."; /evidence="ECO:0000269|PubMed:24018379"; MUTAGEN 492; /note="K->R: Severe mitotic defects leading to prometaphase delay. Increased localization at kinetochores leading to increased levels of phosphorylated BUBR1."; /evidence="ECO:0000269|PubMed:23455478"; MUTAGEN 538; /note="H->A: In pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with M-540."; /evidence="ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:16760428, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:19468302"; MUTAGEN 540; /note="K->M: In pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with A-538."; /evidence="ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:16760428, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:19468302
uniprot
proteins
post_translational_modification
PTM: Catalytic activity is enhanced by phosphorylation of Thr-210. Phosphorylation at Thr-210 is first detected on centrosomes in the G2 phase of the cell cycle, peaks in prometaphase and gradually disappears from centrosomes during anaphase. Dephosphorylation at Thr-210 at centrosomes is probably mediated by protein phosphatase 1C (PP1C), via interaction with PPP1R12A/MYPT1. Autophosphorylation and phosphorylation of Ser-137 may not be significant for the activation of PLK1 during mitosis, but may enhance catalytic activity during recovery after DNA damage checkpoint. Phosphorylated in vitro by STK10. {ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12442251, ECO:0000269|PubMed:12639966, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18615013}.; PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) in anaphase and following DNA damage, leading to its degradation by the proteasome. Ubiquitination is mediated via its interaction with FZR1/CDH1. Ubiquitination and subsequent degradation prevents entry into mitosis and is essential to maintain an efficient G2 DNA damage checkpoint. Monoubiquitination at Lys-492 by the BCR(KLHL22) ubiquitin ligase complex does not lead to degradation: it promotes PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. {ECO:0000269|PubMed:18662541, ECO:0000269|PubMed:23455478}.
uniprot
proteins
protein_family
CDC5/Polo subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Ser/Thr protein kinase family
uniprot
proteins
pubmed
11202906
uniprot
proteins
pubmed
12207013
uniprot
proteins
pubmed
12442251
uniprot
proteins
pubmed
12447691
uniprot
proteins
pubmed
12524548
uniprot
proteins
pubmed
12639966
uniprot
proteins
pubmed
12738781
uniprot
proteins
pubmed
12852856
uniprot
proteins
pubmed
12939256
uniprot
proteins
pubmed
14532005
uniprot
proteins
pubmed
14592974
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14734534
uniprot
proteins
pubmed
15070733
uniprot
proteins
pubmed
15148369
uniprot
proteins
pubmed
15469984
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616186
uniprot
proteins
pubmed
15661742
uniprot
proteins
pubmed
16198290
uniprot
proteins
pubmed
16247472
uniprot
proteins
pubmed
16439210
uniprot
proteins
pubmed
16645325
uniprot
proteins
pubmed
16760428
uniprot
proteins
pubmed
16980960
uniprot
proteins
pubmed
17081991
uniprot
proteins
pubmed
17218258
uniprot
proteins
pubmed
17307877
uniprot
proteins
pubmed
17310276
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17351640
uniprot
proteins
pubmed
17376779
uniprot
proteins
pubmed
17461553
uniprot
proteins
pubmed
17495026
uniprot
proteins
pubmed
17617734
uniprot
proteins
pubmed
17943598
uniprot
proteins
pubmed
17981789
uniprot
proteins
pubmed
18005335
uniprot
proteins
pubmed
18174154
uniprot
proteins
pubmed
18329369
uniprot
proteins
pubmed
18331714
uniprot
proteins
pubmed
18391401
uniprot
proteins
pubmed
18418051
uniprot
proteins
pubmed
18477460
uniprot
proteins
pubmed
18521620
uniprot
proteins
pubmed
18615013
uniprot
proteins
pubmed
18662541
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18794143
uniprot
proteins
pubmed
19029337
uniprot
proteins
pubmed
19160488
uniprot
proteins
pubmed
19351716
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19468300
uniprot
proteins
pubmed
19468302
uniprot
proteins
pubmed
19473992
uniprot
proteins
pubmed
19509060
uniprot
proteins
pubmed
19596235
uniprot
proteins
pubmed
19597481
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20671765
uniprot
proteins
pubmed
20679239
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21402792
uniprot
proteins
pubmed
21857149
uniprot
proteins
pubmed
21880710
uniprot
proteins
pubmed
22325354
uniprot
proteins
pubmed
22753416
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23455152
uniprot
proteins
pubmed
23455478
uniprot
proteins
pubmed
23509069
uniprot
proteins
pubmed
24018379
uniprot
proteins
pubmed
24067371
uniprot
proteins
pubmed
25503564
uniprot
proteins
pubmed
25659891
uniprot
proteins
pubmed
25986610
uniprot
proteins
pubmed
26811421
uniprot
proteins
pubmed
27979967
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28512243
uniprot
proteins
pubmed
29191835
uniprot
proteins
pubmed
30715179
uniprot
proteins
pubmed
32799774
uniprot
proteins
pubmed
34260926
uniprot
proteins
pubmed
37440612
uniprot
proteins
pubmed
37674080
uniprot
proteins
pubmed
41361016
uniprot
proteins
pubmed
7478607
uniprot
proteins
pubmed
7902533
uniprot
proteins
pubmed
7962193
uniprot
proteins
pubmed
8018557
uniprot
proteins
pubmed
8127874
uniprot
proteins
pubmed
8991084
uniprot
proteins
pubmed
9083047
uniprot
proteins
sequence_length
603
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:24018379}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:30715179}. Midbody {ECO:0000269|PubMed:30715179, ECO:0000269|PubMed:41361016}. Note=localization at the centrosome starts at the G1/S transition (PubMed:24018379). During early stages of mitosis, the phosphorylated form is detected on centrosomes and kinetochores. Localizes to the outer kinetochore. Presence of SGO1 and interaction with the phosphorylated form of BUB1 is required for the kinetochore localization. Localizes onto the central spindle by phosphorylating and docking at midzone proteins KIF20A/MKLP2 and PRC1. Colocalizes with FRY to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle. Localization to the centrosome is required for S phase progression (PubMed:24018379). Colocalizes with HSF1 at the spindle poles during prometaphase (PubMed:18794143). {ECO:0000269|PubMed:18794143, ECO:0000269|PubMed:24018379}.
uniprot
proteins