Product: PLK1 Antibody
Catalog: AF2685
Description: Rabbit polyclonal antibody to PLK1
Application: WB IHC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Zebrafish, Bovine, Horse, Sheep, Rabbit, Dog, Xenopus
Mol.Wt.: 62kDa; 68kD(Calculated).
Uniprot: P53350
RRID: AB_2847781

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Clonality:
Polyclonal
Specificity:
PLK1 Antibody detects endogenous levels of PLK1.
RRID:
AB_2847781
Cite Format: Affinity Biosciences Cat# AF2685, RRID:AB_2847781.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Cell cycle regulated protein kinase; PLK 1; PLK; PLK-1; plk1; PLK1_HUMAN; Polo like kinase 1; Polo-like kinase 1; Serine/threonine protein kinase 13; Serine/threonine protein kinase PLK1; Serine/threonine-protein kinase 13; Serine/threonine-protein kinase PLK1; STPK 13; STPK13;

Immunogens

Immunogen:

A synthesized peptide derived from human PLK1.

Uniprot:
Gene(ID):
Expression:
P53350 PLK1_HUMAN:

Placenta and colon.

Sequence:
MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERPREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS

PTMs - P53350 As Substrate

Site PTM Type Enzyme
S2 Acetylation
S2 Phosphorylation
T6 Phosphorylation
K9 Acetylation
K9 Ubiquitination
K19 Ubiquitination
K38 Ubiquitination
S49 Phosphorylation Q13153 (PAK1)
K61 Ubiquitination
K66 Ubiquitination
K76 Ubiquitination
K82 Ubiquitination
K86 Ubiquitination
K91 Ubiquitination
S99 Phosphorylation
S103 Phosphorylation
S137 Phosphorylation P41279 (MAP3K8) , Q13237 (PRKG2) , Q9NYY3 (PLK2)
K143 Ubiquitination
K146 Ubiquitination
K178 Ubiquitination
K200 Ubiquitination
K209 Ubiquitination
T210 Phosphorylation P41279 (MAP3K8) , O14965 (AURKA) , O94804 (STK10) , Q96GD4 (AURKB)
T214 Phosphorylation
Y217 Phosphorylation
S224 Phosphorylation
K225 Ubiquitination
K265 Ubiquitination
K272 Ubiquitination
Y309 Phosphorylation
S326 Phosphorylation P49137 (MAPKAPK2)
S330 Phosphorylation
S331 Phosphorylation
S335 Phosphorylation
K338 Ubiquitination
T341 Phosphorylation
K345 Ubiquitination
K358 Ubiquitination
T366 Phosphorylation
S375 Phosphorylation
S383 Phosphorylation P49137 (MAPKAPK2)
S387 Phosphorylation
K388 Ubiquitination
K413 Ubiquitination
S418 Phosphorylation
Y425 Phosphorylation
Y445 Phosphorylation
S450 Phosphorylation
T459 Phosphorylation
S461 Phosphorylation
Y462 Phosphorylation
T464 Phosphorylation
S466 Phosphorylation
K474 Ubiquitination
K480 Ubiquitination
K492 Sumoylation
K492 Ubiquitination
T498 Phosphorylation
S565 Phosphorylation
K574 Ubiquitination
S578 Phosphorylation
K589 Ubiquitination
S597 Phosphorylation

PTMs - P53350 As Enzyme

Substrate Site Source
O00139 (KIF2A) T554 Uniprot
O14641 (DVL2) T206 Uniprot
O14920 (IKBKB) S733 Uniprot
O14920 (IKBKB) S740 Uniprot
O14920 (IKBKB) S750 Uniprot
O15169 (AXIN1) S157 Uniprot
O15259 (NPHP1) T87 Uniprot
O15350 (TP73) T27 Uniprot
O15392 (BIRC5) S20 Uniprot
O15392 (BIRC5) T21 Uniprot
O43663 (PRC1) S615 Uniprot
O43663 (PRC1) T616 Uniprot
O60260 (PRKN) S378 Uniprot
O60285 (NUAK1) S476 Uniprot
O60285 (NUAK1) S480 Uniprot
O60563 (CCNT1) S564 Uniprot
O60566 (BUB1B) S676 Uniprot
O60566 (BUB1B) T680 Uniprot
O60566 (BUB1B) T792 Uniprot
O60566 (BUB1B) T1008 Uniprot
O75116 (ROCK2) T967 Uniprot
O75116 (ROCK2) S1099 Uniprot
O75116 (ROCK2) S1133 Uniprot
O75116 (ROCK2) S1374 Uniprot
O94901 (SUN1) S138 Uniprot
O95251 (KAT7) S57 Uniprot
O95425 (SVIL) S238 Uniprot
O95613 (PCNT) T1209 Uniprot
O95613 (PCNT) T1221 Uniprot
O95613 (PCNT) S1235 Uniprot
O95613 (PCNT) S1241 Uniprot
O96017-12 (CHEK2) T26 Uniprot
O96017 (CHEK2) T68 Uniprot
O96017 (CHEK2) S164 Uniprot
O96017 (CHEK2) T205 Uniprot
O96017 (CHEK2) S210 Uniprot
P04049 (RAF1) S338 Uniprot
P04049 (RAF1) S339 Uniprot
P06748-1 (NPM1) S4 Uniprot
P08670 (VIM) S83 Uniprot
P08670 (VIM) S459 Uniprot
P11388 (TOP2A) S1337 Uniprot
P11388 (TOP2A) T1343 Uniprot
P11388 (TOP2A) S1525 Uniprot
P13693 (TPT1) S46 Uniprot
P13693 (TPT1) S64 Uniprot
P14635-1 (CCNB1) S126 Uniprot
P14635 (CCNB1) S128 Uniprot
P14635 (CCNB1) S133 Uniprot
P14635-1 (CCNB1) S147 Uniprot
P18031 (PTPN1) S286 Uniprot
P18031 (PTPN1) S393 Uniprot
P25490 (YY1) T39 Uniprot
P30260 (CDC27) T205 Uniprot
P30260 (CDC27) T209 Uniprot
P30260 (CDC27) S426 Uniprot
P30260 (CDC27) T430 Uniprot
P30260 (CDC27) S434 Uniprot
P30260 (CDC27) S435 Uniprot
P30260 (CDC27) T446 Uniprot
P30291 (WEE1) S53 Uniprot
P30291 (WEE1) S123 Uniprot
P30305 (CDC25B) S50 Uniprot
P30305 (CDC25B) T58 Uniprot
P30305 (CDC25B) T127 Uniprot
P30305 (CDC25B) T167 Uniprot
P30305 (CDC25B) S209 Uniprot
P30305 (CDC25B) T265 Uniprot
P30305 (CDC25B) S291 Uniprot
P30305 (CDC25B) S353 Uniprot
P30305 (CDC25B) S375 Uniprot
P30305 (CDC25B) S397 Uniprot
P30305 (CDC25B) T404 Uniprot
P30305 (CDC25B) S465 Uniprot
P30305 (CDC25B) S513 Uniprot
P30307-1 (CDC25C) S198 Uniprot
P30622 (CLIP1) S195 Uniprot
P30622 (CLIP1) S312 Uniprot
P30622 (CLIP1) S1364 Uniprot
P30626 (SRI) T155 Uniprot
P35222 (CTNNB1) S718 Uniprot
P35568 (IRS1) S24 Uniprot
P36507 (MAP2K2) S222 Uniprot
P36507 (MAP2K2) S226 Uniprot
P36956 (SREBF1) S467 Uniprot
P37840 (SNCA) S129 Uniprot
P38398 (BRCA1) S1164 Uniprot
P47736 (RAP1GAP) S525 Uniprot
P51587 (BRCA2) S193 Uniprot
P51587 (BRCA2) T203 Uniprot
P51587 (BRCA2) S205 Uniprot
P51587 (BRCA2) S206 Uniprot
P51587 (BRCA2) T207 Uniprot
P51587 (BRCA2) S239 Uniprot
P54274 (TERF1) S435 Uniprot
P60484 (PTEN) S380 Uniprot
P60484 (PTEN) T382 Uniprot
P60484 (PTEN) T383 Uniprot
P62826 (RAN) S135 Uniprot
P78527 (PRKDC) S3205 Uniprot
Q00613 (HSF1) S216 Uniprot
Q00839 (HNRNPU) S59 Uniprot
Q00987 (MDM2) S260 Uniprot
Q01538-1 (MYT1) S429 Uniprot
Q02750 (MAP2K1) S218 Uniprot
Q02750 (MAP2K1) S222 Uniprot
Q06609 (RAD51) S14 Uniprot
Q07817 (BCL2L1) S62 Uniprot
Q08050 (FOXM1) S730 Uniprot
Q08050 (FOXM1) S739 Uniprot
Q12834 (CDC20) S170 Uniprot
Q12888 (TP53BP1) S1618 Uniprot
Q13042 (CDC16) S112 Uniprot
Q13158 (FADD) S194 Uniprot
Q13188 (STK3) S15 Uniprot
Q13188 (STK3) S18 Uniprot
Q13188 (STK3) S316 Uniprot
Q13416 (ORC2) S188 Uniprot
Q13526 (PIN1) S65 Uniprot
Q14203 (DCTN1) S179 Uniprot
Q14674 (ESPL1) T1363 Uniprot
Q14674 (ESPL1) S1399 Uniprot
Q15022 (SUZ12) S539 Uniprot
Q15022 (SUZ12) S541 Uniprot
Q15022 (SUZ12) S546 Uniprot
Q15468 (STIL) S1108 Uniprot
Q15468 (STIL) S1116 Uniprot
Q16143 (SNCB) S118 Uniprot
Q2M2Z5 (KIZ) T379 Uniprot
Q2NKX8 (ERCC6L) T1063 Uniprot
Q38SD2 (LRRK1) S1817 Uniprot
Q3KR16 (PLEKHG6) T574 Uniprot
Q49MG5 (MAP9) S289 Uniprot
Q53EZ4 (CEP55) S436 Uniprot
Q5FBB7 (SGO1) S73 Uniprot
Q5FBB7 (SGO1) T146 Uniprot
Q6PGQ7 (BORA) S497 Uniprot
Q6PGQ7 (BORA) T501 Uniprot
Q71F23 (CENPU) S77 Uniprot
Q71F23 (CENPU) T78 Uniprot
Q7L2Z9 (CENPQ) T123 Uniprot
Q7L2Z9 (CENPQ) T135 Uniprot
Q7L2Z9 (CENPQ) S138 Uniprot
Q7L2Z9 (CENPQ) S139 Uniprot
Q7L2Z9 (CENPQ) S248 Uniprot
Q7L2Z9 (CENPQ) S249 Uniprot
Q7L2Z9 (CENPQ) S253 Uniprot
Q7L2Z9 (CENPQ) S255 Uniprot
Q7L2Z9 (CENPQ) T256 Uniprot
Q8IWB6 (TEX14) S437 Uniprot
Q8N4N8 (KIF2B) T125 Uniprot
Q8N4N8 (KIF2B) S204 Uniprot
Q8NHV4 (NEDD1) T382 Uniprot
Q8NHV4 (NEDD1) S397 Uniprot
Q8NHV4 (NEDD1) S426 Uniprot
Q8NHV4 (NEDD1) S637 Uniprot
Q8TEP8-3 (CEP192) T44 Uniprot
Q92994 (BRF1) S450 Uniprot
Q96BK5 (PINX1) S110 Uniprot
Q96BK5 (PINX1) S117 Uniprot
Q96BK5 (PINX1) T141 Uniprot
Q96BK5 (PINX1) S226 Uniprot
Q96BK5 (PINX1) T317 Uniprot
Q96CV9 (OPTN) S177 Uniprot
Q96T23 (RSF1) S1359 Uniprot
Q99640 (PKMYT1) S426 Uniprot
Q99640 (PKMYT1) T495 Uniprot
Q99661 (KIF2C) S592 Uniprot
Q99661 (KIF2C) S595 Uniprot
Q99661 (KIF2C) S621 Uniprot
Q99661 (KIF2C) S632 Uniprot
Q99661 (KIF2C) S633 Uniprot
Q99661 (KIF2C) S715 Uniprot
Q99741 (CDC6) T37 Uniprot
Q9BQQ3 (GORASP1) S189 Uniprot
Q9BVS4 (RIOK2) S335 Uniprot
Q9BVS4 (RIOK2) S380 Uniprot
Q9BVS4 (RIOK2) S548 Uniprot
Q9H0H5 (RACGAP1) S149 Uniprot
Q9H0H5 (RACGAP1) S157 Uniprot
Q9H0H5 (RACGAP1) S164 Uniprot
Q9H0H5 (RACGAP1) S170 Uniprot
Q9H0H5 (RACGAP1) S214 Uniprot
Q9H0H5 (RACGAP1) T260 Uniprot
Q9H1A4 (ANAPC1) T291 Uniprot
Q9H1A4 (ANAPC1) S355 Uniprot
Q9H1A4 (ANAPC1) S373 Uniprot
Q9H1A4 (ANAPC1) S377 Uniprot
Q9H1A4 (ANAPC1) T520 Uniprot
Q9H1A4 (ANAPC1) T530 Uniprot
Q9H1A4 (ANAPC1) S547 Uniprot
Q9H1A4 (ANAPC1) S686 Uniprot
Q9H1A4 (ANAPC1) S688 Uniprot
Q9H1A4 (ANAPC1) T701 Uniprot
Q9H2D6 (TRIOBP) T447 Uniprot
Q9H2D6-5 (TRIOBP) T457 Uniprot
Q9H2D6 (TRIOBP) T2229 Uniprot
Q9H8V3-4 (ECT2) T815 Uniprot
Q9HAW4 (CLSPN) S30 Uniprot
Q9NS56 (TOPORS) S718 Uniprot
Q9NYZ3 (GTSE1) S223 Uniprot
Q9NYZ3 (GTSE1) S435 Uniprot
Q9UBB4 (ATXN10) S77 Uniprot
Q9UBB4 (ATXN10) T82 Uniprot
Q9UBW7 (ZMYM2) S303 Uniprot
Q9UBW7 (ZMYM2) S305 Uniprot
Q9UBW7 (ZMYM2) S309 Uniprot
Q9UJX2 (CDC23) T562 Uniprot
Q9UJX2 (CDC23) T565 Uniprot
Q9UJX3 (ANAPC7) S51 Uniprot
Q9UJX3 (ANAPC7) S57 Uniprot
Q9UJX3 (ANAPC7) S64 Uniprot
Q9UJX5 (ANAPC4) S779 Uniprot
Q9UKT4 (FBXO5) S145 Uniprot
Q9UKT4 (FBXO5) S149 Uniprot
Q9Y265 (RUVBL1) T239 Uniprot
Q9Y266 (NUDC) S274 Uniprot
Q9Y266 (NUDC) S326 Uniprot
Q9Y2I6 (NINL) S87 Uniprot
Q9Y2I6 (NINL) S88 Uniprot
Q9Y2I6-1 (NINL) T161 Uniprot
Q9Y2I6 (NINL) S686 Uniprot
Q9Y2T1 (AXIN2) S311 Uniprot
Q9Y2Z0 (SUGT1) S331 Uniprot
Q9Y5T5 (USP16) S330 Uniprot
Q9Y5T5 (USP16) S386 Uniprot
Q9Y5T5 (USP16) S486 Uniprot
Q9Y6D9 (MAD1L1) S22 Uniprot
Q9Y6D9 (MAD1L1) S29 Uniprot
Q9Y6D9 (MAD1L1) T680 Uniprot

Research Backgrounds

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. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. 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. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. 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. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function. 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. 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. 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. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning. 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. Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope. Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock. 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. Regulates mitotic progression by phosphorylating RIOK2.

PTMs:

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.

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.

Subcellular Location:

Nucleus. Chromosome>Centromere>Kinetochore. Cytoplasm>Cytoskeleton>Microtubule organizing center>Centrosome. Cytoplasm>Cytoskeleton>Spindle. Midbody.
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).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Placenta and colon.

Subunit Structure:

Interacts with CEP170 and EVI5. Interacts and phosphorylates ERCC6L. Interacts with FAM29A. Interacts with SLX4/BTBD12 and TTDN1. Interacts with BUB1B. Interacts (via POLO-box domain) with the phosphorylated form of BUB1, CENPU and CDC25C. Interacts with isoform 3 of SGO1. Interacts with BORA, KIF2A and AURKA. Interacts with TOPORS and CYLD. Interacts with ECT2; the interaction is stimulated upon phosphorylation of ECT2 on 'Thr-444'. Interacts with PRC1. Interacts with KIF20A/MKLP2 (when phosphorylated), leading to the recruitment at the central spindle. Interacts (via POLO box domains) with PPP1R12A/MYPT1 (when previously phosphorylated by CDK1). Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. Interacts with BIRC6/bruce. Interacts with CDK1-phosphorylated FRY; this interaction occurs in mitotic cells, but not in interphase cells. FRY interaction facilitates AURKA-mediated PLK1 phosphorylation. Interacts with CDK1-phosphorylated DCTN6 during mitotic prometaphase; the interaction facilitates recruitment to kinetochores. Interacts with CEP68; the interaction phosphorylates CEP68. Interacts (via POLO-box domain) with DCTN1. Interacts with FOPNL in later G1, S, G2 and M phases of the cell cycle; this interaction recruits PLK1 to centrosomes, a step required for S phase progression. Interacts with HSF1; this interaction increases upon heat shock but does not modulate neither HSF1 homotrimerization nor DNA-binding activities. Interacts with HNRNPU; this interaction induces phosphorylation of HNRNPU in mitosis. Interacts (via its N-terminus) to RIOK2. Interacts with KLHL22.

Family&Domains:

The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK1 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them. PLK1 can also create its own docking sites by mediating phosphorylation of serine-[phosphothreonine/phosphoserine]-(proline/X) motifs subsequently recognized by the POLO box domains.

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.

Research Fields

· Cellular Processes > Cell growth and death > Cell cycle.   (View pathway)

· Cellular Processes > Cell growth and death > Oocyte meiosis.   (View pathway)

· Environmental Information Processing > Signal transduction > FoxO signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Progesterone-mediated oocyte maturation.

References

1). Z-Guggulsterone Induces Cell Cycle Arrest and Apoptosis by Targeting the p53/CCNB1/PLK1 Pathway in Triple-Negative Breast Cancer. ACS Omega, 2023 (PubMed: 36687039) [IF=4.1]

Application: IHC    Species: Mouse    Sample:

Figure 7 Z-GS suppresses in vivo TNBC tumorigenesis. (A,B) Images showing xenograft subcutaneous tumors in nude mice and dissected tumors, respectively. (C) Tumor volume growth curves. (D) Xenograft tumor weights treated with Z-GS (20 and 40 mg/kg) were significantly reduced (n = 5/group) when compared with controls. (E) Immunohistochemistry images showing p53, CCNB1, and PLK1 expression in control and Z-GS treatment groups. Scale bar 50 μm. Data are presented as the mean ± standard deviation. *p < 0.05 and ***p < 0.001 when compared with controls.

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