P53350 (PLK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase PLK1
EC=2.7.11.21

Alternative name(s):
Polo-like kinase 1
Short name=PLK-1
Serine/threonine-protein kinase 13
Short name=STPK13

Gene names

Name:	PLK1
Synonyms:	PLK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	603 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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, MLF1IP, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, PLK1S1/KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGOL1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1 and WEE1. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating PLK1S1/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, MLF1IP, 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, MLF1IP, 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 SGOL1: required for spindle pole localization of isoform 3 of SGOL1 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.26 Ref.27 Ref.28 Ref.32 Ref.34 Ref.36 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.47 Ref.48 Ref.51 Ref.52 Ref.53 Ref.55 Ref.56 Ref.62 Ref.68
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by phosphorylation of Thr-210 by AURKA; phosphorylation by AURKA is enhanced by BORA. Once activated, activity is stimulated by binding target proteins. Binding of target proteins has no effect on the non-activated kinase. 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. Ref.48 Ref.66
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, MLF1IP and CDC25C. Interacts with isoform 3 of SGOL1. 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 SGOL2. 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. Ref.16 Ref.23 Ref.24 Ref.25 Ref.27 Ref.31 Ref.33 Ref.37 Ref.38 Ref.39 Ref.41 Ref.42 Ref.45 Ref.50 Ref.51 Ref.53 Ref.55 Ref.60 Ref.61 Ref.62 Ref.66 Ref.68
Subcellular location	Nucleus. Chromosome › centromere › kinetochore. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle. Midbody. Note: During early stages of mitosis, the phosphorylated form is detected on centrosomes and kinetochores. Localizes to the outer kinetochore. Presence of SGOL1 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. Ref.8 Ref.11 Ref.16 Ref.17 Ref.25 Ref.32 Ref.43 Ref.48 Ref.53 Ref.55 Ref.56 Ref.61 Ref.62 Ref.66 Ref.68
Tissue specificity	Placenta and colon.
Developmental stage	Accumulates to a maximum during the G2 and M phases, declines to a nearly undetectable level following mitosis and throughout G1 phase, and then begins to accumulate again during S phase.
Induction	By growth-stimulating agents. Ref.48 Ref.66
Domain	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. Ref.16 Ref.36 Ref.62
Post-translational modification	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. Ref.10 Ref.12 Ref.14 Ref.43 Ref.48 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. Ref.18 Ref.38
Involvement in disease	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.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily. Contains 2 POLO box domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2 DNA damage checkpoint Inferred from direct assay Ref.38. Source: UniProtKB G2/M transition of mitotic cell cycle Inferred from direct assay Ref.47. Source: UniProtKB activation of mitotic anaphase-promoting complex activity Inferred from direct assay Ref.21. Source: UniProtKB anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome cell proliferation Traceable author statement Ref.4. Source: ProtInc centrosome organization Inferred from mutant phenotype Ref.43Ref.8. Source: UniProtKB cytokinesis Inferred from direct assay Ref.36Ref.56. Source: UniProtKB microtubule bundle formation Inferred from direct assay Ref.16. Source: UniProtKB mitotic metaphase/anaphase transition Traceable author statement. Source: Reactome mitotic prometaphase Traceable author statement. Source: Reactome mitotic prophase Traceable author statement. Source: Reactome negative regulation of apoptotic process Inferred from mutant phenotype Ref.44. Source: UniProtKB negative regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from mutant phenotype PubMed 21041660. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.44. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay PubMed 16885022. Source: UniProtKB positive regulation of peptidyl-threonine phosphorylation Inferred from mutant phenotype PubMed 21041660. Source: BHF-UCL protein destabilization Inferred from direct assay PubMed 16885022. Source: UniProtKB protein localization to chromatin Inferred from direct assay PubMed 21111234. Source: UniProtKB protein ubiquitination Inferred from direct assay PubMed 16885022. Source: UniProtKB regulation of mitotic anaphase Inferred from mutant phenotype PubMed 21041660. Source: BHF-UCL regulation of protein binding Inferred from mutant phenotype PubMed 21041660. Source: BHF-UCL
Cellular_component	centrosome Inferred from direct assay Ref.17Ref.43Ref.48PubMed 21399614Ref.8. Source: UniProtKB condensed nuclear chromosome outer kinetochore Inferred from direct assay PubMed 18195732. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome midbody Inferred from direct assay Ref.55. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome spindle microtubule Inferred from direct assay PubMed 21041660. Source: BHF-UCL spindle midzone Inferred from direct assay Ref.56. Source: UniProtKB spindle pole Inferred from direct assay PubMed 21041660. Source: BHF-UCL
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from direct assay Ref.16. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.17Ref.16Ref.21Ref.36Ref.44Ref.43Ref.47Ref.55Ref.56. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BIRC6	Q9NR09	3	EBI-476768,EBI-1765160
CHEK2	O96017	6	EBI-476768,EBI-1180783
EIF4B	P23588	3	EBI-476768,EBI-970310
EVI5	O60447	2	EBI-476768,EBI-852291
FADD	Q13158	9	EBI-476768,EBI-494804
HSPA1B	P08107	5	EBI-476768,EBI-629985
MCM7	P33993	4	EBI-476768,EBI-355924
OFD1	O75665	2	EBI-476768,EBI-716327
PHC2	Q8IXK0	2	EBI-476768,EBI-713786
SLX4	Q8IY92	6	EBI-476768,EBI-2370740
TANK	Q92844	3	EBI-476768,EBI-356349

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 603

603

Serine/threonine-protein kinase PLK1

PRO_0000086556

Regions

Domain

53 – 305

253

Protein kinase

Domain

417 – 480

64

POLO box 1

Domain

515 – 584

70

POLO box 2

Nucleotide binding

59 – 67

9

ATP

Nucleotide binding

178 – 181

4

ATP

Region

194 – 221

28

Activation loop

Region

493 – 507

15

Linker

Region

538 – 540

3

Important for interaction with phosphorylated proteins By similarity

Motif

337 – 340

4

D-box that targets the protein for proteasomal degradation in anaphase

Sites

Active site

176

1

Proton acceptor

Binding site

82

1

ATP

Binding site

131

1

ATP; via carbonyl oxygen

Binding site

194

1

ATP

Amino acid modifications

Modified residue

6

1

Phosphothreonine Ref.46

Modified residue

103

1

Phosphoserine Ref.46

Modified residue

137

1

Phosphoserine Probable

Modified residue

210

1

Phosphothreonine; by AURKA Ref.10 Ref.43 Ref.46 Ref.48 Ref.49 Ref.54 Ref.58

Modified residue

214

1

Phosphothreonine Ref.46 Ref.49 Ref.54

Modified residue

269

1

Phosphoserine; by autocatalysis By similarity

Modified residue

335

1

Phosphoserine Ref.12

Modified residue

375

1

Phosphoserine Ref.46

Modified residue

450

1

Phosphoserine Ref.46

Modified residue

498

1

Phosphothreonine Ref.46

Natural variations

Natural variant

12

1

R → L in a lung squamous cell carcinoma sample; somatic mutation. Ref.69

VAR_041018

Natural variant

261

1

L → F. Ref.69
Corresponds to variant rs35056440 [ dbSNP | Ensembl ].

VAR_041019

Natural variant

297

1

N → D.
Corresponds to variant rs16972799 [ dbSNP | Ensembl ].

VAR_051659

Natural variant

332

1

L → V. Ref.69
Corresponds to variant rs45489499 [ dbSNP | Ensembl ].

VAR_041020

Natural variant

463

1

L → H. Ref.69
Corresponds to variant rs45569335 [ dbSNP | Ensembl ].

VAR_041021

Natural variant

518

1

R → H. Ref.69
Corresponds to variant rs56027600 [ dbSNP | Ensembl ].

VAR_041022

Natural variant

595

1

S → L.
Corresponds to variant rs34001032 [ dbSNP | Ensembl ].

VAR_051660

Natural variant

599

1

R → H.
Corresponds to variant rs34954545 [ dbSNP | Ensembl ].

VAR_051661

Experimental info

Mutagenesis

67

1

C → V in analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with G-130. Ref.56

Mutagenesis

82

1

K → M or R: Kinase defective mutant, abolishes activity. Ref.10 Ref.11 Ref.44 Ref.47 Ref.48

Mutagenesis

130

1

L → G in analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with V-67. Ref.56

Mutagenesis

137

1

S → A: No change in activity. Increases activity and restores recovery after DNA damage checkpoint; when associated with D-210. Ref.10 Ref.48

Mutagenesis

137

1

S → D: Increases activity. Results in a block in G1/S. Ref.10 Ref.48

Mutagenesis

176

1

D → N: Abolishes kinase activity. Ref.48

Mutagenesis

194

1

D → A: Does not interfere with FRY-binding. Ref.61

Mutagenesis

210

1

T → A: Abolishes activity. Abolishes checkpoint recovery. Ref.10 Ref.11 Ref.47 Ref.48 Ref.64

Mutagenesis

210

1

T → D: Increases activity and restores recovery after DNA damage checkpoint. Ref.10 Ref.11 Ref.47 Ref.48 Ref.64

Mutagenesis

210

1

T → V: Reduced catalytic activity, but no effect on affinity for ATP. Ref.10 Ref.11 Ref.47 Ref.48 Ref.64

Mutagenesis

337

1

R → A: Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-340. Ref.18 Ref.38

Mutagenesis

340

1

L → A: Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-337. Ref.18 Ref.38

Mutagenesis

414

1

W → F: Abolishes interaction with CDC25C and reduces centrosomal localization. Ref.66

Mutagenesis

538

1

H → A in pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with M-540. Ref.25 Ref.43 Ref.56 Ref.62

Mutagenesis

540

1

K → M in pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with A-538. Ref.25 Ref.43 Ref.56 Ref.62

Sequence conflict

2

1

S → T in AAA56634. Ref.1

Sequence conflict

11

1

A → P in AAA56634. Ref.1

Sequence conflict

58

1

F → L in AAA56634. Ref.1

Sequence conflict

60

1

G → S in AAA56634. Ref.1

Sequence conflict

73

1

A → V in AAA36659. Ref.2

Sequence conflict

73

1

A → V in AAB36946. Ref.7

Sequence conflict

123

1

N → T in CAA62260. Ref.6

Sequence conflict

141

1

L → P in CAA53536. Ref.4

Sequence conflict

227

1

G → E in CAA53536. Ref.4

Sequence conflict

301

1

N → G in AAA36659. Ref.2

Sequence conflict

495

1

A → G in AAA36659. Ref.2

Sequence conflict

501

1

E → Q in AAA36659. Ref.2

Secondary structure

1

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603

Helix Strand Turn

Details...

Beta strand

42 – 46

5

Turn

47 – 50

4

Beta strand

51 – 62

12

Beta strand

65 – 72

8

Turn

73 – 75

3

Beta strand

78 – 85

8

Helix

86 – 88

3

Helix

92 – 106

15

Beta strand

116 – 121

6

Beta strand

123 – 131

9

Helix

138 – 145

8

Helix

150 – 169

20

Helix

179 – 181

3

Beta strand

182 – 184

3

Beta strand

190 – 192

3

Helix

220 – 223

4

Beta strand

224 – 226

3

Helix

231 – 246

16

Helix

256 – 264

9

Helix

276 – 285

10

Helix

290 – 292

3

Helix

296 – 301

6

Helix

303 – 306

4

Helix

316 – 319

4

Helix

373 – 386

14

Helix

389 – 391

3

Beta strand

392 – 394

3

Helix

397 – 400

4

Helix

403 – 405

3

Beta strand

411 – 416

6

Turn

418 – 420

3

Beta strand

421 – 427

7

Beta strand

432 – 436

5

Beta strand

441 – 444

4

Beta strand

448 – 454

7

Beta strand

460 – 467

8

Helix

470 – 472

3

Helix

473 – 489

17

Turn

493 – 496

4

Turn

503 – 505

3

Beta strand

511 – 516

6

Beta strand

518 – 525

8

Beta strand

530 – 534

5

Turn

535 – 537

3

Beta strand

540 – 544

5

Turn

545 – 548

4

Beta strand

549 – 553

5

Beta strand

559 – 563

5

Helix

564 – 570

7

Helix

574 – 591

18

Sequences

	Sequence		Length	Mass (Da)
	P53350 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 178C2F13C10E8206	FASTA	603	68,255
	10 20 30 40 50 60 MSAAVTAGKL ARAPADPGKA GVPGVAAPGA PAAAPPAKEI PEVLVDPRSR RRYVRGRFLG 70 80 90 100 110 120 KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQREKMSM EISIHRSLAH QHVVGFHGFF 130 140 150 160 170 180 EDNDFVFVVL ELCRRRSLLE LHKRRKALTE PEARYYLRQI VLGCQYLHRN RVIHRDLKLG 190 200 210 220 230 240 NLFLNEDLEV KIGDFGLATK VEYDGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI 250 260 270 280 290 300 MYTLLVGKPP FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTINELL 310 320 330 340 350 360 NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGLENP LPERPREKEE 370 380 390 400 410 420 PVVRETGEVV DCHLSDMLQQ LHSVNASKPS ERGLVRQEEA EDPACIPIFW VSKWVDYSDK 430 440 450 460 470 480 YGLGYQLCDN SVGVLFNDST RLILYNDGDS LQYIERDGTE SYLTVSSHPN SLMKKITLLK 490 500 510 520 530 540 YFRNYMSEHL LKAGANITPR EGDELARLPY LRTWFRTRSA IILHLSNGSV QINFFQDHTK 550 560 570 580 590 600 LILCPLMAAV TYIDEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL KAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of human and murine homologues of the Drosophila polo serine-threonine kinase." Hamanaka R., Maloid S., Smith M.R., O'Connell C.D., Longo D.L., Ferris D.K. Cell Growth Differ. 5:249-257(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Cell cycle- and terminal differentiation-associated regulation of the mouse mRNA encoding a conserved mitotic protein kinase." Lake R.J., Jelinek W.R. Mol. Cell. Biol. 13:7793-7801(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5." Golsteyn R.M., Schultz S.J., Bartek J., Ziemiecki A., Ried T., Nigg E.A. J. Cell Sci. 107:1509-1517(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Induction and down-regulation of PLK, a human serine/threonine kinase expressed in proliferating cells and tumors." Holtrich U., Wolf G., Braeuninger A., Karn T., Boehme B., Ruebsamen-Waigmann H., Strebhardt K. Proc. Natl. Acad. Sci. U.S.A. 91:1736-1740(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon and Lung.
[6]	"Identification and functional characterization of the human and murine polo-like kinase (Plk) promoter." Brauninger A., Strebhardt K., Rubsamen-Waigmann H. Oncogene 11:1793-1800(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
[7]	"Cell cycle regulation of the human polo-like kinase (PLK) promoter." Uchiumi T., Longo D.L., Ferris D.K. J. Biol. Chem. 272:9166-9174(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
[8]	"Antibody microinjection reveals an essential role for human polo-like kinase 1 (Plk1) in the functional maturation of mitotic centrosomes." Lane H.A., Nigg E.A. J. Cell Biol. 135:1701-1713(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CENTROSOME MATURATION, SUBCELLULAR LOCATION.
[9]	"The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase." Roshak A.K., Capper E.A., Imburgia C., Fornwald J., Scott G., Marshall L.A. Cell. Signal. 12:405-411(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CDC25C.
[10]	"Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase." Jang Y.-J., Ma S., Terada Y., Erikson R.L. J. Biol. Chem. 277:44115-44120(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-137 AND THR-210, MUTAGENESIS OF LYS-82; SER-137 AND THR-210.
[11]	"Cooperative phosphorylation including the activity of polo-like kinase 1 regulates the subcellular localization of cyclin B1." Yuan J., Eckerdt F., Bereiter-Hahn J., Kurunci-Csacsko E., Kaufmann M., Strebhardt K. Oncogene 21:8282-8292(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CCNB1, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-82 AND THR-210.
[12]	"Identification of phosphorylation sites in the polo-like kinases Plx1 and Plk1 by a novel strategy based on element and electrospray high resolution mass spectrometry." Wind M., Kelm O., Nigg E.A., Lehmann W.D. Proteomics 2:1516-1523(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-335.
[13]	"Polo-like kinase 1 regulates Nlp, a centrosome protein involved in microtubule nucleation." Casenghi M., Meraldi P., Weinhart U., Duncan P.I., Korner R., Nigg E.A. Dev. Cell 5:113-125(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF NINL.
[14]	"Stk10, a new member of the polo-like kinase kinase family highly expressed in hematopoietic tissue." Walter S.A., Cutler R.E. Jr., Martinez R., Gishizky M., Hill R.J. J. Biol. Chem. 278:18221-18228(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY STK10.
[15]	"Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate." Nakajima H., Toyoshima-Morimoto F., Taniguchi E., Nishida E. J. Biol. Chem. 278:25277-25280(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PKMYT1.
[16]	"Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis." Neef R., Preisinger C., Sutcliffe J., Kopajtich R., Nigg E.A., Mayer T.U., Barr F.A. J. Cell Biol. 162:863-875(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF KIF20A, DOMAIN POLO BOX, SUBCELLULAR LOCATION, INTERACTION WITH KIF20A.
[17]	"Active cyclin B1-Cdk1 first appears on centrosomes in prophase." Jackman M., Lindon C., Nigg E.A., Pines J. Nat. Cell Biol. 5:143-148(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CCNB1, SUBCELLULAR LOCATION.
[18]	"Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells." Lindon C., Pines J. J. Cell Biol. 164:233-241(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PROTEASOMAL DEGRADATION, IDENTIFICATION OF D-BOX MOTIF, MUTAGENESIS OF ARG-337 AND LEU-340.
[19]	"Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbetaTrCP-dependent destruction of the APC inhibitor Emi1." Hansen D.V., Loktev A.V., Ban K.H., Jackson P.K. Mol. Biol. Cell 15:5623-5634(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FBXO5.
[20]	"M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP." Watanabe N., Arai H., Nishihara Y., Taniguchi M., Watanabe N., Hunter T., Osada H. Proc. Natl. Acad. Sci. U.S.A. 101:4419-4424(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF WEE1.
[21]	"Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome." Moshe Y., Boulaire J., Pagano M., Hershko A. Proc. Natl. Acad. Sci. U.S.A. 101:7937-7942(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FBXO5.
[22]	"Cdk1/Erk2- and Plk1-dependent phosphorylation of a centrosome protein, Cep55, is required for its recruitment to midbody and cytokinesis." Fabbro M., Zhou B.-B., Takahashi M., Sarcevic B., Lal P., Graham M.E., Gabrielli B.G., Robinson P.J., Nigg E.A., Ono Y., Khanna K.K. Dev. Cell 9:477-488(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CEP55.
[23]	"The forkhead-associated domain protein Cep170 interacts with Polo-like kinase 1 and serves as a marker for mature centrioles." Guarguaglini G., Duncan P.I., Stierhof Y.D., Holmstroem T., Duensing S., Nigg E.A. Mol. Biol. Cell 16:1095-1107(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CEP170.
[24]	"The evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor emi1." Eldridge A.G., Loktev A.V., Hansen D.V., Verschuren E.W., Reimann J.D.R., Jackson P.K. Cell 124:367-380(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EVI5.
[25]	"Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is required for the kinetochore localization of Plk1." Qi W., Tang Z., Yu H. Mol. Biol. Cell 17:3705-3716(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BUB1 AND BUB1B, MUTAGENESIS OF HIS-538 AND LYS-540.
[26]	"The Plk1 target Kizuna stabilizes mitotic centrosomes to ensure spindle bipolarity." Oshimori N., Ohsugi M., Yamamoto T. Nat. Cell Biol. 8:1095-1101(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PLK1S1.
[27]	"Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase stimulates association of the mitotic kinase Plk1 and accumulation of GTP-bound RhoA." Niiya F., Tatsumoto T., Lee K.S., Miki T. Oncogene 25:827-837(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF ECT2, INTERACTION WITH ECT2.
[28]	"Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation." Kang Y.H., Park J.-E., Yu L.-R., Soung N.-K., Yun S.-M., Bang J.K., Seong Y.-S., Yu H., Garfield S., Veenstra T.D., Lee K.S. Mol. Cell 24:409-422(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MLF1IP.
[29]	"Expression of polo-like kinase 1 (PLK1) protein predicts the survival of patients with gastric carcinoma." Kanaji S., Saito H., Tsujitani S., Matsumoto S., Tatebe S., Kondo A., Ozaki M., Ito H., Ikeguchi M. Oncology 70:126-133(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CANCER.
[30]	"A cell proliferation and chromosomal instability signature in anaplastic thyroid carcinoma." Salvatore G., Nappi T.C., Salerno P., Jiang Y., Garbi C., Ugolini C., Miccoli P., Basolo F., Castellone M.D., Cirafici A.M., Melillo R.M., Fusco A., Bittner M.L., Santoro M. Cancer Res. 67:10148-10158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CANCER.
[31]	"PICH, a centromere-associated SNF2 family ATPase, is regulated by Plk1 and required for the spindle checkpoint." Baumann C., Koerner R., Hofmann K., Nigg E.A. Cell 128:101-114(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ERCC6L.
[32]	"Shugoshin 1 plays a central role in kinetochore assembly and is required for kinetochore targeting of Plk1." Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J., Stukenberg T., Kallio M.J. Cell Cycle 6:1579-1585(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[33]	"TTDN1 is a Plk1-interacting protein involved in maintenance of cell cycle integrity." Zhang Y., Tian Y., Chen Q., Chen D., Zhai Z., Shu H.-B. Cell. Mol. Life Sci. 64:632-640(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TTDN1.
[34]	"Polo-like kinase 1 facilitates chromosome alignment during prometaphase through BubR1." Matsumura S., Toyoshima F., Nishida E. J. Biol. Chem. 282:15217-15227(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF BUB1B.
[35]	"Expression of PLK1 and survivin in diffuse large B-cell lymphoma." Liu L., Zhang M., Zou P. Leuk. Lymphoma 48:2179-2183(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CANCER.
[36]	"Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1." Neef R., Gruneberg U., Kopajtich R., Li X., Nigg E.A., Sillje H., Barr F.A. Nat. Cell Biol. 9:436-444(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PRC1, DOMAIN POLO BOX.
[37]	"The tumor suppressor CYLD regulates entry into mitosis." Stegmeier F., Sowa M.E., Nalepa G., Gygi S.P., Harper J.W., Elledge S.J. Proc. Natl. Acad. Sci. U.S.A. 104:8869-8874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CYLD, MASS SPECTROMETRY.
[38]	"The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint." Bassermann F., Frescas D., Guardavaccaro D., Busino L., Peschiaroli A., Pagano M. Cell 134:256-267(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY THE APC/C COMPLEX, INTERACTION WITH FZR1, MUTAGENESIS OF ARG-337 AND LEU-340.
[39]	"Final stages of cytokinesis and midbody ring formation are controlled by BRUCE." Pohl C., Jentsch S. Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BIRC6/BRUCE.
[40]	"p73-mediated transcriptional activity is negatively regulated by polo-like kinase 1." Soond S.M., Barry S.P., Melino G., Knight R.A., Latchman D.S., Stephanou A. Cell Cycle 7:1214-1223(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TP73.
[41]	"Plk1 regulates mitotic Aurora A function through betaTrCP-dependent degradation of hBora." Chan E.H., Santamaria A., Sillje H.H., Nigg E.A. Chromosoma 117:457-469(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PHOSPHORYLATED BORA.
[42]	"sSgo1, a major splice variant of Sgo1, functions in centriole cohesion where it is regulated by Plk1." Wang X., Yang Y., Duan Q., Jiang N., Huang Y., Darzynkiewicz Z., Dai W. Dev. Cell 14:331-341(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF SGOL1, INTERACTION WITH SGOL1.
[43]	"Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1." Yamashiro S., Yamakita Y., Totsukawa G., Goto H., Kaibuchi K., Ito M., Hartshorne D.J., Matsumura F. Dev. Cell 14:787-797(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A, PHOSPHORYLATION AT THR-210, DEPHOSPHORYLATION BY PPP1C, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-538 AND LYS-540.
[44]	"Inhibitory role of Plk1 in the regulation of p73-dependent apoptosis through physical interaction and phosphorylation." Koida N., Ozaki T., Yamamoto H., Ono S., Koda T., Ando K., Okoshi R., Kamijo T., Omura K., Nakagawara A. J. Biol. Chem. 283:8555-8563(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TP73, MUTAGENESIS OF LYS-82.
[45]	"FAM29A promotes microtubule amplification via recruitment of the NEDD1-gamma-tubulin complex to the mitotic spindle." Zhu H., Coppinger J.A., Jang C.-Y., Yates J.R. III, Fang G. J. Cell Biol. 183:835-848(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FAM29A.
[46]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-103; THR-210; THR-214; SER-375; SER-450 AND THR-498, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[47]	"Plk1-dependent phosphorylation of FoxM1 regulates a transcriptional programme required for mitotic progression." Fu Z., Malureanu L., Huang J., Wang W., Li H., van Deursen J.M., Tindall D.J., Chen J. Nat. Cell Biol. 10:1076-1082(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FOXM1, MUTAGENESIS OF LYS-82 AND THR-210.
[48]	"Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery." Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R., Freire R., Clouin C., Taylor S.S., Yaffe M.B., Medema R.H. Nature 455:119-123(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-210 BY AURKA, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-82; SER-137; ASP-176 AND THR-210.
[49]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[50]	"Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair." Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., Elledge S.J., Harper J.W. Cell 138:63-77(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SLX4.
[51]	"Plk1-mediated phosphorylation of Topors regulates p53 stability." Yang X., Li H., Zhou Z., Wang W.H., Deng A., Andrisani O., Liu X. J. Biol. Chem. 284:18588-18592(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TOPORS, INTERACTION WITH TOPORS.
[52]	"Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for targeting of the gammaTuRC to the centrosome." Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q., Zhang C. J. Cell Sci. 122:2240-2251(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS NEDD1 KINASE.
[53]	"Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a." Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G. J. Cell Sci. 122:1334-1341(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH KIF2A, SUBCELLULAR LOCATION.
[54]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, MASS SPECTROMETRY.
[55]	"Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation." Wolfe B.A., Takaki T., Petronczki M., Glotzer M. PLoS Biol. 7:E1000110-E1000110(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RACGAP1, INTERACTION WITH PRC1, SUBCELLULAR LOCATION.
[56]	"Plk1 self-organization and priming phosphorylation of HsCYK-4 at the spindle midzone regulate the onset of division in human cells." Burkard M.E., Maciejowski J., Rodriguez-Bravo V., Repka M., Lowery D.M., Clauser K.R., Zhang C., Shokat K.M., Carr S.A., Yaffe M.B., Jallepalli P.V. PLoS Biol. 7:E1000111-E1000111(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RACGAP1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-67; LEU-130; HIS-538 AND LYS-540.
[57]	"Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy." Strebhardt K. Nat. Rev. Drug Discov. 9:643-660(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION, REVIEW ON ENZYME REGULATION.
[58]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[59]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[60]	"The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and facilitates chromosome alignment." Dunsch A.K., Linnane E., Barr F.A., Gruneberg U. J. Cell Biol. 192:959-968(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH KNSTRN; SPAG5; DYNLL1 AND SGOL2.
[61]	"Furry protein promotes Aurora A-mediated polo-like kinase 1 activation." Ikeda M., Chiba S., Ohashi K., Mizuno K. J. Biol. Chem. 287:27670-27681(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FRY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-194.
[62]	"The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain." Elia A.E., Rellos P., Haire L.F., Chao J.W., Ivins F.J., Hoepker K., Mohammad D., Cantley L.C., Smerdon S.J., Yaffe M.B. Cell 115:83-95(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 367-603 IN COMPLEX WITH PHOSPHORYLATED PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN POLO BOX, INTERACTION WITH CDC25C, MUTAGENESIS OF HIS-538 AND LYS-540.
[63]	"The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex." Cheng K.Y., Lowe E.D., Sinclair J., Nigg E.A., Johnson L.N. EMBO J. 22:5757-5768(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 367-603 IN COMPLEX WITH PHOSPHORYLATED PEPTIDE.
[64]	"Structure of the catalytic domain of human polo-like kinase 1." Kothe M., Kohls D., Low S., Coli R., Cheng A.C., Jacques S.L., Johnson T.L., Lewis C., Loh C., Nonomiya J., Sheils A.L., Verdries K.A., Wynn T.A., Kuhn C., Ding Y.H. Biochemistry 46:5960-5971(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 13-345 OF MUTANT VAL-210 IN COMPLEXES WITH ATP ANALOGS, MUTAGENESIS OF THR-210.
[65]	"Selectivity-determining residues in Plk1." Kothe M., Kohls D., Low S., Coli R., Rennie G.R., Feru F., Kuhn C., Ding Y.H. Chem. Biol. Drug Des. 70:540-546(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 37-330 IN COMPLEX WITH SYNTHETIC INHIBITOR BI 2536.
[66]	"Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization." Garcia-Alvarez B., de Carcer G., Ibanez S., Bragado-Nilsson E., Montoya G. Proc. Natl. Acad. Sci. U.S.A. 104:3107-3112(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 365-603 IN COMPLEX WITH CDC25C, SUBCELLULAR LOCATION, INTERACTION WITH CDC25C, ENZYME REGULATION, MUTAGENESIS OF TRP-414.
[67]	"Structure of wild-type Plk-1 kinase domain in complex with a selective DARPin." Bandeiras T.M., Hillig R.C., Matias P.M., Eberspaecher U., Fanghanel J., Thomaz M., Miranda S., Crusius K., Putter V., Amstutz P., Gulotti-Georgieva M., Binz H.K., Holz C., Schmitz A.A., Lang C., Donner P., Egner U., Carrondo M.A., Muller-Tiemann B. Acta Crystallogr. D 64:339-353(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-345 IN COMPLEX WITH A DARPIN.
[68]	"Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1." Yun S.M., Moulaei T., Lim D., Bang J.K., Park J.E., Shenoy S.R., Liu F., Kang Y.H., Liao C., Soung N.K., Lee S., Yoon D.Y., Lim Y., Lee D.H., Otaka A., Appella E., McMahon J.B., Nicklaus M.C. , Burke T.R. Jr., Yaffe M.B., Wlodawer A., Lee K.S. Nat. Struct. Mol. Biol. 16:876-882(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 371-603 IN COMPLEX WITH PHOSPHOPEPTIDE, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PHOSPHORYLATED MLF1IP.
[69]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-12; PHE-261; VAL-332; HIS-463 AND HIS-518.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U01038 mRNA. Translation: AAA56634.1.
L19559 mRNA. Translation: AAA36659.1.
X73458 mRNA. Translation: CAA51837.1.
X75932 mRNA. Translation: CAA53536.1.
BC002369 mRNA. Translation: AAH02369.1.
BC003002 mRNA. Translation: AAH03002.1.
BC014846 mRNA. Translation: AAH14846.1.
X90725 Genomic DNA. Translation: CAA62260.1.
U78073 Genomic DNA. Translation: AAB36946.1.

IPI

IPI00021248.

PIR

S34130.

RefSeq

NP_005021.2. NM_005030.3.

UniGene

Hs.592049.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q4K	X-ray	2.30	A/B/C	345-603	[»]
1Q4O	X-ray	2.20	A/B	367-603	[»]
1UMW	X-ray	1.90	A/B	367-603	[»]
2OGQ	X-ray	1.95	A	365-603	[»]
2OJX	X-ray	2.85	A	365-603	[»]
2OU7	X-ray	2.40	A	13-345	[»]
2OWB	X-ray	2.10	A	13-345	[»]
2RKU	X-ray	1.95	A	37-330	[»]
2V5Q	X-ray	2.30	A/B	33-345	[»]
2YAC	X-ray	2.20	A	36-345	[»]
3BZI	X-ray	2.10	A	365-603	[»]
3C5L	X-ray	2.33	A	373-593	[»]
3FC2	X-ray	2.45	A	13-345	[»]
3FVH	X-ray	1.58	A	371-603	[»]
3HIH	X-ray	1.70	A/B	371-593	[»]
3HIK	X-ray	1.77	A	367-603	[»]
3KB7	X-ray	2.50	A	36-345	[»]
3P2W	X-ray	1.66	A	371-594	[»]
3P2Z	X-ray	1.79	A	371-594	[»]
3P34	X-ray	1.40	A	371-594	[»]
3P35	X-ray	2.09	A/B/C	371-594	[»]
3P36	X-ray	1.59	A	371-594	[»]
3P37	X-ray	2.38	A/B/C	371-594	[»]
3Q1I	X-ray	1.40	A	371-594	[»]
3RQ7	X-ray	1.55	A	371-603	[»]
3THB	X-ray	2.50	A	13-345	[»]
4A4L	X-ray	2.35	A	36-345	[»]
4A4O	X-ray	2.70	A	36-345	[»]
4DFW	X-ray	1.55	A	367-603	[»]
4E67	X-ray	2.10	A	371-594	[»]
4E9C	X-ray	1.70	A	371-594	[»]
4E9D	X-ray	2.75	A	371-594	[»]
4H5X	X-ray	1.95	A/B	367-603	[»]
4H71	X-ray	1.93	A/B	367-603	[»]
4HCO	X-ray	2.75	A/B	367-603	[»]

DisProt

DP00428.

ProteinModelPortal

P53350.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29696N.

IntAct

P53350. 61 interactions.

MINT

MINT-86316.

STRING

9606.ENSP00000300093.

PTM databases

PhosphoSite

P53350.

Polymorphism databases

DMDM

1709658.

Proteomic databases

PaxDb

P53350.

PRIDE

P53350.

Protocols and materials databases

DNASU

5347.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300093; ENSP00000300093; ENSG00000166851.

GeneID

5347.

KEGG

hsa:5347.

UCSC

uc002dlz.1. human.

Organism-specific databases

CTD

5347.

GeneCards

GC16P023698.

HGNC

HGNC:9077. PLK1.

HPA

HPA051638.
HPA053229.

MIM

602098. gene.

neXtProt

NX_P53350.

PharmGKB

PA33410.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000248546.

HOVERGEN

HBG001843.

InParanoid

P53350.

KO

K06631.

OrthoDB

EOG4JDH6F.

PhylomeDB

P53350.

Enzyme and pathway databases

BRENDA

2.7.11.21. 2681.

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.
foxopathway. FoxO family signaling.

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpress

P53350.

Bgee

P53350.

CleanEx

HS_PLK1.

Genevestigator

P53350.

GermOnline

ENSG00000166851. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P53350.

ChEMBL

CHEMBL3024.

ChiTaRS

PLK1. human.

EvolutionaryTrace

P53350.

GenomeRNAi

5347.

NextBio

20722.

SOURCE

Search...

Entry information

Entry name

PLK1_HUMAN

Accession

Primary (citable) accession number: P53350
Secondary accession number(s): Q15153, Q99746

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 153 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.