Plk1

Functionⁱ

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. 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 (By similarity).By similarity

Catalytic activityⁱ

ATP + a protein = ADP + a phosphoprotein.By similarity

Enzyme regulationⁱ

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 (By similarity).By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	82	ATPPROSITE-ProRule annotation	1
Binding siteⁱ	131	ATP; via carbonyl oxygenPROSITE-ProRule annotation	1
Active siteⁱ	176	Proton acceptorPROSITE-ProRule annotation	1
Binding siteⁱ	194	ATPPROSITE-ProRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	59 – 67	ATPPROSITE-ProRule annotation		9
Nucleotide bindingⁱ	178 – 181	ATPPROSITE-ProRule annotation		4

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
microtubule binding Source: UniProtKB
protein serine/threonine kinase activity Source: UniProtKB

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

centrosome cycle Source: UniProtKB
G2/M transition of mitotic cell cycle Source: UniProtKB
microtubule bundle formation Source: UniProtKB
mitotic cell cycle Source: UniProtKB
mitotic cytokinesis Source: UniProtKB
mitotic sister chromatid segregation Source: UniProtKB
mitotic spindle assembly checkpoint Source: UniProtKB
negative regulation of apoptotic process Source: UniProtKB
negative regulation of transcription by RNA polymerase II Source: UniProtKB
nuclear envelope disassembly Source: UniProtKB
polar body extrusion after meiotic divisions
Source: RGD
Inferred from mutant phenotypeⁱ
- 12784254
positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
positive regulation of ubiquitin protein ligase activity Source: UniProtKB
positive regulation of ubiquitin-protein transferase activity Source: UniProtKB
protein localization to chromatin Source: UniProtKB
protein localization to nuclear envelope Source: UniProtKB
protein phosphorylation
Source: MGI
Inferred from genetic interactionⁱ
- 19638580
response to antibiotic
Source: RGD
Inferred from expression patternⁱ
- 18512786
signal transduction involved in G2 DNA damage checkpoint Source: UniProtKB

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Serine/threonine-protein kinase, Transferase
Biological process	Cell cycle, Cell division, Mitosis
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	2.7.11.21 5301

BRENDAⁱ

2.7.11.21 5301

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Serine/threonine-protein kinase PLK1 (EC:2.7.11.21) Alternative name(s): Polo-like kinase 1 Short name: PLK-1
Gene namesⁱ	Name:Plk1 Synonyms:Plk
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

Rat genome database More...RGDⁱ	3352 Plk1

RGDⁱ

3352 Plk1

Cytoskeleton
- centrosome
  By similarity
  Manual assertion inferred from sequence similarity toⁱ
  - UniProtKB:P53350 (PLK1_HUMAN)
- spindle
  By similarity
  Manual assertion inferred from sequence similarity toⁱ
  - UniProtKB:P53350 (PLK1_HUMAN)
Nucleus
- Nucleus
  By similarity
  Manual assertion inferred from sequence similarity toⁱ
  - UniProtKB:P53350 (PLK1_HUMAN)
Other locations
- kinetochore
  By similarity
  Manual assertion inferred from sequence similarity toⁱ
  - UniProtKB:P53350 (PLK1_HUMAN)
- Midbody
  By similarity
  Manual assertion inferred from sequence similarity toⁱ
  - UniProtKB:P53350 (PLK1_HUMAN)

Note:

localization at the centrosome starts at the G1/S transition (By similarity). 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 (By similarity). Colocalizes with FRY to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle (By similarity). Localization to the centrosome is required for S phase progression (By similarity). Colocalizes with HSF1 at the spindle poles during prometaphase (By similarity).By similarity

Keywords - Cellular componentⁱ

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000086558	1 – 603	Serine/threonine-protein kinase PLK1Add BLAST		603

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Cross-linkⁱ	19	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	103	PhosphoserineBy similarity	1
Modified residueⁱ	137	PhosphoserineBy similarity	1
Modified residueⁱ	210	Phosphothreonine; by AURKABy similarity	1
Modified residueⁱ	214	PhosphothreonineBy similarity	1
Modified residueⁱ	269	Phosphoserine; by autocatalysisBy similarity	1
Modified residueⁱ	335	Phosphoserine; by autocatalysisBy similarity	1
Cross-linkⁱ	338	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	375	PhosphoserineBy similarity	1
Modified residueⁱ	450	PhosphoserineBy similarity	1
Cross-linkⁱ	492	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	498	PhosphothreonineBy similarity	1

Post-translational modificationⁱ

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 (By similarity).By similarity

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 (By similarity).By similarity

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbⁱ	Q62673
PRIDEⁱ	Q62673

PTM databases

iPTMnetⁱ	Q62673
PhosphoSitePlusⁱ	Q62673

Interactionⁱ

Subunit structureⁱ

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) with RIOK2 (By similarity).By similarity

GO - Molecular functionⁱ

microtubule binding Source: UniProtKB

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRINGⁱ	10116.ENSRNOP00000025629

STRINGⁱ

10116.ENSRNOP00000025629

Structureⁱ

3D structure databases

SMRⁱ	Q62673
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	53 – 305	Protein kinasePROSITE-ProRule annotationAdd BLAST	253
Domainⁱ	417 – 480	POLO box 1PROSITE-ProRule annotationAdd BLAST	64
Domainⁱ	515 – 584	POLO box 2PROSITE-ProRule annotationAdd BLAST	70

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	194 – 221	Activation loopBy similarityAdd BLAST	28
Regionⁱ	493 – 507	LinkerBy similarityAdd BLAST	15
Regionⁱ	538 – 540	Important for interaction with phosphorylated proteinsBy similarity	3

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	337 – 340	D-box that targets the protein for proteasomal degradation in anaphaseBy similarity		4

Domainⁱ

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 (By similarity).By similarity

Sequence similaritiesⁱ

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.PROSITE-ProRule annotation

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG0575 Eukaryota ENOG410XQBP LUCA
HOGENOMⁱ	HOG000248546
HOVERGENⁱ	HBG001843
InParanoidⁱ	Q62673
KEGG Orthology (KO) More...KOⁱ	K06631

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd13118 POLO_box_1, 1 hit cd13117 POLO_box_2, 1 hit cd14187 STKc_PLK1, 1 hit
Gene3Dⁱ	3.30.1120.30, 3 hits
InterProⁱ	View protein in InterPro IPR011009 Kinase-like_dom_sf IPR033702 PLK1_cat IPR033701 POLO_box_1 IPR033695 POLO_box_2 IPR000959 POLO_box_dom IPR036947 POLO_box_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00069 Pkinase, 1 hit PF00659 POLO_box, 2 hits
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS50078 POLO_BOX, 2 hits PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q62673-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNAAAKAGKL ARAPADLGKG GVPGDAAPGA PGAAPLAKEI PEVLMDPRSR 
        60         70         80         90        100
RQYVRGRFLG KGGFAKCFEI SDSDTKEVFP GKIVPKSLLL KPHQKEKMSM 
       110        120        130        140        150
EISIHRSLAH QHVVGFHGFF EDSDFVFVVL ELCRRRSLLE LHKRRKALTE 
       160        170        180        190        200
PEARYYLRQI VLGCQYLHRN QVIHRDLKLG NLFLNEDLEV KIGDFGLATK 
       210        220        230        240        250
VEYEGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI MYTLLVGKPP 
       260        270        280        290        300
FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTIHELL 
       310        320        330        340        350
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGVENP 
       360        370        380        390        400
LPDRPREKEE PVVRETNEAI ECHLSDLLQQ LTSVNASKPS ERGLVRQEEA 
       410        420        430        440        450
EDPACIPIFW VSKWVDYSDK YGLGYQLCDN SVGVLFNDST RLILYNDGDS 
       460        470        480        490        500
LQYIERDGTE SYLTVSSHPN SLMKKITLLN YFRNYMSEHL LKAGANITPR 
       510        520        530        540        550
EGDELARLPY LRTWFRTRSA IILHLSNGTV QINFFQDHTK LILCPLMAAV 
       560        570        580        590        600
TYINEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSACNRL 

KAS

Length:603

Mass (Da):68,291

Last modified:December 14, 2011 - v2

Checksum:ⁱD756DD742CB14F6E

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	27	A → V in AAA18885 (Ref. 1) Curated	1
Sequence conflictⁱ	32	G → V in AAA18885 (Ref. 1) Curated	1
Sequence conflictⁱ	45	M → V in AAA18885 (Ref. 1) Curated	1
Sequence conflictⁱ	51	R → Q in AAA18885 (Ref. 1) Curated	1
Sequence conflictⁱ	80	P → A in AAH83926 (PubMed:15489334).Curated	1
Sequence conflictⁱ	102	I → T in AAA18885 (Ref. 1) Curated	1
Sequence conflictⁱ	109	A → E in AAA18885 (Ref. 1) Curated	1
Sequence conflictⁱ	291	T → A in AAA18885 (Ref. 1) Curated	1
Sequence conflictⁱ	543 – 544	LC → RG in AAA18885 (Ref. 1) Curated	2

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U10188 mRNA Translation: AAA18885.1 BC083926 mRNA Translation: AAH83926.1
NCBI Reference Sequences More...RefSeqⁱ	NP_058796.1, NM_017100.1
UniGeneⁱ	Rn.11034

Genome annotation databases

GeneIDⁱ	25515
KEGGⁱ	rno:25515
UCSC genome browser More...UCSCⁱ	RGD:3352 rat

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
Q62673	Serine/threonine-protein kinase PLK1	)	HUMAN		603
UPI000274426C		PANPA		746
Serine/threonine-protein kinase PLK		MACFA		641
PLK1 isoform 5 (Fragment)		PONAB		105
UPI0001DEC3A9		AILME		620
+137

Protein	Similar proteins		Species	Score	Length
Q62673	Serine/threonine-protein kinase PLK1	)	HUMAN		603
UPI000274426C		PANPA		746
Serine/threonine-protein kinase PLK		MACFA		641
PLK1 isoform 5 (Fragment)		PONAB		105
UPI0001DEC3A9		AILME		620
+309

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U10188 mRNA Translation: AAA18885.1 BC083926 mRNA Translation: AAH83926.1
NCBI Reference Sequences More...RefSeqⁱ	NP_058796.1, NM_017100.1
UniGeneⁱ	Rn.11034

3D structure databases

SMRⁱ	Q62673
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	10116.ENSRNOP00000025629

STRINGⁱ

10116.ENSRNOP00000025629

PTM databases

iPTMnetⁱ	Q62673
PhosphoSitePlusⁱ	Q62673

Proteomic databases

PaxDbⁱ	Q62673
PRIDEⁱ	Q62673

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	25515
KEGGⁱ	rno:25515
UCSC genome browser More...UCSCⁱ	RGD:3352 rat

Organism-specific databases

CTDⁱ	5347
Rat genome database More...RGDⁱ	3352 Plk1

Phylogenomic databases

eggNOGⁱ	KOG0575 Eukaryota ENOG410XQBP LUCA
HOGENOMⁱ	HOG000248546
HOVERGENⁱ	HBG001843
InParanoidⁱ	Q62673
KEGG Orthology (KO) More...KOⁱ	K06631

Enzyme and pathway databases

BRENDAⁱ	2.7.11.21 5301

BRENDAⁱ

2.7.11.21 5301

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:Q62673

PROⁱ

PR:Q62673

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd13118 POLO_box_1, 1 hit cd13117 POLO_box_2, 1 hit cd14187 STKc_PLK1, 1 hit
Gene3Dⁱ	3.30.1120.30, 3 hits
InterProⁱ	View protein in InterPro IPR011009 Kinase-like_dom_sf IPR033702 PLK1_cat IPR033701 POLO_box_1 IPR033695 POLO_box_2 IPR000959 POLO_box_dom IPR036947 POLO_box_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00069 Pkinase, 1 hit PF00659 POLO_box, 2 hits
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS50078 POLO_BOX, 2 hits PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PLK1_RAT
Accessionⁱ	Q62673Primary (citable) accession number: Q62673 Secondary accession number(s): F1LNH6, Q5XHX4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
	Last sequence update:	December 14, 2011
	Last modified:	May 23, 2018
	This is version 159 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

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Supporting data

UniProtKB - Q62673 (PLK1_RAT)

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Serine/threonine-protein kinase PLK1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoskeleton

Nucleus

Other locations

Cytoskeleton

Nucleus

Other locations

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

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Documents

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Functionⁱ

Enzyme regulationⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ