Q9H4B4 · PLK3_HUMAN

  • Protein
    Serine/threonine-protein kinase PLK3
  • Gene
    PLK3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1.

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site68-76ATP (UniProtKB | ChEBI)
Binding site91ATP (UniProtKB | ChEBI)
Active site185Proton acceptor

GO annotations

AspectTerm
Cellular Componentcentrosome
Cellular Componentcytoplasm
Cellular Componentdendrite
Cellular ComponentGolgi stack
Cellular Componentkinetochore
Cellular Componentneuronal cell body
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentspindle pole
Molecular FunctionATP binding
Molecular Functionp53 binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processapoptotic process
Biological Processcytoplasmic microtubule organization
Biological ProcessDNA damage response
Biological ProcessDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
Biological Processendomitotic cell cycle
Biological ProcessG1/S transition of mitotic cell cycle
Biological ProcessG2/M transition of mitotic cell cycle
Biological ProcessGolgi disassembly
Biological Processmitotic G1/S transition checkpoint signaling
Biological Processmitotic spindle organization
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processpositive regulation of chaperone-mediated autophagy
Biological Processpositive regulation of intracellular protein transport
Biological Processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia
Biological Processprotein phosphorylation
Biological Processregulation of cell division
Biological Processregulation of cytokinesis
Biological Processregulation of signal transduction by p53 class mediator
Biological Processresponse to osmotic stress
Biological Processresponse to radiation
Biological Processresponse to reactive oxygen species

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein kinase PLK3
  • EC number
  • Alternative names
    • Cytokine-inducible serine/threonine-protein kinase
    • FGF-inducible kinase
    • Polo-like kinase 3 (PLK-3)
    • Proliferation-related kinase

Gene names

    • Name
      PLK3
    • Synonyms
      CNK, FNK, PRK

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9H4B4
  • Secondary accessions
    • Q15767
    • Q5JR99
    • Q96CV1

Proteomes

Organism-specific databases

Subcellular Location

Note: Translocates to the nucleus upon cisplatin treatment. Localizes to the Golgi apparatus during interphase. According to a report, PLK3 localizes only in the nucleolus and not in the centrosome, or in any other location in the cytoplasm (PubMed:17264206).
The discrepancies in results may be explained by the PLK3 antibody specificity, by cell line-specific expression or post-translational modifications

Keywords

Disease & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_02109161in dbSNP:rs17884581
Natural variantVAR_02109268in dbSNP:rs17884316
Mutagenesis91Kinase defective mutant, abolishes activity.
Mutagenesis203Kinase defective mutant, abolishes activity.
Mutagenesis219Kinase-defective mutant.
Natural variantVAR_021093283in dbSNP:rs17880471
Mutagenesis467-468Abolishes localization to the centrosome and ability to induce the G2/M arrest.
Natural variantVAR_021094483in dbSNP:rs17884653
Natural variantVAR_062384491in dbSNP:rs17855444
Natural variantVAR_021095498in dbSNP:rs17880829
Natural variantVAR_021096618in dbSNP:rs17881786

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 705 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000865641-646Serine/threonine-protein kinase PLK3

Post-translational modification

Phosphorylated in an ATM-dependent manner following DNA damage. Phosphorylated as cells enter mitosis and dephosphorylated as cells exit mitosis.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Transcripts are highly detected in placenta, lung, followed by skeletal muscle, heart, pancreas, ovaries and kidney and weakly detected in liver and brain. May have a short half-live. In cells of hematopoietic origin, strongly and exclusively detected in terminally differentiated macrophages. Transcript expression appears to be down-regulated in primary lung tumor.

Induction

Cytokine and cellular adhesion trigger induction. Down-regulated in a majority of lung carcinoma samples.

Developmental stage

Expression is cell cycle regulated with a peak in G1 phase.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts (via the POLO-box domain) with CIB1; leading to inhibit PLK3 kinase activity. Interacts with GOLGB1.

Binary interactions

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-35Disordered
Compositional bias16-33Pro residues
Domain62-314Protein kinase
Region381-417Disordered
Domain463-541POLO box 1
Domain562-645POLO box 2

Domain

The POLO box domains act as phosphopeptide-binding module that recognizes and binds serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK3 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them (By similarity).
The POLO box domains mediate localization to the centrosome

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    646
  • Mass (Da)
    71,629
  • Last updated
    2004-08-16 v2
  • Checksum
    324CA3E9DE482514
MEPAAGFLSPRPFQRAAAAPAPPAGPGPPPSALRGPELEMLAGLPTSDPGRLITDPRSGRTYLKGRLLGKGGFARCYEATDTETGSAYAVKVIPQSRVAKPHQREKILNEIELHRDLQHRHIVRFSHHFEDADNIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLRQILSGLKYLHQRGILHRDLKLGNFFITENMELKVGDFGLAARLEPPEQRKKTICGTPNYVAPEVLLRQGHGPEADVWSLGCVMYTLLCGSPPFETADLKETYRCIKQVHYTLPASLSLPARQLLAAILRASPRDRPSIDQILRHDFFTKGYTPDRLPISSCVTVPDLTPPNPARSLFAKVTKSLFGRKKKSKNHAQERDEVSGLVSGLMRTSVGHQDARPEAPAASGPAPVSLVETAPEDSSPRGTLASSGDGFEEGLTVATVVESALCALRNCIAFMPPAEQNPAPLAQPEPLVWVSKWVDYSNKFGFGYQLSSRRVAVLFNDGTHMALSANRKTVHYNPTSTKHFSFSVGAVPRALQPQLGILRYFASYMEQHLMKGGDLPSVEEVEVPAPPLLLQWVKTDQALLMLFSDGTVQVNFYGDHTKLILSGWEPLLVTFVARNRSACTYLASHLRQLGCSPDLRQRLRYALRLLRDRSPA

Sequence caution

The sequence AAC50637.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict16in Ref. 1; CAC10659
Compositional bias16-33Pro residues
Sequence conflict20in Ref. 1; CAC10659
Sequence conflict99in Ref. 1; CAC10659
Sequence conflict353in Ref. 1; CAC10659
Sequence conflict419in Ref. 1; CAC10659
Sequence conflict464-470in Ref. 1; CAC10659
Sequence conflict522in Ref. 1; CAC10659

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ293866
EMBL· GenBank· DDBJ
CAC10659.1
EMBL· GenBank· DDBJ
mRNA
AY764184
EMBL· GenBank· DDBJ
AAU88146.1
EMBL· GenBank· DDBJ
Genomic DNA
AL592166
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471059
EMBL· GenBank· DDBJ
EAX07021.1
EMBL· GenBank· DDBJ
Genomic DNA
BC013899
EMBL· GenBank· DDBJ
AAH13899.1
EMBL· GenBank· DDBJ
mRNA
U56998
EMBL· GenBank· DDBJ
AAC50637.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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