PLK2

Serine/threonine-protein kinase PLK2 is an enzyme that in humans is encoded by the PLK2 gene. Serum-inducible kinase is a member of the 'polo' family of serine/threonine protein kinases that have a role in normal cell division. [supplied by OMIM]

Protein-coding gene in the species Homo sapiens

PLK2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4I5M, 4I5P, 4I6B, 4I6F, 4I6H, 4RS6, 4XB0
Identifiers
Aliases	PLK2, SNK, hPlk2, hSNK, polo like kinase 2
External IDs	OMIM: 607023; MGI: 1099790; HomoloGene: 21317; GeneCards: PLK2; OMA:PLK2 - orthologs
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q11.2 Start 58,453,982 bp[1] End 58,460,139 bp[1]
Gene location (Mouse) Chr. Chromosome 13 (mouse)[2] Band 13|13 D2.1 Start 110,531,580 bp[2] End 110,537,378 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in spleen apex of heart canal of the cervix ectocervix islet of Langerhans epithelium of colon skin of abdomen Achilles tendon gallbladder tibial nerve Top expressed in CA3 field Region I of hippocampus proper perirhinal cortex entorhinal cortex primary motor cortex primary visual cortex olfactory tubercle choroid plexus of fourth ventricle superior frontal gyrus left lung lobe More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity protein-containing complex binding signal transducer activity ATP-dependent protein binding kinase activity protein binding ATP binding protein serine/threonine kinase activity Cellular component cytoplasm centrosome cell projection intracellular anatomical structure dendrite centriole chromatin cytoskeleton cytosol Biological process positive regulation of protein catabolic process positive regulation of autophagy phosphorylation mitotic cell cycle checkpoint signaling G1 phase mitotic spindle organization Rap protein signal transduction regulation of centriole replication negative regulation of apoptotic process memory regulation of synaptic plasticity protein phosphorylation peptidyl-serine phosphorylation long-term depression mitotic cell cycle positive regulation of I-kappaB kinase/NF-kappaB signaling Ras protein signal transduction positive regulation of protein binding negative regulation of dendritic spine development positive regulation of proteasomal ubiquitin-dependent protein catabolic process long-term potentiation DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10769 20620 Ensembl ENSG00000145632 ENSMUSG00000021701 UniProt Q9NYY3 P53351 RefSeq (mRNA) NM_006622 NM_001252226 NM_152804 RefSeq (protein) NP_001239155 NP_006613 NP_690017 Location (UCSC) Chr 5: 58.45 – 58.46 Mb Chr 13: 110.53 – 110.54 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Serine/threonine-protein kinase PLK2 is an enzyme that in humans is encoded by the PLK2 gene.^[5]

Serum-inducible kinase is a member of the 'polo' family of serine/threonine protein kinases that have a role in normal cell division. [supplied by OMIM]^[5]

References

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1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000145632 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000021701 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ ^{a b} "Entrez Gene: PLK2 polo-like kinase 2 (Drosophila)".

Further reading

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• Kauselmann G, Weiler M, Wulff P, et al. (1999). "The polo-like protein kinases Fnk and Snk associate with a Ca(2+)- and integrin-binding protein and are regulated dynamically with synaptic plasticity". EMBO J. 18 (20): 5528–39. doi:10.1093/emboj/18.20.5528. PMC 1171621. PMID 10523297.
• Ouyang B, Li W, Pan H, et al. (1999). "The physical association and phosphorylation of Cdc25C protein phosphatase by Prk". Oncogene. 18 (44): 6029–36. doi:10.1038/sj.onc.1202983. PMID 10557092.
• Holtrich U, Wolf G, Yuan J, et al. (2000). "Adhesion induced expression of the serine/threonine kinase Fnk in human macrophages". Oncogene. 19 (42): 4832–9. doi:10.1038/sj.onc.1203845. PMID 11039900.
• Liby K, Wu H, Ouyang B, et al. (2002). "Identification of the human homologue of the early-growth response gene Snk, encoding a serum-inducible kinase". DNA Seq. 11 (6): 527–33. doi:10.3109/10425170109041337. PMID 11696980. S2CID 46552280.
• Shimizu-Yoshida Y, Sugiyama K, Rogounovitch T, et al. (2002). "Radiation-inducible hSNK gene is transcriptionally regulated by p53 binding homology element in human thyroid cells". Biochem. Biophys. Res. Commun. 289 (2): 491–8. doi:10.1006/bbrc.2001.5993. PMID 11716500.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ma S, Liu MA, Yuan YL, Erikson RL (2003). "The serum-inducible protein kinase Snk is a G1 phase polo-like kinase that is inhibited by the calcium- and integrin-binding protein CIB". Mol. Cancer Res. 1 (5): 376–84. PMID 12651910.
• Matsuda A, Suzuki Y, Honda G, et al. (2003). "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways". Oncogene. 22 (21): 3307–18. doi:10.1038/sj.onc.1206406. PMID 12761501.
• Burns TF, Fei P, Scata KA, et al. (2003). "Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic catastrophe in paclitaxel (taxol)-exposed cells". Mol. Cell. Biol. 23 (16): 5556–71. doi:10.1128/MCB.23.16.5556-5571.2003. PMC 166320. PMID 12897130.
• Ma S, Charron J, Erikson RL (2003). "Role of Plk2 (Snk) in mouse development and cell proliferation". Mol. Cell. Biol. 23 (19): 6936–43. doi:10.1128/MCB.23.19.6936-6943.2003. PMC 193943. PMID 12972611.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Yogosawa S, Hatakeyama S, Nakayama KI, et al. (2006). "Ubiquitylation and degradation of serum-inducible kinase by hVPS18, a RING-H2 type ubiquitin ligase". J. Biol. Chem. 280 (50): 41619–27. doi:10.1074/jbc.M508397200. PMID 16203730.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Park YY, Kim SH, Kim YJ, et al. (2007). "Polo-like kinase 2 gene expression is regulated by the orphan nuclear receptor estrogen receptor-related receptor gamma (ERRgamma)". Biochem. Biophys. Res. Commun. 362 (1): 107–13. Bibcode:2007BBRC..362..107P. doi:10.1016/j.bbrc.2007.07.170. PMID 17706602.
• Matthew EM, Yen TJ, Dicker DT, et al. (2007). "Replication stress, defective S-phase checkpoint and increased death in Plk2-deficient human cancer cells". Cell Cycle. 6 (20): 2571–8. doi:10.4161/cc.6.20.5079. PMID 17912033.

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