PLK2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PLK2_RAT
• UniProt AC: Q9R012
• Protein Name: Serine/threonine-protein kinase PLK2
• Gene Name: Plk2
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 682
• Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cell projection, dendrite . Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and
• Protein Description: Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress..
• Protein Sequence: MELLRTITYQPAAGTKMCEQALGKACGGDSKKKRPQQPSEDGQSQAQVTPAAPHHHHHHSHSGPEISRIIVDPTTGKRYCRGKVLGKGGFAKCYEMTDLTNNKVYAAKIIPHSRVAKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEAMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYTMPSSLLAPAKHLIASMLSKNPEDRPSLDDIIRHDFFLQGFTPDRLSSSCCHTVPDFHLSSPAKNFFKKAAAALFGGKKDKARYNDTHNKVSKEDEDIYKLRHDLKKTSITQQPSKHRTDEELQPPPTTFAKSGTSAVENKQQIGDAIRMIVRGTLGSCSSSSECLEDSTMGSVADTVARVLRGCLENMPEADCIPKEQLSTSFQWVTKWVDYSNKYGFGYQLSDHTVGVLFNNGAHMSLLPDKKTVHYYAELGQCSVFPATDAPEQFISQVTVLKYFSHYMEENLMDGGDLPSVTDIRRPRLYLLQWLKSDKALMMLFNDGTFQVNFYHDHTKIIICNQNEEYLLTYINEDRISTTFRLTTLLMSGCSLELKHRMEYALNMLLQRCN

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
236	Phosphorylation	PLEHRRRTICGTPNY CCHHHCCCCCCCCCC	20.86	20802490
393	Phosphorylation	SKEDEDIYKLRHDLK CCCHHHHHHHHHHHH	19.11	-
435	Ubiquitination	GTSAVENKQQIGDAI CCCHHHCHHHHHHHH	30.03	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PLK2_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
236	T	Phosphorylation	Catalytic activity is enhanced by phosphorylation of Thr-236.	20802490

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PLK2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VPS18_HUMAN	VPS18	physical	16203730
VPS16_HUMAN	VPS16	physical	16203730
VP33A_HUMAN	VPS33A	physical	16203730
VPS11_HUMAN	VPS11	physical	16203730

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Plk2 attachment to NSF induces homeostatic removal of GluA2 duringchronic overexcitation.";
Evers D.M., Matta J.A., Hoe H.S., Zarkowsky D., Lee S.H., Isaac J.T.,Pak D.T.;
Nat. Neurosci. 13:1199-1207(2010).
Cited for: FUNCTION, INTERACTION WITH NSF, PHOSPHORYLATION AT THR-236, ANDMUTAGENESIS OF LYS-108; THR-236 AND TRP-504.
PubMed: 20802490