PLK3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PLK3_HUMAN
• UniProt AC: Q9H4B4
• Protein Name: Serine/threonine-protein kinase PLK3
• Gene Name: PLK3
• Organism: Homo sapiens (Human).
• Sequence Length: 646
• Subcellular Localization: Cytoplasm. Nucleus. Nucleus, nucleolus. Golgi apparatus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Translocates to the nucleus upon cisplatin treatment. Localizes to the Golgi apparatus during interphase. According to a repo
• Protein Description: Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that 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..
• Protein Sequence: MEPAAGFLSPRPFQRAAAAPAPPAGPGPPPSALRGPELEMLAGLPTSDPGRLITDPRSGRTYLKGRLLGKGGFARCYEATDTETGSAYAVKVIPQSRVAKPHQREKILNEIELHRDLQHRHIVRFSHHFEDADNIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLRQILSGLKYLHQRGILHRDLKLGNFFITENMELKVGDFGLAARLEPPEQRKKTICGTPNYVAPEVLLRQGHGPEADVWSLGCVMYTLLCGSPPFETADLKETYRCIKQVHYTLPASLSLPARQLLAAILRASPRDRPSIDQILRHDFFTKGYTPDRLPISSCVTVPDLTPPNPARSLFAKVTKSLFGRKKKSKNHAQERDEVSGLVSGLMRTSVGHQDARPEAPAASGPAPVSLVETAPEDSSPRGTLASSGDGFEEGLTVATVVESALCALRNCIAFMPPAEQNPAPLAQPEPLVWVSKWVDYSNKFGFGYQLSSRRVAVLFNDGTHMALSANRKTVHYNPTSTKHFSFSVGAVPRALQPQLGILRYFASYMEQHLMKGGDLPSVEEVEVPAPPLLLQWVKTDQALLMLFSDGTVQVNFYGDHTKLILSGWEPLLVTFVARNRSACTYLASHLRQLGCSPDLRQRLRYALRLLRDRSPA

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
9	Phosphorylation	EPAAGFLSPRPFQRA CCCCCCCCCCCCCHH	19.32	24719451
58	Phosphorylation	RLITDPRSGRTYLKG CCCCCCCCCCEEECC	37.71	27251275
61	Phosphorylation	TDPRSGRTYLKGRLL CCCCCCCEEECCEEC	36.41	27251275
70	Ubiquitination	LKGRLLGKGGFARCY ECCEECCCCCCCCEE	56.69	27667366
136	Phosphorylation	FEDADNIYIFLELCS CCCCCCEEEEHHHHC	7.59	21951684
164	Phosphorylation	LLEPEVRYYLRQILS HCCHHHHHHHHHHHH	16.42	22817900
187	Ubiquitination	GILHRDLKLGNFFIT CCCCCCCCCCCEEEE	59.65	22817900
194	Phosphorylation	KLGNFFITENMELKV CCCCEEEECCEEEEE	19.02	-
219	Phosphorylation	PPEQRKKTICGTPNY CHHHHCCCCCCCCCC	25.24	-
277	Phosphorylation	RCIKQVHYTLPASLS HHHHHHCCCCCHHCC	15.89	24043423
278	Phosphorylation	CIKQVHYTLPASLSL HHHHHCCCCCHHCCC	16.04	24043423
282	Phosphorylation	VHYTLPASLSLPARQ HCCCCCHHCCCCHHH	19.29	24043423
284	Phosphorylation	YTLPASLSLPARQLL CCCCHHCCCCHHHHH	29.79	24719451
327	Phosphorylation	PDRLPISSCVTVPDL CCCCCCCCCEECCCC	17.21	22210691
330	Phosphorylation	LPISSCVTVPDLTPP CCCCCCEECCCCCCC	30.56	22210691
346	Ubiquitination	PARSLFAKVTKSLFG HHHHHHHHHHHHHHC	43.00	27667366
348	Phosphorylation	RSLFAKVTKSLFGRK HHHHHHHHHHHHCCC	17.76	19413330
348	O-linked_Glycosylation	RSLFAKVTKSLFGRK HHHHHHHHHHHHCCC	17.76	30379171
349	Ubiquitination	SLFAKVTKSLFGRKK HHHHHHHHHHHCCCC	48.42	27667366
433	Phosphorylation	TVATVVESALCALRN CHHHHHHHHHHHHHH	18.22	-
502	Ubiquitination	MALSANRKTVHYNPT EEEECCCCEEECCCC	55.49	27667366
503	Phosphorylation	ALSANRKTVHYNPTS EEECCCCEEECCCCC	14.85	21712546
506	Phosphorylation	ANRKTVHYNPTSTKH CCCCEEECCCCCCCE	20.64	21712546
510	Phosphorylation	TVHYNPTSTKHFSFS EEECCCCCCCEEEEE	36.39	21712546
515	Phosphorylation	PTSTKHFSFSVGAVP CCCCCEEEEECCCCC	19.14	27732954
614	Phosphorylation	ARNRSACTYLASHLR HCCHHHHHHHHHHHH	22.68	22461510
615	Phosphorylation	RNRSACTYLASHLRQ CCHHHHHHHHHHHHH	10.52	22461510

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

Oops, there are no upstream regulatory protein records of PLK3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PLK3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PLK3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCH2_HUMAN	TRIP13	physical	16189514
P53_HUMAN	TP53	physical	11551930
CHK2_HUMAN	CHEK2	physical	12242661
P53_HUMAN	TP53	physical	12242661
MPIP3_HUMAN	CDC25C	physical	10557092
APRIO_HUMAN	PRNP	physical	18482256
PRIO_HUMAN	PRNP	physical	18482256
AURKA_HUMAN	AURKA	physical	15190214
BUB1B_HUMAN	BUB1B	physical	15190214
SYUA_HUMAN	SNCA	physical	19889641
SYUB_HUMAN	SNCB	physical	19889641
CENPU_HUMAN	CENPU	physical	19597481
PO2F1_HUMAN	POU2F1	physical	25416956
B2CL1_HUMAN	BCL2L1	physical	22617334

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-348, AND MASSSPECTROMETRY.
PubMed: 19413330