PLK4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PLK4_MOUSE
• UniProt AC: Q64702
• Protein Name: Serine/threonine-protein kinase PLK4
• Gene Name: Plk4
• Organism: Mus musculus (Mouse).
• Sequence Length: 925
• Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Nucleus, nucleolus . Cleavage furrow . Associates with centrioles throughout the cell cycle. According to PubMed:11301255, it localizes to the nucleolus during G2, to the
• Protein Description: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Phosphorylates CDC25C and CHEK2. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (By similarity)..
• Protein Sequence: MAACIGERIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSVLELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRMKPFSEREARHFMHQIITGMLYLHSHGILHRDLTLSNILLTRNMNIKIADFGLATQLNMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRRNPADRLSLSSVLDHPFMSRNPSPKSKDVGTVEDSMDSGHATLSTTITASSGTSLSGSLLDRRLLVGQPLPNKITVFQKNKNSSDFSSGDGSNFCTQWGNPEQEANSRGRGRVIEDAEERPHSRYLRRAHSSDRASPSNQSRAKTYSVERCHSVEMLSKPRRSLDENQHSSNHHCLGKTPFPFADQTPQMEMVQQWFGNLQMNAHLGETNEHHTVSPNRDFQDYPDLQDTLRNAWTDTRASKNADTSANVHAVKQLSAMKYMSAHHHKPEVMPQEPGLHPHSEQSKNRSMESTLGYQKPTLRSITSPLIAHRLKPIRQKTKKAVVSILDSEEVCVELLRECASEGYVKEVLQISSDGTMITVYYPNDGRGFPLADRPPLPTDNISRYSFDNLPEKYWRKYQYASRFIQLVRSKTPKITYFTRYAKCILMENSPGADFEVWFYDGAKIHKTENLIHIIEKTGISYNLKNENEVTSLKEEVKVYMDHANEGHRICLSLESVISEEEKRSRGSSFFPIIVGRKPGNTSSPKALSAPPVDPSCCKGEQASASRLSVNSAAFPTQSPGLSPSTVTVEGLGHTATATGTGVSSSLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPDGQTTRYGENEKLPEYIKQKLQCLSSILLMFSNPTPNFQ

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
4	S-nitrosocysteine	----MAACIGERIED ----CCCCCCCCCHH	2.74	-
4	S-nitrosylation	----MAACIGERIED ----CCCCCCCCCHH	2.74	21278135
45	Acetylation	VAIKMIDKKAMYKAG HHHHHCCHHHHHHHC	31.35	-
46	Acetylation	AIKMIDKKAMYKAGM HHHHCCHHHHHHHCC	34.34	-
278	Phosphorylation	PKSKDVGTVEDSMDS CCCCCCCCCCCCCCC	22.14	25777480
282	Phosphorylation	DVGTVEDSMDSGHAT CCCCCCCCCCCCEEE	15.81	20100909
285	Phosphorylation	TVEDSMDSGHATLST CCCCCCCCCEEEEEE	24.68	20100909
289	Phosphorylation	SMDSGHATLSTTITA CCCCCEEEEEEEEEE	18.63	20100909
291	Phosphorylation	DSGHATLSTTITASS CCCEEEEEEEEEECC	21.10	20100909
292	Phosphorylation	SGHATLSTTITASSG CCEEEEEEEEEECCC	25.90	20100909
293	Phosphorylation	GHATLSTTITASSGT CEEEEEEEEEECCCC	16.98	20100909
295	Phosphorylation	ATLSTTITASSGTSL EEEEEEEEECCCCCC	20.56	20100909
297	Phosphorylation	LSTTITASSGTSLSG EEEEEEECCCCCCCC	22.20	20100909
298	Phosphorylation	STTITASSGTSLSGS EEEEEECCCCCCCCC	43.56	20100909
300	Phosphorylation	TITASSGTSLSGSLL EEEECCCCCCCCCEE	28.57	20100909
301	Phosphorylation	ITASSGTSLSGSLLD EEECCCCCCCCCEEC	24.86	20100909
303	Phosphorylation	ASSGTSLSGSLLDRR ECCCCCCCCCEECCE	26.55	20100909
305	Phosphorylation	SGTSLSGSLLDRRLL CCCCCCCCEECCEEC	23.53	20100909
400	Phosphorylation	YSVERCHSVEMLSKP EEHHHCCHHHHHCCC	24.33	-
488	Phosphorylation	AWTDTRASKNADTSA HHHCHHHHCCCCCCC	24.13	24719451
493	Phosphorylation	RASKNADTSANVHAV HHHCCCCCCCCHHHH	27.59	24719451
536	Phosphorylation	SEQSKNRSMESTLGY CHHHCCCCHHHHCCC	35.97	29514104
539	Phosphorylation	SKNRSMESTLGYQKP HCCCCHHHHCCCCCC	21.93	29514104
540	Phosphorylation	KNRSMESTLGYQKPT CCCCHHHHCCCCCCC	15.76	29514104
778	Phosphorylation	TSSPKALSAPPVDPS CCCCCCCCCCCCCHH	43.52	-
793	Phosphorylation	CCKGEQASASRLSVN HCCCCCCCCCCCEEC	26.86	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
282	S	Phosphorylation	Kinase	PLK4	Q64702	PSP
285	S	Phosphorylation	Kinase	PLK4	Q64702	PSP
289	T	Phosphorylation	Kinase	PLK4	Q64702	PSP
291	S	Phosphorylation	Kinase	PLK4	Q64702	PSP
292	T	Phosphorylation	Kinase	PLK4	Q64702	PSP
293	T	Phosphorylation	Kinase	PLK4	Q64702	PSP
295	T	Phosphorylation	Kinase	PLK4	Q64702	PSP
297	S	Phosphorylation	Kinase	PLK4	Q64702	PSP
298	S	Phosphorylation	Kinase	PLK4	Q64702	PSP
300	T	Phosphorylation	Kinase	PLK4	Q64702	PSP
301	S	Phosphorylation	Kinase	PLK4	Q64702	PSP
303	S	Phosphorylation	Kinase	PLK4	Q64702	PSP
305	S	Phosphorylation	Kinase	PLK4	Q64702	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Btrc	Q3ULA2	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PLK4_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PLK4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SET_HUMAN	SET	physical	20360068
NACAM_HUMAN	NACA	physical	20360068
NACA_HUMAN	NACA	physical	20360068
PTMS_HUMAN	PTMS	physical	20360068

Drug and Disease Associations

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