dbPTM

P4K2A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	P4K2A_MOUSE
UniProt AC	Q2TBE6
Protein Name	Phosphatidylinositol 4-kinase type 2-alpha
Gene Name	Pi4k2a
Organism	Mus musculus (Mouse).
Sequence Length	479
Subcellular Localization	Golgi apparatus, trans-Golgi network membrane Lipid-anchor . Membrane raft . Endosome . Cytoplasmic vesicle . Cell projection, dendrite . Cell junction, synapse, presynaptic cell membrane . Cell junction, synapse, synaptosome . Mitochondrion . Membrane
Protein Description	Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3)..
Protein Sequence	MDETSPLVSPERAQPPEYTFPSGSGAHFPQVPGGAVRVAAAAGSGPSPPCSPGHDRERQPLLDRARGAAAQGQTHTVAVQAQALAAQAAVAAHAVQTHRERNDFPEDPEFEVVVRQAEVAIECSIYPERIYQGSSGSYFVKDSQGRIVAVFKPKNEEPYGHLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDCPMDNSSCRDTDWVMVREPVIKVAAIDNGLAFPLKHPDSWRAYPFYWAWLPQAKVPFSQEIKDLILPKISDPNFIKDLEEDLYELFKRDPGFDRGQFHKQIAVMRGQILNLTQALKDNKSPLHLVQMPPVIVETARSHQRSASESYTQSFQSRKPFFSWW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDETSPLV -------CCCCCCCC	10.69	-
4	Phosphorylation	----MDETSPLVSPE ----CCCCCCCCCCC	31.23	30387612
5	Phosphorylation	---MDETSPLVSPER ---CCCCCCCCCCCC	17.75	30635358
9	Phosphorylation	DETSPLVSPERAQPP CCCCCCCCCCCCCCC	28.82	26824392
44	Phosphorylation	RVAAAAGSGPSPPCS EEEHHCCCCCCCCCC	42.69	26824392
47	Phosphorylation	AAAGSGPSPPCSPGH HHCCCCCCCCCCCCC	45.03	27087446
51	Phosphorylation	SGPSPPCSPGHDRER CCCCCCCCCCCCCCC	39.42	27087446
141	Ubiquitination	SSGSYFVKDSQGRIV CCCCEEEECCCCCEE	41.59	22790023
174	S-palmitoylation	TKWLQKLCCPCCFGR HHHHHHHHCHHHCCC	2.91	-
175	S-palmitoylation	KWLQKLCCPCCFGRD HHHHHHHCHHHCCCC	4.13	-
177	S-palmitoylation	LQKLCCPCCFGRDCL HHHHHCHHHCCCCEE	1.55	-
178	S-palmitoylation	QKLCCPCCFGRDCLV HHHHCHHHCCCCEEE	2.15	-
183	S-palmitoylation	PCCFGRDCLVLNQGY HHHCCCCEEEECCCH	2.46	28680068
240	Ubiquitination	GKRLALEKVPKVGQR CCCHHHHCCCCCCHH	65.76	22790023
268	Ubiquitination	QLFVEGYKDADYWLR EEEEECCCCHHHHHH	58.24	-
272	Phosphorylation	EGYKDADYWLRRFEA ECCCCHHHHHHHHCC	14.20	-
325	Phosphorylation	YDCPMDNSSCRDTDW EECCCCCCCCCCCCE	26.93	23684622
326	Phosphorylation	DCPMDNSSCRDTDWV ECCCCCCCCCCCCEE	21.30	21082442
341	Ubiquitination	MVREPVIKVAAIDNG EEECCEEEEEEEECC	26.51	22790023
354	Ubiquitination	NGLAFPLKHPDSWRA CCEEECCCCCCCCCC	54.02	22790023
402	Phosphorylation	KDLEEDLYELFKRDP HHHHHHHHHHHHHCC	23.94	29899451
435	Ubiquitination	LNLTQALKDNKSPLH HHHHHHHHHCCCCCC	63.37	22790023
460	Phosphorylation	TARSHQRSASESYTQ HCHHHCCCCCHHHHH	29.58	27087446
462	Phosphorylation	RSHQRSASESYTQSF HHHCCCCCHHHHHHH	28.46	27087446
464	Phosphorylation	HQRSASESYTQSFQS HCCCCCHHHHHHHHH	30.87	27742792
465	Phosphorylation	QRSASESYTQSFQSR CCCCCHHHHHHHHHC	12.54	25619855
466	Phosphorylation	RSASESYTQSFQSRK CCCCHHHHHHHHHCC	27.32	27149854
468	Phosphorylation	ASESYTQSFQSRKPF CCHHHHHHHHHCCCC	19.90	23684622
471	Phosphorylation	SYTQSFQSRKPFFSW HHHHHHHHCCCCCCC	40.02	25619855
473	Ubiquitination	TQSFQSRKPFFSWW- HHHHHHCCCCCCCC-	51.96	-

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
5	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
47	S	Phosphorylation	Kinase	GSK3A	P49840	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of P4K2A_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of P4K2A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC_HUMAN	UBC	physical	23146885
UBC_RAT	Ubc	physical	23146885
NEDD4_RAT	Nedd4	physical	23146885
UBP15_HUMAN	USP15	physical	23146885
TOM1_HUMAN	TOM1	physical	23146885
MYOF_HUMAN	MYOF	physical	23146885
SNX18_HUMAN	SNX18	physical	23146885
SNX9_HUMAN	SNX9	physical	23146885
SH3G2_HUMAN	SH3GL2	physical	23146885
SH3G1_HUMAN	SH3GL1	physical	23146885

Drug and Disease Associations

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

Regulatory Network of P4K2A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-51 AND SER-462,AND MASS SPECTROMETRY.	17242355 [Abstract]