dbPTM

PK3C3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PK3C3_MOUSE
UniProt AC	Q6PF93
Protein Name	Phosphatidylinositol 3-kinase catalytic subunit type 3
Gene Name	Pik3c3 {ECO:0000312\|MGI:MGI:2445019}
Organism	Mus musculus (Mouse).
Sequence Length	887
Subcellular Localization	Midbody . Late endosome . Cytoplasmic vesicle, autophagosome . As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes (By similarity). Localizes also to d
Protein Description	Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for transport from early to late endosomes (By similarity)..
Protein Sequence	MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGSAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQTSASESLSNSGVSSGDIDSSQIITNPLPPVASPPPASKAKEVSDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSETGPYGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
159	Phosphorylation	DGSEPTRTPGRTSST CCCCCCCCCCCCCCC	32.35	20513426
163	Phosphorylation	PTRTPGRTSSTLSED CCCCCCCCCCCCCHH	32.70	30635358
164	Phosphorylation	TRTPGRTSSTLSEDQ CCCCCCCCCCCCHHH	21.69	30635358
165	Phosphorylation	RTPGRTSSTLSEDQM CCCCCCCCCCCHHHH	32.52	28973931
166	Phosphorylation	TPGRTSSTLSEDQMS CCCCCCCCCCHHHHH	33.79	30635358
168	Phosphorylation	GRTSSTLSEDQMSRL CCCCCCCCHHHHHHH	38.93	30635358
177	Ubiquitination	DQMSRLAKLTKAHRQ HHHHHHHHHHHHHHC	62.37	27667366
197	Phosphorylation	VDWLDRLTFREIEMI CCHHHHHHHHHHEEC	22.88	21454597
207	Phosphorylation	EIEMINESEKRSSNF HHEECCCCHHCCCCC	43.88	21454597
243	Phosphorylation	YEKDGDESSPILTSF EEECCCCCCCEEEEE	46.27	23984901
244	Phosphorylation	EKDGDESSPILTSFE EECCCCCCCEEEEEE	17.57	25521595
248	Phosphorylation	DESSPILTSFELVKV CCCCCEEEEEEEEEC	31.90	21743459
249	Phosphorylation	ESSPILTSFELVKVP CCCCEEEEEEEEECC	17.18	21743459
261	Phosphorylation	KVPDPQMSMENLVES ECCCCCCCHHHHHHH	20.07	29899451
268	Phosphorylation	SMENLVESKHHKLAR CHHHHHHHHHHHHHH	29.79	29899451
276	Phosphorylation	KHHKLARSLRSGPSD HHHHHHHHHHCCCCC	23.64	-
279	Phosphorylation	KLARSLRSGPSDHDL HHHHHHHCCCCCCCC	61.42	25338131
282	Phosphorylation	RSLRSGPSDHDLKPN HHHHCCCCCCCCCCC	51.61	27841257
422	Phosphorylation	LEPTKKDSQTSASES CCCCCCCCCCCCCHH	44.21	25293948
424	Phosphorylation	PTKKDSQTSASESLS CCCCCCCCCCCHHHH	30.16	25293948
425	Phosphorylation	TKKDSQTSASESLSN CCCCCCCCCCHHHHC	23.35	25293948
427	Phosphorylation	KDSQTSASESLSNSG CCCCCCCCHHHHCCC	27.73	25293948
429	Phosphorylation	SQTSASESLSNSGVS CCCCCCHHHHCCCCC	34.30	25293948
431	Phosphorylation	TSASESLSNSGVSSG CCCCHHHHCCCCCCC	37.92	25293948
433	Phosphorylation	ASESLSNSGVSSGDI CCHHHHCCCCCCCCC	36.88	25293948
436	Phosphorylation	SLSNSGVSSGDIDSS HHHCCCCCCCCCCHH	31.93	25293948
437	Phosphorylation	LSNSGVSSGDIDSSQ HHCCCCCCCCCCHHH	37.77	25293948
442	Phosphorylation	VSSGDIDSSQIITNP CCCCCCCHHHEECCC	25.20	25293948
443	Phosphorylation	SSGDIDSSQIITNPL CCCCCCHHHEECCCC	22.96	25293948
455	Phosphorylation	NPLPPVASPPPASKA CCCCCCCCCCCCHHC	37.87	29514104
460	Phosphorylation	VASPPPASKAKEVSD CCCCCCCHHCCCCCC	38.63	25293948
525	Phosphorylation	LNVMRRFSQALLKGD HHHHHHHHHHHHCCC	16.84	17622165
530	Acetylation	RFSQALLKGDKSVRV HHHHHHHCCCHHHHH	66.95	7615463
533	Acetylation	QALLKGDKSVRVMRS HHHHCCCHHHHHHHH	60.56	7615473
668	Phosphorylation	ENLDLKLTPYKVLAT CCCCCCCCCCEEEEE	24.00	20469934
670	Phosphorylation	LDLKLTPYKVLATST CCCCCCCCEEEEECC	14.43	20469934
778	Acetylation	KPLPPPMKLNKEMVE CCCCCCCCCCHHHHC	55.47	7721275
790	Phosphorylation	MVEGMGGTQSEQYQE HHCCCCCCCHHHHHH	24.16	30635358
792	Phosphorylation	EGMGGTQSEQYQEFR CCCCCCCHHHHHHHH	26.89	30635358
795	Phosphorylation	GGTQSEQYQEFRKQC CCCCHHHHHHHHHHH	13.12	30635358
800	Acetylation	EQYQEFRKQCYTAFL HHHHHHHHHHHHHHH	50.47	7721285

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
159	T	Phosphorylation	Kinase	CDK5	P49615	PSP
163	T	Phosphorylation	Kinase	AMPK	-	Uniprot
165	S	Phosphorylation	Kinase	AMPK	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PK3C3_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 PK3C3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
BECN1_MOUSE	Becn1	physical	23569248

Drug and Disease Associations

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

Regulatory Network of PK3C3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND MASSSPECTROMETRY.	17622165 [Abstract]