dbPTM

PK3C3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PK3C3_HUMAN
UniProt AC	Q8NEB9
Protein Name	Phosphatidylinositol 3-kinase catalytic subunit type 3
Gene Name	PIK3C3 {ECO:0000312\|HGNC:HGNC:8974}
Organism	Homo sapiens (Human).
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 (Probable). Localizes also to discre
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. [PubMed: 20643123]
Protein Sequence	MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
25	Phosphorylation	NVQLKIGSLEGKREQ EEEEEECCCCCHHHH	27.07	19369195
29	Acetylation	KIGSLEGKREQKSYK EECCCCCHHHHHHHH	43.30	560012611
29	Ubiquitination	KIGSLEGKREQKSYK EECCCCCHHHHHHHH	43.30	-
34	Acetylation	EGKREQKSYKAVLED CCHHHHHHHHHHHCC	31.40	19413330
36	Ubiquitination	KREQKSYKAVLEDPM HHHHHHHHHHHCCCC	38.83	-
36	Methylation	KREQKSYKAVLEDPM HHHHHHHHHHHCCCC	38.83	115974985
96	Ubiquitination	EWLKLPVKYPDLPRN HHCCCCCCCCCCCCC	49.48	-
109	Phosphorylation	RNAQVALTIWDVYGP CCCEEEEEEEECCCC	15.41	30576142
114	Phosphorylation	ALTIWDVYGPGKAVP EEEEEECCCCCCEEC	18.35	30576142
125	Phosphorylation	KAVPVGGTTVSLFGK CEECCCCEEEEHHHH	20.35	21406692
126	Phosphorylation	AVPVGGTTVSLFGKY EECCCCEEEEHHHHC	16.04	21406692
128	Phosphorylation	PVGGTTVSLFGKYGM CCCCEEEEHHHHCCH	18.85	21406692
132	Ubiquitination	TTVSLFGKYGMFRQG EEEEHHHHCCHHHCC	31.15	-
132	Acetylation	TTVSLFGKYGMFRQG EEEEHHHHCCHHHCC	31.15	25953088
133	Phosphorylation	TVSLFGKYGMFRQGM EEEHHHHCCHHHCCC	17.75	30576142
144	Ubiquitination	RQGMHDLKVWPNVEA HCCCCCCCCCCCCCC	48.59	-
158	Ubiquitination	ADGSEPTKTPGRTSS CCCCCCCCCCCCCCC	64.54	21906983
159	Phosphorylation	DGSEPTKTPGRTSST CCCCCCCCCCCCCCC	33.19	20513426
163	Phosphorylation	PTKTPGRTSSTLSED CCCCCCCCCCCCCHH	32.70	20513426
164	Phosphorylation	TKTPGRTSSTLSEDQ CCCCCCCCCCCCHHH	21.69	20513426
165	Phosphorylation	KTPGRTSSTLSEDQM CCCCCCCCCCCHHHH	32.52	28857561
168	Phosphorylation	GRTSSTLSEDQMSRL CCCCCCCCHHHHHHH	38.93	-
179	Phosphorylation	MSRLAKLTKAHRQGH HHHHHHHHHHHHCCC	26.02	26437602
207	Phosphorylation	EIEMINESEKRSSNF HHEECCCCHHCCCCC	43.88	22210691
209	Ubiquitination	EMINESEKRSSNFMY EECCCCHHCCCCCEE	67.85	-
229	Ubiquitination	RCVKCDDKEYGIVYY EEEECCCCEEEEEEE	39.31	-
231	Phosphorylation	VKCDDKEYGIVYYEK EECCCCEEEEEEEEE	20.21	27642862
238	Ubiquitination	YGIVYYEKDGDESSP EEEEEEEECCCCCCC	51.38	-
243	Phosphorylation	YEKDGDESSPILTSF EEECCCCCCCEEEEE	46.27	29255136
244	Phosphorylation	EKDGDESSPILTSFE EECCCCCCCEEEEEE	17.57	19664994
248	Phosphorylation	DESSPILTSFELVKV CCCCCEEEEEEEEEC	31.90	29255136
249	Phosphorylation	ESSPILTSFELVKVP CCCCEEEEEEEEECC	17.18	29255136
261	Phosphorylation	KVPDPQMSMENLVES ECCCCCCCHHHHHHH	20.07	19369195
268	Phosphorylation	SMENLVESKHHKLAR CHHHHHHHHHHHHHH	29.79	17494752
269	Ubiquitination	MENLVESKHHKLARS HHHHHHHHHHHHHHH	35.90	-
276	Phosphorylation	KHHKLARSLRSGPSD HHHHHHHHHHCCCCC	23.64	24719451
279	Phosphorylation	KLARSLRSGPSDHDL HHHHHHHCCCCCCCC	61.42	23186163
282	Phosphorylation	RSLRSGPSDHDLKPN HHHHCCCCCCCCCCC	51.61	30108239
287	Ubiquitination	GPSDHDLKPNAATRD CCCCCCCCCCCCCHH	42.13	-
287	Methylation	GPSDHDLKPNAATRD CCCCCCCCCCCCCHH	42.13	-
305	Phosphorylation	IIVSYPPTKQLTYEE EEEECCCCCCCCHHH	27.24	-
310	Phosphorylation	PPTKQLTYEEQDLVW CCCCCCCHHHHHHHH	26.51	-
321	Phosphorylation	DLVWKFRYYLTNQEK HHHHHHHHHHHCHHH	13.13	23403867
322	Phosphorylation	LVWKFRYYLTNQEKA HHHHHHHHHHCHHHH	11.64	23403867
324	Phosphorylation	WKFRYYLTNQEKALT HHHHHHHHCHHHHHH	20.80	23403867
328	Ubiquitination	YYLTNQEKALTKFLK HHHHCHHHHHHHHHH	38.64	-
346	Ubiquitination	WDLPQEAKQALELLG CCCCHHHHHHHHHHC	35.04	-
379	Phosphorylation	TNPTVRRYAVARLRQ CCHHHHHHHHHHHHC	8.55	-
395	Phosphorylation	DDEDLLMYLLQLVQA CHHHHHHHHHHHHHH	12.29	-
412	Ubiquitination	YENFDDIKNGLEPTK CCCHHHHHCCCCCCC	52.54	-
448	Phosphorylation	DSSQIITSPLPSVSS CHHHEECCCCCCCCC	17.65	17192257
452	Phosphorylation	IITSPLPSVSSPPPA EECCCCCCCCCCCCC	42.17	22199227
454	Phosphorylation	TSPLPSVSSPPPASK CCCCCCCCCCCCCCC	41.27	22199227
455	Phosphorylation	SPLPSVSSPPPASKT CCCCCCCCCCCCCCC	38.99	17192257
460	Phosphorylation	VSSPPPASKTKEVPD CCCCCCCCCCCCCCC	46.78	22199227
463	Ubiquitination	PPPASKTKEVPDGEN CCCCCCCCCCCCCCC	61.52	-
488	Phosphorylation	SRACKNSTLANYLYW HHHHCCCHHHHHEEE	39.00	-
513	Phosphorylation	TQQRDPKTHEMYLNV CCCCCCCHHHHHHHH	28.58	18187866
517	Phosphorylation	DPKTHEMYLNVMRRF CCCHHHHHHHHHHHH	7.67	18187866
525	Phosphorylation	LNVMRRFSQALLKGD HHHHHHHHHHHHCCC	16.84	20873877
534	Phosphorylation	ALLKGDKSVRVMRSL HHHCCCHHHHHHHHH	21.64	24260401
547	Phosphorylation	SLLAAQQTFVDRLVH HHHHHHHHHHHHHHH	17.34	22210691
557	Acetylation	DRLVHLMKAVQRESG HHHHHHHHHHHHHCC	52.33	25953088
582	Ubiquitination	ALLGDNEKMNLSDVE HHHCCCCCCCCCCCE	39.07	-
600	Ubiquitination	LPLEPQVKIRGIIPE CCCCCCCEEEEECHH	22.80	-
613	Methylation	PETATLFKSALMPAQ HHHHHHHHHHHCEEE	37.62	115974993
617	Sulfoxidation	TLFKSALMPAQLFFK HHHHHHHCEEEEEEE	2.30	21406390
624	Acetylation	MPAQLFFKTEDGGKY CEEEEEEECCCCCEE	43.61	19413330
625	Phosphorylation	PAQLFFKTEDGGKYP EEEEEEECCCCCEEE	33.87	19413330
630	Ubiquitination	FKTEDGGKYPVIFKH EECCCCCEEEEEEEC	52.49	2189047
631	Phosphorylation	KTEDGGKYPVIFKHG ECCCCCEEEEEEECC	13.15	24719451
666	Ubiquitination	RKENLDLKLTPYKVL HHCCCCCCCCCCEEE	50.40	-
668	Phosphorylation	ENLDLKLTPYKVLAT CCCCCCCCCCEEEEE	24.00	20513426
670	Phosphorylation	LDLKLTPYKVLATST CCCCCCCCEEEEECC	14.43	20049867
706	Ubiquitination	SIQNFFRKYAPSENG HHHHHHHHHCCCCCC	40.38	-
771	Acetylation	YILGRDPKPLPPPMK CCCCCCCCCCCCCCC	64.57	560012599
781	Ubiquitination	PPPMKLNKEMVEGMG CCCCCCCHHHHCCCC	58.59	-
781	Acetylation	PPPMKLNKEMVEGMG CCCCCCCHHHHCCCC	58.59	560012605
790	Phosphorylation	MVEGMGGTQSEQYQE HHCCCCCCCHHHHHH	24.16	26437602
795	Phosphorylation	GGTQSEQYQEFRKQC CCCCHHHHHHHHHHH	13.12	24114839
803	Phosphorylation	QEFRKQCYTAFLHLR HHHHHHHHHHHHHHH	9.90	-
840	Sumoylation	LEPDKTVKKVQDKFR CCCCCHHHHHHHHHC	53.08	-
840	Sumoylation	LEPDKTVKKVQDKFR CCCCCHHHHHHHHHC	53.08	-
845	Sumoylation	TVKKVQDKFRLDLSD HHHHHHHHHCCCCCH	18.45	-
845	Sumoylation	TVKKVQDKFRLDLSD HHHHHHHHHCCCCCH	18.45	-
884	Phosphorylation	QIHKFAQYWRK---- HHHHHHHHHHC----	12.07	-

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	CDK1	P06493	PSP
159	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
163	T	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
165	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
249	S	Phosphorylation	Kinase	ULK1	O75385	PSP
249	S	Phosphorylation	Kinase	ULK2	Q8IYT8	PSP
249	S	Phosphorylation	Kinase	ULK3	Q6PHR2	PSP
668	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL20	Q9Y2M5	PMID:26687681

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PK3C3_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PI3R4_HUMAN	PIK3R4	physical	20562859
UVRAG_HUMAN	UVRAG	physical	20562859
BAKOR_HUMAN	ATG14	physical	20562859
CLP1L_HUMAN	CLPTM1L	physical	20562859
NRBF2_HUMAN	NRBF2	physical	20562859
BECN1_HUMAN	BECN1	physical	20562859
RUBIC_HUMAN	KIAA0226	physical	20562859
UBP11_HUMAN	USP11	physical	20562859
BECN1_HUMAN	BECN1	physical	21936852
BECN1_HUMAN	BECN1	physical	18628207
MYH9_HUMAN	MYH9	physical	23569248
MYH1_HUMAN	MYH1	physical	23569248
KIF1B_HUMAN	KIF1B	physical	23569248
DREB_HUMAN	DBN1	physical	23569248
TIF1B_HUMAN	TRIM28	physical	23569248
HS90A_HUMAN	HSP90AA1	physical	23569248
GRP78_HUMAN	HSPA5	physical	23569248
ANM5_HUMAN	PRMT5	physical	23569248
BECN1_HUMAN	BECN1	physical	18843052
UVRAG_HUMAN	UVRAG	physical	18843052
BAKOR_HUMAN	ATG14	physical	18843052
BAKOR_HUMAN	ATG14	physical	19050071
BECN1_HUMAN	BECN1	physical	19050071
PI3R4_HUMAN	PIK3R4	physical	26344197
UBP18_HUMAN	USP18	physical	25906440
BECN1_HUMAN	BECN1	physical	28757208
PI3R4_HUMAN	PIK3R4	physical	28757208

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.

Regulatory Network of PK3C3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; THR-163; SER-165;SER-244; SER-261; SER-452; SER-454 AND SER-455, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-448 ANDSER-455, AND MASS SPECTROMETRY.	18691976 [Abstract]
"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-625, AND MASSSPECTROMETRY.	19413330 [Abstract]