dbPTM

P3C2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	P3C2B_HUMAN
UniProt AC	O00750
Protein Name	Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta
Gene Name	PIK3C2B
Organism	Homo sapiens (Human).
Sequence Length	1634
Subcellular Localization	Microsome . Cell membrane . Cytoplasm, cytosol . Nucleus . Endoplasmic reticulum . Found mostly in the microsome, but also in the plasma membrane and cytosol. Nuclear in testis.
Protein Description	Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns. Does not phosphorylate PtdIns(4,5)P2. May be involved in EGF and PDGF signaling cascades..
Protein Sequence	MSSTQGNGEHWKSLESVGISRKELAMAEALQMEYDALSRLRHDKEENRAKQNADPSLISWDEPGVDFYSKPAGRRTDLKLLRGLSGSDPTLNYNSLSPQEGPPNHSTSQGPQPGSDPWPKGSLSGDYLYIFDGSDGGVSSSPGPGDIEGSCKKLSPPPLPPRASIWDTPPLPPRKGSPSSSKISQPSDINTFSLVEQLPGKLLEHRILEEEEVLGGGGQGRLLGSVDYDGINDAITRLNLKSTYDAEMLRDATRGWKEGRGPLDFSKDTSGKPVARSKTMPPQVPPRTYASRYGNRKNATPGKNRRISAAPVGSRPHTVANGHELFEVSEERDEEVAAFCHMLDILRSGSDIQDYFLTGYVWSAVTPSPEHLGDEVNLKVTVLCDRLQEALTFTCNCSSTVDLLIYQTLCYTHDDLRNVDVGDFVLKPCGLEEFLQNKHALGSHEYIQYCRKFDIDIRLQLMEQKVVRSDLARTVNDDQSPSTLNYLVHLQERPVKQTISRQALSLLFDTYHNEVDAFLLADGDFPLKADRVVQSVKAICNALAAVETPEITSALNQLPPCPSRMQPKIQKDPSVLAVRENREKVVEALTAAILDLVELYCNTFNADFQTAVPGSRKHDLVQEACHFARSLAFTVYATHRIPIIWATSYEDFYLSCSLSHGGKELCSPLQTRRAHFSKYLFHLIVWDQQICFPVQVNRLPRETLLCATLYALPIPPPGSSSEANKQRRVPEALGWVTTPLFNFRQVLTCGRKLLGLWPATQENPSARWSAPNFHQPDSVILQIDFPTSAFDIKFTSPPGDKFSPRYEFGSLREEDQRKLKDIMQKESLYWLTDADKKRLWEKRYYCHSEVSSLPLVLASAPSWEWACLPDIYVLLKQWTHMNHQDALGLLHATFPDQEVRRMAVQWIGSLSDAELLDYLPQLVQALKYECYLDSPLVRFLLKRAVSDLRVTHYFFWLLKDGLKDSQFSIRYQYLLAALLCCCGKGLREEFNRQCWLVNALAKLAQQVREAAPSARQGILRTGLEEVKQFFALNGSCRLPLSPSLLVKGIVPRDCSYFNSNAVPLKLSFQNVDPLGENIRVIFKCGDDLRQDMLTLQMIRIMSKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLRKIQVEHGVTGSFKDRPLADWLQKHNPGEDEYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLKTTGHMFHIDFGRFLGHAQMFGNIKRDRAPFVFTSDMAYVINGGDKPSSRFHDFVDLCCQAYNLIRKHTHLFLNLLGLMLSCGIPELSDLEDLKYVYDALRPQDTEANATTYFTRLIESSLGSVATKLNFFIHNLAQMKFTGSDDRLTLSFASRTHTLKSSGRISDVFLCRHEKIFHPNKGYIYVVKVMRENTHEATYIQRTFEEFQELHNKLRLLFPSSHLPSFPSRFVIGRSRGEAVAERRREELNGYIWHLIHAPPEVAECDLVYTFFHPLPRDEKAMGTSPAPKSSDGTWARPVGKVGGEVKLSISYKNNKLFIMVMHIRGLQLLQDGNDPDPYVKIYLLPDPQKTTKRKTKVARKTCNPTYNEMLVYDGIPKGDLQQRELQLSVLSEQGFWENVLLGEVNIRLRELDLAQEKTGWFALGSRSHGTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSTQGNGE ------CCCCCCCCH	54.09	20068231
3	Phosphorylation	-----MSSTQGNGEH -----CCCCCCCCHH	36.29	20068231
4	Phosphorylation	----MSSTQGNGEHW ----CCCCCCCCHHH	50.19	20068231
12	Ubiquitination	QGNGEHWKSLESVGI CCCCHHHHCHHHCCC	47.25	21890473
13	Phosphorylation	GNGEHWKSLESVGIS CCCHHHHCHHHCCCC	31.98	25849741
20	Phosphorylation	SLESVGISRKELAMA CHHHCCCCHHHHHHH	31.22	29485707
22	Ubiquitination	ESVGISRKELAMAEA HHCCCCHHHHHHHHH	50.73	21890473
34	Phosphorylation	AEALQMEYDALSRLR HHHHHHHHHHHHHHH	10.94	28796482
44	Ubiquitination	LSRLRHDKEENRAKQ HHHHHHHHHHHHHHH	61.88	-
50	Ubiquitination	DKEENRAKQNADPSL HHHHHHHHHCCCHHH	40.63	-
68	Phosphorylation	DEPGVDFYSKPAGRR CCCCCCCCCCCCCCC	16.01	21945579
69	Phosphorylation	EPGVDFYSKPAGRRT CCCCCCCCCCCCCCC	31.96	21945579
70	Ubiquitination	PGVDFYSKPAGRRTD CCCCCCCCCCCCCCC	27.75	21890473
76	Phosphorylation	SKPAGRRTDLKLLRG CCCCCCCCCHHHHHC	44.30	20068231
79	Ubiquitination	AGRRTDLKLLRGLSG CCCCCCHHHHHCCCC	48.57	-
85	Phosphorylation	LKLLRGLSGSDPTLN HHHHHCCCCCCCCCC	38.79	23401153
87	Phosphorylation	LLRGLSGSDPTLNYN HHHCCCCCCCCCCCC	36.72	30576142
90	Phosphorylation	GLSGSDPTLNYNSLS CCCCCCCCCCCCCCC	32.40	30576142
93	Phosphorylation	GSDPTLNYNSLSPQE CCCCCCCCCCCCCCC	14.83	30576142
95	Phosphorylation	DPTLNYNSLSPQEGP CCCCCCCCCCCCCCC	21.62	28450419
97	Phosphorylation	TLNYNSLSPQEGPPN CCCCCCCCCCCCCCC	25.10	25921289
115	Phosphorylation	SQGPQPGSDPWPKGS CCCCCCCCCCCCCCC	47.38	-
127	Phosphorylation	KGSLSGDYLYIFDGS CCCCCCCEEEEEECC	12.63	22817900
134	Phosphorylation	YLYIFDGSDGGVSSS EEEEEECCCCCCCCC	34.62	28348404
139	Phosphorylation	DGSDGGVSSSPGPGD ECCCCCCCCCCCCCC	28.51	28348404
140	Phosphorylation	GSDGGVSSSPGPGDI CCCCCCCCCCCCCCC	37.84	28348404
141	Phosphorylation	SDGGVSSSPGPGDIE CCCCCCCCCCCCCCC	26.77	28348404
155	Phosphorylation	EGSCKKLSPPPLPPR CCCCCCCCCCCCCCC	44.21	25159151
168	Phosphorylation	PRASIWDTPPLPPRK CCCCCCCCCCCCCCC	16.29	21815630
177	Phosphorylation	PLPPRKGSPSSSKIS CCCCCCCCCCCCCCC	25.33	26055452
179	Phosphorylation	PPRKGSPSSSKISQP CCCCCCCCCCCCCCC	49.28	-
182	Ubiquitination	KGSPSSSKISQPSDI CCCCCCCCCCCCCCC	48.61	-
191	Phosphorylation	SQPSDINTFSLVEQL CCCCCCCHHHHHHHC	18.22	21964256
193	Phosphorylation	PSDINTFSLVEQLPG CCCCCHHHHHHHCCC	29.48	21964256
201	Ubiquitination	LVEQLPGKLLEHRIL HHHHCCCCHHHEEEC	48.21	21890473
225	Phosphorylation	GQGRLLGSVDYDGIN CCCCCCCCCCCCCCC	16.28	21945579
228	Phosphorylation	RLLGSVDYDGINDAI CCCCCCCCCCCCHHH	17.57	21945579
241	Ubiquitination	AITRLNLKSTYDAEM HHHHCCCCCCCCHHH	39.41	21890473
242	Phosphorylation	ITRLNLKSTYDAEML HHHCCCCCCCCHHHH	35.05	23403867
243	Phosphorylation	TRLNLKSTYDAEMLR HHCCCCCCCCHHHHH	24.67	23403867
244	Phosphorylation	RLNLKSTYDAEMLRD HCCCCCCCCHHHHHH	21.90	23403867
267	Ubiquitination	RGPLDFSKDTSGKPV CCCCCCCCCCCCCCC	66.09	-
277	Phosphorylation	SGKPVARSKTMPPQV CCCCCCCCCCCCCCC	23.81	29083192
279	Phosphorylation	KPVARSKTMPPQVPP CCCCCCCCCCCCCCC	35.84	24245541
293	Phosphorylation	PRTYASRYGNRKNAT CCCCHHHCCCCCCCC	19.09	22461510
308	Phosphorylation	PGKNRRISAAPVGSR CCCCCCCCCCCCCCC	19.30	26657352
314	Phosphorylation	ISAAPVGSRPHTVAN CCCCCCCCCCCCCCC	42.76	30576142
452	Ubiquitination	EYIQYCRKFDIDIRL HHHHHHHHCCCHHHH	43.77	-
465	Ubiquitination	RLQLMEQKVVRSDLA HHHHHHHHHHHHHHH	29.41	-
469	Phosphorylation	MEQKVVRSDLARTVN HHHHHHHHHHHHHHC	25.93	-
496	Ubiquitination	HLQERPVKQTISRQA HHHCCCCCHHHHHHH	44.39	-
535	Phosphorylation	KADRVVQSVKAICNA CHHHHHHHHHHHHHH	17.61	24719451
571	Ubiquitination	RMQPKIQKDPSVLAV CCCCCCCCCCCEEEH	75.08	-
617	Ubiquitination	TAVPGSRKHDLVQEA CCCCCCCCCHHHHHH	43.07	-
738	Phosphorylation	EALGWVTTPLFNFRQ HHHCCCCCCCCCHHH	14.36	-
752	Ubiquitination	QVLTCGRKLLGLWPA HHHHHCHHHHCCCCC	33.09	-
801	Ubiquitination	FTSPPGDKFSPRYEF ECCCCCCCCCCCCCC	54.37	21890473
818	Ubiquitination	LREEDQRKLKDIMQK CCHHHHHHHHHHHHH	55.01	-
825	Ubiquitination	KLKDIMQKESLYWLT HHHHHHHHHCCCCCC	31.71	-
836	Ubiquitination	YWLTDADKKRLWEKR CCCCHHHHHHHHHCC	41.32	-
837	Ubiquitination	WLTDADKKRLWEKRY CCCHHHHHHHHHCCC	53.95	-
1027	Ubiquitination	RTGLEEVKQFFALNG HHCHHHHHHHHHCCC	44.67	-
1041	Phosphorylation	GSCRLPLSPSLLVKG CCEECCCCHHHEECC	15.54	26270265
1043	Phosphorylation	CRLPLSPSLLVKGIV EECCCCHHHEECCCC	30.84	26270265
1047	Ubiquitination	LSPSLLVKGIVPRDC CCHHHEECCCCCCCC	42.78	21890473
1055	Phosphorylation	GIVPRDCSYFNSNAV CCCCCCCCCCCCCCE	36.73	29978859
1056	Phosphorylation	IVPRDCSYFNSNAVP CCCCCCCCCCCCCEE	17.08	29978859
1059	Phosphorylation	RDCSYFNSNAVPLKL CCCCCCCCCCEEEEE	19.10	29978859
1065	Ubiquitination	NSNAVPLKLSFQNVD CCCCEEEEEEEECCC	35.69	-
1067	Phosphorylation	NAVPLKLSFQNVDPL CCEEEEEEEECCCCC	24.17	29978859
1140	Ubiquitination	PNAETLRKIQVEHGV CCHHHHHHEEHHHCC	40.37	-
1148	Phosphorylation	IQVEHGVTGSFKDRP EEHHHCCCCCCCCCC	31.53	27251275
1150	Phosphorylation	VEHGVTGSFKDRPLA HHHCCCCCCCCCCHH	21.54	27251275
1152	Ubiquitination	HGVTGSFKDRPLADW HCCCCCCCCCCHHHH	55.30	21890473
1162	Ubiquitination	PLADWLQKHNPGEDE CHHHHHHHHCCCCHH	43.08	-
1228	Ubiquitination	AQMFGNIKRDRAPFV HHHHCCCCCCCCCEE	52.85	-
1377	Ubiquitination	VFLCRHEKIFHPNKG EEEEEECCCCCCCCC	44.54	-
1383	Ubiquitination	EKIFHPNKGYIYVVK CCCCCCCCCEEEEEE	58.50	-
1401	Phosphorylation	ENTHEATYIQRTFEE CCCCHHHHHHHHHHH	11.34	-
1415	Ubiquitination	EFQELHNKLRLLFPS HHHHHHHHHHHHCCC	25.00	-
1422	Phosphorylation	KLRLLFPSSHLPSFP HHHHHCCCCCCCCCC	24.05	24719451
1423	Phosphorylation	LRLLFPSSHLPSFPS HHHHCCCCCCCCCCC	29.31	28348404
1427	Phosphorylation	FPSSHLPSFPSRFVI CCCCCCCCCCCCEEC	57.03	23312004
1482	Ubiquitination	HPLPRDEKAMGTSPA CCCCCCCCCCCCCCC	48.22	-
1486	Phosphorylation	RDEKAMGTSPAPKSS CCCCCCCCCCCCCCC	20.60	29396449
1487	Phosphorylation	DEKAMGTSPAPKSSD CCCCCCCCCCCCCCC	17.21	23312004
1491	Ubiquitination	MGTSPAPKSSDGTWA CCCCCCCCCCCCCEE	65.77	-
1503	Ubiquitination	TWARPVGKVGGEVKL CEEECCCCCCCEEEE	37.63	-
1513	Phosphorylation	GEVKLSISYKNNKLF CEEEEEEEEECCEEE	27.03	26126808
1514	Phosphorylation	EVKLSISYKNNKLFI EEEEEEEEECCEEEE	18.96	26126808
1515	Ubiquitination	VKLSISYKNNKLFIM EEEEEEEECCEEEEE	47.45	-
1541	Phosphorylation	DGNDPDPYVKIYLLP CCCCCCCCEEEEECC	23.04	22817900
1552	Ubiquitination	YLLPDPQKTTKRKTK EECCCCCCCCCCCCH	64.65	-
1563	Ubiquitination	RKTKVARKTCNPTYN CCCHHCHHHCCCCCH	47.92	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM27	P14373	PMID:22128329

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of P3C2B_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 P3C2B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SHC1_HUMAN	SHC1	physical	11533253
GRB2_HUMAN	GRB2	physical	11533253
EGFR_HUMAN	EGFR	physical	11533253
TRI27_HUMAN	TRIM27	physical	22128329
FAS_HUMAN	FASN	physical	26344197

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 P3C2B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASSSPECTROMETRY.	18669648 [Abstract]