dbPTM

P85B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	P85B_HUMAN
UniProt AC	O00459
Protein Name	Phosphatidylinositol 3-kinase regulatory subunit beta
Gene Name	PIK3R2
Organism	Homo sapiens (Human).
Sequence Length	728
Subcellular Localization
Protein Description	Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy. [PubMed: 23604317 Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity]
Protein Sequence	MAGPEGFQYRALYPFRRERPEDLELLPGDVLVVSRAALQALGVAEGGERCPQSVGWMPGLNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPRDGAPEPGLTLPDLPEQFSPPDVAPPLLVKLVEAIERTGLDSESHYRPELPAPRTDWSLSDVDQWDTAALADGIKSFLLALPAPLVTPEASAEARRALREAAGPVGPALEPPTLPLHRALTLRFLLQHLGRVASRAPALGPAVRALGATFGPLLLRAPPPPSSPPPGGAPDGSEPSPDFPALLVEKLLQEHLEEQEVAPPALPPKPPKAKPASTVLANGGSPPSLQDAEWYWGDISREEVNEKLRDTPDGTFLVRDASSKIQGEYTLTLRKGGNNKLIKVFHRDGHYGFSEPLTFCSVVDLINHYRHESLAQYNAKLDTRLLYPVSKYQQDQIVKEDSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQQLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQKKINEWLGIKNETEDQYALMEDEDDLPHHEERTWYVGKINRTQAEEMLSGKRDGTFLIRESSQRGCYACSVVVDGDTKHCVIYRTATGFGFAEPYNLYGSLKELVLHYQHASLVQHNDALTVTLAHPVRAPGPGPPPAAR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	PGDVLVVSRAALQAL CCCEEEEEHHHHHHH	14.55	24719451
74	Phosphorylation	RGDFPGTYVEFLGPV CCCCCCCCEEECCCH	12.14	27642862
119	Phosphorylation	PDLPEQFSPPDVAPP CCCCHHCCCCCCCHH	34.91	20873877
249	Phosphorylation	AVRALGATFGPLLLR HHHHHHCCCHHHHHC	27.59	29514088
262	Phosphorylation	LRAPPPPSSPPPGGA HCCCCCCCCCCCCCC	62.34	30278072
263	Phosphorylation	RAPPPPSSPPPGGAP CCCCCCCCCCCCCCC	47.39	30278072
273	Phosphorylation	PGGAPDGSEPSPDFP CCCCCCCCCCCCCHH	54.43	30206219
276	Phosphorylation	APDGSEPSPDFPALL CCCCCCCCCCHHHHH	32.80	28450419
321	Phosphorylation	TVLANGGSPPSLQDA EEEECCCCCCCHHCC	34.73	24719451
343	Ubiquitination	SREEVNEKLRDTPDG CHHHHHHHHHCCCCC	43.55	-
365	Phosphorylation	SSKIQGEYTLTLRKG CCCCCEEEEEEEEEC	17.55	22817900
371	Acetylation	EYTLTLRKGGNNKLI EEEEEEEECCCCEEE	74.43	7708131
376	Acetylation	LRKGGNNKLIKVFHR EEECCCCEEEEEEEC	56.44	7708143
376	Ubiquitination	LRKGGNNKLIKVFHR EEECCCCEEEEEEEC	56.44	-
413	Phosphorylation	RHESLAQYNAKLDTR CCHHHHHHHCCCCCH	16.10	27642862
423	Phosphorylation	KLDTRLLYPVSKYQQ CCCCHHHHCCHHHCH	13.23	22817900
438	Phosphorylation	DQIVKEDSVEAVGAQ HCCCCHHHHHHHHHH	23.97	26471730
447	Ubiquitination	EAVGAQLKVYHQQYQ HHHHHHHHHHHHHHH	28.77	29967540
449	Phosphorylation	VGAQLKVYHQQYQDK HHHHHHHHHHHHHHH	7.72	26356563
453	Phosphorylation	LKVYHQQYQDKSREY HHHHHHHHHHHHHHH	16.47	28152594
456	Ubiquitination	YHQQYQDKSREYDQL HHHHHHHHHHHHHHH	35.57	29967540
457	Phosphorylation	HQQYQDKSREYDQLY HHHHHHHHHHHHHHH	38.34	21945579
460	Phosphorylation	YQDKSREYDQLYEEY HHHHHHHHHHHHHHH	14.10	21945579
464	Phosphorylation	SREYDQLYEEYTRTS HHHHHHHHHHHHHHH	10.90	22322096
467	Phosphorylation	YDQLYEEYTRTSQEL HHHHHHHHHHHHHHH	6.92	21945579
468	Phosphorylation	DQLYEEYTRTSQELQ HHHHHHHHHHHHHHH	30.65	21945579
477	Ubiquitination	TSQELQMKRTAIEAF HHHHHHHHHHHHHHH	33.37	-
487	Phosphorylation	AIEAFNETIKIFEEQ HHHHHHHHHHHHHHC	28.77	20068231
500	Ubiquitination	EQGQTQEKCSKEYLE HCCCCHHHHCHHHHH	33.71	32015554
505	Phosphorylation	QEKCSKEYLERFRRE HHHHCHHHHHHHHHH	20.01	23898821
541	Sumoylation	EIHESRTKLEQQLRA HHHHHHHHHHHHHHH	49.25	-
541	Sumoylation	EIHESRTKLEQQLRA HHHHHHHHHHHHHHH	49.25	-
541	Ubiquitination	EIHESRTKLEQQLRA HHHHHHHHHHHHHHH	49.25	29967540
562	Phosphorylation	EIDKRMNSLKPDLMQ HHHHHHHHCCHHHHH	28.55	24719451
564	Ubiquitination	DKRMNSLKPDLMQLR HHHHHHCCHHHHHHH	35.98	32015554
564	Acetylation	DKRMNSLKPDLMQLR HHHHHHCCHHHHHHH	35.98	19811393
577	Phosphorylation	LRKIRDQYLVWLTQK HHHHHHHHHHHHCHH	13.91	20090780
582	Phosphorylation	DQYLVWLTQKGARQK HHHHHHHCHHCHHHH	16.72	-
598	Sumoylation	INEWLGIKNETEDQY HHHHHCCCCCCHHHE	47.10	-
598	Sumoylation	INEWLGIKNETEDQY HHHHHCCCCCCHHHE	47.10	-
601	Phosphorylation	WLGIKNETEDQYALM HHCCCCCCHHHEEEC	55.01	28796482
605	Phosphorylation	KNETEDQYALMEDED CCCCHHHEEECCCCC	17.64	27273156
621	Phosphorylation	LPHHEERTWYVGKIN CCCHHHCEEEEEEEC	25.16	28387310
626	Ubiquitination	ERTWYVGKINRTQAE HCEEEEEEECHHHHH	27.11	29967540
639	Ubiquitination	AEEMLSGKRDGTFLI HHHHHCCCCCCCEEE	43.89	29967540
643	Phosphorylation	LSGKRDGTFLIRESS HCCCCCCCEEEEECC	21.40	28857561
649	Phosphorylation	GTFLIRESSQRGCYA CCEEEEECCCCCEEE	23.17	27251275
650	Phosphorylation	TFLIRESSQRGCYAC CEEEEECCCCCEEEE	21.10	27251275
655	Phosphorylation	ESSQRGCYACSVVVD ECCCCCEEEEEEEEC	17.29	1314371
658	Phosphorylation	QRGCYACSVVVDGDT CCCEEEEEEEECCCC	15.13	27251275
671	Phosphorylation	DTKHCVIYRTATGFG CCCEEEEEEECCCCC	4.98	-
686	Phosphorylation	FAEPYNLYGSLKELV CCCCCHHHHHHHHHH	10.88	18083107
688	Phosphorylation	EPYNLYGSLKELVLH CCCHHHHHHHHHHHH	23.78	28060719

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	FBXL2	Q9UKC9	PMID:23604317
-	K	Ubiquitination	E3 ubiquitin ligase	CBLB	Q13191	PMID:11087752

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of P85B_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 P85B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBL_HUMAN	CBL	physical	7629144
CRKL_HUMAN	CRKL	physical	9092574
PK3CA_HUMAN	PIK3CA	physical	19380743
PK3CB_HUMAN	PIK3CB	physical	19380743
IQGA1_HUMAN	IQGAP1	physical	19380743
K2C1_HUMAN	KRT1	physical	19380743
K22E_HUMAN	KRT2	physical	19380743
K1C10_HUMAN	KRT10	physical	19380743
PK3CD_HUMAN	PIK3CD	physical	19380743
PTN11_HUMAN	PTPN11	physical	19380743
HSP7C_HUMAN	HSPA8	physical	19380743
CBL_HUMAN	CBL	physical	19380743
K1C9_HUMAN	KRT9	physical	19380743
K2C5_HUMAN	KRT5	physical	19380743
SHIP2_HUMAN	INPPL1	physical	19380743
K2C6C_HUMAN	KRT6C	physical	19380743
SHC1_HUMAN	SHC1	physical	19380743
ACTB_HUMAN	ACTB	physical	19380743
MYH10_HUMAN	MYH10	physical	19380743
GAB2_HUMAN	GAB2	physical	19380743
SEMG1_HUMAN	SEMG1	physical	19380743
K1C16_HUMAN	KRT16	physical	19380743
SEMG2_HUMAN	SEMG2	physical	19380743
K1C14_HUMAN	KRT14	physical	19380743
GRB2_HUMAN	GRB2	physical	19380743
TBA1C_HUMAN	TUBA1C	physical	19380743
HS71L_HUMAN	HSPA1L	physical	19380743
SPTB2_HUMAN	SPTBN1	physical	19380743
K1C17_HUMAN	KRT17	physical	19380743
K2C79_HUMAN	KRT79	physical	19380743
P85A_HUMAN	PIK3R1	physical	19380743
CRK_HUMAN	CRK	physical	19380743
HSP76_HUMAN	HSPA6	physical	19380743
MYH9_HUMAN	MYH9	physical	19380743
TBB5_HUMAN	TUBB	physical	19380743
ACACA_HUMAN	ACACA	physical	19380743
K1C15_HUMAN	KRT15	physical	19380743
BCR_HUMAN	BCR	physical	19380743
COR1C_HUMAN	CORO1C	physical	19380743
P55G_HUMAN	PIK3R3	physical	19380743
EF1A1_HUMAN	EEF1A1	physical	19380743
DDX3X_HUMAN	DDX3X	physical	19380743
RS10_HUMAN	RPS10	physical	19380743
MYH14_HUMAN	MYH14	physical	19380743
FUS_HUMAN	FUS	physical	19380743
TBB6_HUMAN	TUBB6	physical	19380743
RS5_HUMAN	RPS5	physical	19380743
RS7_HUMAN	RPS7	physical	19380743
A4_HUMAN	APP	physical	21832049
EGFR_HUMAN	EGFR	physical	16273093
ERBB2_HUMAN	ERBB2	physical	16273093
ERBB3_HUMAN	ERBB3	physical	16273093
FBXL2_HUMAN	FBXL2	physical	23604317
PK3CA_HUMAN	PIK3CA	physical	23604317
STAB1_HUMAN	STAB1	physical	21988832
1433T_HUMAN	YWHAQ	physical	7479742
KRT38_HUMAN	KRT38	physical	25416956
IKZF3_HUMAN	IKZF3	physical	25416956
K1C20_HUMAN	KRT20	physical	25416956
RINT1_HUMAN	RINT1	physical	25416956
MR1L1_HUMAN	MRFAP1L1	physical	25416956
DYDC1_HUMAN	DYDC1	physical	25416956
SQSTM_HUMAN	SQSTM1	physical	9564850
PK3CB_HUMAN	PIK3CB	physical	26186194
HAUS1_HUMAN	HAUS1	physical	26186194
HAUS4_HUMAN	HAUS4	physical	26186194
P85A_HUMAN	PIK3R1	physical	26186194
P55G_HUMAN	PIK3R3	physical	26186194
RCBT2_HUMAN	RCBTB2	physical	26186194
GHR_HUMAN	GHR	physical	9632636
CBL_HUMAN	CBL	physical	25814554
HAUS4_HUMAN	HAUS4	physical	28514442
RCBT2_HUMAN	RCBTB2	physical	28514442
P55G_HUMAN	PIK3R3	physical	28514442
HAUS1_HUMAN	HAUS1	physical	28514442
P85A_HUMAN	PIK3R1	physical	28514442
PK3CB_HUMAN	PIK3CB	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603387	Megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome 1 (MPPH1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01064	Isoprenaline

Regulatory Network of P85B_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-262 AND SER-263, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-605, AND MASSSPECTROMETRY.	19690332 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464 AND TYR-605, ANDMASS SPECTROMETRY.	17389395 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-365; TYR-464 ANDTYR-467, AND MASS SPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464, AND MASSSPECTROMETRY.	15951569 [Abstract]