dbPTM

P85A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	P85A_HUMAN
UniProt AC	P27986
Protein Name	Phosphatidylinositol 3-kinase regulatory subunit alpha
Gene Name	PIK3R1
Organism	Homo sapiens (Human).
Sequence Length	724
Subcellular Localization
Protein Description	Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling. [PubMed: 17626883]
Protein Sequence	MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEEIGWLNGYNETTGERGDFPGTYVEYIGRKKISPPTPKPRPPRPLPVAPGSSKTEADVEQQALTLPDLAEQFAPPDIAPPLLIKLVEAIEKKGLECSTLYRTQSSSNLAELRQLLDCDTPSVDLEMIDVHVLADAFKRYLLDLPNPVIPAAVYSEMISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTLQYLLKHFFKLSQTSSKNLLNARVLSEIFSPMLFRFSAASSDNTENLIKVIEILISTEWNERQPAPALPPKPPKPTTVANNGMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFSSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEIQRIMHNYDKLKSRISEIIDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSAEGYQYR ------CCCCCCHHH	34.72	22814378
2	Phosphorylation	------MSAEGYQYR ------CCCCCCHHH	34.72	29978859
6	Phosphorylation	--MSAEGYQYRALYD --CCCCCCHHHHHHC	8.22	29978859
8	Phosphorylation	MSAEGYQYRALYDYK CCCCCCHHHHHHCHH	6.86	29978859
12	Phosphorylation	GYQYRALYDYKKERE CCHHHHHHCHHHHHH	19.08	29978859
14	Phosphorylation	QYRALYDYKKEREED HHHHHHCHHHHHHHH	15.48	29978859
43	Phosphorylation	SLVALGFSDGQEARP CEEEECCCCCCCCCH	38.75	-
59	Phosphorylation	EIGWLNGYNETTGER HCCCCCCCCCCCCCC	14.57	-
73	Phosphorylation	RGDFPGTYVEYIGRK CCCCCCCCEEEECCC	9.37	-
76	Phosphorylation	FPGTYVEYIGRKKIS CCCCCEEEECCCCCC	9.91	27196784
83	Phosphorylation	YIGRKKISPPTPKPR EECCCCCCCCCCCCC	33.43	28270605
86	Phosphorylation	RKKISPPTPKPRPPR CCCCCCCCCCCCCCC	47.53	28270605
147	Phosphorylation	EKKGLECSTLYRTQS HHCCCCCHHHEECCC	16.45	-
148	Phosphorylation	KKGLECSTLYRTQSS HCCCCCHHHEECCCC	39.19	-
152	Phosphorylation	ECSTLYRTQSSSNLA CCHHHEECCCCCCHH	21.17	23401153
154	Phosphorylation	STLYRTQSSSNLAEL HHHEECCCCCCHHHH	34.81	21082442
155	Phosphorylation	TLYRTQSSSNLAELR HHEECCCCCCHHHHH	17.27	28450419
156	Phosphorylation	LYRTQSSSNLAELRQ HEECCCCCCHHHHHH	40.90	28450419
167	Acetylation	ELRQLLDCDTPSVDL HHHHHHCCCCCCCCH	6.73	19608861
203	Phosphorylation	PVIPAAVYSEMISLA CCCCHHHHHHHHHHC	8.32	-
208	Phosphorylation	AVYSEMISLAPEVQS HHHHHHHHHCCCCCC	19.71	-
230	Acetylation	LKKLIRSPSIPHQYW HHHHHCCCCCCHHHH	26.82	19608861
260	Acetylation	TSSKNLLNARVLSEI CCCHHHHCHHHHHHH	28.94	19608861
265	Phosphorylation	LLNARVLSEIFSPML HHCHHHHHHHHHHHH	26.28	24825855
269	Phosphorylation	RVLSEIFSPMLFRFS HHHHHHHHHHHHHHH	18.30	-
279	Phosphorylation	LFRFSAASSDNTENL HHHHHCCCCCCHHHH	37.63	23917254
280	Phosphorylation	FRFSAASSDNTENLI HHHHCCCCCCHHHHH	30.10	23186163
346	Ubiquitination	SREEVNEKLRDTADG CHHHHHHHHHHCCCC	43.55	-
368	Phosphorylation	STKMHGDYTLTLRKG CCCCCCEEEEEEEEC	14.29	22210691
369	Phosphorylation	TKMHGDYTLTLRKGG CCCCCEEEEEEEECC	20.29	22210691
371	Phosphorylation	MHGDYTLTLRKGGNN CCCEEEEEEEECCCC	19.40	22210691
379	Ubiquitination	LRKGGNNKLIKIFHR EEECCCCCEEEEEEC	56.44	-
419 (in isoform 4)	Ubiquitination	-	54.40	-
419	Acetylation	SLAQYNPKLDVKLLY HHHHHCCCCCEEEEE	54.40	25953088
419	Ubiquitination	SLAQYNPKLDVKLLY HHHHHCCCCCEEEEE	54.40	-
426	Phosphorylation	KLDVKLLYPVSKYQQ CCCEEEEEECCHHCC	16.42	-
431	Phosphorylation	LLYPVSKYQQDQVVK EEEECCHHCCCCCCC	12.14	29083192
438	Ubiquitination	YQQDQVVKEDNIEAV HCCCCCCCCCCHHHH	61.57	-
448	Ubiquitination	NIEAVGKKLHEYNTQ CHHHHHHHHHHHHHH	49.50	-
452	Phosphorylation	VGKKLHEYNTQFQEK HHHHHHHHHHHHHHH	16.86	21082442
454	Phosphorylation	KKLHEYNTQFQEKSR HHHHHHHHHHHHHHH	29.83	28152594
459	Sumoylation	YNTQFQEKSREYDRL HHHHHHHHHHHHHHH	43.99	-
459	Ubiquitination	YNTQFQEKSREYDRL HHHHHHHHHHHHHHH	43.99	-
459	Sumoylation	YNTQFQEKSREYDRL HHHHHHHHHHHHHHH	43.99	-
460	Phosphorylation	NTQFQEKSREYDRLY HHHHHHHHHHHHHHH	29.59	26699800
463	Phosphorylation	FQEKSREYDRLYEEY HHHHHHHHHHHHHHH	12.78	28796482
467	Phosphorylation	SREYDRLYEEYTRTS HHHHHHHHHHHHHHH	13.96	22322096
470	Phosphorylation	YDRLYEEYTRTSQEI HHHHHHHHHHHHHHH	6.92	21082442
471	Phosphorylation	DRLYEEYTRTSQEIQ HHHHHHHHHHHHHHH	30.65	28152594
490	Phosphorylation	AIEAFNETIKIFEEQ HHHHHHHHHHHHHHH	28.77	20068231
504	Phosphorylation	QCQTQERYSKEYIEK HHHHHHHHHHHHHHH	24.28	28152594
505	Phosphorylation	CQTQERYSKEYIEKF HHHHHHHHHHHHHHH	25.82	28152594
506	Ubiquitination	QTQERYSKEYIEKFK HHHHHHHHHHHHHHH	45.67	-
508	Phosphorylation	QERYSKEYIEKFKRE HHHHHHHHHHHHHHC	20.37	28152594
513	Ubiquitination	KEYIEKFKREGNEKE HHHHHHHHHCCCHHH	61.68	-
514	Methylation	EYIEKFKREGNEKEI HHHHHHHHCCCHHHH	61.25	115384929
519	Acetylation	FKREGNEKEIQRIMH HHHCCCHHHHHHHHH	65.21	25953088
519	Ubiquitination	FKREGNEKEIQRIMH HHHCCCHHHHHHHHH	65.21	-
523	Methylation	GNEKEIQRIMHNYDK CCHHHHHHHHHCHHH	33.58	115384939
528	Phosphorylation	IQRIMHNYDKLKSRI HHHHHHCHHHHHHHH	10.36	18083107
530	Acetylation	RIMHNYDKLKSRISE HHHHCHHHHHHHHHH	47.67	19608861
541	Phosphorylation	RISEIIDSRRRLEED HHHHHHHHHHHHHHH	19.78	-
550	Ubiquitination	RRLEEDLKKQAAEYR HHHHHHHHHHHHHHH	55.98	-
556	Phosphorylation	LKKQAAEYREIDKRM HHHHHHHHHHHHHHH	14.60	19534553
567	Ubiquitination	DKRMNSIKPDLIQLR HHHHHHCCCCHHHHH	32.09	-
567 (in isoform 4)	Ubiquitination	-	32.09	-
576	Phosphorylation	DLIQLRKTRDQYLMW CHHHHHHCHHHHHHH	32.80	28450419
580	Phosphorylation	LRKTRDQYLMWLTQK HHHCHHHHHHHHHHH	11.65	22617229
603	Phosphorylation	EWLGNENTEDQYSLV HHHCCCCCHHHHCCC	34.46	28796482
607	Phosphorylation	NENTEDQYSLVEDDE CCCCHHHHCCCCCCC	19.12	22322096
608	Phosphorylation	ENTEDQYSLVEDDED CCCHHHHCCCCCCCC	21.95	15932879
608	Dephosphorylation	ENTEDQYSLVEDDED CCCHHHHCCCCCCCC	21.95	15016818
623	Phosphorylation	LPHHDEKTWNVGSSN CCCCCCCCCCCCCCC	21.89	17081983
628	Phosphorylation	EKTWNVGSSNRNKAE CCCCCCCCCCCHHHH	21.84	17081983
629	Phosphorylation	KTWNVGSSNRNKAEN CCCCCCCCCCHHHHH	33.60	17081983
633	Malonylation	VGSSNRNKAENLLRG CCCCCCHHHHHHHHC	54.57	26320211
633	Ubiquitination	VGSSNRNKAENLLRG CCCCCCHHHHHHHHC	54.57	-
641 (in isoform 4)	Ubiquitination	-	40.66	-
645	Phosphorylation	LRGKRDGTFLVRESS HHCCCCCCEEEEECC	20.34	22210691
651	Phosphorylation	GTFLVRESSKQGCYA CCEEEEECCCCCEEE	32.07	23312004
652	Phosphorylation	TFLVRESSKQGCYAC CEEEEECCCCCEEEE	25.01	23312004
657	Phosphorylation	ESSKQGCYACSVVVD ECCCCCEEEEEEEEC	19.91	23312004
668	Acetylation	VVVDGEVKHCVINKT EEECCEEEEEEECCC	27.30	25953088
674	Ubiquitination	VKHCVINKTATGYGF EEEEEECCCCCCCCC	28.54	-
675	Phosphorylation	KHCVINKTATGYGFA EEEEECCCCCCCCCC	25.59	28442448
677	Phosphorylation	CVINKTATGYGFAEP EEECCCCCCCCCCCC	35.85	28442448
679	Phosphorylation	INKTATGYGFAEPYN ECCCCCCCCCCCCCC	12.52	20090780
688	Phosphorylation	FAEPYNLYSSLKELV CCCCCCHHHHHHHHH	7.80	15608670
689	Phosphorylation	AEPYNLYSSLKELVL CCCCCHHHHHHHHHH	32.15	28348404
690	Phosphorylation	EPYNLYSSLKELVLH CCCCHHHHHHHHHHH	29.88	28348404

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
83	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
154	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
154	S	Phosphorylation	Kinase	SIK2	Q9H0K1	GPS
203	Y	Phosphorylation	Kinase	RET	P07949	PSP
368	Y	Phosphorylation	Kinase	INSR	P06213	PSP
508	Y	Phosphorylation	Kinase	PDGFRB	P09619	GPS
541	S	Phosphorylation	Kinase	SIK2	Q9H0K1	GPS
580	Y	Phosphorylation	Kinase	INSR	P06213	PSP
607	Y	Phosphorylation	Kinase	INSR	P06213	PSP
607	Y	Phosphorylation	Kinase	SRC	P12931	GPS
607	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
608	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
608	S	Phosphorylation	Kinase	PK3CA	P42336	PhosphoELM
688	Y	Phosphorylation	Kinase	LCK	P06239	GPS
688	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:24113870
-	K	Ubiquitination	E3 ubiquitin ligase	CBLB	Q13191	PMID:11087752

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
608	S	Phosphorylation		18348712
Phosphorylated by PIK3CA at Ser-608; phosphorylation is stimulated by insulin and PDGF.

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 P85A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CTNB1_MOUSE	Ctnnb1	physical	10477752
P85A_HUMAN	PIK3R1	physical	8294442
WASP_HUMAN	WAS	physical	8805332
VAV_HUMAN	VAV1	physical	9891995
GAB1_HUMAN	GAB1	physical	9891995
IRS1_HUMAN	IRS1	physical	1381348
PK3CA_HUMAN	PIK3CA	physical	7929193
RRAS2_HUMAN	RRAS2	physical	11850823
EPOR_HUMAN	EPOR	physical	9162069
VAV_HUMAN	VAV1	physical	9162069
KHDR1_HUMAN	KHDRBS1	physical	11604231
IL1R1_HUMAN	IL1R1	physical	9360994
EZRI_HUMAN	EZR	physical	10377409
BCAR1_HUMAN	BCAR1	physical	10799562
CD28_HUMAN	CD28	physical	8621607
GRB2_HUMAN	GRB2	physical	7759531
EPHA2_HUMAN	EPHA2	physical	7982920
EPOR_HUMAN	EPOR	physical	7559499
IKBA_HUMAN	NFKBIA	physical	9892650
TBA1B_HUMAN	TUBA1B	physical	7592789
RASH_HUMAN	HRAS	physical	10212255
BCAP_CHICK	PIK3AP1	physical	11163197
ERBB3_HUMAN	ERBB3	physical	10383151
AGAP2_HUMAN	AGAP2	physical	11136977
CBL_HUMAN	CBL	physical	9461587
CD7_HUMAN	CD7	physical	8918688
RHG01_HUMAN	ARHGAP1	physical	8253717
FES_HUMAN	FES	physical	8916957
SH3K1_HUMAN	SH3KBP1	physical	10921882
PTN11_HUMAN	PTPN11	physical	9918857
SHIP1_HUMAN	INPP5D	physical	9918857
ADA12_HUMAN	ADAM12	physical	11313349
RASH_HUMAN	HRAS	physical	9150145
HCST_HUMAN	HCST	physical	10426994
LTK_HUMAN	LTK	physical	9223670
CBLB_HUMAN	CBLB	physical	10022120
GAB1_HUMAN	GAB1	physical	9658397
FGFR2_HUMAN	FGFR2	physical	18374639
CBL_HUMAN	CBL	physical	18374639
ATS2_HUMAN	ADAMTS2	physical	18624398
CXCL2_HUMAN	CXCL2	physical	18624398
CP4AB_HUMAN	CYP4A11	physical	18624398
TTHY_HUMAN	TTR	physical	18624398
KHDR1_HUMAN	KHDRBS1	physical	22745667
SH3K1_HUMAN	SH3KBP1	physical	15476827
PK3CA_HUMAN	PIK3CA	physical	15377662
CBL_HUMAN	CBL	physical	11944898
CRK_HUMAN	CRK	physical	11418612
CBL_HUMAN	CBL	physical	11418612
KSYK_HUMAN	SYK	physical	15536084
ZAP70_HUMAN	ZAP70	physical	15536084
CBL_HUMAN	CBL	physical	8941725
CBL_HUMAN	CBL	physical	11030146
FLT3_HUMAN	FLT3	physical	16982329
CBL_HUMAN	CBL	physical	8896416
CBL_HUMAN	CBL	physical	19861161
KIT_HUMAN	KIT	physical	17452978
PGFRA_HUMAN	PDGFRA	physical	17452978
GRB10_HUMAN	GRB10	physical	12783867
PK3CA_HUMAN	PIK3CA	physical	16135792
BRCA1_HUMAN	BRCA1	physical	16135792
ABL1_HUMAN	ABL1	physical	16135792
CRKL_HUMAN	CRKL	physical	16135792
SHC1_HUMAN	SHC1	physical	16135792
GAB2_HUMAN	GAB2	physical	16135792
CBL_HUMAN	CBL	physical	16135792
PGFRB_HUMAN	PDGFRB	physical	16135792
JAK2_HUMAN	JAK2	physical	16135792
ALK_HUMAN	ALK	physical	16135792
CBL_HUMAN	CBL	physical	9259313
CBL_HUMAN	CBL	physical	9174058
CBL_HUMAN	CBL	physical	9988765
ABL1_HUMAN	ABL1	physical	16219545
CBL_HUMAN	CBL	physical	16219545
SHC1_HUMAN	SHC1	physical	16219545
GRB2_HUMAN	GRB2	physical	16219545
CBL_HUMAN	CBL	physical	8612729
CBL_HUMAN	CBL	physical	16289966
CMIP_HUMAN	CMIP	physical	20018188
PK3CA_HUMAN	PIK3CA	physical	20018188
CBL_HUMAN	CBL	physical	8621719
CBL_HUMAN	CBL	physical	11157475
CBL_HUMAN	CBL	physical	7642581
CBL_HUMAN	CBL	physical	10918571
PTN11_HUMAN	PTPN11	physical	9361008
CBL_HUMAN	CBL	physical	9541596
GRB2_HUMAN	GRB2	physical	9541596
GAB2_HUMAN	GAB2	physical	14530346
CBL_HUMAN	CBL	physical	14530346
PK3CB_HUMAN	PIK3CB	physical	22939629
EP300_HUMAN	EP300	physical	21057544
CBL_HUMAN	CBL	physical	8662998
EGFR_HUMAN	EGFR	physical	8662998
ESR1_HUMAN	ESR1	physical	11029009
IRS1_HUMAN	IRS1	physical	8175658
KHDR1_HUMAN	KHDRBS1	physical	8175658
DAB2P_HUMAN	DAB2IP	physical	19903888
M3K5_HUMAN	MAP3K5	physical	19903888
TNR5_HUMAN	CD40	physical	21200133
LOX5_HUMAN	ALOX5	physical	21200133
CBL_HUMAN	CBL	physical	24113870
EPOR_HUMAN	EPOR	physical	24113870
EPN1_HUMAN	EPN1	physical	24113870
NUCL_HUMAN	NCL	physical	16571724
SQSTM_HUMAN	SQSTM1	physical	9564850
PK3CA_HUMAN	PIK3CA	physical	20713702
PK3CB_HUMAN	PIK3CB	physical	20713702
IRS1_HUMAN	IRS1	physical	25814554
PDE4D_HUMAN	PDE4D	physical	10571082
PK3CA_HUMAN	PIK3CA	physical	26496610
PK3CB_HUMAN	PIK3CB	physical	26496610
PK3CD_HUMAN	PIK3CD	physical	26496610
IRS2_HUMAN	IRS2	physical	26496610
CAF1A_HUMAN	CHAF1A	physical	26496610
NYAP2_HUMAN	NYAP2	physical	26496610
PLCG2_HUMAN	PLCG2	physical	25241761
SOS1_HUMAN	SOS1	physical	25241761
RASH_HUMAN	HRAS	physical	25241761
CTNB1_HUMAN	CTNNB1	physical	25241761
CSF1R_HUMAN	CSF1R	physical	25241761
SRC_HUMAN	SRC	physical	25241761
PK3CB_HUMAN	PIK3CB	physical	25241761
RXRA_HUMAN	RXRA	physical	20541701
SHC1_HUMAN	SHC1	physical	19889638
FAK1_HUMAN	PTK2	physical	19889638
VGFR1_HUMAN	FLT1	physical	20805333
PK3CA_HUMAN	PIK3CA	physical	11526404
CBLB_HUMAN	CBLB	physical	11526404
CD3Z_HUMAN	CD247	physical	11526404
KBTB2_HUMAN	KBTBD2	physical	27708159
CUL3_HUMAN	CUL3	physical	27708159
WEE1_HUMAN	WEE1	genetic	28319113
VHL_HUMAN	VHL	genetic	28319113
TAU_HUMAN	MAPT	physical	19681044
ERBB3_HUMAN	ERBB3	physical	18803287
GBB1_HUMAN	GNB1	physical	19117013
PK3CA_HUMAN	PIK3CA	physical	19117013
AKT1_HUMAN	AKT1	physical	19117013
GRB2_HUMAN	GRB2	physical	18346204
PROM1_HUMAN	PROM1	physical	23569237
ERBB3_HUMAN	ERBB3	physical	15812817
TNR6_HUMAN	FAS	physical	18328427
IRS1_HUMAN	IRS1	physical	17640984
RET_HUMAN	RET	physical	10995764
FAK1_HUMAN	PTK2	physical	11119718

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615214	Agammaglobulinemia 7, autosomal recessive (AGM7)
269880	SHORT syndrome (SHORTS)
616005	Immunodeficiency 36 (IMD36)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01064	Isoprenaline

Regulatory Network of P85A_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-530, AND MASS SPECTROMETRY.	19608861 [Abstract]
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 THR-152; SER-154; TYR-452AND TYR-580, AND MASS SPECTROMETRY.	19369195 [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-452; TYR-467; TYR-508;TYR-556; TYR-580 AND TYR-679, AND MASS SPECTROMETRY.	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-607, AND MASSSPECTROMETRY.	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-452; TYR-467; TYR-556AND TYR-580, AND MASS SPECTROMETRY.	18083107 [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-607, AND MASSSPECTROMETRY.	15951569 [Abstract]

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