dbPTM

BCAR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BCAR1_HUMAN
UniProt AC	P56945
Protein Name	Breast cancer anti-estrogen resistance protein 1
Gene Name	BCAR1
Organism	Homo sapiens (Human).
Sequence Length	870
Subcellular Localization	Cell junction, focal adhesion . Cytoplasm . Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation..
Protein Description	Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells..
Protein Sequence	MNHLNVLAKALYDNVAESPDELSFRKGDIMTVLEQDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPAGPGPGPPATPAQPQPGLHAPAPPASQYTPMLPNTYQPQPDSVYLVPTPSKAQQGLYQVPGPSPQFQSPPAKQTSTFSKQTPHHPFPSPATDLYQVPPGPGGPAQDIYQVPPSAGMGHDIYQVPPSMDTRSWEGTKPPAKVVVPTRVGQGYVYEAAQPEQDEYDIPRHLLAPGPQDIYDVPPVRGLLPSQYGQEVYDTPPMAVKGPNGRDPLLEVYDVPPSVEKGLPPSNHHAVYDVPPSVSKDVPDGPLLREETYDVPPAFAKAKPFDPARTPLVLAAPPPDSPPAEDVYDVPPPAPDLYDVPPGLRRPGPGTLYDVPRERVLPPEVADGGVVDSGVYAVPPPAEREAPAEGKRLSASSTGSTRSSQSASSLEVAGPGREPLELEVAVEALARLQQGVSATVAHLLDLAGSAGATGSWRSPSEPQEPLVQDLQAAVAAVQSAVHELLEFARSAVGNAAHTSDRALHAKLSRQLQKMEDVHQTLVAHGQALDAGRGGSGATLEDLDRLVACSRAVPEDAKQLASFLHGNASLLFRRTKATAPGPEGGGTLHPNPTDKTSSIQSRPLPSPPKFTSQDSPDGQYENSEGGWMEDYDYVHLQGKEEFEKTQKELLEKGSITRQGKSQLELQQLKQFERLEQEVSRPIDHDLANWTPAQPLAPGRTGGLGPSDRQLLLFYLEQCEANLTTLTNAVDAFFTAVATNQPPKIFVAHSKFVILSAHKLVFIGDTLSRQAKAADVRSQVTHYSNLLCDLLRGIVATTKAAALQYPSPSAAQDMVERVKELGHSTQQFRRVLGQLAAA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNHLNVLA -------CCHHHHHH	6.86	-
2 (in isoform 8)	Phosphorylation	-	48.64	-
12	Phosphorylation	NVLAKALYDNVAESP HHHHHHHHHHHCCCC	15.44	21937722
15 (in isoform 7)	Phosphorylation	-	5.97	-
18	Phosphorylation	LYDNVAESPDELSFR HHHHHCCCCCCCCCC	28.10	21815630
18 (in isoform 8)	Phosphorylation	-	28.10	25159151
23	Phosphorylation	AESPDELSFRKGDIM CCCCCCCCCCCCCEE	22.43	28674419
67	Phosphorylation	LKILVGMYDKKPAGP EEEEEEEECCCCCCC	20.77	21945579
113	Phosphorylation	TYQPQPDSVYLVPTP CCCCCCCCEEEECCC	21.24	25884760
115	Phosphorylation	QPQPDSVYLVPTPSK CCCCCCEEEECCCCH	13.11	26356563
119	Phosphorylation	DSVYLVPTPSKAQQG CCEEEECCCCHHHCC	32.49	26356563
121	Phosphorylation	VYLVPTPSKAQQGLY EEEECCCCHHHCCCC	43.00	26356563
128	Phosphorylation	SKAQQGLYQVPGPSP CHHHCCCCCCCCCCC	17.81	21945579
134	Phosphorylation	LYQVPGPSPQFQSPP CCCCCCCCCCCCCCC	36.93	21945579
139	Phosphorylation	GPSPQFQSPPAKQTS CCCCCCCCCCCCCCC	33.85	21945579
143	Acetylation	QFQSPPAKQTSTFSK CCCCCCCCCCCCCCC	60.94	7495575
145	Phosphorylation	QSPPAKQTSTFSKQT CCCCCCCCCCCCCCC	29.09	23312004
146	Phosphorylation	SPPAKQTSTFSKQTP CCCCCCCCCCCCCCC	25.59	23312004
147	Phosphorylation	PPAKQTSTFSKQTPH CCCCCCCCCCCCCCC	35.00	23312004
149	Phosphorylation	AKQTSTFSKQTPHHP CCCCCCCCCCCCCCC	24.76	23312004
152	Phosphorylation	TSTFSKQTPHHPFPS CCCCCCCCCCCCCCC	28.46	26356563
159	Phosphorylation	TPHHPFPSPATDLYQ CCCCCCCCCCCCCCC	27.78	26356563
162	Phosphorylation	HPFPSPATDLYQVPP CCCCCCCCCCCCCCC	29.89	26356563
165	Phosphorylation	PSPATDLYQVPPGPG CCCCCCCCCCCCCCC	15.41	26356563
174 (in isoform 6)	Phosphorylation	-	32.44	24719451
179	Phosphorylation	GGPAQDIYQVPPSAG CCCHHHCCCCCCCCC	16.26	26356563
184	Phosphorylation	DIYQVPPSAGMGHDI HCCCCCCCCCCCCCC	31.24	26356563
185 (in isoform 6)	Phosphorylation	-	20.12	24719451
192	Phosphorylation	AGMGHDIYQVPPSMD CCCCCCCCCCCCCCC	14.98	26356563
197	Phosphorylation	DIYQVPPSMDTRSWE CCCCCCCCCCCCCCC	24.18	26356563
200	Phosphorylation	QVPPSMDTRSWEGTK CCCCCCCCCCCCCCC	20.26	26356563
202	Phosphorylation	PPSMDTRSWEGTKPP CCCCCCCCCCCCCCC	31.41	27251275
222	Phosphorylation	PTRVGQGYVYEAAQP ECCCCCCEEEEECCC	7.62	21945579
224	Phosphorylation	RVGQGYVYEAAQPEQ CCCCCEEEEECCCCC	7.43	21945579
234	Phosphorylation	AQPEQDEYDIPRHLL CCCCCCCCCCCHHHC	27.71	21945579
248 (in isoform 6)	Phosphorylation	-	2.39	24719451
249	Phosphorylation	APGPQDIYDVPPVRG CCCCCCCCCCCCCCC	21.12	21945579
260	Phosphorylation	PVRGLLPSQYGQEVY CCCCCCHHHCCCCCC	35.68	21945579
262	Phosphorylation	RGLLPSQYGQEVYDT CCCCHHHCCCCCCCC	25.72	21945579
267	Phosphorylation	SQYGQEVYDTPPMAV HHCCCCCCCCCCCEE	17.22	21945579
269	Phosphorylation	YGQEVYDTPPMAVKG CCCCCCCCCCCEECC	16.17	21945579
280 (in isoform 6)	Phosphorylation	-	49.35	27251275
287	Phosphorylation	RDPLLEVYDVPPSVE CCCCEEEEECCCCHH	11.22	21945579
292	Phosphorylation	EVYDVPPSVEKGLPP EEEECCCCHHCCCCC	36.52	21945579
295 (in isoform 6)	Phosphorylation	-	64.69	24719451
300	Phosphorylation	VEKGLPPSNHHAVYD HHCCCCCCCCCCCCC	47.02	21945579
306	Phosphorylation	PSNHHAVYDVPPSVS CCCCCCCCCCCCCCC	16.41	21945579
306 (in isoform 3)	Phosphorylation	-	16.41	25850435
311	Phosphorylation	AVYDVPPSVSKDVPD CCCCCCCCCCCCCCC	32.71	21945579
313	Phosphorylation	YDVPPSVSKDVPDGP CCCCCCCCCCCCCCC	27.72	21945579
313 (in isoform 6)	Phosphorylation	-	27.72	24719451
324 (in isoform 3)	Phosphorylation	-	55.44	27642862
326	Phosphorylation	GPLLREETYDVPPAF CCCCCCCCCCCCHHH	21.92	21945579
327	Phosphorylation	PLLREETYDVPPAFA CCCCCCCCCCCHHHH	20.44	21945579
344	Phosphorylation	KPFDPARTPLVLAAP CCCCCCCCCEEEECC	24.07	29496963
352 (in isoform 6)	Phosphorylation	-	40.37	27642862
355	Phosphorylation	LAAPPPDSPPAEDVY EECCCCCCCCHHHCC	38.26	25159151
357 (in isoform 6)	Phosphorylation	-	52.84	27642862
359 (in isoform 6)	Phosphorylation	-	54.50	27642862
362	Phosphorylation	SPPAEDVYDVPPPAP CCCHHHCCCCCCCCC	24.44	15870699
372	Phosphorylation	PPPAPDLYDVPPGLR CCCCCCCCCCCCCCC	23.44	25106551
372 (in isoform 6)	Phosphorylation	-	23.44	27642862
385	Phosphorylation	LRRPGPGTLYDVPRE CCCCCCCCCCCCCHH	25.86	21945579
387	Phosphorylation	RPGPGTLYDVPRERV CCCCCCCCCCCHHHC	18.09	21945579
401 (in isoform 6)	Phosphorylation	-	60.60	24719451
407	Phosphorylation	ADGGVVDSGVYAVPP CCCCEECCCCEECCC	20.67	21945579
410	Phosphorylation	GVVDSGVYAVPPPAE CEECCCCEECCCCHH	12.85	21945579
428	Phosphorylation	PAEGKRLSASSTGST CCCCCCCCCCCCCCC	30.09	28355574
430	Phosphorylation	EGKRLSASSTGSTRS CCCCCCCCCCCCCCC	25.67	23927012
431	Phosphorylation	GKRLSASSTGSTRSS CCCCCCCCCCCCCCC	36.18	23927012
432	Phosphorylation	KRLSASSTGSTRSSQ CCCCCCCCCCCCCCC	32.43	23927012
433 (in isoform 6)	Phosphorylation	-	29.03	24719451
434	Phosphorylation	LSASSTGSTRSSQSA CCCCCCCCCCCCCCC	22.27	23927012
435	Phosphorylation	SASSTGSTRSSQSAS CCCCCCCCCCCCCCC	35.60	23927012
437	Phosphorylation	SSTGSTRSSQSASSL CCCCCCCCCCCCCCE	32.58	23663014
438	Phosphorylation	STGSTRSSQSASSLE CCCCCCCCCCCCCEE	25.51	23663014
440	Phosphorylation	GSTRSSQSASSLEVA CCCCCCCCCCCEEEC	31.87	23663014
442	Phosphorylation	TRSSQSASSLEVAGP CCCCCCCCCEEECCC	40.48	23663014
443	Phosphorylation	RSSQSASSLEVAGPG CCCCCCCCEEECCCC	28.41	27732954
474 (in isoform 6)	Phosphorylation	-	2.94	24719451
477 (in isoform 6)	Phosphorylation	-	2.61	24719451
480 (in isoform 6)	Phosphorylation	-	6.16	27251275
484 (in isoform 6)	Phosphorylation	-	15.66	27251275
486 (in isoform 6)	Phosphorylation	-	14.43	27251275
492	Ubiquitination	GATGSWRSPSEPQEP CCCCCCCCCCCCCCC	26.90	21890473
532	Phosphorylation	AVGNAAHTSDRALHA HHHHHHHHHHHHHHH	27.83	23312004
533	Phosphorylation	VGNAAHTSDRALHAK HHHHHHHHHHHHHHH	18.42	23312004
569	Phosphorylation	LDAGRGGSGATLEDL HCCCCCCCCCCHHHH	28.25	28857561
602	Phosphorylation	SFLHGNASLLFRRTK HHHHCCHHHEEEECC	29.61	28857561
608	Phosphorylation	ASLLFRRTKATAPGP HHHEEEECCCCCCCC	22.30	22210691
620	Phosphorylation	PGPEGGGTLHPNPTD CCCCCCCCCCCCCCC	25.76	22210691
626	Phosphorylation	GTLHPNPTDKTSSIQ CCCCCCCCCCCCCCC	57.69	22210691
629	Phosphorylation	HPNPTDKTSSIQSRP CCCCCCCCCCCCCCC	30.43	23403867
630	Phosphorylation	PNPTDKTSSIQSRPL CCCCCCCCCCCCCCC	31.05	23403867
631	Phosphorylation	NPTDKTSSIQSRPLP CCCCCCCCCCCCCCC	29.85	23403867
634	Phosphorylation	DKTSSIQSRPLPSPP CCCCCCCCCCCCCCC	33.91	23403867
639	Phosphorylation	IQSRPLPSPPKFTSQ CCCCCCCCCCCCCCC	62.61	30266825
644	Phosphorylation	LPSPPKFTSQDSPDG CCCCCCCCCCCCCCC	31.44	26356563
645	Phosphorylation	PSPPKFTSQDSPDGQ CCCCCCCCCCCCCCC	34.81	26356563
648	Phosphorylation	PKFTSQDSPDGQYEN CCCCCCCCCCCCCCC	19.77	26356563
648 (in isoform 6)	Phosphorylation	-	19.77	27251275
653	Phosphorylation	QDSPDGQYENSEGGW CCCCCCCCCCCCCCC	23.70	26356563
656	Phosphorylation	PDGQYENSEGGWMED CCCCCCCCCCCCCCC	26.19	26356563
664	Phosphorylation	EGGWMEDYDYVHLQG CCCCCCCCCEEEECC	8.89	15870699
666	Phosphorylation	GWMEDYDYVHLQGKE CCCCCCCEEEECCHH	5.41	27259358
680	Acetylation	EEFEKTQKELLEKGS HHHHHHHHHHHHCCC	56.41	25953088
685 (in isoform 6)	Phosphorylation	-	58.91	24719451
693	Ubiquitination	GSITRQGKSQLELQQ CCCCCCCCHHHHHHH	27.04	-
694	Phosphorylation	SITRQGKSQLELQQL CCCCCCCHHHHHHHH	46.99	26657352
694 (in isoform 6)	Phosphorylation	-	46.99	27251275
702	Ubiquitination	QLELQQLKQFERLEQ HHHHHHHHHHHHHHH	48.91	21890473
702	Ubiquitination	QLELQQLKQFERLEQ HHHHHHHHHHHHHHH	48.91	2189047
720	Ubiquitination	RPIDHDLANWTPAQP CCCCCCCCCCCCCCC	18.64	21890473
720	Ubiquitination	RPIDHDLANWTPAQP CCCCCCCCCCCCCCC	18.64	21890473
723	Phosphorylation	DHDLANWTPAQPLAP CCCCCCCCCCCCCCC	14.46	28555341
740 (in isoform 6)	Phosphorylation	-	45.54	24719451
748	Ubiquitination	RQLLLFYLEQCEANL HHHHHHHHHHHHCHH	2.61	21890473
748	Ubiquitination	RQLLLFYLEQCEANL HHHHHHHHHHHHCHH	2.61	21890473
813	Phosphorylation	ADVRSQVTHYSNLLC HHHHHHHHHHHHHHH	13.88	30631047
815	Phosphorylation	VRSQVTHYSNLLCDL HHHHHHHHHHHHHHH	7.01	-
831	Acetylation	RGIVATTKAAALQYP HHHHHHHHHHHHCCC	31.50	26051181
831	Ubiquitination	RGIVATTKAAALQYP HHHHHHHHHHHHCCC	31.50	-
851	Ubiquitination	QDMVERVKELGHSTQ HHHHHHHHHHCCHHH	54.14	-

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
12	Y	Phosphorylation	Kinase	BMX	P51813	GPS
128	Y	Phosphorylation	Kinase	FGFR1	P11362	PhosphoELM
128	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
165	Y	Phosphorylation	Kinase	PTK6	Q13882	GPS
249	Y	Phosphorylation	Kinase	ABL1	P00519	Uniprot
249	Y	Phosphorylation	Kinase	FGFR1	P11362	PhosphoELM
306	Y	Phosphorylation	Kinase	FGFR1	P11362	PhosphoELM
327	Y	Phosphorylation	Kinase	FGFR1	P11362	PhosphoELM
410	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
410	Y	Phosphorylation	Kinase	FGFR1	P11362	PhosphoELM
653	Y	Phosphorylation	Kinase	SRC	P12931	GPS
653	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
664	Y	Phosphorylation	Kinase	SYK	P43405	GPS
664	Y	Phosphorylation	Kinase	PTK6	Q13882	GPS
666	Y	Phosphorylation	Kinase	SYK	P43405	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BCAR1_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 BCAR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPGF1_HUMAN	RAPGEF1	physical	9748234
FAK1_HUMAN	PTK2	physical	8810278
PAXI_HUMAN	PXN	physical	8810278
TENS1_HUMAN	TNS1	physical	8810278
SRC_HUMAN	SRC	physical	12397603
CRKL_HUMAN	CRKL	physical	8810278
CRK_HUMAN	CRK	physical	15492270
ABL1_HUMAN	ABL1	physical	8810278
SRCN1_HUMAN	SRCIN1	physical	14657239
CRK_HUMAN	CRK	physical	14657239
RHG32_HUMAN	ARHGAP32	physical	12819203
PTN12_HUMAN	PTPN12	physical	12714323
DOCK1_HUMAN	DOCK1	physical	12615911
SRC_HUMAN	SRC	physical	12615911
CRK_HUMAN	CRK	physical	12615911
E2F2_HUMAN	E2F2	physical	16169070
EFS_HUMAN	EFS	physical	16169070
FXYD6_HUMAN	FXYD6	physical	16169070
PR15A_HUMAN	PPP1R15A	physical	16169070
TBA1A_MOUSE	Tuba1a	physical	16169070
VPS11_HUMAN	VPS11	physical	16169070
GRP78_HUMAN	HSPA5	physical	16169070
PTN12_HUMAN	PTPN12	physical	9285683
SRC_HUMAN	SRC	physical	11514617
SRC_HUMAN	SRC	physical	10739664
FYN_HUMAN	FYN	physical	10739664
NPHP1_HUMAN	NPHP1	physical	10739664
SH3K1_HUMAN	SH3KBP1	physical	11071869
LCK_HUMAN	LCK	physical	9020138
HCK_HUMAN	HCK	physical	9020138
P85A_HUMAN	PIK3R1	physical	10799562
PTN12_HUMAN	PTPN12	physical	9748319
FAK1_HUMAN	PTK2	physical	8649427
FYN_HUMAN	FYN	physical	9188452
PTN11_HUMAN	PTPN11	physical	9188452
FAK1_HUMAN	PTK2	physical	11577104
VINC_HUMAN	VCL	physical	11577104
PAXI_HUMAN	PXN	physical	11577104
CD2AP_HUMAN	CD2AP	physical	10339567
PTN1_HUMAN	PTPN1	physical	8940134
CRK_HUMAN	CRK	physical	10329689
SHIP2_HUMAN	INPPL1	physical	11158326
NCK1_HUMAN	NCK1	physical	12135674
1433Z_HUMAN	YWHAZ	physical	10026197
CRK_HUMAN	CRK	physical	16267043
FAK1_HUMAN	PTK2	physical	15673687
CRK_HUMAN	CRK	physical	10747099
CRK_HUMAN	CRK	physical	17038317
ACK1_HUMAN	TNK2	physical	17038317
RAN_HUMAN	RAN	physical	11032817
CBL_HUMAN	CBL	physical	8683103
NPHP1_HUMAN	NPHP1	physical	18477472
CRK_HUMAN	CRK	physical	11839772
FAK1_HUMAN	PTK2	physical	11839772
CRK_HUMAN	CRK	physical	18835194
CRKL_HUMAN	CRKL	physical	18835194
CRK_HUMAN	CRK	physical	22974441
NCK1_HUMAN	NCK1	physical	22974441
BMX_HUMAN	BMX	physical	22974441
CRKL_HUMAN	CRKL	physical	22974441
MMP14_HUMAN	MMP14	physical	18164686
ARMX3_HUMAN	ARMCX3	physical	22863883
GMPR2_HUMAN	GMPR2	physical	22863883
KI13A_HUMAN	KIF13A	physical	22863883
SEN34_HUMAN	TSEN34	physical	22863883
ALK_HUMAN	ALK	physical	16105984
ERBB2_HUMAN	ERBB2	physical	26716506
PTEN_HUMAN	PTEN	physical	9927060
SRC_HUMAN	SRC	physical	16849545

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 BCAR1_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-134; SER-139; THR-269AND SER-292, AND MASS SPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND MASSSPECTROMETRY.	17081983 [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-128; TYR-234; TYR-249;TYR-267; TYR-287; TYR-327 AND TYR-387, 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-234; TYR-267; TYR-327;TYR-362; TYR-387 AND TYR-410, AND MASS 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-128; TYR-234; TYR-249AND TYR-387, 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-327, 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-249 AND TYR-327, ANDMASS SPECTROMETRY.	15951569 [Abstract]
"Phosphoproteome analysis of HeLa cells using stable isotope labelingwith amino acids in cell culture (SILAC)."; Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.; J. Proteome Res. 4:1661-1671(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128; TYR-222; TYR-224;TYR-234; TYR-249 AND TYR-387, AND MASS SPECTROMETRY.	16212419 [Abstract]