dbPTM

EPHA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EPHA2_HUMAN
UniProt AC	P29317
Protein Name	Ephrin type-A receptor 2
Gene Name	EPHA2
Organism	Homo sapiens (Human).
Sequence Length	976
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Cell projection, ruffle membrane Single-pass type I membrane protein . Cell projection, lamellipodium membrane Single-pass type I membrane protein . Cell junction, focal adhesion . Present at
Protein Description	Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.; (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins..
Protein Sequence	MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
67	Phosphorylation	NDMPIYMYSVCNVMS HCCCEEEEEEHHCCC	4.87	-
136	Ubiquitination	DYGTNFQKRLFTKID CCCCCHHHHHHEECC	47.10	21890473
141	Ubiquitination	FQKRLFTKIDTIAPD HHHHHHEECCEECCC	31.11	21890473
153	Phosphorylation	APDEITVSSDFEARH CCCEEEECCCCEEEE	18.62	19060867
154	Phosphorylation	PDEITVSSDFEARHV CCEEEECCCCEEEEE	41.82	29507054
162	Ubiquitination	DFEARHVKLNVEERS CCEEEEEECCCEECC	28.37	21890473
197	Phosphorylation	ALLSVRVYYKKCPEL HHHHHHHHHHHCHHH	10.05	22210691
198	Phosphorylation	LLSVRVYYKKCPELL HHHHHHHHHHCHHHH	10.91	22210691
277	Phosphorylation	EDACQACSPGFFKFE HHHHHHCCCCEEEEE	30.95	-
365	Phosphorylation	EDIVYSVTCEQCWPE CCEEEEEEEHHHCCC	12.37	28102081
373	Phosphorylation	CEQCWPESGECGPCE EHHHCCCCCCCCCCE	35.49	26657352
407	N-linked_Glycosylation	SDLEPHMNYTFTVEA HHCCCCCCEEEEEEE	29.65	UniProtKB CARBOHYD
426	Phosphorylation	SGLVTSRSFRTASVS CEEEECCEEEEEEEE	20.88	17855441
429	Phosphorylation	VTSRSFRTASVSINQ EECCEEEEEEEEECC	22.67	-
433	Phosphorylation	SFRTASVSINQTEPP EEEEEEEEECCCCCC	17.21	17855441
435	N-linked_Glycosylation	RTASVSINQTEPPKV EEEEEEECCCCCCEE	34.90	19159218
437	Phosphorylation	ASVSINQTEPPKVRL EEEEECCCCCCEEEE	46.07	17855441
570	Phosphorylation	KNQRARQSPEDVYFS HCHHHHCCCCCCCCC	25.38	30266825
575	Phosphorylation	RQSPEDVYFSKSEQL HCCCCCCCCCCHHHC	17.92	27273156
577	Phosphorylation	SPEDVYFSKSEQLKP CCCCCCCCCHHHCCC	20.00	30266825
578	Ubiquitination	PEDVYFSKSEQLKPL CCCCCCCCHHHCCCC	48.38	21890473
578	Ubiquitination	PEDVYFSKSEQLKPL CCCCCCCCHHHCCCC	48.38	21890473
579	Phosphorylation	EDVYFSKSEQLKPLK CCCCCCCHHHCCCCC	29.40	22322096
583	Malonylation	FSKSEQLKPLKTYVD CCCHHHCCCCCCCCC	48.26	26320211
583	Ubiquitination	FSKSEQLKPLKTYVD CCCHHHCCCCCCCCC	48.26	21906983
586	Ubiquitination	SEQLKPLKTYVDPHT HHHCCCCCCCCCCCC	46.46	21890473
587	Phosphorylation	EQLKPLKTYVDPHTY HHCCCCCCCCCCCCC	36.14	21945579
588	Phosphorylation	QLKPLKTYVDPHTYE HCCCCCCCCCCCCCC	10.98	21945579
593	Phosphorylation	KTYVDPHTYEDPNQA CCCCCCCCCCCCCCH	33.71	21945579
594	Phosphorylation	TYVDPHTYEDPNQAV CCCCCCCCCCCCCHH	18.46	22322096
603	Ubiquitination	DPNQAVLKFTTEIHP CCCCHHHEEECEECH	33.78	-
612	S-nitrosylation	TTEIHPSCVTRQKVI ECEECHHHCCCCEEE	4.22	2212679
617	Ubiquitination	PSCVTRQKVIGAGEF HHHCCCCEEECCCCC	32.31	21890473
628	Phosphorylation	AGEFGEVYKGMLKTS CCCCHHHHHEEEECC	9.49	25159151
629	Ubiquitination	GEFGEVYKGMLKTSS CCCHHHHHEEEECCC	42.91	-
635	Phosphorylation	YKGMLKTSSGKKEVP HHEEEECCCCCCCCC	35.19	23879269
636	Phosphorylation	KGMLKTSSGKKEVPV HEEEECCCCCCCCCE	60.92	23879269
639	Ubiquitination	LKTSSGKKEVPVAIK EECCCCCCCCCEEEE	68.42	21890473
646	Ubiquitination	KEVPVAIKTLKAGYT CCCCEEEEEECCCCC	37.76	-
647	Phosphorylation	EVPVAIKTLKAGYTE CCCEEEEEECCCCCH	27.64	17192257
649	Ubiquitination	PVAIKTLKAGYTEKQ CEEEEEECCCCCHHH	45.02	-
655	Ubiquitination	LKAGYTEKQRVDFLG ECCCCCHHHCCCHHH	35.29	-
685	Phosphorylation	LEGVISKYKPMMIIT EEHHHHHCCCEEEEE	17.34	26356563
686	Ubiquitination	EGVISKYKPMMIITE EHHHHHCCCEEEEEH	30.12	21890473
692	Phosphorylation	YKPMMIITEYMENGA CCCEEEEEHHHHCCC	15.33	-
694	Phosphorylation	PMMIITEYMENGALD CEEEEEHHHHCCCHH	10.90	27259358
712	Phosphorylation	REKDGEFSVLQLVGM HHCCCCCCHHHHHHH	20.02	-
728	Ubiquitination	RGIAAGMKYLANMNY HHHHHHHHHHHCCCC	35.87	-
735	Phosphorylation	KYLANMNYVHRDLAA HHHHCCCCCCHHHHH	6.20	27259358
749	Phosphorylation	ARNILVNSNLVCKVS HHCEEECCCEEEEEC	24.86	-
754	Ubiquitination	VNSNLVCKVSDFGLS ECCCEEEEECHHCCC	36.98	-
756	Phosphorylation	SNLVCKVSDFGLSRV CCEEEEECHHCCCHH	16.83	-
761	Phosphorylation	KVSDFGLSRVLEDDP EECHHCCCHHCCCCC	22.26	22817900
771	Phosphorylation	LEDDPEATYTTSGGK CCCCCCCEEECCCCE	21.53	21945579
772	Phosphorylation	EDDPEATYTTSGGKI CCCCCCEEECCCCEE	18.31	22322096
773	Phosphorylation	DDPEATYTTSGGKIP CCCCCEEECCCCEEE	15.32	21945579
774	Phosphorylation	DPEATYTTSGGKIPI CCCCEEECCCCEEEE	18.24	21945579
775	Phosphorylation	PEATYTTSGGKIPIR CCCEEECCCCEEEEE	37.44	21945579
778	Ubiquitination	TYTTSGGKIPIRWTA EEECCCCEEEEEEEC	49.16	21890473
790	Phosphorylation	WTAPEAISYRKFTSA EECCCCCCCCCCCCH	26.40	25348954
791	Phosphorylation	TAPEAISYRKFTSAS ECCCCCCCCCCCCHH	16.23	27273156
828	Sumoylation	LSNHEVMKAINDGFR CCCHHHHHHHCCCCC	51.82	-
847	Phosphorylation	MDCPSAIYQLMMQCW CCCHHHHHHHHHHHH	8.70	27259358
869	Phosphorylation	PKFADIVSILDKLIR CCHHHHHHHHHHHHC	20.12	24114839
873	Ubiquitination	DIVSILDKLIRAPDS HHHHHHHHHHCCCCH	42.22	-
880	Phosphorylation	KLIRAPDSLKTLADF HHHCCCCHHHCCCCC	30.61	29514088
882	Ubiquitination	IRAPDSLKTLADFDP HCCCCHHHCCCCCCC	45.50	21890473
883	Phosphorylation	RAPDSLKTLADFDPR CCCCHHHCCCCCCCC	32.26	23403867
892	Phosphorylation	ADFDPRVSIRLPSTS CCCCCCEEEECCCCC	11.85	30266825
897	Phosphorylation	RVSIRLPSTSGSEGV CEEEECCCCCCCCCC	39.53	29255136
898	Phosphorylation	VSIRLPSTSGSEGVP EEEECCCCCCCCCCC	34.86	29255136
899	Phosphorylation	SIRLPSTSGSEGVPF EEECCCCCCCCCCCC	44.66	29255136
901	Phosphorylation	RLPSTSGSEGVPFRT ECCCCCCCCCCCCEE	30.83	29255136
908	Phosphorylation	SEGVPFRTVSEWLES CCCCCCEEHHHHHHH	28.85	28176443
910	Phosphorylation	GVPFRTVSEWLESIK CCCCEEHHHHHHHHH	23.57	28176443
915	Phosphorylation	TVSEWLESIKMQQYT EHHHHHHHHHHHHHH	25.91	28176443
921	Phosphorylation	ESIKMQQYTEHFMAA HHHHHHHHHHHHHHH	9.37	21082442
922	Phosphorylation	SIKMQQYTEHFMAAG HHHHHHHHHHHHHHC	20.74	27273156
930	Phosphorylation	EHFMAAGYTAIEKVV HHHHHHCHHHHHHHH	6.56	19573808
931	Phosphorylation	HFMAAGYTAIEKVVQ HHHHHCHHHHHHHHH	21.90	28442448
935	Ubiquitination	AGYTAIEKVVQMTND HCHHHHHHHHHHCCH	41.41	-
940	Phosphorylation	IEKVVQMTNDDIKRI HHHHHHHCCHHHHHH	20.57	27470641
945	Ubiquitination	QMTNDDIKRIGVRLP HHCCHHHHHHCCCCC	44.98	21890473
945	2-Hydroxyisobutyrylation	QMTNDDIKRIGVRLP HHCCHHHHHHCCCCC	44.98	-
960	Phosphorylation	GHQKRIAYSLLGLKD CCHHHHHHHHCCCCC	9.47	21945579
961	Phosphorylation	HQKRIAYSLLGLKDQ CHHHHHHHHCCCCCH	14.22	21945579
971	Phosphorylation	GLKDQVNTVGIPI-- CCCCHHCCCCCCC--	22.66	27470641

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
575	Y	Phosphorylation	Kinase	EPHA2	P29317	PSP
588	Y	Phosphorylation	Kinase	EPHA2	P29317	PSP
594	Y	Phosphorylation	Kinase	EPHA2	P29317	PSP
628	Y	Phosphorylation	Kinase	EPHA2	P29317	PSP
694	Y	Phosphorylation	Kinase	EPHA2	P29317	PSP
735	Y	Phosphorylation	Kinase	EPHA2	P29317	PSP
772	Y	Phosphorylation	Kinase	EPHA2	P29317	PSP
897	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
897	S	Phosphorylation	Kinase	P90RSK	Q15418	PSP
897	S	Phosphorylation	Kinase	RSK2	P51812	PSP
897	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
897	S	Phosphorylation	Kinase	PKA	-	Uniprot
921	Y	Phosphorylation	Kinase	EPHA2	P29317	PSP
960	Y	Phosphorylation	Kinase	EPHA2	P29317	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:12496371
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:19567782

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
897	S	Phosphorylation	19573808
Phosphorylated at Ser-897 by PKA; blocks cell retraction induced by EPHA2 kinase activity.
897	S	Phosphorylation	19573808
Phosphorylated at Ser-897 by PKB; serum-induced phosphorylation which targets EPHA2 to the cell leading edge and stimulates cell migration.
897	S	Phosphorylation	19573808
Phosphorylated at Ser-897 in response to TNF by RPS6KA1 and RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell migration.

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 EPHA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRB2_HUMAN	GRB2	physical	12400011
PTN11_HUMAN	PTPN11	physical	10655584
PPAC_HUMAN	ACP1	physical	12167657
EPHA2_HUMAN	EPHA2	physical	18797457
CBL_HUMAN	CBL	physical	12496371
A4_HUMAN	APP	physical	21832049
HS90A_HUMAN	HSP90AA1	physical	22939624
GATD1_HUMAN	GATAD1	physical	21988832
IMA4_HUMAN	KPNA3	physical	21988832
RBL1_HUMAN	RBL1	physical	21988832
NUDT9_HUMAN	NUDT9	physical	21988832
CDK17_HUMAN	CDK17	physical	21988832
PSME2_HUMAN	PSME2	physical	21988832
LSM7_HUMAN	LSM7	physical	21988832
CBL_HUMAN	CBL	physical	23874206
CLH1_HUMAN	CLTC	physical	23874206
AP2M1_HUMAN	AP2M1	physical	23874206
AP2B1_HUMAN	AP2B1	physical	23874206
AP2A1_HUMAN	AP2A1	physical	23874206
AP2S1_HUMAN	AP2S1	physical	23874206
EPS15_HUMAN	EPS15	physical	23874206
SLAP1_HUMAN	SLA	physical	24457997
FACD2_HUMAN	FANCD2	physical	26496610
SSRG_HUMAN	SSR3	physical	26496610
TGFR1_HUMAN	TGFBR1	physical	26496610
ZBT14_HUMAN	ZBTB14	physical	26496610
VPS4B_HUMAN	VPS4B	physical	26496610
SCAM3_HUMAN	SCAMP3	physical	26496610
HEXI1_HUMAN	HEXIM1	physical	26496610
GOLI4_HUMAN	GOLIM4	physical	26496610
NDUAD_HUMAN	NDUFA13	physical	26496610
SMRCD_HUMAN	SMARCAD1	physical	26496610
RT35_HUMAN	MRPS35	physical	26496610
MILK1_HUMAN	MICALL1	physical	26496610
DUS18_HUMAN	DUSP18	physical	28065597
DUS19_HUMAN	DUSP19	physical	28065597
DUPD1_HUMAN	DUPD1	physical	28065597
DUS26_HUMAN	DUSP26	physical	28065597
EPHA2_HUMAN	EPHA2	physical	28065597
PPM1L_HUMAN	PPM1L	physical	28065597
ILKAP_HUMAN	ILKAP	physical	28065597
PTPRR_HUMAN	PTPRR	physical	28065597
PTN7_HUMAN	PTPN7	physical	28065597
PTN11_HUMAN	PTPN11	physical	28065597
DUS14_HUMAN	DUSP14	physical	28065597
STYX_HUMAN	STYX	physical	28065597
TPTE_HUMAN	TPTE	physical	28065597
TPTE2_HUMAN	TPTE2	physical	28065597

Drug and Disease Associations

Kegg Disease
H01202	Cataract
OMIM Disease
116600	Cataract 6, multiple types (CTRCT6)
Kegg Drug
D03658	Dasatinib (INN)
D06414	Dasatinib hydrate (JAN); Dasatinib (USAN); Sprycel (TN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EPHA2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-435, AND MASSSPECTROMETRY.	19159218 [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 SER-153; SER-373; SER-570;TYR-575; THR-587; TYR-588; THR-593; TYR-594; TYR-628; THR-647;THR-771; TYR-772; SER-790; TYR-791; SER-869; SER-880; SER-897;THR-898; SER-899; SER-901; SER-910 AND TYR-960, AND MASS SPECTROMETRY.	19369195 [Abstract]
"EphA2 mediates ligand-dependent inhibition and ligand-independentpromotion of cell migration and invasion via a reciprocal regulatoryloop with Akt."; Miao H., Li D.Q., Mukherjee A., Guo H., Petty A., Cutter J.,Basilion J.P., Sedor J., Wu J., Danielpour D., Sloan A.E., Cohen M.L.,Wang B.; Cancer Cell 16:9-20(2009). Cited for: DISEASE, FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION, MUTAGENESISOF ASP-739 AND SER-897, AND PHOSPHORYLATION AT SER-897 BY PKB.	19573808 [Abstract]
"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-570; SER-892 ANDSER-901, AND MASS SPECTROMETRY.	18669648 [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-570; TYR-575; SER-579;TYR-594; TYR-628; THR-647; TYR-772; SER-897; THR-898; SER-899 ANDSER-901, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; TYR-594; TYR-772;SER-897; THR-898 AND SER-901, AND MASS SPECTROMETRY.	17192257 [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-575; TYR-588; TYR-594;TYR-772 AND TYR-960, 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-575; TYR-588 ANDTYR-772, 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-575; TYR-588; TYR-594AND TYR-772, 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-588; TYR-594; TYR-772;TYR-921 AND TYR-930, AND MASS SPECTROMETRY.	15951569 [Abstract]

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