dbPTM

ESYT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ESYT1_HUMAN
UniProt AC	Q9BSJ8
Protein Name	Extended synaptotagmin-1
Gene Name	ESYT1
Organism	Homo sapiens (Human).
Sequence Length	1104
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein. Cell membrane Peripheral membrane protein. Localizes primarily to the endoplasmic reticulum. Recruited to sites of contact between the endoplasmic reticulum and the cell membrane in respon
Protein Description	Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels. Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane..
Protein Sequence	MERSPGEGPSPSPMDQPSAPSDPTDQPPAAHAKPDPGSGGQPAGPGAAGEALAVLTSFGRRLLVLIPVYLAGAVGLSVGFVLFGLALYLGWRRVRDEKERSLRAARQLLDDEEQLTAKTLYMSHRELPAWVSFPDVEKAEWLNKIVAQVWPFLGQYMEKLLAETVAPAVRGSNPHLQTFTFTRVELGEKPLRIIGVKVHPGQRKEQILLDLNISYVGDVQIDVEVKKYFCKAGVKGMQLHGVLRVILEPLIGDLPFVGAVSMFFIRRPTLDINWTGMTNLLDIPGLSSLSDTMIMDSIAAFLVLPNRLLVPLVPDLQDVAQLRSPLPRGIIRIHLLAARGLSSKDKYVKGLIEGKSDPYALVRLGTQTFCSRVIDEELNPQWGETYEVMVHEVPGQEIEVEVFDKDPDKDDFLGRMKLDVGKVLQASVLDDWFPLQGGQGQVHLRLEWLSLLSDAEKLEQVLQWNWGVSSRPDPPSAAILVVYLDRAQDLPLKKGNKEPNPMVQLSIQDVTQESKAVYSTNCPVWEEAFRFFLQDPQSQELDVQVKDDSRALTLGALTLPLARLLTAPELILDQWFQLSSSGPNSRLYMKLVMRILYLDSSEICFPTVPGCPGAWDVDSENPQRGSSVDAPPRPCHTTPDSQFGTEHVLRIHVLEAQDLIAKDRFLGGLVKGKSDPYVKLKLAGRSFRSHVVREDLNPRWNEVFEVIVTSVPGQELEVEVFDKDLDKDDFLGRCKVRLTTVLNSGFLDEWLTLEDVPSGRLHLRLERLTPRPTAAELEEVLQVNSLIQTQKSAELAAALLSIYMERAEDLPLRKGTKHLSPYATLTVGDSSHKTKTISQTSAPVWDESASFLIRKPHTESLELQVRGEGTGVLGSLSLPLSELLVADQLCLDRWFTLSSGQGQVLLRAQLGILVSQHSGVEAHSHSYSHSSSSLSEEPELSGGPPHITSSAPELRQRLTHVDSPLEAPAGPLGQVKLTLWYYSEERKLVSIVHGCRSLRQNGRDPPDPYVSLLLLPDKNRGTKRRTSQKKRTLSPEFNERFEWELPLDEAQRRKLDVSVKSNSSFMSRERELLGKVQLDLAETDLSQGVARWYDLMDNKDKGSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MERSPGEG -------CCCCCCCC	42.26	19413330
4	Phosphorylation	----MERSPGEGPSP ----CCCCCCCCCCC	40.31	23663014
10	Phosphorylation	RSPGEGPSPSPMDQP CCCCCCCCCCCCCCC	49.19	23663014
12	Phosphorylation	PGEGPSPSPMDQPSA CCCCCCCCCCCCCCC	36.87	23663014
18	Phosphorylation	PSPMDQPSAPSDPTD CCCCCCCCCCCCCCC	47.37	23312004
24	O-linked_Glycosylation	PSAPSDPTDQPPAAH CCCCCCCCCCCCCCC	52.86	OGP
77	Phosphorylation	LAGAVGLSVGFVLFG HHHHHHHHHHHHHHH	17.79	-
88	Phosphorylation	VLFGLALYLGWRRVR HHHHHHHHHCHHHHH	9.50	30576142
116	Phosphorylation	LDDEEQLTAKTLYMS CCCHHHHHHHHHHHH	26.29	28857561
118	Ubiquitination	DEEQLTAKTLYMSHR CHHHHHHHHHHHHHC	33.55	21890473
118 (in isoform 2)	Ubiquitination	-	33.55	21890473
118 (in isoform 1)	Ubiquitination	-	33.55	21890473
119	Phosphorylation	EEQLTAKTLYMSHRE HHHHHHHHHHHHHCC	22.21	23090842
121	Phosphorylation	QLTAKTLYMSHRELP HHHHHHHHHHHCCCC	11.21	25884760
123	Phosphorylation	TAKTLYMSHRELPAW HHHHHHHHHCCCCCC	13.06	23090842
132	Phosphorylation	RELPAWVSFPDVEKA CCCCCCCCCCCHHHH	21.99	28857561
138	Ubiquitination	VSFPDVEKAEWLNKI CCCCCHHHHHHHHHH	51.99	21890473
138 (in isoform 2)	Ubiquitination	-	51.99	21890473
138	Acetylation	VSFPDVEKAEWLNKI CCCCCHHHHHHHHHH	51.99	26822725
138 (in isoform 1)	Ubiquitination	-	51.99	21890473
170	Methylation	ETVAPAVRGSNPHLQ HHHHHHHCCCCCCCE	44.95	-
172	Phosphorylation	VAPAVRGSNPHLQTF HHHHHCCCCCCCEEE	36.30	29978859
178	Phosphorylation	GSNPHLQTFTFTRVE CCCCCCEEEEEEEEE	30.88	27067055
180	Phosphorylation	NPHLQTFTFTRVELG CCCCEEEEEEEEEEC	27.73	27067055
182	Phosphorylation	HLQTFTFTRVELGEK CCEEEEEEEEEECCC	30.65	27067055
189	Acetylation	TRVELGEKPLRIIGV EEEEECCCCEEEEEE	47.78	23749302
189	Ubiquitination	TRVELGEKPLRIIGV EEEEECCCCEEEEEE	47.78	1890473
189 (in isoform 2)	Ubiquitination	-	47.78	21890473
189 (in isoform 1)	Ubiquitination	-	47.78	21890473
197	Ubiquitination	PLRIIGVKVHPGQRK CEEEEEEEECCCCCH	29.61	21890473
197 (in isoform 2)	Ubiquitination	-	29.61	21890473
197	Malonylation	PLRIIGVKVHPGQRK CEEEEEEEECCCCCH	29.61	26320211
197	Acetylation	PLRIIGVKVHPGQRK CEEEEEEEECCCCCH	29.61	25953088
197 (in isoform 1)	Ubiquitination	-	29.61	21890473
231	Ubiquitination	EVKKYFCKAGVKGMQ EHHHHHHHHCCCHHC	37.97	-
235	Malonylation	YFCKAGVKGMQLHGV HHHHHCCCHHCHHHH	47.98	26320211
269	Phosphorylation	MFFIRRPTLDINWTG EEEECCCCCCCCCCC	34.94	-
324	Phosphorylation	QDVAQLRSPLPRGII HHHHHHCCCCCCHHH	39.10	25849741
344	Ubiquitination	AARGLSSKDKYVKGL HHCCCCCCCHHHHHH	55.66	-
347	Phosphorylation	GLSSKDKYVKGLIEG CCCCCCHHHHHHCCC	19.96	29978859
349	Ubiquitination	SSKDKYVKGLIEGKS CCCCHHHHHHCCCCC	44.93	-
349 (in isoform 2)	Ubiquitination	-	44.93	-
355	Ubiquitination	VKGLIEGKSDPYALV HHHHCCCCCCCCHHH	38.61	21906983
355 (in isoform 2)	Ubiquitination	-	38.61	21890473
355	Malonylation	VKGLIEGKSDPYALV HHHHCCCCCCCCHHH	38.61	32601280
355 (in isoform 1)	Ubiquitination	-	38.61	21890473
356	Phosphorylation	KGLIEGKSDPYALVR HHHCCCCCCCCHHHE	55.46	20860994
359	Phosphorylation	IEGKSDPYALVRLGT CCCCCCCCHHHEECC	19.98	25884760
366	Phosphorylation	YALVRLGTQTFCSRV CHHHEECCCCHHHHH	29.09	26471730
371	Phosphorylation	LGTQTFCSRVIDEEL ECCCCHHHHHCCCCC	25.95	26471730
409	Ubiquitination	VFDKDPDKDDFLGRM EECCCCCCCCCCCCC	65.66	-
417	Ubiquitination	DDFLGRMKLDVGKVL CCCCCCCCCCHHHHH	39.93	-
417	Acetylation	DDFLGRMKLDVGKVL CCCCCCCCCCHHHHH	39.93	25953088
422	Ubiquitination	RMKLDVGKVLQASVL CCCCCHHHHHHHHEE	39.35	-
422 (in isoform 2)	Ubiquitination	-	39.35	-
453	Phosphorylation	LEWLSLLSDAEKLEQ HHHHHHHCCHHHHHH	39.82	-
493	Ubiquitination	RAQDLPLKKGNKEPN HHHCCCCCCCCCCCC	57.61	-
493	Malonylation	RAQDLPLKKGNKEPN HHHCCCCCCCCCCCC	57.61	26320211
493	Acetylation	RAQDLPLKKGNKEPN HHHCCCCCCCCCCCC	57.61	25953088
494 (in isoform 2)	Phosphorylation	-	75.33	-
495 (in isoform 2)	Phosphorylation	-	49.18	-
497	Ubiquitination	LPLKKGNKEPNPMVQ CCCCCCCCCCCCCEE	81.08	-
497	Malonylation	LPLKKGNKEPNPMVQ CCCCCCCCCCCCCEE	81.08	26320211
497 (in isoform 1)	Ubiquitination	-	81.08	21890473
498 (in isoform 2)	Phosphorylation	-	55.07	-
506	Phosphorylation	PNPMVQLSIQDVTQE CCCCEEEEEEECHHH	10.91	27251275
507 (in isoform 2)	Ubiquitination	-	5.72	21890473
511	Phosphorylation	QLSIQDVTQESKAVY EEEEEECHHHHHHHH	34.60	-
514	Phosphorylation	IQDVTQESKAVYSTN EEECHHHHHHHHCCC	18.98	27251275
546	Ubiquitination	QELDVQVKDDSRALT CCCCEEECCCHHHHH	38.43	21906983
546 (in isoform 1)	Ubiquitination	-	38.43	21890473
553	Phosphorylation	KDDSRALTLGALTLP CCCHHHHHHHHHHHH	23.35	27050516
556 (in isoform 2)	Ubiquitination	-	10.65	21890473
580	Phosphorylation	DQWFQLSSSGPNSRL HHHHHHCCCCCCHHH	48.16	-
588	Phosphorylation	SGPNSRLYMKLVMRI CCCCHHHHHHHHHHH	7.35	-
626	Phosphorylation	SENPQRGSSVDAPPR CCCCCCCCCCCCCCC	29.40	23927012
627	Phosphorylation	ENPQRGSSVDAPPRP CCCCCCCCCCCCCCC	27.17	23401153
635	S-palmitoylation	VDAPPRPCHTTPDSQ CCCCCCCCCCCCCHH	4.74	21044946
637	Phosphorylation	APPRPCHTTPDSQFG CCCCCCCCCCCHHCC	46.90	23927012
637	O-linked_Glycosylation	APPRPCHTTPDSQFG CCCCCCCCCCCHHCC	46.90	OGP
638	Phosphorylation	PPRPCHTTPDSQFGT CCCCCCCCCCHHCCC	11.05	28464451
641	Phosphorylation	PCHTTPDSQFGTEHV CCCCCCCHHCCCCCE	28.72	23927012
645	Phosphorylation	TPDSQFGTEHVLRIH CCCHHCCCCCEEEEE	24.98	23927012
662	Ubiquitination	EAQDLIAKDRFLGGL EHHHHHHCCCCCCHH	42.30	-
671	Ubiquitination	RFLGGLVKGKSDPYV CCCCHHCCCCCCCCC	66.71	-
673	Ubiquitination	LGGLVKGKSDPYVKL CCHHCCCCCCCCCEE	46.07	-
674	Phosphorylation	GGLVKGKSDPYVKLK CHHCCCCCCCCCEEE	53.11	28152594
677	Phosphorylation	VKGKSDPYVKLKLAG CCCCCCCCCEEEECC	18.40	28152594
679	Acetylation	GKSDPYVKLKLAGRS CCCCCCCEEEECCCC	33.78	19608861
679	Ubiquitination	GKSDPYVKLKLAGRS CCCCCCCEEEECCCC	33.78	19608861
679	Malonylation	GKSDPYVKLKLAGRS CCCCCCCEEEECCCC	33.78	32601280
681 (in isoform 2)	Ubiquitination	-	30.49	-
681	Ubiquitination	SDPYVKLKLAGRSFR CCCCCEEEECCCCHH	30.49	-
686	Phosphorylation	KLKLAGRSFRSHVVR EEEECCCCHHHHCHH	24.88	30266825
727	Ubiquitination	VFDKDLDKDDFLGRC EECCCCCCCCCHHCC	67.50	-
739	Phosphorylation	GRCKVRLTTVLNSGF HCCEEEEEEEECCCC	12.32	21130716
740	Phosphorylation	RCKVRLTTVLNSGFL CCEEEEEEEECCCCC	27.82	21130716
744	Phosphorylation	RLTTVLNSGFLDEWL EEEEEECCCCCCCCE	27.10	21130716
817	Acetylation	LPLRKGTKHLSPYAT CCCCCCCCCCCCCCE	51.74	19608861
817	Ubiquitination	LPLRKGTKHLSPYAT CCCCCCCCCCCCCCE	51.74	21890473
817 (in isoform 1)	Ubiquitination	-	51.74	21890473
820	Phosphorylation	RKGTKHLSPYATLTV CCCCCCCCCCCEEEE	18.65	29255136
822	Phosphorylation	GTKHLSPYATLTVGD CCCCCCCCCEEEECC	14.61	25159151
824	Phosphorylation	KHLSPYATLTVGDSS CCCCCCCEEEECCCC	19.67	30266825
826	Phosphorylation	LSPYATLTVGDSSHK CCCCCEEEECCCCCC	20.35	30266825
827 (in isoform 2)	Ubiquitination	-	10.11	21890473
830	Phosphorylation	ATLTVGDSSHKTKTI CEEEECCCCCCCCEE	28.54	23927012
831	Phosphorylation	TLTVGDSSHKTKTIS EEEECCCCCCCCEEE	33.47	23927012
833	Ubiquitination	TVGDSSHKTKTISQT EECCCCCCCCEEECC	54.38	-
833	Malonylation	TVGDSSHKTKTISQT EECCCCCCCCEEECC	54.38	26320211
834	Phosphorylation	VGDSSHKTKTISQTS ECCCCCCCCEEECCC	28.17	20068231
835	Ubiquitination	GDSSHKTKTISQTSA CCCCCCCCEEECCCC	48.98	21906983
835 (in isoform 1)	Ubiquitination	-	48.98	21890473
836	Phosphorylation	DSSHKTKTISQTSAP CCCCCCCEEECCCCC	30.96	20068231
838	Phosphorylation	SHKTKTISQTSAPVW CCCCCEEECCCCCCC	32.41	20068231
840	Phosphorylation	KTKTISQTSAPVWDE CCCEEECCCCCCCCC	21.77	20068231
841	Phosphorylation	TKTISQTSAPVWDES CCEEECCCCCCCCCC	23.96	20068231
845 (in isoform 2)	Ubiquitination	-	11.55	21890473
848	Phosphorylation	SAPVWDESASFLIRK CCCCCCCCCCEEEEC	27.09	20068231
850	Phosphorylation	PVWDESASFLIRKPH CCCCCCCCEEEECCC	29.84	28857561
855	Ubiquitination	SASFLIRKPHTESLE CCCEEEECCCCCCEE	33.87	21906983
855 (in isoform 1)	Ubiquitination	-	33.87	21890473
858	Phosphorylation	FLIRKPHTESLELQV EEEECCCCCCEEEEE	35.48	26471730
860	Phosphorylation	IRKPHTESLELQVRG EECCCCCCEEEEEEC	28.44	20873877
865 (in isoform 2)	Ubiquitination	-	15.42	21890473
896	Phosphorylation	LCLDRWFTLSSGQGQ HHHCCEEECCCCCCH	20.83	25850435
924	Phosphorylation	HSGVEAHSHSYSHSS CCCCCEECCCCCCCC	22.60	28348404
926	Phosphorylation	GVEAHSHSYSHSSSS CCCEECCCCCCCCCC	31.20	28348404
927	Phosphorylation	VEAHSHSYSHSSSSL CCEECCCCCCCCCCC	12.65	28348404
928	Phosphorylation	EAHSHSYSHSSSSLS CEECCCCCCCCCCCC	21.65	28348404
930	Phosphorylation	HSHSYSHSSSSLSEE ECCCCCCCCCCCCCC	26.44	26657352
931	Phosphorylation	SHSYSHSSSSLSEEP CCCCCCCCCCCCCCC	20.65	26657352
932	Phosphorylation	HSYSHSSSSLSEEPE CCCCCCCCCCCCCCH	38.01	28348404
933	Phosphorylation	SYSHSSSSLSEEPEL CCCCCCCCCCCCCHH	37.55	26657352
935	Phosphorylation	SHSSSSLSEEPELSG CCCCCCCCCCCHHHC	41.69	26657352
941	Phosphorylation	LSEEPELSGGPPHIT CCCCCHHHCCCCCCC	39.79	28464451
948	Phosphorylation	SGGPPHITSSAPELR HCCCCCCCCCCHHHH	17.37	26657352
949	Phosphorylation	GGPPHITSSAPELRQ CCCCCCCCCCHHHHH	24.73	26074081
950	Phosphorylation	GPPHITSSAPELRQR CCCCCCCCCHHHHHH	38.91	26074081
959	Phosphorylation	PELRQRLTHVDSPLE HHHHHHHHCCCCCCC	23.26	30266825
963	Phosphorylation	QRLTHVDSPLEAPAG HHHHCCCCCCCCCCC	30.23	29255136
981	Phosphorylation	QVKLTLWYYSEERKL EEEEEEEEEECCHHH	10.54	-
982	Phosphorylation	VKLTLWYYSEERKLV EEEEEEEEECCHHHH	9.68	-
987	Ubiquitination	WYYSEERKLVSIVHG EEEECCHHHHHHHHH	57.42	-
997 (in isoform 2)	Ubiquitination	-	31.79	-
1009	Phosphorylation	GRDPPDPYVSLLLLP CCCCCCCCEEEEECC	15.28	21082442
1011	Phosphorylation	DPPDPYVSLLLLPDK CCCCCCEEEEECCCC	13.88	25849741
1011	O-linked_Glycosylation	DPPDPYVSLLLLPDK CCCCCCEEEEECCCC	13.88	23301498
1018	Ubiquitination	SLLLLPDKNRGTKRR EEEECCCCCCCCCCC	46.75	-
1022	Phosphorylation	LPDKNRGTKRRTSQK CCCCCCCCCCCCCCC	20.38	-
1032	Phosphorylation	RTSQKKRTLSPEFNE CCCCCCCCCCHHHHH	40.23	30266825
1034	Phosphorylation	SQKKRTLSPEFNERF CCCCCCCCHHHHHHC	23.05	19664994
1054	Ubiquitination	LDEAQRRKLDVSVKS CCHHHHHCCCEECCC	51.75	-
1054	Malonylation	LDEAQRRKLDVSVKS CCHHHHHCCCEECCC	51.75	26320211
1058	Phosphorylation	QRRKLDVSVKSNSSF HHHCCCEECCCCCCC	24.40	20860994
1060	Ubiquitination	RKLDVSVKSNSSFMS HCCCEECCCCCCCHH	36.09	2190698
1060 (in isoform 1)	Ubiquitination	-	36.09	21890473
1061	Phosphorylation	KLDVSVKSNSSFMSR CCCEECCCCCCCHHH	39.53	23312004
1063	Phosphorylation	DVSVKSNSSFMSRER CEECCCCCCCHHHHH	31.85	20044836
1064	Phosphorylation	VSVKSNSSFMSRERE EECCCCCCCHHHHHH	29.26	23663014
1067	Phosphorylation	KSNSSFMSRERELLG CCCCCCHHHHHHHHC	29.04	23663014
1070 (in isoform 2)	Ubiquitination	-	38.46	21890473
1075	Ubiquitination	RERELLGKVQLDLAE HHHHHHCCEEHHHHH	27.12	-
1083	Phosphorylation	VQLDLAETDLSQGVA EEHHHHHCCHHHHHH	36.31	29507054
1093	Phosphorylation	SQGVARWYDLMDNKD HHHHHHHHHHHCCCC	8.14	28796482
1099	Ubiquitination	WYDLMDNKDKGSS-- HHHHHCCCCCCCC--	57.46	-
1103	Phosphorylation	MDNKDKGSS------ HCCCCCCCC------	38.32	23401153
1104	Phosphorylation	DNKDKGSS------- CCCCCCCC-------	53.56	23927012

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
324	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ESYT1_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 ESYT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYH10_HUMAN	MYH10	physical	22939629
SFXN3_HUMAN	SFXN3	physical	22939629
SYJ2B_HUMAN	SYNJ2BP	physical	22119785
ESYT2_HUMAN	ESYT2	physical	22119785
PRAF3_HUMAN	ARL6IP5	physical	22119785
YIF1B_HUMAN	YIF1B	physical	22119785
TMX1_HUMAN	TMX1	physical	27173435

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 ESYT1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-817, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-1034, AND MASSSPECTROMETRY.	19690332 [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-963 AND SER-1034, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-963, AND MASSSPECTROMETRY.	17924679 [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-822, AND MASSSPECTROMETRY.	19534553 [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-822 AND TYR-1009, ANDMASS 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-822 AND TYR-1009, ANDMASS SPECTROMETRY.	15592455 [Abstract]