dbPTM

CALD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CALD1_HUMAN
UniProt AC	Q05682
Protein Name	Caldesmon
Gene Name	CALD1
Organism	Homo sapiens (Human).
Sequence Length	793
Subcellular Localization	Cytoplasm, cytoskeleton. Cytoplasm, myofibril. On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle)..
Protein Description	Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity)..
Protein Sequence	MDDFERRRELRRQKREEMRLEAERIAYQRNDDDEEEAARERRRRARQERLRQKQEEESLGQVTDQVEVNAQNSVPDEEAKTTTTNTQVEGDDEAAFLERLARREERRQKRLQEALERQKEFDPTITDASLSLPSRRMQNDTAENETTEKEEKSESRQERYEIEETETVTKSYQKNDWRDAEENKKEDKEKEEEEEEKPKRGSIGENQVEVMVEEKTTESQEETVVMSLKNGQISSEEPKQEEEREQGSDEISHHEKMEEEDKERAEAERARLEAEERERIKAEQDKKIADERARIEAEEKAAAQERERREAEERERMREEEKRAAEERQRIKEEEKRAAEERQRIKEEEKRAAEERQRIKEEEKRAAEERQRARAEEEEKAKVEEQKRNKQLEEKKHAMQETKIKGEKVEQKIEGKWVNEKKAQEDKLQTAVLKKQGEEKGTKVQAKREKLQEDKPTFKKEEIKDEKIKKDKEPKEEVKSFMDRKKGFTEVKSQNGEFMTHKLKHTENTFSRPGGRASVDTKEAEGAPQVEAGKRLEELRRRRGETESEEFEKLKQKQQEAALELEELKKKREERRKVLEEEEQRRKQEEADRKLREEEEKRRLKEEIERRRAEAAEKRQKMPEDGLSDDKKPFKCFTPKGSSLKIEERAEFLNKSVQKSSGVKSTHQAAIVSKIDSRLEQYTSAIEGTKSAKPTKPAASDLPVPAEGVRNIKSMWEKGNVFSSPTAAGTPNKETAGLKVGVSSRINEWLTKTPDGNKSPAPKPSDLRPGDVSSKRNLWEKQSVDKVTSPTKV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Sulfoxidation	-------MDDFERRR -------CCHHHHHH	11.42	28183972
5 (in isoform 3)	Phosphorylation	-	52.88	23663014
5 (in isoform 5)	Phosphorylation	-	52.88	23663014
7 (in isoform 3)	Phosphorylation	-	29.27	22617229
7 (in isoform 5)	Phosphorylation	-	29.27	22617229
12 (in isoform 3)	Phosphorylation	-	60.02	30266825
12 (in isoform 5)	Phosphorylation	-	60.02	30266825
17 (in isoform 3)	Phosphorylation	-	33.37	30266825
17 (in isoform 5)	Phosphorylation	-	33.37	30266825
21 (in isoform 3)	Phosphorylation	-	37.81	30266825
21 (in isoform 5)	Phosphorylation	-	37.81	30266825
27	Phosphorylation	LEAERIAYQRNDDDE HHHHHHHHHCCCCHH	12.97	22817900
53	Acetylation	RQERLRQKQEEESLG HHHHHHHHHHHHHHC	53.92	26051181
58	Phosphorylation	RQKQEEESLGQVTDQ HHHHHHHHHCCCCCC	40.87	26657352
63	Phosphorylation	EESLGQVTDQVEVNA HHHHCCCCCCCHHCC	16.90	26657352
73	Phosphorylation	VEVNAQNSVPDEEAK CHHCCCCCCCCHHHC	23.97	24972180
81	Phosphorylation	VPDEEAKTTTTNTQV CCCHHHCCCCCCCEE	36.10	27251275
82	Phosphorylation	PDEEAKTTTTNTQVE CCHHHCCCCCCCEEC	30.80	27251275
83	Phosphorylation	DEEAKTTTTNTQVEG CHHHCCCCCCCEECC	24.23	30242111
84	Phosphorylation	EEAKTTTTNTQVEGD HHHCCCCCCCEECCC	33.89	29970186
86	Phosphorylation	AKTTTTNTQVEGDDE HCCCCCCCEECCCHH	31.72	26657352
119	Ubiquitination	QEALERQKEFDPTIT HHHHHHHHHHCCCHH	67.57	-
124	Phosphorylation	RQKEFDPTITDASLS HHHHHCCCHHHHHHC	38.05	29255136
126	Phosphorylation	KEFDPTITDASLSLP HHHCCCHHHHHHCCC	28.17	23403867
129	Phosphorylation	DPTITDASLSLPSRR CCCHHHHHHCCCCHH	22.69	30266825
131	Phosphorylation	TITDASLSLPSRRMQ CHHHHHHCCCCHHHC	35.42	30266825
134	Phosphorylation	DASLSLPSRRMQNDT HHHHCCCCHHHCCCC	37.50	30266825
137	Sulfoxidation	LSLPSRRMQNDTAEN HCCCCHHHCCCCCCC	4.19	30846556
141	Phosphorylation	SRRMQNDTAENETTE CHHHCCCCCCCCCCH	43.34	21712546
146	Phosphorylation	NDTAENETTEKEEKS CCCCCCCCCHHHHHH	52.41	21601212
147	Phosphorylation	DTAENETTEKEEKSE CCCCCCCCHHHHHHH	38.59	21601212
149	Acetylation	AENETTEKEEKSESR CCCCCCHHHHHHHHH	69.91	26051181
152	Acetylation	ETTEKEEKSESRQER CCCHHHHHHHHHHHH	61.69	26051181
153	Phosphorylation	TTEKEEKSESRQERY CCHHHHHHHHHHHHH	44.05	30242111
155	Phosphorylation	EKEEKSESRQERYEI HHHHHHHHHHHHHHE	46.48	24719451
160	Phosphorylation	SESRQERYEIEETET HHHHHHHHHEEEHHH	22.10	24927040
165	Phosphorylation	ERYEIEETETVTKSY HHHHEEEHHHHCHHH	24.94	26356563
167	Phosphorylation	YEIEETETVTKSYQK HHEEEHHHHCHHHHC	40.68	21406692
169	Phosphorylation	IEETETVTKSYQKND EEEHHHHCHHHHCCC	22.99	26657352
170	Ubiquitination	EETETVTKSYQKNDW EEHHHHCHHHHCCCC	42.71	-
171	Phosphorylation	ETETVTKSYQKNDWR EHHHHCHHHHCCCCC	24.35	28857561
172	Phosphorylation	TETVTKSYQKNDWRD HHHHCHHHHCCCCCC	25.68	-
174	Acetylation	TVTKSYQKNDWRDAE HHCHHHHCCCCCCHH	48.95	23236377
174	Ubiquitination	TVTKSYQKNDWRDAE HHCHHHHCCCCCCHH	48.95	-
196 (in isoform 3)	Phosphorylation	-	77.32	25159151
196 (in isoform 5)	Phosphorylation	-	77.32	22167270
197	Sumoylation	KEEEEEEKPKRGSIG HHHHHHHCCCCCCCC	60.15	-
197	Sumoylation	KEEEEEEKPKRGSIG HHHHHHHCCCCCCCC	60.15	-
202	Phosphorylation	EEKPKRGSIGENQVE HHCCCCCCCCCCEEE	31.30	29255136
202 (in isoform 2)	Phosphorylation	-	31.30	25159151
202 (in isoform 4)	Phosphorylation	-	31.30	22167270
202 (in isoform 6)	Phosphorylation	-	31.30	25159151
216	Phosphorylation	EVMVEEKTTESQEET EEEEEECCCCCCHHE	38.79	23312004
217	Phosphorylation	VMVEEKTTESQEETV EEEEECCCCCCHHEE	44.71	26657352
219	Phosphorylation	VEEKTTESQEETVVM EEECCCCCCHHEEEE	40.58	26657352
223	Phosphorylation	TTESQEETVVMSLKN CCCCCHHEEEEEECC	20.04	23312004
227	Phosphorylation	QEETVVMSLKNGQIS CHHEEEEEECCCCCC	25.28	27499020
235	Phosphorylation	LKNGQISSEEPKQEE ECCCCCCCCCHHHHH	47.83	26657352
248	Phosphorylation	EEEREQGSDEISHHE HHHHHHCCHHCHHHH	31.59	26657352
252	Phosphorylation	EQGSDEISHHEKMEE HHCCHHCHHHHHHHH	19.42	28509920
402	Phosphorylation	KKHAMQETKIKGEKV HHHHHHHHHHCCHHH	22.60	20860994
427	Acetylation	EKKAQEDKLQTAVLK HHHHHHHHHHHHHHH	41.56	11791317
427 (in isoform 6)	Phosphorylation	-	41.56	20166139
431 (in isoform 6)	Phosphorylation	-	7.53	21712546
459	Sumoylation	QEDKPTFKKEEIKDE HCCCCCCCHHHHCCH	62.85	28112733
479	Malonylation	KEPKEEVKSFMDRKK CCCHHHHHHHHHHHC	41.05	26320211
479	Ubiquitination	KEPKEEVKSFMDRKK CCCHHHHHHHHHHHC	41.05	-
480	Phosphorylation	EPKEEVKSFMDRKKG CCHHHHHHHHHHHCC	30.86	28857561
493	Phosphorylation	KGFTEVKSQNGEFMT CCCEEEECCCCCEEE	33.77	28348404
500	Phosphorylation	SQNGEFMTHKLKHTE CCCCCEEEEECCCCC	22.60	19664995
502	Malonylation	NGEFMTHKLKHTENT CCCEEEEECCCCCCC	50.49	26320211
504	2-Hydroxyisobutyrylation	EFMTHKLKHTENTFS CEEEEECCCCCCCCC	53.97	-
504	Acetylation	EFMTHKLKHTENTFS CEEEEECCCCCCCCC	53.97	27452117
506	Phosphorylation	MTHKLKHTENTFSRP EEEECCCCCCCCCCC	29.37	23403867
509	Phosphorylation	KLKHTENTFSRPGGR ECCCCCCCCCCCCCC	19.43	23403867
511	Phosphorylation	KHTENTFSRPGGRAS CCCCCCCCCCCCCCC	35.21	27134283
518	O-linked_Glycosylation	SRPGGRASVDTKEAE CCCCCCCCCCCCCCC	21.11	30379171
518	Phosphorylation	SRPGGRASVDTKEAE CCCCCCCCCCCCCCC	21.11	25159151
521	Phosphorylation	GGRASVDTKEAEGAP CCCCCCCCCCCCCCC	28.73	23403867
522	Malonylation	GRASVDTKEAEGAPQ CCCCCCCCCCCCCCC	50.92	26320211
534	Acetylation	APQVEAGKRLEELRR CCCHHHHHHHHHHHH	61.94	7610153
546	Phosphorylation	LRRRRGETESEEFEK HHHHHCCCCHHHHHH	47.86	29255136
548	Phosphorylation	RRRGETESEEFEKLK HHHCCCCHHHHHHHH	50.25	25850435
553	Acetylation	TESEEFEKLKQKQQE CCHHHHHHHHHHHHH	67.32	26051181
553	Malonylation	TESEEFEKLKQKQQE CCHHHHHHHHHHHHH	67.32	26320211
569	Acetylation	ALELEELKKKREERR HHHHHHHHHHHHHHH	60.57	26051181
569	Ubiquitination	ALELEELKKKREERR HHHHHHHHHHHHHHH	60.57	-
605	Malonylation	EEEKRRLKEEIERRR HHHHHHHHHHHHHHH	52.03	26320211
622	Sulfoxidation	AAEKRQKMPEDGLSD HHHHHHHCCCCCCCC	3.12	28183972
628	Phosphorylation	KMPEDGLSDDKKPFK HCCCCCCCCCCCCCC	49.66	29255136
631	2-Hydroxyisobutyrylation	EDGLSDDKKPFKCFT CCCCCCCCCCCCCCC	68.30	-
631	Malonylation	EDGLSDDKKPFKCFT CCCCCCCCCCCCCCC	68.30	26320211
632	Acetylation	DGLSDDKKPFKCFTP CCCCCCCCCCCCCCC	63.78	26051181
632	Malonylation	DGLSDDKKPFKCFTP CCCCCCCCCCCCCCC	63.78	26320211
638	Phosphorylation	KKPFKCFTPKGSSLK CCCCCCCCCCCCCCC	33.29	29214152
640	Acetylation	PFKCFTPKGSSLKIE CCCCCCCCCCCCCHH	69.26	20167786
642	Phosphorylation	KCFTPKGSSLKIEER CCCCCCCCCCCHHHH	38.33	23403867
643	Phosphorylation	CFTPKGSSLKIEERA CCCCCCCCCCHHHHH	42.21	23911959
645	Sumoylation	TPKGSSLKIEERAEF CCCCCCCCHHHHHHH	50.44	-
645	Acetylation	TPKGSSLKIEERAEF CCCCCCCCHHHHHHH	50.44	20167786
645	Sumoylation	TPKGSSLKIEERAEF CCCCCCCCHHHHHHH	50.44	28112733
655	2-Hydroxyisobutyrylation	ERAEFLNKSVQKSSG HHHHHHHHHHHHHCC	54.90	-
655	Acetylation	ERAEFLNKSVQKSSG HHHHHHHHHHHHHCC	54.90	26051181
655	Malonylation	ERAEFLNKSVQKSSG HHHHHHHHHHHHHCC	54.90	26320211
655	Ubiquitination	ERAEFLNKSVQKSSG HHHHHHHHHHHHHCC	54.90	-
656	Phosphorylation	RAEFLNKSVQKSSGV HHHHHHHHHHHHCCC	28.80	23927012
660	Phosphorylation	LNKSVQKSSGVKSTH HHHHHHHHCCCCCHH	18.42	26462736
661	Phosphorylation	NKSVQKSSGVKSTHQ HHHHHHHCCCCCHHH	55.42	22617229
665	Phosphorylation	QKSSGVKSTHQAAIV HHHCCCCCHHHHHHH	28.81	24275569
666	Phosphorylation	KSSGVKSTHQAAIVS HHCCCCCHHHHHHHH	16.58	28857561
673	Phosphorylation	THQAAIVSKIDSRLE HHHHHHHHHHHHHHH	20.13	23911959
674	Ubiquitination	HQAAIVSKIDSRLEQ HHHHHHHHHHHHHHH	39.37	-
677	Phosphorylation	AIVSKIDSRLEQYTS HHHHHHHHHHHHHHH	42.09	28857561
682	Phosphorylation	IDSRLEQYTSAIEGT HHHHHHHHHHHHCCC	8.03	25159151
683	Phosphorylation	DSRLEQYTSAIEGTK HHHHHHHHHHHCCCC	16.04	26356563
684	Phosphorylation	SRLEQYTSAIEGTKS HHHHHHHHHHCCCCC	23.47	21712546
689	Phosphorylation	YTSAIEGTKSAKPTK HHHHHCCCCCCCCCC	14.72	26356563
690	Ubiquitination	TSAIEGTKSAKPTKP HHHHCCCCCCCCCCC	60.31	-
691	O-linked_Glycosylation	SAIEGTKSAKPTKPA HHHCCCCCCCCCCCC	41.17	OGP
691	Phosphorylation	SAIEGTKSAKPTKPA HHHCCCCCCCCCCCC	41.17	26055452
693	Acetylation	IEGTKSAKPTKPAAS HCCCCCCCCCCCCHH	61.38	26051181
693	Malonylation	IEGTKSAKPTKPAAS HCCCCCCCCCCCCHH	61.38	26320211
695	Phosphorylation	GTKSAKPTKPAASDL CCCCCCCCCCCHHCC	49.29	28857561
696	Malonylation	TKSAKPTKPAASDLP CCCCCCCCCCHHCCC	40.98	26320211
700	O-linked_Glycosylation	KPTKPAASDLPVPAE CCCCCCHHCCCCCHH	41.61	OGP
700	Phosphorylation	KPTKPAASDLPVPAE CCCCCCHHCCCCCHH	41.61	28857561
713	Ubiquitination	AEGVRNIKSMWEKGN HHHHCCHHHHHHHCC	37.49	-
714	Phosphorylation	EGVRNIKSMWEKGNV HHHCCHHHHHHHCCC	25.90	28857561
718	Acetylation	NIKSMWEKGNVFSSP CHHHHHHHCCCCCCC	40.03	26051181
718	Ubiquitination	NIKSMWEKGNVFSSP CHHHHHHHCCCCCCC	40.03	-
723	Phosphorylation	WEKGNVFSSPTAAGT HHHCCCCCCCCCCCC	31.00	25463755
724	Phosphorylation	EKGNVFSSPTAAGTP HHCCCCCCCCCCCCC	18.14	29255136
726	Phosphorylation	GNVFSSPTAAGTPNK CCCCCCCCCCCCCCC	30.96	19664994
730	Phosphorylation	SSPTAAGTPNKETAG CCCCCCCCCCCCCCC	20.97	29255136
733	Acetylation	TAAGTPNKETAGLKV CCCCCCCCCCCCCEE	58.61	26051181
733	Malonylation	TAAGTPNKETAGLKV CCCCCCCCCCCCCEE	58.61	26320211
733	Ubiquitination	TAAGTPNKETAGLKV CCCCCCCCCCCCCEE	58.61	-
735	Phosphorylation	AGTPNKETAGLKVGV CCCCCCCCCCCEEEC	27.86	25463755
743	Phosphorylation	AGLKVGVSSRINEWL CCCEEECHHHHHHHH	14.15	29514088
744	Phosphorylation	GLKVGVSSRINEWLT CCEEECHHHHHHHHH	34.47	29514088
751	Phosphorylation	SRINEWLTKTPDGNK HHHHHHHHCCCCCCC	33.67	22167270
752	Acetylation	RINEWLTKTPDGNKS HHHHHHHCCCCCCCC	56.76	18603641
752	Malonylation	RINEWLTKTPDGNKS HHHHHHHCCCCCCCC	56.76	26320211
753	Phosphorylation	INEWLTKTPDGNKSP HHHHHHCCCCCCCCC	22.75	22167270
758	Acetylation	TKTPDGNKSPAPKPS HCCCCCCCCCCCCCC	64.44	18603663
759	Phosphorylation	KTPDGNKSPAPKPSD CCCCCCCCCCCCCCC	30.23	22167270
763	Malonylation	GNKSPAPKPSDLRPG CCCCCCCCCCCCCCC	60.30	26320211
765	Phosphorylation	KSPAPKPSDLRPGDV CCCCCCCCCCCCCCC	56.24	20201521
773	Phosphorylation	DLRPGDVSSKRNLWE CCCCCCCCCCCCCCH	34.58	23927012
774	Phosphorylation	LRPGDVSSKRNLWEK CCCCCCCCCCCCCHH	35.17	23403867
775	2-Hydroxyisobutyrylation	RPGDVSSKRNLWEKQ CCCCCCCCCCCCHHC	37.49	-
775	Methylation	RPGDVSSKRNLWEKQ CCCCCCCCCCCCHHC	37.49	-
775	Ubiquitination	RPGDVSSKRNLWEKQ CCCCCCCCCCCCHHC	37.49	-
783	Phosphorylation	RNLWEKQSVDKVTSP CCCCHHCCCCCCCCC	43.27	23927012
786	Malonylation	WEKQSVDKVTSPTKV CHHCCCCCCCCCCCC	45.30	26320211
788	Phosphorylation	KQSVDKVTSPTKV-- HCCCCCCCCCCCC--	34.43	25463755
789	Phosphorylation	QSVDKVTSPTKV--- CCCCCCCCCCCC---	33.29	22167270
791	Phosphorylation	VDKVTSPTKV----- CCCCCCCCCC-----	44.18	30266825
792	2-Hydroxyisobutyrylation	DKVTSPTKV------ CCCCCCCCC------	49.70	-

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
534	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
534	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
714	S	Phosphorylation	Kinase	PAK2	Q13177	PSP
730	T	Phosphorylation	Kinase	CDK2	P24941	PSP
744	S	Phosphorylation	Kinase	PAK2	Q13177	PSP
759	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
789	S	Phosphorylation	Kinase	MAPK1	P63085	GPS
789	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CALD1_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 CALD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CSK21_HUMAN	CSNK2A1	physical	22863883

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 CALD1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724; THR-726 ANDTHR-730, AND MASS SPECTROMETRY.	19413330 [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-656; SER-724; THR-730;THR-735; THR-753; SER-759 AND SER-789, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-759 ANDSER-765, AND MASS SPECTROMETRY.	17287340 [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-656; SER-723; SER-724AND THR-730, AND MASS SPECTROMETRY.	17924679 [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 TYR-27; SER-202; SER-724;THR-730 AND SER-759, AND MASS SPECTROMETRY.	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-682, AND MASSSPECTROMETRY.	19534553 [Abstract]