dbPTM

EMD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EMD_HUMAN
UniProt AC	P50402
Protein Name	Emerin
Gene Name	EMD
Organism	Homo sapiens (Human).
Sequence Length	254
Subcellular Localization	Nucleus inner membrane Single-pass membrane protein Nucleoplasmic side . Nucleus outer membrane. Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates
Protein Description	Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C..
Protein Sequence	MDNYADLSDTELTTLLRRYNIPHGPVVGSTRRLYEKKIFEYETQRRRLSPPSSSAASSYSFSDLNSTRGDADMYDLPKKEDALLYQSKGYNDDYYEESYFTTRTYGEPESAGPSRAVRQSVTSFPDADAFHHQVHDDDLLSSSEEECKDRERPMYGRDSAYQSITHYRPVSASRSSLDLSYYPTSSSTSFMSSSSSSSSWLTRRAIRPENRAPGAGLGQDRQVPLWGQLLLFLVFVIVLFFIYHFMQAEEGNPF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDNYADLS -------CCCCCCCC	7.32	20068231
4	Phosphorylation	----MDNYADLSDTE ----CCCCCCCCHHH	9.38	26552605
8	Phosphorylation	MDNYADLSDTELTTL CCCCCCCCHHHHHHH	42.93	25159151
10	Phosphorylation	NYADLSDTELTTLLR CCCCCCHHHHHHHHH	29.53	22617229
13	Phosphorylation	DLSDTELTTLLRRYN CCCHHHHHHHHHHCC	14.79	22115753
14	Phosphorylation	LSDTELTTLLRRYNI CCHHHHHHHHHHCCC	36.10	30108239
19	Phosphorylation	LTTLLRRYNIPHGPV HHHHHHHCCCCCCCC	15.83	28796482
29	Phosphorylation	PHGPVVGSTRRLYEK CCCCCCCCCHHHHHH	13.71	25159151
30	Phosphorylation	HGPVVGSTRRLYEKK CCCCCCCCHHHHHHH	17.55	25159151
34	Phosphorylation	VGSTRRLYEKKIFEY CCCCHHHHHHHCHHH	24.72	22817900
37	2-Hydroxyisobutyrylation	TRRLYEKKIFEYETQ CHHHHHHHCHHHHHH	40.46	-
37	Malonylation	TRRLYEKKIFEYETQ CHHHHHHHCHHHHHH	40.46	26320211
37	Ubiquitination	TRRLYEKKIFEYETQ CHHHHHHHCHHHHHH	40.46	29967540
41	Phosphorylation	YEKKIFEYETQRRRL HHHHCHHHHHHHHCC	17.33	25884760
43	Phosphorylation	KKIFEYETQRRRLSP HHCHHHHHHHHCCCC	26.86	26552605
49	O-linked_Glycosylation	ETQRRRLSPPSSSAA HHHHHCCCCCCCCCH	32.71	30059200
49	Phosphorylation	ETQRRRLSPPSSSAA HHHHHCCCCCCCCCH	32.71	22167270
52	Phosphorylation	RRRLSPPSSSAASSY HHCCCCCCCCCHHCC	40.07	22167270
53	Phosphorylation	RRLSPPSSSAASSYS HCCCCCCCCCHHCCC	29.75	22167270
53	O-linked_Glycosylation	RRLSPPSSSAASSYS HCCCCCCCCCHHCCC	29.75	30059200
54	Phosphorylation	RLSPPSSSAASSYSF CCCCCCCCCHHCCCH	31.99	22167270
54	O-linked_Glycosylation	RLSPPSSSAASSYSF CCCCCCCCCHHCCCH	31.99	30059200
57	O-linked_Glycosylation	PPSSSAASSYSFSDL CCCCCCHHCCCHHHC	29.53	30059200
57	Phosphorylation	PPSSSAASSYSFSDL CCCCCCHHCCCHHHC	29.53	30278072
58	O-linked_Glycosylation	PSSSAASSYSFSDLN CCCCCHHCCCHHHCC	21.77	30059200
58	Phosphorylation	PSSSAASSYSFSDLN CCCCCHHCCCHHHCC	21.77	23927012
59	Phosphorylation	SSSAASSYSFSDLNS CCCCHHCCCHHHCCC	15.96	23927012
60	Phosphorylation	SSAASSYSFSDLNST CCCHHCCCHHHCCCC	21.88	25159151
62	O-linked_Glycosylation	AASSYSFSDLNSTRG CHHCCCHHHCCCCCC	34.94	30059200
62	Phosphorylation	AASSYSFSDLNSTRG CHHCCCHHHCCCCCC	34.94	23927012
66	Phosphorylation	YSFSDLNSTRGDADM CCHHHCCCCCCCCCH	27.12	23927012
66	O-linked_Glycosylation	YSFSDLNSTRGDADM CCHHHCCCCCCCCCH	27.12	30059200
67	Phosphorylation	SFSDLNSTRGDADMY CHHHCCCCCCCCCHH	37.28	23927012
73	Sulfoxidation	STRGDADMYDLPKKE CCCCCCCHHCCCHHH	2.76	21406390
74	Phosphorylation	TRGDADMYDLPKKED CCCCCCHHCCCHHHC	18.18	28674151
78	Ubiquitination	ADMYDLPKKEDALLY CCHHCCCHHHCEEHH	75.89	33845483
78	2-Hydroxyisobutyrylation	ADMYDLPKKEDALLY CCHHCCCHHHCEEHH	75.89	-
79	Ubiquitination	DMYDLPKKEDALLYQ CHHCCCHHHCEEHHH	59.91	21906983
79	Acetylation	DMYDLPKKEDALLYQ CHHCCCHHHCEEHHH	59.91	26051181
79	2-Hydroxyisobutyrylation	DMYDLPKKEDALLYQ CHHCCCHHHCEEHHH	59.91	-
85	Phosphorylation	KKEDALLYQSKGYND HHHCEEHHHCCCCCC	16.16	30266825
87	O-linked_Glycosylation	EDALLYQSKGYNDDY HCEEHHHCCCCCCCC	17.94	19691289
87	Phosphorylation	EDALLYQSKGYNDDY HCEEHHHCCCCCCCC	17.94	30266825
88	Ubiquitination	DALLYQSKGYNDDYY CEEHHHCCCCCCCCC	50.30	21906983
88	Ubiquitination	DALLYQSKGYNDDYY CEEHHHCCCCCCCCC	50.30	21890473
88	2-Hydroxyisobutyrylation	DALLYQSKGYNDDYY CEEHHHCCCCCCCCC	50.30	-
90	Phosphorylation	LLYQSKGYNDDYYEE EHHHCCCCCCCCCCC	21.10	24043423
94	Phosphorylation	SKGYNDDYYEESYFT CCCCCCCCCCCCCEE	18.68	20007894
95	Phosphorylation	KGYNDDYYEESYFTT CCCCCCCCCCCCEEE	21.88	20007894
98	Phosphorylation	NDDYYEESYFTTRTY CCCCCCCCCEEECCC	17.38	25849741
99	Phosphorylation	DDYYEESYFTTRTYG CCCCCCCCEEECCCC	14.28	24043423
101	Phosphorylation	YYEESYFTTRTYGEP CCCCCCEEECCCCCC	13.72	28796482
102	Phosphorylation	YEESYFTTRTYGEPE CCCCCEEECCCCCCC	15.89	28796482
103	Methylation	EESYFTTRTYGEPES CCCCEEECCCCCCCC	23.93	-
104	Phosphorylation	ESYFTTRTYGEPESA CCCEEECCCCCCCCC	33.51	28796482
105	Phosphorylation	SYFTTRTYGEPESAG CCEEECCCCCCCCCC	19.05	21082442
110	Phosphorylation	RTYGEPESAGPSRAV CCCCCCCCCCCCHHH	49.60	25159151
114	Phosphorylation	EPESAGPSRAVRQSV CCCCCCCCHHHHHHC	31.77	28796482
120	Phosphorylation	PSRAVRQSVTSFPDA CCHHHHHHCCCCCCC	19.46	23927012
122	Phosphorylation	RAVRQSVTSFPDADA HHHHHHCCCCCCCCH	29.87	23927012
123	Phosphorylation	AVRQSVTSFPDADAF HHHHHCCCCCCCCHH	32.40	23927012
141	Phosphorylation	VHDDDLLSSSEEECK CCCHHHHCCCHHHHH	38.83	26503892
142	Phosphorylation	HDDDLLSSSEEECKD CCHHHHCCCHHHHHH	41.56	26503892
143	Phosphorylation	DDDLLSSSEEECKDR CHHHHCCCHHHHHHC	45.73	26503892
148	Ubiquitination	SSSEEECKDRERPMY CCCHHHHHHCCCCCC	64.20	33845483
155	Phosphorylation	KDRERPMYGRDSAYQ HHCCCCCCCCCCHHH	16.22	22817900
159	Phosphorylation	RPMYGRDSAYQSITH CCCCCCCCHHHHCCC	27.75	23927012
161	Phosphorylation	MYGRDSAYQSITHYR CCCCCCHHHHCCCCC	13.52	27273156
163	Phosphorylation	GRDSAYQSITHYRPV CCCCHHHHCCCCCCC	19.44	25159151
165	Phosphorylation	DSAYQSITHYRPVSA CCHHHHCCCCCCCCC	20.36	23401153
167	Phosphorylation	AYQSITHYRPVSASR HHHHCCCCCCCCCCC	14.15	23459991
171	Phosphorylation	ITHYRPVSASRSSLD CCCCCCCCCCCCCCC	24.18	22167270
171	O-linked_Glycosylation	ITHYRPVSASRSSLD CCCCCCCCCCCCCCC	24.18	30059200
173	Phosphorylation	HYRPVSASRSSLDLS CCCCCCCCCCCCCCE	25.78	22167270
173	O-linked_Glycosylation	HYRPVSASRSSLDLS CCCCCCCCCCCCCCE	25.78	30059200
175	Phosphorylation	RPVSASRSSLDLSYY CCCCCCCCCCCCEEC	32.53	28348404
176	Phosphorylation	PVSASRSSLDLSYYP CCCCCCCCCCCEECC	25.45	25849741
180	Phosphorylation	SRSSLDLSYYPTSSS CCCCCCCEECCCCCC	23.45	28450419
181	Phosphorylation	RSSLDLSYYPTSSST CCCCCCEECCCCCCC	22.29	28450419
182	Phosphorylation	SSLDLSYYPTSSSTS CCCCCEECCCCCCCC	9.17	28450419
184	Phosphorylation	LDLSYYPTSSSTSFM CCCEECCCCCCCCCC	25.72	28450419
185	Phosphorylation	DLSYYPTSSSTSFMS CCEECCCCCCCCCCC	20.14	28450419
186	Phosphorylation	LSYYPTSSSTSFMSS CEECCCCCCCCCCCC	39.86	28450419
187	Phosphorylation	SYYPTSSSTSFMSSS EECCCCCCCCCCCCC	28.04	28450419
188	Phosphorylation	YYPTSSSTSFMSSSS ECCCCCCCCCCCCCC	28.12	26074081
189	Phosphorylation	YPTSSSTSFMSSSSS CCCCCCCCCCCCCCC	22.39	26074081
192	Phosphorylation	SSSTSFMSSSSSSSS CCCCCCCCCCCCCCC	25.67	27251275
193	Phosphorylation	SSTSFMSSSSSSSSW CCCCCCCCCCCCCCH	23.58	27080861
194	Phosphorylation	STSFMSSSSSSSSWL CCCCCCCCCCCCCHH	27.25	27080861
195	Phosphorylation	TSFMSSSSSSSSWLT CCCCCCCCCCCCHHH	35.87	27080861
196	Phosphorylation	SFMSSSSSSSSWLTR CCCCCCCCCCCHHHH	35.87	27080861

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
49	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
49	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
49	S	Phosphorylation	Kinase	PKA	-	Uniprot
59	Y	Phosphorylation	Kinase	SRC	P12931	PSP
74	Y	Phosphorylation	Kinase	SRC	P12931	PSP
95	Y	Phosphorylation	Kinase	SRC	P12931	PSP
167	Y	Phosphorylation	Kinase	ABL1	P00519	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FATE1_HUMAN	FATE1	physical	16189514
CREB3_HUMAN	CREB3	physical	16189514
BEND7_HUMAN	BEND7	physical	16189514
LMNA_HUMAN	LMNA	physical	12755701
YTDC1_HUMAN	YTHDC1	physical	12755701
LIPL_HUMAN	LPL	physical	12755701
VAV_HUMAN	VAV1	physical	12755701
PSME1_HUMAN	PSME1	physical	12755701
ACTH_HUMAN	ACTG2	physical	12670476
LMNA_HUMAN	LMNA	physical	12670476
LMNB1_HUMAN	LMNB1	physical	12670476
CSN6_HUMAN	COPS6	physical	16169070
DPPA4_HUMAN	DPPA4	physical	16169070
SH3G2_HUMAN	SH3GL2	physical	16169070
SH3G3_HUMAN	SH3GL3	physical	16169070
GMCL1_HUMAN	GMCL1	physical	12493765
LMNA_HUMAN	LMNA	physical	11173535
SIKE1_HUMAN	SIKE1	physical	17620012
LMO7_HUMAN	LMO7	physical	17620012
MYH9_HUMAN	MYH9	physical	17620012
SPTN1_HUMAN	SPTAN1	physical	17620012
MYO1E_HUMAN	MYO1E	physical	17620012
CNN3_HUMAN	CNN3	physical	17620012
ACTB_HUMAN	ACTB	physical	17620012
MYO1C_HUMAN	MYO1C	physical	17620012
BAF_HUMAN	BANF1	physical	17620012
LMNB1_HUMAN	LMNB1	physical	17620012
LMNA_HUMAN	LMNA	physical	17620012
HDAC3_HUMAN	HDAC3	physical	17620012
HDAC1_HUMAN	HDAC1	physical	17620012
RBL1_HUMAN	RBL1	physical	17620012
SP130_HUMAN	SAP130	physical	17620012
HNRPK_HUMAN	HNRNPK	physical	17620012
LSM8_HUMAN	LSM8	physical	17620012
LSM2_HUMAN	LSM2	physical	17620012
LA_HUMAN	SSB	physical	17620012
DX39B_HUMAN	DDX39B	physical	17620012
ZRAB2_HUMAN	ZRANB2	physical	17620012
HNRPU_HUMAN	HNRNPU	physical	17620012
C1QBP_HUMAN	C1QBP	physical	17620012
1433B_HUMAN	YWHAB	physical	17620012
BCCIP_HUMAN	BCCIP	physical	17620012
G3BP1_HUMAN	G3BP1	physical	17620012
CDC37_HUMAN	CDC37	physical	17620012
PDCD4_HUMAN	PDCD4	physical	17620012
HDGF_HUMAN	HDGF	physical	17620012
THA_HUMAN	THRA	physical	17620012
MCM2_HUMAN	MCM2	physical	17620012
MCM4_HUMAN	MCM4	physical	17620012
MCM6_HUMAN	MCM6	physical	17620012
TBL1X_HUMAN	TBL1X	physical	17620012
TBL1R_HUMAN	TBL1XR1	physical	17620012
TIF1B_HUMAN	TRIM28	physical	17620012
SMRC1_HUMAN	SMARCC1	physical	17620012
SMRC2_HUMAN	SMARCC2	physical	17620012
SNF5_HUMAN	SMARCB1	physical	17620012
MED4_HUMAN	MED4	physical	17620012
RCOR1_HUMAN	RCOR1	physical	17620012
DPY30_HUMAN	DPY30	physical	17620012
CHD4_HUMAN	CHD4	physical	17620012
SAP18_HUMAN	SAP18	physical	17620012
1433T_HUMAN	YWHAQ	physical	17620012
1433E_HUMAN	YWHAE	physical	17620012
LMO7_HUMAN	LMO7	physical	17067998
PCGF2_HUMAN	PCGF2	physical	19727227
EGF_HUMAN	EGF	physical	19727227
SMU1_HUMAN	SMU1	physical	22939629
FAS_HUMAN	FASN	physical	22939629
BAF_HUMAN	BANF1	physical	11792821
CTNB1_HUMAN	CTNNB1	physical	16858403
BCLF1_HUMAN	BCLAF1	physical	15009215
TBB5_HUMAN	TUBB	physical	23443559
HBD_HUMAN	HBD	physical	23443559
FANCI_HUMAN	FANCI	physical	23443559
GGYF2_HUMAN	GIGYF2	physical	23443559
ECHA_HUMAN	HADHA	physical	23443559
HNRPU_HUMAN	HNRNPU	physical	23443559
IRS4_HUMAN	IRS4	physical	23443559
PLPL6_HUMAN	PNPLA6	physical	23443559
PRKDC_HUMAN	PRKDC	physical	23443559
SC16A_HUMAN	SEC16A	physical	23443559
U520_HUMAN	SNRNP200	physical	23443559
SPT6H_HUMAN	SUPT6H	physical	23443559
TBA1C_HUMAN	TUBA1C	physical	23443559
TBB2A_HUMAN	TUBB2A	physical	23443559
TBB4B_HUMAN	TUBB4B	physical	23443559
TBB3_HUMAN	TUBB3	physical	23443559
WDR6_HUMAN	WDR6	physical	23443559
XRCC6_HUMAN	XRCC6	physical	23443559
EMD_HUMAN	EMD	physical	25416956
ZN165_HUMAN	ZNF165	physical	25416956
ZN232_HUMAN	ZNF232	physical	25416956
ABT1_HUMAN	ABT1	physical	25416956
LUZP4_HUMAN	LUZP4	physical	25416956
PAK5_HUMAN	PAK7	physical	25416956
AEN_HUMAN	AEN	physical	25416956
CCD33_HUMAN	CCDC33	physical	25416956
EFHC2_HUMAN	EFHC2	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
T3JAM_HUMAN	TRAF3IP3	physical	25416956
FATE1_HUMAN	FATE1	physical	25416956
CTSR1_HUMAN	CATSPER1	physical	25416956
MB213_HUMAN	MAB21L3	physical	25416956
BEND7_HUMAN	BEND7	physical	25416956
TRI42_HUMAN	TRIM42	physical	25416956
SPTA1_HUMAN	SPTA1	physical	16889989
BAF_HUMAN	BANF1	physical	19789182

Drug and Disease Associations

Kegg Disease
H00563	Emery-Dreifuss muscular dystrophy
OMIM Disease
310300	Emery-Dreifuss muscular dystrophy 1, X-linked (EDMD1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EMD_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]
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-49 AND SER-60, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-8; SER-49 AND SER-171,AND MASS SPECTROMETRY.	19369195 [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-49; SER-52; SER-54;SER-60; SER-66 AND SER-87, 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-8; SER-29 AND SER-49,AND MASS SPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-54; TYR-59 ANDSER-60, AND MASS SPECTROMETRY.	18220336 [Abstract]
"The Emery-Dreifuss muscular dystrophy associated-protein emerin isphosphorylated on serine 49 by protein kinase A."; Roberts R.C., Sutherland-Smith A.J., Wheeler M.A., Jensen O.N.,Emerson L.J., Spiliotis I.I., Tate C.G., Kendrick-Jones J.,Ellis J.A.; FEBS J. 273:4562-4575(2006). Cited for: PHOSPHORYLATION AT SER-49, SUBCELLULAR LOCATION, INTERACTION WITHLMNA, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-49.	16972941 [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-49; TYR-74; SER-120 ANDTYR-167, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND TYR-167, ANDMASS SPECTROMETRY.	15144186 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND MASSSPECTROMETRY.	16094384 [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-85; TYR-95 AND TYR-99,AND MASS SPECTROMETRY.	15592455 [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-59; TYR-74; TYR-85;TYR-161 AND TYR-167, AND MASS SPECTROMETRY.	16212419 [Abstract]