dbPTM

TRA2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRA2A_HUMAN
UniProt AC	Q13595
Protein Name	Transformer-2 protein homolog alpha
Gene Name	TRA2A
Organism	Homo sapiens (Human).
Sequence Length	282
Subcellular Localization	Nucleus .
Protein Description	Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing..
Protein Sequence	MSDVEENNFEGRESRSQSKSPTGTPARVKSESRSGSRSPSRVSKHSESHSRSRSKSRSRSRRHSHRRYTRSRSHSHSHRRRSRSRSYTPEYRRRRSRSHSPMSNRRRHTGSRANPDPNTCLGVFGLSLYTTERDLREVFSRYGPLSGVNVVYDQRTGRSRGFAFVYFERIDDSKEAMERANGMELDGRRIRVDYSITKRAHTPTPGIYMGRPTHSGGGGGGGGGGGGGGGGRRRDSYYDRGYDRGYDRYEDYDYRYRRRSPSPYYSRYRSRSRSRSYSPRRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSDVEENNF ------CCHHHHCCC	50.82	20068231
2	Phosphorylation	------MSDVEENNF ------CCHHHHCCC	50.82	29255136
14	Phosphorylation	NNFEGRESRSQSKSP CCCCCCCCCCCCCCC	35.55	29255136
16	Phosphorylation	FEGRESRSQSKSPTG CCCCCCCCCCCCCCC	48.35	25159151
18	Phosphorylation	GRESRSQSKSPTGTP CCCCCCCCCCCCCCC	36.03	25159151
20	Phosphorylation	ESRSQSKSPTGTPAR CCCCCCCCCCCCCCC	32.70	28355574
22	Phosphorylation	RSQSKSPTGTPARVK CCCCCCCCCCCCCHH	61.86	29255136
24	Phosphorylation	QSKSPTGTPARVKSE CCCCCCCCCCCHHCC	19.09	28355574
30	Phosphorylation	GTPARVKSESRSGSR CCCCCHHCCCCCCCC	37.64	25159151
32	Phosphorylation	PARVKSESRSGSRSP CCCHHCCCCCCCCCC	38.55	19651622
34	Phosphorylation	RVKSESRSGSRSPSR CHHCCCCCCCCCCCH	50.85	19651622
36	Phosphorylation	KSESRSGSRSPSRVS HCCCCCCCCCCCHHH	30.72	28102081
38	Phosphorylation	ESRSGSRSPSRVSKH CCCCCCCCCCHHHHC	28.99	19651622
40	Phosphorylation	RSGSRSPSRVSKHSE CCCCCCCCHHHHCCC	46.70	19651622
43	Phosphorylation	SRSPSRVSKHSESHS CCCCCHHHHCCCCCC	24.44	28985074
46	Phosphorylation	PSRVSKHSESHSRSR CCHHHHCCCCCCCCC	44.52	26091039
48	Phosphorylation	RVSKHSESHSRSRSK HHHHCCCCCCCCCCC	29.76	26091039
50	Phosphorylation	SKHSESHSRSRSKSR HHCCCCCCCCCCCCH	41.03	17081983
64	Phosphorylation	RSRSRRHSHRRYTRS HHHHHHHHHHHHHHC	19.51	22817900
68	Phosphorylation	RRHSHRRYTRSRSHS HHHHHHHHHHCCCCC	13.37	24719451
69	Phosphorylation	RHSHRRYTRSRSHSH HHHHHHHHHCCCCCC	21.98	29449344
71	Phosphorylation	SHRRYTRSRSHSHSH HHHHHHHCCCCCCCC	30.27	20363803
73	Ubiquitination	RRYTRSRSHSHSHRR HHHHHCCCCCCCCCC	30.50	-
73	Phosphorylation	RRYTRSRSHSHSHRR HHHHHCCCCCCCCCC	30.50	20363803
73 (in isoform 2)	Ubiquitination	-	30.50	21890473
75	Phosphorylation	YTRSRSHSHSHRRRS HHHCCCCCCCCCCHH	28.12	30242111
77	Phosphorylation	RSRSHSHSHRRRSRS HCCCCCCCCCCHHHC	23.00	19651622
82	Phosphorylation	SHSHRRRSRSRSYTP CCCCCCHHHCCCCCH	32.56	20164059
84	Phosphorylation	SHRRRSRSRSYTPEY CCCCHHHCCCCCHHH	27.16	22167270
86	Phosphorylation	RRRSRSRSYTPEYRR CCHHHCCCCCHHHHH	34.31	22167270
87	Phosphorylation	RRSRSRSYTPEYRRR CHHHCCCCCHHHHHH	25.79	22167270
88	Phosphorylation	RSRSRSYTPEYRRRR HHHCCCCCHHHHHHH	15.76	19664994
91	Phosphorylation	SRSYTPEYRRRRSRS CCCCCHHHHHHHHCC	15.60	22167270
96	Phosphorylation	PEYRRRRSRSHSPMS HHHHHHHHCCCCCCC	36.00	22167270
97 (in isoform 2)	Ubiquitination	-	36.26	21890473
97	Ubiquitination	EYRRRRSRSHSPMSN HHHHHHHCCCCCCCC	36.26	-
98	Phosphorylation	YRRRRSRSHSPMSNR HHHHHHCCCCCCCCC	29.57	22167270
100	Phosphorylation	RRRSRSHSPMSNRRR HHHHCCCCCCCCCCC	24.44	22167270
103	Phosphorylation	SRSHSPMSNRRRHTG HCCCCCCCCCCCCCC	30.48	22167270
109	Phosphorylation	MSNRRRHTGSRANPD CCCCCCCCCCCCCCC	34.73	20068231
111	Phosphorylation	NRRRHTGSRANPDPN CCCCCCCCCCCCCCC	29.40	24719451
119	Phosphorylation	RANPDPNTCLGVFGL CCCCCCCCEEHHHCE	17.94	20068231
130	Phosphorylation	VFGLSLYTTERDLRE HHCEEEEECHHHHHH	27.72	20068231
131	Phosphorylation	FGLSLYTTERDLREV HCEEEEECHHHHHHH	18.57	20068231
140	Phosphorylation	RDLREVFSRYGPLSG HHHHHHHHHHCCCCC	29.75	24719451
142	Phosphorylation	LREVFSRYGPLSGVN HHHHHHHHCCCCCEE	23.15	24719451
146	Phosphorylation	FSRYGPLSGVNVVYD HHHHCCCCCEEEEEE	43.77	24719451
152	Phosphorylation	LSGVNVVYDQRTGRS CCCEEEEEECCCCCC	11.32	28152594
155 (in isoform 4)	Phosphorylation	-	35.93	28634120
158 (in isoform 4)	Phosphorylation	-	23.67	25849741
160	Methylation	DQRTGRSRGFAFVYF ECCCCCCCCEEEEEE	42.77	54560267
160 (in isoform 4)	Phosphorylation	-	42.77	25849741
162 (in isoform 4)	Phosphorylation	-	4.66	28842319
164 (in isoform 4)	Phosphorylation	-	4.23	22617229
166	Phosphorylation	SRGFAFVYFERIDDS CCCEEEEEEEECCCH	8.02	-
170 (in isoform 4)	Phosphorylation	-	5.63	25849741
173	Phosphorylation	YFERIDDSKEAMERA EEEECCCHHHHHHHH	28.75	23403867
174	Acetylation	FERIDDSKEAMERAN EEECCCHHHHHHHHC	57.39	26051181
174 (in isoform 1)	Ubiquitination	-	57.39	21890473
174	Ubiquitination	FERIDDSKEAMERAN EEECCCHHHHHHHHC	57.39	21906983
188	Methylation	NGMELDGRRIRVDYS CCCEECCEEEEEEEE	30.44	-
194	Phosphorylation	GRRIRVDYSITKRAH CEEEEEEEEEECCCC	10.10	20068231
195	Phosphorylation	RRIRVDYSITKRAHT EEEEEEEEEECCCCC	21.22	21815630
197	Phosphorylation	IRVDYSITKRAHTPT EEEEEEEECCCCCCC	14.45	20068231
198	Ubiquitination	RVDYSITKRAHTPTP EEEEEEECCCCCCCC	46.01	21890473
198	Ubiquitination	RVDYSITKRAHTPTP EEEEEEECCCCCCCC	46.01	21890473
198	Sumoylation	RVDYSITKRAHTPTP EEEEEEECCCCCCCC	46.01	28112733
198 (in isoform 1)	Ubiquitination	-	46.01	21890473
198	Acetylation	RVDYSITKRAHTPTP EEEEEEECCCCCCCC	46.01	25953088
198	Ubiquitination	RVDYSITKRAHTPTP EEEEEEECCCCCCCC	46.01	21890473
202	Phosphorylation	SITKRAHTPTPGIYM EEECCCCCCCCCEEC	28.07	29255136
204	Phosphorylation	TKRAHTPTPGIYMGR ECCCCCCCCCEECCC	34.99	22167270
208	Phosphorylation	HTPTPGIYMGRPTHS CCCCCCEECCCCCCC	10.22	21945579
213	Phosphorylation	GIYMGRPTHSGGGGG CEECCCCCCCCCCCC	27.58	23927012
215	Phosphorylation	YMGRPTHSGGGGGGG ECCCCCCCCCCCCCC	41.43	25159151
232	Methylation	GGGGGGGRRRDSYYD CCCCCCCCCCCCCCC	33.46	-
236	Phosphorylation	GGGRRRDSYYDRGYD CCCCCCCCCCCCCCC	24.63	23401153
237	Phosphorylation	GGRRRDSYYDRGYDR CCCCCCCCCCCCCCC	17.42	20044836
238	Phosphorylation	GRRRDSYYDRGYDRG CCCCCCCCCCCCCCC	11.78	24702127
240	Methylation	RRDSYYDRGYDRGYD CCCCCCCCCCCCCCC	29.47	115918877
246	Phosphorylation	DRGYDRGYDRYEDYD CCCCCCCCCCCCCCC	9.72	28796482
249	Phosphorylation	YDRGYDRYEDYDYRY CCCCCCCCCCCCHHH	15.39	28796482
252	Phosphorylation	GYDRYEDYDYRYRRR CCCCCCCCCHHHHCC	11.70	28796482
254	Phosphorylation	DRYEDYDYRYRRRSP CCCCCCCHHHHCCCC	11.87	28796482
255	Asymmetric dimethylarginine	RYEDYDYRYRRRSPS CCCCCCHHHHCCCCC	18.65	-
255	Methylation	RYEDYDYRYRRRSPS CCCCCCHHHHCCCCC	18.65	-
256	Phosphorylation	YEDYDYRYRRRSPSP CCCCCHHHHCCCCCC	11.40	-
260	Phosphorylation	DYRYRRRSPSPYYSR CHHHHCCCCCCCHHH	28.11	26846344
262	Phosphorylation	RYRRRSPSPYYSRYR HHHCCCCCCCHHHHH	27.12	19664994
264	Phosphorylation	RRRSPSPYYSRYRSR HCCCCCCCHHHHHCC	20.57	20201521
265	Phosphorylation	RRSPSPYYSRYRSRS CCCCCCCHHHHHCCC	7.05	23927012
266	Phosphorylation	RSPSPYYSRYRSRSR CCCCCCHHHHHCCCC	19.59	26846344
268	Phosphorylation	PSPYYSRYRSRSRSR CCCCHHHHHCCCCCC	13.65	25884760
270	Phosphorylation	PYYSRYRSRSRSRSY CCHHHHHCCCCCCCC	26.18	29116813
272	Phosphorylation	YSRYRSRSRSRSYSP HHHHHCCCCCCCCCC	35.54	26846344
274	Phosphorylation	RYRSRSRSRSYSPRR HHHCCCCCCCCCCCC	27.16	26846344
276	Phosphorylation	RSRSRSRSYSPRRY- HCCCCCCCCCCCCC-	31.07	26846344
277	Phosphorylation	SRSRSRSYSPRRY-- CCCCCCCCCCCCC--	22.91	26846344
278	Phosphorylation	RSRSRSYSPRRY--- CCCCCCCCCCCC---	17.12	28355574
282	Phosphorylation	RSYSPRRY------- CCCCCCCC-------	24.96	21406692

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
Oops, there are no upstream regulatory protein records of TRA2A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRA2A_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 TRA2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DHX15_HUMAN	DHX15	physical	22365833
SR140_HUMAN	U2SURP	physical	22365833
YTDC1_HUMAN	YTHDC1	physical	21988832
LARP7_HUMAN	LARP7	physical	26186194
SRRM1_HUMAN	SRRM1	physical	26186194
RT09_HUMAN	MRPS9	physical	26186194
RT26_HUMAN	MRPS26	physical	26186194
TR150_HUMAN	THRAP3	physical	26186194
LC7L2_HUMAN	LUC7L2	physical	26186194
LUC7L_HUMAN	LUC7L	physical	26186194
ZN768_HUMAN	ZNF768	physical	26186194
PTCD1_HUMAN	PTCD1	physical	26186194
PTCD3_HUMAN	PTCD3	physical	26186194
SRRM2_HUMAN	SRRM2	physical	26186194
NCBP3_HUMAN	C17orf85	physical	26186194
ZFR_HUMAN	ZFR	physical	26186194
PABP4_HUMAN	PABPC4	physical	26186194
RBBP6_HUMAN	RBBP6	physical	26186194
ELAV2_HUMAN	ELAVL2	physical	26186194
RL6_HUMAN	RPL6	physical	26186194
RT23_HUMAN	MRPS23	physical	26186194
RT27_HUMAN	MRPS27	physical	26186194
TRUB2_HUMAN	TRUB2	physical	26186194
RT06_HUMAN	MRPS6	physical	26186194
RL26L_HUMAN	RPL26L1	physical	26186194
MTEF3_HUMAN	MTERF3	physical	26186194
PAIP1_HUMAN	PAIP1	physical	26186194
RT18B_HUMAN	MRPS18B	physical	26186194
RM32_HUMAN	MRPL32	physical	26186194
PEO1_HUMAN	C10orf2	physical	26186194
RT10_HUMAN	MRPS10	physical	26186194
RT29_HUMAN	DAP3	physical	26186194
MEPCE_HUMAN	MEPCE	physical	26186194
RENT1_HUMAN	UPF1	physical	26186194
PPIG_HUMAN	PPIG	physical	26186194
LARP1_HUMAN	LARP1	physical	26186194
LAR1B_HUMAN	LARP1B	physical	26186194
PHAX_HUMAN	PHAX	physical	26186194
RT31_HUMAN	MRPS31	physical	26186194
MKRN1_HUMAN	MKRN1	physical	26186194
RT18C_HUMAN	MRPS18C	physical	26186194
RT05_HUMAN	MRPS5	physical	26186194
RT07_HUMAN	MRPS7	physical	26186194
RT22_HUMAN	MRPS22	physical	26186194
RT15_HUMAN	MRPS15	physical	26186194
RT35_HUMAN	MRPS35	physical	26186194
RT25_HUMAN	MRPS25	physical	26186194
U3IP2_HUMAN	RRP9	physical	26186194
NGRN_HUMAN	NGRN	physical	26186194
RT02_HUMAN	MRPS2	physical	26186194
MOV10_HUMAN	MOV10	physical	26186194
RT33_HUMAN	MRPS33	physical	26186194
SRRT_HUMAN	SRRT	physical	26186194
PRPF3_HUMAN	PRPF3	physical	26186194
RT11_HUMAN	MRPS11	physical	26186194
PININ_HUMAN	PNN	physical	26186194
SRP14_HUMAN	SRP14	physical	26186194
GAR1_HUMAN	GAR1	physical	26186194
RT24_HUMAN	MRPS24	physical	26186194
CLK3_HUMAN	CLK3	physical	26186194
CASC3_HUMAN	CASC3	physical	26186194
WDR33_HUMAN	WDR33	physical	26186194
KC1E_HUMAN	CSNK1E	physical	26186194
KC1D_HUMAN	CSNK1D	physical	26186194
YTDC1_HUMAN	YTHDC1	physical	26186194
RT14_HUMAN	MRPS14	physical	26186194
G3PT_HUMAN	GAPDHS	physical	26186194
ZCHC3_HUMAN	ZCCHC3	physical	26186194
MKRN2_HUMAN	MKRN2	physical	26186194
ZC11A_HUMAN	ZC3H11A	physical	26186194
NOA1_HUMAN	NOA1	physical	26186194
TRA2B_HUMAN	TRA2B	physical	26186194
ISY1_HUMAN	ISY1	physical	26186194
SRSF8_HUMAN	SRSF8	physical	26186194
CLK1_HUMAN	CLK1	physical	26186194
SRSF7_HUMAN	SRSF7	physical	26186194
ABC3F_HUMAN	APOBEC3F	physical	26186194
SRS12_HUMAN	SRSF12	physical	26186194
SRS10_HUMAN	SRSF10	physical	26186194
CLK2_HUMAN	CLK2	physical	26186194
RM34_HUMAN	MRPL34	physical	26186194
RT21_HUMAN	MRPS21	physical	26186194
CLK2_HUMAN	CLK2	physical	28514442
CLK3_HUMAN	CLK3	physical	28514442
CLK1_HUMAN	CLK1	physical	28514442
SRS12_HUMAN	SRSF12	physical	28514442
RU17_HUMAN	SNRNP70	physical	28514442
RBBP6_HUMAN	RBBP6	physical	28514442
PPIG_HUMAN	PPIG	physical	28514442
PEO1_HUMAN	C10orf2	physical	28514442
SRSF8_HUMAN	SRSF8	physical	28514442
MEPCE_HUMAN	MEPCE	physical	28514442
ELAV2_HUMAN	ELAVL2	physical	28514442
MKRN1_HUMAN	MKRN1	physical	28514442
U3IP2_HUMAN	RRP9	physical	28514442
RT35_HUMAN	MRPS35	physical	28514442
TRA2B_HUMAN	TRA2B	physical	28514442
LAR1B_HUMAN	LARP1B	physical	28514442
ZCH18_HUMAN	ZC3H18	physical	28514442
PININ_HUMAN	PNN	physical	28514442
RT05_HUMAN	MRPS5	physical	28514442
WDR33_HUMAN	WDR33	physical	28514442
CASC3_HUMAN	CASC3	physical	28514442
RT09_HUMAN	MRPS9	physical	28514442
LC7L2_HUMAN	LUC7L2	physical	28514442
PTCD3_HUMAN	PTCD3	physical	28514442
RT07_HUMAN	MRPS7	physical	28514442
ABC3F_HUMAN	APOBEC3F	physical	28514442
RT23_HUMAN	MRPS23	physical	28514442
LARP1_HUMAN	LARP1	physical	28514442
G3PT_HUMAN	GAPDHS	physical	28514442
RENT1_HUMAN	UPF1	physical	28514442
RT31_HUMAN	MRPS31	physical	28514442
RT02_HUMAN	MRPS2	physical	28514442
NCBP3_HUMAN	C17orf85	physical	28514442
MOV10_HUMAN	MOV10	physical	28514442
TRUB2_HUMAN	TRUB2	physical	28514442
KC1E_HUMAN	CSNK1E	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
ISY1_HUMAN	ISY1	physical	28514442
RT11_HUMAN	MRPS11	physical	28514442
SRRM1_HUMAN	SRRM1	physical	28514442
NGRN_HUMAN	NGRN	physical	28514442
RT33_HUMAN	MRPS33	physical	28514442
RT29_HUMAN	DAP3	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
MTEF3_HUMAN	MTERF3	physical	28514442
RT25_HUMAN	MRPS25	physical	28514442
PHAX_HUMAN	PHAX	physical	28514442
SRS10_HUMAN	SRSF10	physical	28514442
RT15_HUMAN	MRPS15	physical	28514442
PAIP1_HUMAN	PAIP1	physical	28514442
RT26_HUMAN	MRPS26	physical	28514442
RT22_HUMAN	MRPS22	physical	28514442
LARP7_HUMAN	LARP7	physical	28514442
PABP4_HUMAN	PABPC4	physical	28514442
RT18C_HUMAN	MRPS18C	physical	28514442
GAR1_HUMAN	GAR1	physical	28514442
NCOA5_HUMAN	NCOA5	physical	28514442
YTDC1_HUMAN	YTHDC1	physical	28514442
TR150_HUMAN	THRAP3	physical	28514442
PABP1_HUMAN	PABPC1	physical	28514442
SYF2_HUMAN	SYF2	physical	28514442
LUC7L_HUMAN	LUC7L	physical	28514442
RT10_HUMAN	MRPS10	physical	28514442
ZFR_HUMAN	ZFR	physical	28514442
RT14_HUMAN	MRPS14	physical	28514442
RM34_HUMAN	MRPL34	physical	28514442
RT06_HUMAN	MRPS6	physical	28514442
PTCD1_HUMAN	PTCD1	physical	28514442

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 TRA2A_HUMAN

Related Literatures of Post-Translational Modification

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-260 AND SER-262, ANDMASS SPECTROMETRY.	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-2, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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-2; SER-14; THR-202;THR-204; SER-260 AND SER-262, 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-84; SER-86; THR-88;THR-202; THR-204; SER-215; SER-260 AND SER-262, 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-260 AND SER-262, ANDMASS 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-260 AND SER-262, ANDMASS SPECTROMETRY.	17924679 [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-260 AND SER-262, ANDMASS SPECTROMETRY.	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-2; SER-14; SER-16;SER-18; SER-84; SER-86; THR-88; SER-96; SER-98; SER-100 AND THR-204,AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASSSPECTROMETRY.	16097034 [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-264 AND TYR-265, ANDMASS SPECTROMETRY.	18083107 [Abstract]