dbPTM

DCP1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DCP1A_HUMAN
UniProt AC	Q9NPI6
Protein Name	mRNA-decapping enzyme 1A
Gene Name	DCP1A
Organism	Homo sapiens (Human).
Sequence Length	582
Subcellular Localization	Cytoplasm, P-body . Nucleus . Co-localizes with NANOS3 in the processing bodies (By similarity). Predominantly cytoplasmic, in processing bodies (PB) (PubMed:16364915). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interacti
Protein Description	Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1..
Protein Sequence	MEALSRAGQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVVEEETRRSQQAARDKQSPSQANGCSDHRPIDILEMLSRAKDEYERNQMGDSNISSPGLQPSTQLSNLGSTETLEEMPSGSQDKSAPSGHKHLTVEELFGTSLPKEQPAVVGLDSEEMERLPGDASQKEPNSFLPFPFEQLGGAPQSETLGVPSAAHHSVQPEITTPVLITPASITQSNEKHAPTYTIPLSPVLSPTLPAEAPTAQVPPSLPRNSTMMQAVKTTPRQRSPLLNQPVPELSHASLIANQSPFRAPLNVTNTAGTSLPSVDLLQKLRLTPQHDQIQTQPLGKGAMVASFSPAAGQLATPESFIEPPSKTAAARVAASASLSNMVLAPLQSMQQNQDPEVFVQPKVLSSAIQVAGAPLVTATTTAVSSVLLAPSVFQQTVTRSSDLERKASSPSPLTIGTPESQRKPSIILSKSQLQDTLIHLIKNDSSFLSTLHEVYLQVLTKNKDNHNL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MEALSRAGQEMS ---CHHHHHHHHHHH	27.42	20068231
12	Phosphorylation	SRAGQEMSLAALKQH HHHHHHHHHHHHHHC	17.69	20068231
22	Phosphorylation	ALKQHDPYITSIADL HHHHCCCCHHHHHHH	23.92	20068231
47	Ubiquitination	PKANQWEKTDIEGTL CCCCCCEEECCCCEE	48.84	22053931
48	Ubiquitination	KANQWEKTDIEGTLF CCCCCEEECCCCEEE	30.60	29967540
60	Phosphorylation	TLFVYRRSASPYHGF EEEEEEECCCCCCCE	24.89	28787133
62	Phosphorylation	FVYRRSASPYHGFTI EEEEECCCCCCCEEE	27.51	23401153
64	Phosphorylation	YRRSASPYHGFTIVN EEECCCCCCCEEEEE	16.45	28122231
68	Phosphorylation	ASPYHGFTIVNRLNM CCCCCCEEEEECCCC	28.71	23403867
70	Ubiquitination	PYHGFTIVNRLNMHN CCCCEEEEECCCCCC	2.87	29967540
94	Ubiquitination	EFQLHEPFLLYRNAS HHEECCCEEHHCCCC	7.18	29967540
108	Ubiquitination	SLSIYSIWFYDKNDC CEEEEEEEEECCCHH	4.64	29967540
120	Acetylation	NDCHRIAKLMADVVE CHHHHHHHHHHHHHH	36.10	25953088
120	Ubiquitination	NDCHRIAKLMADVVE CHHHHHHHHHHHHHH	36.10	29967540
130	Phosphorylation	ADVVEEETRRSQQAA HHHHHHHHHHHHHHH	34.36	26074081
133	Phosphorylation	VEEETRRSQQAARDK HHHHHHHHHHHHHHC	24.29	26074081
140	Ubiquitination	SQQAARDKQSPSQAN HHHHHHHCCCHHHCC	47.31	-
142	Phosphorylation	QAARDKQSPSQANGC HHHHHCCCHHHCCCC	32.05	26846344
143	Ubiquitination	AARDKQSPSQANGCS HHHHCCCHHHCCCCC	28.15	29967540
144	Phosphorylation	ARDKQSPSQANGCSD HHHCCCHHHCCCCCC	47.36	26846344
150	Phosphorylation	PSQANGCSDHRPIDI HHHCCCCCCCCCHHH	37.54	26846344
156	Phosphorylation	CSDHRPIDILEMLSR CCCCCCHHHHHHHHH	41.94	32142685
157	Ubiquitination	SDHRPIDILEMLSRA CCCCCHHHHHHHHHC	3.48	29967540
160	Phosphorylation	RPIDILEMLSRAKDE CCHHHHHHHHHCHHH	3.55	32142685
162	Phosphorylation	IDILEMLSRAKDEYE HHHHHHHHHCHHHHH	28.96	23927012
168	Phosphorylation	LSRAKDEYERNQMGD HHHCHHHHHHHCCCC	30.26	28796482
168 (in isoform 2)	Phosphorylation	-	30.26	20068231
171 (in isoform 2)	Phosphorylation	-	25.01	20068231
174 (in isoform 2)	Phosphorylation	-	25.98	20068231
176	Phosphorylation	ERNQMGDSNISSPGL HHHCCCCCCCCCCCC	30.27	21712546
179	Phosphorylation	QMGDSNISSPGLQPS CCCCCCCCCCCCCCC	34.43	30278072
180	Phosphorylation	MGDSNISSPGLQPST CCCCCCCCCCCCCCH	21.13	30278072
186	Phosphorylation	SSPGLQPSTQLSNLG CCCCCCCCHHHHCCC	18.80	21955146
187	Phosphorylation	SPGLQPSTQLSNLGS CCCCCCCHHHHCCCC	39.97	21955146
187	Ubiquitination	SPGLQPSTQLSNLGS CCCCCCCHHHHCCCC	39.97	24816145
190	Phosphorylation	LQPSTQLSNLGSTET CCCCHHHHCCCCCCC	21.86	30278072
191	Ubiquitination	QPSTQLSNLGSTETL CCCHHHHCCCCCCCH	57.95	29967540
194	Phosphorylation	TQLSNLGSTETLEEM HHHHCCCCCCCHHHC	26.66	25022875
195	Phosphorylation	QLSNLGSTETLEEMP HHHCCCCCCCHHHCC	31.06	21712546
197	Phosphorylation	SNLGSTETLEEMPSG HCCCCCCCHHHCCCC	39.29	25022875
198	Phosphorylation	NLGSTETLEEMPSGS CCCCCCCHHHCCCCC	4.23	32142685
203	Phosphorylation	ETLEEMPSGSQDKSA CCHHHCCCCCCCCCC	50.17	20873877
205	Phosphorylation	LEEMPSGSQDKSAPS HHHCCCCCCCCCCCC	39.27	20873877
215	Ubiquitination	KSAPSGHKHLTVEEL CCCCCCCCCEEHHHH	43.78	29967540
218	Phosphorylation	PSGHKHLTVEELFGT CCCCCCEEHHHHHCC	26.12	28060719
225	Phosphorylation	TVEELFGTSLPKEQP EHHHHHCCCCCCCCC	21.54	29255136
225	Ubiquitination	TVEELFGTSLPKEQP EHHHHHCCCCCCCCC	21.54	24816145
226	Phosphorylation	VEELFGTSLPKEQPA HHHHHCCCCCCCCCC	42.95	29255136
229	Ubiquitination	LFGTSLPKEQPAVVG HHCCCCCCCCCCEEC	74.42	29967540
238	Ubiquitination	QPAVVGLDSEEMERL CCCEECCCHHHHHCC	48.34	29967540
239	O-linked_Glycosylation	PAVVGLDSEEMERLP CCEECCCHHHHHCCC	40.26	23301498
242	Phosphorylation	VGLDSEEMERLPGDA ECCCHHHHHCCCCCC	2.97	32142685
243	Phosphorylation	GLDSEEMERLPGDAS CCCHHHHHCCCCCCC	55.11	32142685
247	Phosphorylation	EEMERLPGDASQKEP HHHHCCCCCCCCCCC	47.94	32142685
274	Ubiquitination	GAPQSETLGVPSAAH CCCCHHCCCCCCHHC	5.97	24816145
276	Ubiquitination	PQSETLGVPSAAHHS CCHHCCCCCCHHCCC	3.68	29967540
277	Phosphorylation	QSETLGVPSAAHHSV CHHCCCCCCHHCCCC	19.22	32142685
280	Phosphorylation	TLGVPSAAHHSVQPE CCCCCCHHCCCCCCC	12.79	32142685
281	Phosphorylation	LGVPSAAHHSVQPEI CCCCCHHCCCCCCCC	17.30	32142685
289	Phosphorylation	HSVQPEITTPVLITP CCCCCCCCCCEEECC	24.32	26074081
290	Phosphorylation	SVQPEITTPVLITPA CCCCCCCCCEEECCC	19.63	26074081
295	Phosphorylation	ITTPVLITPASITQS CCCCEEECCCCCCCC	14.51	-
308	Ubiquitination	QSNEKHAPTYTIPLS CCCCCCCCEEEEECC	26.17	24816145
309	Phosphorylation	SNEKHAPTYTIPLSP CCCCCCCEEEEECCC	33.80	29255136
310	Phosphorylation	NEKHAPTYTIPLSPV CCCCCCEEEEECCCC	11.12	30278072
311	Phosphorylation	EKHAPTYTIPLSPVL CCCCCEEEEECCCCC	20.71	29255136
315	Phosphorylation	PTYTIPLSPVLSPTL CEEEEECCCCCCCCC	13.96	29255136
319	Phosphorylation	IPLSPVLSPTLPAEA EECCCCCCCCCCCCC	18.97	29255136
321	Phosphorylation	LSPVLSPTLPAEAPT CCCCCCCCCCCCCCC	41.83	29255136
325	Ubiquitination	LSPTLPAEAPTAQVP CCCCCCCCCCCCCCC	53.92	29967540
328	Phosphorylation	TLPAEAPTAQVPPSL CCCCCCCCCCCCCCC	36.45	29255136
329	Phosphorylation	LPAEAPTAQVPPSLP CCCCCCCCCCCCCCC	13.81	32142685
334	Phosphorylation	PTAQVPPSLPRNSTM CCCCCCCCCCCCCHH	44.96	23927012
339	Phosphorylation	PPSLPRNSTMMQAVK CCCCCCCCHHHHHHH	20.96	26074081
340	Phosphorylation	PSLPRNSTMMQAVKT CCCCCCCHHHHHHHC	21.88	26074081
346	Acetylation	STMMQAVKTTPRQRS CHHHHHHHCCHHHCC	50.09	25953088
346	Ubiquitination	STMMQAVKTTPRQRS CHHHHHHHCCHHHCC	50.09	24816145
347	Phosphorylation	TMMQAVKTTPRQRSP HHHHHHHCCHHHCCC	35.12	28450419
348	Phosphorylation	MMQAVKTTPRQRSPL HHHHHHCCHHHCCCC	15.68	27422710
353	Phosphorylation	KTTPRQRSPLLNQPV HCCHHHCCCCCCCCC	16.15	29255136
359	Ubiquitination	RSPLLNQPVPELSHA CCCCCCCCCCCCCHH	42.42	29967540
361	Ubiquitination	PLLNQPVPELSHASL CCCCCCCCCCCHHHH	43.42	29967540
363	Phosphorylation	LNQPVPELSHASLIA CCCCCCCCCHHHHHC	3.58	32142685
364	Phosphorylation	NQPVPELSHASLIAN CCCCCCCCHHHHHCC	18.49	23927012
366	Phosphorylation	PVPELSHASLIANQS CCCCCCHHHHHCCCC	11.58	32142685
367	Phosphorylation	VPELSHASLIANQSP CCCCCHHHHHCCCCC	18.19	23927012
369	Phosphorylation	ELSHASLIANQSPFR CCCHHHHHCCCCCCC	2.91	32142685
373	Phosphorylation	ASLIANQSPFRAPLN HHHHCCCCCCCCCCE	26.30	25159151
376	Asymmetric dimethylarginine	IANQSPFRAPLNVTN HCCCCCCCCCCEEEC	38.38	-
376	Methylation	IANQSPFRAPLNVTN HCCCCCCCCCCEEEC	38.38	24129315
378	Ubiquitination	NQSPFRAPLNVTNTA CCCCCCCCCEEECCC	21.88	29967540
382	Phosphorylation	FRAPLNVTNTAGTSL CCCCCEEECCCCCCC	26.27	20068231
384	Phosphorylation	APLNVTNTAGTSLPS CCCEEECCCCCCCCC	19.66	20068231
387	Phosphorylation	NVTNTAGTSLPSVDL EEECCCCCCCCCHHH	25.32	28348404
388	O-linked_Glycosylation	VTNTAGTSLPSVDLL EECCCCCCCCCHHHH	37.05	23301498
388	Phosphorylation	VTNTAGTSLPSVDLL EECCCCCCCCCHHHH	37.05	28348404
391	Phosphorylation	TAGTSLPSVDLLQKL CCCCCCCCHHHHHHH	33.29	20068231
397	Ubiquitination	PSVDLLQKLRLTPQH CCHHHHHHHCCCCCC	35.23	29967540
399	Ubiquitination	VDLLQKLRLTPQHDQ HHHHHHHCCCCCCCC	43.48	29967540
401	Phosphorylation	LLQKLRLTPQHDQIQ HHHHHCCCCCCCCCC	17.92	29255136
402	Phosphorylation	LQKLRLTPQHDQIQT HHHHCCCCCCCCCCC	33.82	32142685
404	Phosphorylation	KLRLTPQHDQIQTQP HHCCCCCCCCCCCCC	30.10	32142685
407	Phosphorylation	LTPQHDQIQTQPLGK CCCCCCCCCCCCCCC	6.27	32142685
409	Phosphorylation	PQHDQIQTQPLGKGA CCCCCCCCCCCCCCC	33.51	23927012
416	Ubiquitination	TQPLGKGAMVASFSP CCCCCCCCEEEEECC	7.86	29967540
420	Phosphorylation	GKGAMVASFSPAAGQ CCCCEEEEECCCCCC	18.17	25850435
422	Phosphorylation	GAMVASFSPAAGQLA CCEEEEECCCCCCCC	15.90	25159151
430	Phosphorylation	PAAGQLATPESFIEP CCCCCCCCCHHHCCC	35.86	25159151
433	Phosphorylation	GQLATPESFIEPPSK CCCCCCHHHCCCCCH	32.50	22199227
439	Phosphorylation	ESFIEPPSKTAAARV HHHCCCCCHHHHHHH	54.04	26074081
448	Ubiquitination	TAAARVAASASLSNM HHHHHHHHHHHHHHH	11.63	29967540
449	Phosphorylation	AAARVAASASLSNMV HHHHHHHHHHHHHHC	14.51	20068231
451	Phosphorylation	ARVAASASLSNMVLA HHHHHHHHHHHHCHH	29.81	32142685
453	Phosphorylation	VAASASLSNMVLAPL HHHHHHHHHHCHHHH	22.00	33259812
456	Phosphorylation	SASLSNMVLAPLQSM HHHHHHHCHHHHHHH	4.89	32142685
462	Phosphorylation	MVLAPLQSMQQNQDP HCHHHHHHHHHCCCC	26.66	20068231
465	Ubiquitination	APLQSMQQNQDPEVF HHHHHHHHCCCCCHH	40.69	29967540
482	Ubiquitination	PKVLSSAIQVAGAPL HHHHHHHHHHCCCCC	3.51	29967540
485	Phosphorylation	LSSAIQVAGAPLVTA HHHHHHHCCCCCEEE	7.64	32142685
487	Phosphorylation	SAIQVAGAPLVTATT HHHHHCCCCCEEECC	5.63	32142685
490	Phosphorylation	QVAGAPLVTATTTAV HHCCCCCEEECCHHH	3.13	32142685
491	O-linked_Glycosylation	VAGAPLVTATTTAVS HCCCCCEEECCHHHH	26.43	23301498
493	O-linked_Glycosylation	GAPLVTATTTAVSSV CCCCEEECCHHHHHH	18.47	23301498
494	O-linked_Glycosylation	APLVTATTTAVSSVL CCCEEECCHHHHHHH	15.42	23301498
495	O-linked_Glycosylation	PLVTATTTAVSSVLL CCEEECCHHHHHHHH	22.25	23301498
498	O-linked_Glycosylation	TATTTAVSSVLLAPS EECCHHHHHHHHCHH	16.56	23301498
499	O-linked_Glycosylation	ATTTAVSSVLLAPSV ECCHHHHHHHHCHHH	15.36	23301498
499	Ubiquitination	ATTTAVSSVLLAPSV ECCHHHHHHHHCHHH	15.36	29967540
515	O-linked_Glycosylation	QQTVTRSSDLERKAS CCCCCCCHHHHHHCC	42.81	23301498
520	Ubiquitination	RSSDLERKASSPSPL CCHHHHHHCCCCCCC	43.15	29967540
522	Phosphorylation	SDLERKASSPSPLTI HHHHHHCCCCCCCCC	45.90	29255136
523	Phosphorylation	DLERKASSPSPLTIG HHHHHCCCCCCCCCC	33.97	29255136
525	Phosphorylation	ERKASSPSPLTIGTP HHHCCCCCCCCCCCC	34.19	19664994
528	Phosphorylation	ASSPSPLTIGTPESQ CCCCCCCCCCCCHHH	22.27	29255136
531	Phosphorylation	PSPLTIGTPESQRKP CCCCCCCCCHHHCCC	21.74	19664994
534	Phosphorylation	LTIGTPESQRKPSII CCCCCCHHHCCCEEE	36.17	30266825
537	Ubiquitination	GTPESQRKPSIILSK CCCHHHCCCEEEEEH	35.16	29967540
539	Phosphorylation	PESQRKPSIILSKSQ CHHHCCCEEEEEHHH	25.87	23882029
543	Phosphorylation	RKPSIILSKSQLQDT CCCEEEEEHHHHHHH	21.61	30576142
545	Phosphorylation	PSIILSKSQLQDTLI CEEEEEHHHHHHHHH	32.52	25159151

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
315	S	Phosphorylation	Kinase	MAPK8	P45983	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DCP1A_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 DCP1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD4_HUMAN	SMAD4	physical	11836524
DCP2_HUMAN	DCP2	physical	12417715
RENT1_HUMAN	UPF1	physical	12417715
DDX6_HUMAN	DDX6	physical	16364915
EDC3_HUMAN	EDC3	physical	16364915
HS71L_HUMAN	HSPA1L	physical	16364915
EDC4_HUMAN	EDC4	physical	16364915
DCP2_HUMAN	DCP2	physical	16364915
DCP1B_HUMAN	DCP1B	physical	16364915
AASS_HUMAN	AASS	physical	24778252
BAG4_HUMAN	BAG4	physical	24778252
DCP1B_HUMAN	DCP1B	physical	24778252
DDX6_HUMAN	DDX6	physical	24778252
EDC3_HUMAN	EDC3	physical	24778252
EDC4_HUMAN	EDC4	physical	24778252
EI2BD_HUMAN	EIF2B4	physical	24778252
KANK2_HUMAN	KANK2	physical	24778252
PFKAM_HUMAN	PFKM	physical	24778252
PNRC1_HUMAN	PNRC1	physical	24778252
PCH2_HUMAN	TRIP13	physical	24778252
DCP1B_HUMAN	DCP1B	physical	25036637
DDX6_HUMAN	DDX6	physical	25036637
EDC3_HUMAN	EDC3	physical	25036637
EDC4_HUMAN	EDC4	physical	25036637
DCP2_HUMAN	DCP2	physical	25036637
RITA1_HUMAN	RITA1	physical	25416956
DDX6_HUMAN	DDX6	physical	26496610
MP2K1_HUMAN	MAP2K1	physical	26496610
P5CS_HUMAN	ALDH18A1	physical	26496610
TBX3_HUMAN	TBX3	physical	26496610
BAG4_HUMAN	BAG4	physical	26496610
MARF1_HUMAN	KIAA0430	physical	26496610
PNRC1_HUMAN	PNRC1	physical	26496610
EDC4_HUMAN	EDC4	physical	26496610
TRM6_HUMAN	TRMT6	physical	26496610
EDC3_HUMAN	EDC3	physical	26496610
DCP2_HUMAN	DCP2	physical	26496610
PATL1_HUMAN	PATL1	physical	26496610
PPR37_HUMAN	PPP1R37	physical	26496610
EDC4_HUMAN	EDC4	physical	27315556
XRN1_HUMAN	XRN1	physical	27315556
EDC3_HUMAN	EDC3	physical	27315556
TRAF6_HUMAN	TRAF6	physical	27315556
DCP2_HUMAN	DCP2	physical	27315556

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 DCP1A_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-180; SER-315; SER-319;SER-353; SER-522; SER-523; SER-525 AND THR-531, AND MASS SPECTROMETRY.	19690332 [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-522; SER-523; SER-525AND THR-531, 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-142; SER-315; SER-319;SER-334; THR-401; SER-522; SER-523; SER-525 AND THR-531, AND MASSSPECTROMETRY.	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-315; SER-319; SER-353AND THR-401, 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-315; SER-319; SER-334AND THR-531, AND MASS SPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND MASSSPECTROMETRY.	18187866 [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-353, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND SER-525, ANDMASS SPECTROMETRY.	15302935 [Abstract]