dbPTM

PCBP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PCBP2_HUMAN
UniProt AC	Q15366
Protein Name	Poly(rC)-binding protein 2
Gene Name	PCBP2
Organism	Homo sapiens (Human).
Sequence Length	365
Subcellular Localization	Nucleus . Cytoplasm . Loosely bound in the nucleus. May shuttle between the nucleus and the cytoplasm.
Protein Description	Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. Major cellular poly(rC)-binding protein. Binds also poly(rU). Negatively regulates cellular antiviral responses mediated by MAVS signaling. [PubMed: 19881509 It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation]
Protein Sequence	MDTGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTNAIFKAFAMIIDKLEEDISSSMTNSTAASRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGIPQSIIECVKQICVVMLETLSQSPPKGVTIPYRPKPSSSPVIFAGGQDRYSTGSDSASFPHTTPSMCLNPDLEGPPLEAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSGIESSSPEVKGYWGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINVRLSSETGGMGSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MDTGVIEGGL -----CCCCCCCCCE	31.86	28387310
13	Phosphorylation	IEGGLNVTLTIRLLM CCCCEEEEEEEEHHH	19.67	28387310
15	Phosphorylation	GGLNVTLTIRLLMHG CCEEEEEEEEHHHCC	8.49	20068231
23	Acetylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHHC	34.25	21680723
23	Sumoylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHHC	34.25	-
23	Ubiquitination	IRLLMHGKEVGSIIG EEHHHCCHHHHHHHC	34.25	21890473
23	Sumoylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHHC	34.25	-
23	Ubiquitination	IRLLMHGKEVGSIIG EEHHHCCHHHHHHHC	34.25	21890473
23	Ubiquitination	IRLLMHGKEVGSIIG EEHHHCCHHHHHHHC	34.25	21890473
23	Ubiquitination	IRLLMHGKEVGSIIG EEHHHCCHHHHHHHC	34.25	21890473
23	Ubiquitination	IRLLMHGKEVGSIIG EEHHHCCHHHHHHHC	34.25	21890473
23	Ubiquitination	IRLLMHGKEVGSIIG EEHHHCCHHHHHHHC	34.25	21890473
23	Ubiquitination	IRLLMHGKEVGSIIG EEHHHCCHHHHHHHC	34.25	21890473
27	Phosphorylation	MHGKEVGSIIGKKGE HCCHHHHHHHCCCCH	19.06	28387310
31	Acetylation	EVGSIIGKKGESVKK HHHHHHCCCCHHHHH	47.39	23749302
31	Sumoylation	EVGSIIGKKGESVKK HHHHHHCCCCHHHHH	47.39	-
31	Ubiquitination	EVGSIIGKKGESVKK HHHHHHCCCCHHHHH	47.39	21906983
31	Sumoylation	EVGSIIGKKGESVKK HHHHHHCCCCHHHHH	47.39	-
31	Ubiquitination	EVGSIIGKKGESVKK HHHHHHCCCCHHHHH	47.39	21890473
31	Ubiquitination	EVGSIIGKKGESVKK HHHHHHCCCCHHHHH	47.39	21890473
31	Ubiquitination	EVGSIIGKKGESVKK HHHHHHCCCCHHHHH	47.39	21890473
31	Ubiquitination	EVGSIIGKKGESVKK HHHHHHCCCCHHHHH	47.39	21890473
31	Ubiquitination	EVGSIIGKKGESVKK HHHHHHCCCCHHHHH	47.39	21890473
31	Ubiquitination	EVGSIIGKKGESVKK HHHHHHCCCCHHHHH	47.39	21890473
50	Phosphorylation	SGARINISEGNCPER HCCCEEECCCCCCCC	34.66	21815630
54	S-nitrosocysteine	INISEGNCPERIITL EEECCCCCCCCEEEE	5.64	-
54	Glutathionylation	INISEGNCPERIITL EEECCCCCCCCEEEE	5.64	22555962
54	S-nitrosylation	INISEGNCPERIITL EEECCCCCCCCEEEE	5.64	19483679
54	S-palmitoylation	INISEGNCPERIITL EEECCCCCCCCEEEE	5.64	29575903
60	Phosphorylation	NCPERIITLAGPTNA CCCCCEEEECCHHHH	14.26	22210691
70	Acetylation	GPTNAIFKAFAMIID CHHHHHHHHHHHHHH	36.16	69191
74	Sulfoxidation	AIFKAFAMIIDKLEE HHHHHHHHHHHHHHH	1.92	30846556
86	Phosphorylation	LEEDISSSMTNSTAA HHHHHHHHCCCCCCC	23.88	24719451
87	Sulfoxidation	EEDISSSMTNSTAAS HHHHHHHCCCCCCCC	4.43	30846556
88	Phosphorylation	EDISSSMTNSTAASR HHHHHHCCCCCCCCC	28.15	28555341
90	Phosphorylation	ISSSMTNSTAASRPP HHHHCCCCCCCCCCC	15.40	28555341
91	Phosphorylation	SSSMTNSTAASRPPV HHHCCCCCCCCCCCE	28.45	22210691
94	Phosphorylation	MTNSTAASRPPVTLR CCCCCCCCCCCEEEE	42.74	22210691
99	Phosphorylation	AASRPPVTLRLVVPA CCCCCCEEEEEEEEH	16.37	-
107	Phosphorylation	LRLVVPASQCGSLIG EEEEEEHHHHHHHHC	21.67	23898821
109	S-nitrosocysteine	LVVPASQCGSLIGKG EEEEHHHHHHHHCCC	3.56	-
109	Glutathionylation	LVVPASQCGSLIGKG EEEEHHHHHHHHCCC	3.56	22555962
109	S-nitrosylation	LVVPASQCGSLIGKG EEEEHHHHHHHHCCC	3.56	19483679
109	S-palmitoylation	LVVPASQCGSLIGKG EEEEHHHHHHHHCCC	3.56	29575903
111	Phosphorylation	VPASQCGSLIGKGGC EEHHHHHHHHCCCCC	25.17	25159151
115	Sumoylation	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	-
115	Ubiquitination	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	-
115	Sumoylation	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	28112733
115	Ubiquitination	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	21890473
115	Ubiquitination	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	21890473
115	Acetylation	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	25953088
115	Malonylation	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	26320211
115	Ubiquitination	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	21890473
115	Ubiquitination	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	21890473
115	Ubiquitination	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	21890473
115	Ubiquitination	QCGSLIGKGGCKIKE HHHHHHCCCCCEEEH	45.17	21890473
119	Ubiquitination	LIGKGGCKIKEIRES HHCCCCCEEEHHHHH	61.15	-
126	Phosphorylation	KIKEIRESTGAQVQV EEEHHHHHHCCEEEE	23.46	25627689
127	Phosphorylation	IKEIRESTGAQVQVA EEHHHHHHCCEEEEE	31.61	25159151
154	Phosphorylation	TIAGIPQSIIECVKQ HHCCCCHHHHHHHHH	21.85	21712546
158	S-nitrosocysteine	IPQSIIECVKQICVV CCHHHHHHHHHHHHH	3.06	-
158	Glutathionylation	IPQSIIECVKQICVV CCHHHHHHHHHHHHH	3.06	22555962
158	S-nitrosylation	IPQSIIECVKQICVV CCHHHHHHHHHHHHH	3.06	19483679
158	S-palmitoylation	IPQSIIECVKQICVV CCHHHHHHHHHHHHH	3.06	26865113
160	Ubiquitination	QSIIECVKQICVVML HHHHHHHHHHHHHHH	45.67	-
169	Phosphorylation	ICVVMLETLSQSPPK HHHHHHHHHCCCCCC	27.96	30266825
169 (in isoform 3)	Phosphorylation	-	27.96	20068231
169 (in isoform 4)	Phosphorylation	-	27.96	20068231
169 (in isoform 6)	Phosphorylation	-	27.96	20068231
169 (in isoform 7)	Phosphorylation	-	27.96	20068231
171	Phosphorylation	VVMLETLSQSPPKGV HHHHHHHCCCCCCCC	35.71	30266825
173	Phosphorylation	MLETLSQSPPKGVTI HHHHHCCCCCCCCCC	39.53	29255136
175 (in isoform 3)	Phosphorylation	-	51.81	20068231
175 (in isoform 4)	Phosphorylation	-	51.81	26356563
175 (in isoform 6)	Phosphorylation	-	51.81	20068231
175 (in isoform 7)	Phosphorylation	-	51.81	26356563
178 (in isoform 3)	Phosphorylation	-	5.68	17081983
178 (in isoform 4)	Phosphorylation	-	5.68	26356563
178 (in isoform 6)	Phosphorylation	-	5.68	17081983
178 (in isoform 7)	Phosphorylation	-	5.68	26356563
179	Phosphorylation	QSPPKGVTIPYRPKP CCCCCCCCCCCCCCC	25.55	30278072
179 (in isoform 5)	Phosphorylation	-	25.55	26356563
179 (in isoform 8)	Phosphorylation	-	25.55	26356563
181	Ubiquitination	PPKGVTIPYRPKPSS CCCCCCCCCCCCCCC	15.09	21890473
182	Phosphorylation	PKGVTIPYRPKPSSS CCCCCCCCCCCCCCC	35.38	23927012
182 (in isoform 5)	Phosphorylation	-	35.38	26356563
182 (in isoform 8)	Phosphorylation	-	35.38	26356563
183 (in isoform 3)	Phosphorylation	-	27.67	25849741
183 (in isoform 4)	Phosphorylation	-	27.67	26356563
183 (in isoform 6)	Phosphorylation	-	27.67	25849741
183 (in isoform 7)	Phosphorylation	-	27.67	26356563
184 (in isoform 4)	Phosphorylation	-	47.25	26356563
184 (in isoform 7)	Phosphorylation	-	47.25	26356563
185	Acetylation	VTIPYRPKPSSSPVI CCCCCCCCCCCCCEE	48.83	23749302
185	Ubiquitination	VTIPYRPKPSSSPVI CCCCCCCCCCCCCEE	48.83	21890473
185 (in isoform 4)	Phosphorylation	-	48.83	26356563
185 (in isoform 7)	Phosphorylation	-	48.83	26356563
185	Sumoylation	VTIPYRPKPSSSPVI CCCCCCCCCCCCCEE	48.83	28112733
185	Ubiquitination	VTIPYRPKPSSSPVI CCCCCCCCCCCCCEE	48.83	21890473
185	Ubiquitination	VTIPYRPKPSSSPVI CCCCCCCCCCCCCEE	48.83	21890473
187	Phosphorylation	IPYRPKPSSSPVIFA CCCCCCCCCCCEEEE	49.96	22167270
187 (in isoform 5)	Phosphorylation	-	49.96	26356563
187 (in isoform 8)	Phosphorylation	-	49.96	26356563
188	Phosphorylation	PYRPKPSSSPVIFAG CCCCCCCCCCEEEEC	47.38	29255136
188 (in isoform 5)	Phosphorylation	-	47.38	26356563
188 (in isoform 8)	Phosphorylation	-	47.38	26356563
189	Phosphorylation	YRPKPSSSPVIFAGG CCCCCCCCCEEEECC	27.76	19664994
189 (in isoform 5)	Phosphorylation	-	27.76	26356563
189 (in isoform 8)	Phosphorylation	-	27.76	26356563
195 (in isoform 4)	Phosphorylation	-	24.44	26356563
195 (in isoform 7)	Phosphorylation	-	24.44	26356563
196 (in isoform 4)	Phosphorylation	-	23.84	26356563
196 (in isoform 7)	Phosphorylation	-	23.84	26356563
199 (in isoform 5)	Phosphorylation	-	21.29	26356563
199 (in isoform 8)	Phosphorylation	-	21.29	26356563
200 (in isoform 5)	Phosphorylation	-	20.90	26356563
200 (in isoform 8)	Phosphorylation	-	20.90	26356563
201	Phosphorylation	AGGQDRYSTGSDSAS ECCCCCCCCCCCCCC	27.47	26356563
201 (in isoform 4)	Phosphorylation	-	27.47	25884760
201 (in isoform 7)	Phosphorylation	-	27.47	25884760
202	Phosphorylation	GGQDRYSTGSDSASF CCCCCCCCCCCCCCC	31.60	26356563
204	Phosphorylation	QDRYSTGSDSASFPH CCCCCCCCCCCCCCC	28.60	26356563
205 (in isoform 5)	Phosphorylation	-	49.95	25884760
205 (in isoform 8)	Phosphorylation	-	49.95	25884760
206	Phosphorylation	RYSTGSDSASFPHTT CCCCCCCCCCCCCCC	27.75	26356563
208	Phosphorylation	STGSDSASFPHTTPS CCCCCCCCCCCCCHH	43.17	26356563
209 (in isoform 4)	Phosphorylation	-	5.27	26356563
209 (in isoform 7)	Phosphorylation	-	5.27	26356563
212	Phosphorylation	DSASFPHTTPSMCLN CCCCCCCCCHHHCCC	40.41	26356563
213	Phosphorylation	SASFPHTTPSMCLNP CCCCCCCCHHHCCCC	15.44	26356563
213 (in isoform 5)	Phosphorylation	-	15.44	26356563
213 (in isoform 8)	Phosphorylation	-	15.44	26356563
215	Phosphorylation	SFPHTTPSMCLNPDL CCCCCCHHHCCCCCC	21.75	26356563
230	Phosphorylation	EGPPLEAYTIQGQYA CCCCCEEEEEECCCC	8.59	26356563
231	Phosphorylation	GPPLEAYTIQGQYAI CCCCEEEEEECCCCC	17.55	26356563
231	O-linked_Glycosylation	GPPLEAYTIQGQYAI CCCCEEEEEECCCCC	17.55	OGP
235 (in isoform 4)	Phosphorylation	-	14.22	25627689
236	Phosphorylation	AYTIQGQYAIPQPDL EEEEECCCCCCCCCH	17.21	16094384
236 (in isoform 4)	Phosphorylation	-	17.21	18669648
237 (in isoform 4)	Phosphorylation	-	10.09	25849741
239 (in isoform 5)	Phosphorylation	-	31.32	25627689
240 (in isoform 5)	Phosphorylation	-	37.72	18669648
241 (in isoform 5)	Phosphorylation	-	32.97	25849741
243 (in isoform 4)	Phosphorylation	-	6.07	-
244	Phosphorylation	AIPQPDLTKLHQLAM CCCCCCHHHHHHHHH	38.65	-
245	Ubiquitination	IPQPDLTKLHQLAMQ CCCCCHHHHHHHHHH	51.79	-
247 (in isoform 5)	Phosphorylation	-	23.36	-
254	Phosphorylation	HQLAMQQSHFPMTHG HHHHHHHCCCCCCCC	15.37	22167270
259	Phosphorylation	QQSHFPMTHGNTGFS HHCCCCCCCCCCCCC	27.20	29255136
263	Phosphorylation	FPMTHGNTGFSGIES CCCCCCCCCCCCCCC	44.17	29255136
266	Phosphorylation	THGNTGFSGIESSSP CCCCCCCCCCCCCCC	39.96	23401153
266 (in isoform 3)	Phosphorylation	-	39.96	25627689
266	Acetylation	THGNTGFSGIESSSP CCCCCCCCCCCCCCC	39.96	-
266	Ubiquitination	THGNTGFSGIESSSP CCCCCCCCCCCCCCC	39.96	-
267 (in isoform 3)	Phosphorylation	-	25.97	18669648
268 (in isoform 3)	Phosphorylation	-	4.49	25849741
270	Phosphorylation	TGFSGIESSSPEVKG CCCCCCCCCCCCCCC	33.91	23401153
270 (in isoform 2)	Phosphorylation	-	33.91	25627689
271	Phosphorylation	GFSGIESSSPEVKGY CCCCCCCCCCCCCCE	36.80	23401153
271 (in isoform 2)	Phosphorylation	-	36.80	18669648
272	Phosphorylation	FSGIESSSPEVKGYW CCCCCCCCCCCCCEE	34.07	29255136
272 (in isoform 2)	Phosphorylation	-	34.07	25849741
274 (in isoform 3)	Phosphorylation	-	59.83	-
275	Ubiquitination	IESSSPEVKGYWGLD CCCCCCCCCCEEECC	7.09	21906983
276	Sumoylation	ESSSPEVKGYWGLDA CCCCCCCCCEEECCC	44.62	-
278	Phosphorylation	SSPEVKGYWGLDASA CCCCCCCEEECCCCC	7.21	-
278 (in isoform 2)	Phosphorylation	-	7.21	-
279	Ubiquitination	SPEVKGYWGLDASAQ CCCCCCEEECCCCCC	15.00	21890473
288	Ubiquitination	LDASAQTTSHELTIP CCCCCCCEECEECCC	18.92	21890473
289	Phosphorylation	DASAQTTSHELTIPN CCCCCCEECEECCCC	20.53	-
292	Ubiquitination	AQTTSHELTIPNDLI CCCEECEECCCCCHH	4.38	21890473
309	Acetylation	IIGRQGAKINEIRQM HHCCCCCCHHHHHHH	53.54	23749302
309	Sumoylation	IIGRQGAKINEIRQM HHCCCCCCHHHHHHH	53.54	-
309	Ubiquitination	IIGRQGAKINEIRQM HHCCCCCCHHHHHHH	53.54	-
309	Sumoylation	IIGRQGAKINEIRQM HHCCCCCCHHHHHHH	53.54	-
314	Methylation	GAKINEIRQMSGAQI CCCHHHHHHHCCCEE	21.70	-
316	Sulfoxidation	KINEIRQMSGAQIKI CHHHHHHHCCCEEEE	2.61	28183972
317	Phosphorylation	INEIRQMSGAQIKIA HHHHHHHCCCEEEEC	23.73	28857561
319	Ubiquitination	EIRQMSGAQIKIANP HHHHHCCCEEEECCC	10.71	21890473
322	Sumoylation	QMSGAQIKIANPVEG HHCCCEEEECCCCCC	24.56	-
322	Ubiquitination	QMSGAQIKIANPVEG HHCCCEEEECCCCCC	24.56	21890473
322	Sumoylation	QMSGAQIKIANPVEG HHCCCEEEECCCCCC	24.56	28112733
323	Ubiquitination	MSGAQIKIANPVEGS HCCCEEEECCCCCCC	4.84	21890473
323	Ubiquitination	MSGAQIKIANPVEGS HCCCEEEECCCCCCC	4.84	21890473
330	Phosphorylation	IANPVEGSTDRQVTI ECCCCCCCCCCEEEE	17.40	20873877
331	Phosphorylation	ANPVEGSTDRQVTIT CCCCCCCCCCEEEEE	46.16	20873877
340	Phosphorylation	RQVTITGSAASISLA CEEEEECCHHHHHHH	16.41	20068231
345	Phosphorylation	TGSAASISLAQYLIN ECCHHHHHHHHHHHH	18.37	20068231
356	Phosphorylation	YLINVRLSSETGGMG HHHHCCCCCCCCCCC	18.63	29396449
357	Phosphorylation	LINVRLSSETGGMGS HHHCCCCCCCCCCCC	43.71	30108239
359	Phosphorylation	NVRLSSETGGMGSS- HCCCCCCCCCCCCC-	40.77	30108239
362	Sulfoxidation	LSSETGGMGSS---- CCCCCCCCCCC----	5.07	30846556
364	Phosphorylation	SETGGMGSS------ CCCCCCCCC------	24.79	30278072
365	Phosphorylation	ETGGMGSS------- CCCCCCCC-------	38.21	23401153

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
173	S	Phosphorylation	Kinase	ERK2	P28482	PSP
173	S	Phosphorylation	Kinase	ERK1	P27361	PSP
189	S	Phosphorylation	Kinase	ERK2	P28482	PSP
189	S	Phosphorylation	Kinase	ERK1	P27361	PSP
213	T	Phosphorylation	Kinase	ERK2	P28482	PSP
213	T	Phosphorylation	Kinase	ERK1	P27361	PSP
272	S	Phosphorylation	Kinase	ERK2	P28482	PSP
272	S	Phosphorylation	Kinase	ERK1	P27361	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PCBP2_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 PCBP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCBP2_HUMAN	PCBP2	physical	10772858
PTBP1_HUMAN	PTBP1	physical	10772858
HNRPK_HUMAN	HNRNPK	physical	10772858
HNRPL_HUMAN	HNRNPL	physical	10772858
HNRPD_HUMAN	HNRNPD	physical	10373504
PABP1_HUMAN	PABPC1	physical	10373504
ITCH_HUMAN	ITCH	physical	19881509
MAVS_HUMAN	MAVS	physical	19881509
IFIH1_HUMAN	IFIH1	physical	19881509
PPIB_HUMAN	PPIB	physical	22939629
SF3B2_HUMAN	SF3B2	physical	22365833
SLU7_HUMAN	SLU7	physical	22365833
WDR83_HUMAN	WDR83	physical	22365833
MEP50_HUMAN	WDR77	physical	22365833
PCBP2_HUMAN	PCBP2	physical	22365833
NKAP_HUMAN	NKAP	physical	22365833
BRCA1_HUMAN	BRCA1	physical	22431556
SNRPA_HUMAN	SNRPA	physical	25416956
PCBP1_HUMAN	PCBP1	physical	23640898

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 PCBP2_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-189, 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-187, 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-173, AND MASSSPECTROMETRY.	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-272, 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-173 AND SER-189, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-189, ANDMASS SPECTROMETRY.	19007248 [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-187; SER-189 ANDSER-272, 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 SER-173, AND MASSSPECTROMETRY.	17081983 [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-236, AND MASSSPECTROMETRY.	16094384 [Abstract]