dbPTM

NUFP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NUFP2_HUMAN
UniProt AC	Q7Z417
Protein Name	Nuclear fragile X mental retardation-interacting protein 2
Gene Name	NUFIP2
Organism	Homo sapiens (Human).
Sequence Length	695
Subcellular Localization	Nucleus . Cytoplasm . Cytoplasm, Stress granule . Distribution is cell cycle-modulated, being cytoplasmic in the G2/M phase and accumulating in nucleus during the G1 phase (PubMed:12837692).
Protein Description	Binds RNA..
Protein Sequence	MEEKPGQPQPQHHHSHHHPHHHPQQQQQQPHHHHHYYFYNHSHNHHHHHHHQQPHQYLQHGAEGSPKAQPKPLKHEQKHTLQQHQETPKKKTGYGELNGNAGEREISLKNLSSDEATNPISRVLNGNQQVVDTSLKQTVKANTFGKAGIKTKNFIQKNSMDKKNGKSYENKSGENQSVDKSDTIPIPNGVVTNNSGYITNGYMGKGADNDGSGSESGYTTPKKRKARRNSAKGCENLNIVQDKIMQQETSVPTLKQGLETFKPDYSEQKGNRVDGSKPIWKYETGPGGTSRGKPAVGDMLRKSSDSKPGVSSKKFDDRPKGKHASAVASKEDSWTLFKPPPVFPVDNSSAKIVPKISYASKVKENLNKTIQNSSVSPTSSSSSSSSTGETQTQSSSRLSQVPMSALKSVTSANFSNGPVLAGTDGNVYPPGGQPLLTTAANTLTPISSGTDSVLQDMSLTSAAVEQIKTSLFIYPSNMQTMLLSTAQVDLPSQTDQQNLGDIFQNQWGLSFINEPSAGPETVTGKSSEHKVMEVTFQGEYPATLVSQGAEIIPSGTEHPVFPKAYELEKRTSPQVLGSILKSGTTSESGALSLEPSHIGDLQKADTSSQGALVFLSKDYEIESQNPLASPTNTLLGSAKEQRYQRGLERNDSWGSFDLRAAIVYHTKEMESIWNLQKQDPKRIITYNEAMDSPDQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
65	Phosphorylation	LQHGAEGSPKAQPKP HHCCCCCCCCCCCCC	18.09	26074081
74	Sumoylation	KAQPKPLKHEQKHTL CCCCCCCCHHHHHHH	54.33	-
74	Sumoylation	KAQPKPLKHEQKHTL CCCCCCCCHHHHHHH	54.33	17000644
74	Ubiquitination	KAQPKPLKHEQKHTL CCCCCCCCHHHHHHH	54.33	27667366
78	Sumoylation	KPLKHEQKHTLQQHQ CCCCHHHHHHHHHHC	35.26	28112733
78	Ubiquitination	KPLKHEQKHTLQQHQ CCCCHHHHHHHHHHC	35.26	29967540
87	Phosphorylation	TLQQHQETPKKKTGY HHHHHCCCCCCCCCC	33.56	29255136
91	Ubiquitination	HQETPKKKTGYGELN HCCCCCCCCCCCCCC	53.99	27667366
92	Phosphorylation	QETPKKKTGYGELNG CCCCCCCCCCCCCCC	44.51	28152594
94	Phosphorylation	TPKKKTGYGELNGNA CCCCCCCCCCCCCCC	16.80	28152594
107	Phosphorylation	NAGEREISLKNLSSD CCCCCEEEEECCCCC	28.65	23312004
109	Acetylation	GEREISLKNLSSDEA CCCEEEEECCCCCCC	49.40	25953088
109	Sumoylation	GEREISLKNLSSDEA CCCEEEEECCCCCCC	49.40	28112733
109	Ubiquitination	GEREISLKNLSSDEA CCCEEEEECCCCCCC	49.40	21906983
112	Phosphorylation	EISLKNLSSDEATNP EEEEECCCCCCCCCH	45.17	29255136
113	Phosphorylation	ISLKNLSSDEATNPI EEEECCCCCCCCCHH	42.51	19664994
117	Phosphorylation	NLSSDEATNPISRVL CCCCCCCCCHHHHHH	39.21	22167270
121	Phosphorylation	DEATNPISRVLNGNQ CCCCCHHHHHHCCCC	20.00	23403867
133	Phosphorylation	GNQQVVDTSLKQTVK CCCEEEECCHHHHHH	25.09	25627689
134	Phosphorylation	NQQVVDTSLKQTVKA CCEEEECCHHHHHHH	29.16	25627689
136	Methylation	QVVDTSLKQTVKANT EEEECCHHHHHHHCC	43.63	-
136	Sumoylation	QVVDTSLKQTVKANT EEEECCHHHHHHHCC	43.63	28112733
136	Ubiquitination	QVVDTSLKQTVKANT EEEECCHHHHHHHCC	43.63	32015554
140	Acetylation	TSLKQTVKANTFGKA CCHHHHHHHCCCCCC	39.03	19608861
140	Methylation	TSLKQTVKANTFGKA CCHHHHHHHCCCCCC	39.03	19608861
140	Ubiquitination	TSLKQTVKANTFGKA CCHHHHHHHCCCCCC	39.03	19608861
143	Phosphorylation	KQTVKANTFGKAGIK HHHHHHCCCCCCCCC	38.33	69338417
146	Acetylation	VKANTFGKAGIKTKN HHHCCCCCCCCCCCC	38.97	25953088
146	Sumoylation	VKANTFGKAGIKTKN HHHCCCCCCCCCCCC	38.97	28112733
146	Ubiquitination	VKANTFGKAGIKTKN HHHCCCCCCCCCCCC	38.97	29967540
150	Acetylation	TFGKAGIKTKNFIQK CCCCCCCCCCCHHHH	53.15	69309
151	Phosphorylation	FGKAGIKTKNFIQKN CCCCCCCCCCHHHHC	29.33	46156011
152	Acetylation	GKAGIKTKNFIQKNS CCCCCCCCCHHHHCC	44.87	26051181
152	Ubiquitination	GKAGIKTKNFIQKNS CCCCCCCCCHHHHCC	44.87	29967540
157	Sumoylation	KTKNFIQKNSMDKKN CCCCHHHHCCCCCCC	46.29	28112733
157	Ubiquitination	KTKNFIQKNSMDKKN CCCCHHHHCCCCCCC	46.29	29967540
159	Phosphorylation	KNFIQKNSMDKKNGK CCHHHHCCCCCCCCC	35.08	28857561
163	Ubiquitination	QKNSMDKKNGKSYEN HHCCCCCCCCCCCCC	67.67	30230243
171	Sumoylation	NGKSYENKSGENQSV CCCCCCCCCCCCCCC	48.15	28112733
181	Phosphorylation	ENQSVDKSDTIPIPN CCCCCCCCCCCCCCC	35.21	26074081
183	Phosphorylation	QSVDKSDTIPIPNGV CCCCCCCCCCCCCCE	35.43	68701191
192	Phosphorylation	PIPNGVVTNNSGYIT CCCCCEEECCCCEEE	26.69	26074081
195	Phosphorylation	NGVVTNNSGYITNGY CCEEECCCCEEECCC	34.73	26074081
197	Phosphorylation	VVTNNSGYITNGYMG EEECCCCEEECCCCC	12.37	26074081
199	Phosphorylation	TNNSGYITNGYMGKG ECCCCEEECCCCCCC	17.69	26074081
202	Phosphorylation	SGYITNGYMGKGADN CCEEECCCCCCCCCC	12.55	26074081
212	Phosphorylation	KGADNDGSGSESGYT CCCCCCCCCCCCCCC	41.85	19664994
214	Phosphorylation	ADNDGSGSESGYTTP CCCCCCCCCCCCCCH	30.22	29255136
216	Phosphorylation	NDGSGSESGYTTPKK CCCCCCCCCCCCHHH	38.50	22167270
218	Phosphorylation	GSGSESGYTTPKKRK CCCCCCCCCCHHHHH	19.40	23927012
219	Phosphorylation	SGSESGYTTPKKRKA CCCCCCCCCHHHHHH	39.90	25159151
220	Phosphorylation	GSESGYTTPKKRKAR CCCCCCCCHHHHHHH	25.32	23927012
230	Phosphorylation	KRKARRNSAKGCENL HHHHHHHCCCCCCHH	29.55	23401153
243	Acetylation	NLNIVQDKIMQQETS HHHHHHHHHHCCCCC	24.00	25953088
243	Ubiquitination	NLNIVQDKIMQQETS HHHHHHHHHHCCCCC	24.00	29967540
245	Sulfoxidation	NIVQDKIMQQETSVP HHHHHHHHCCCCCCC	4.08	21406390
249	Phosphorylation	DKIMQQETSVPTLKQ HHHHCCCCCCCHHHH	30.59	28857561
250	Phosphorylation	KIMQQETSVPTLKQG HHHCCCCCCCHHHHH	25.91	25159151
253	Phosphorylation	QQETSVPTLKQGLET CCCCCCCHHHHHHHH	44.42	28555341
255	Ubiquitination	ETSVPTLKQGLETFK CCCCCHHHHHHHHHC	44.81	29967540
260	Phosphorylation	TLKQGLETFKPDYSE HHHHHHHHHCCCCCC	41.84	25627689
262	Sumoylation	KQGLETFKPDYSEQK HHHHHHHCCCCCCCC	44.38	-
262	Acetylation	KQGLETFKPDYSEQK HHHHHHHCCCCCCCC	44.38	21466224
262	Sumoylation	KQGLETFKPDYSEQK HHHHHHHCCCCCCCC	44.38	17000644
265	Phosphorylation	LETFKPDYSEQKGNR HHHHCCCCCCCCCCC	23.72	68853961
266	Phosphorylation	ETFKPDYSEQKGNRV HHHCCCCCCCCCCCC	40.71	25159151
269	Methylation	KPDYSEQKGNRVDGS CCCCCCCCCCCCCCC	54.85	-
277	Acetylation	GNRVDGSKPIWKYET CCCCCCCCCCEEEEC	46.16	26051181
277	Ubiquitination	GNRVDGSKPIWKYET CCCCCCCCCCEEEEC	46.16	29967540
281	Sumoylation	DGSKPIWKYETGPGG CCCCCCEEEECCCCC	33.65	-
281	Sumoylation	DGSKPIWKYETGPGG CCCCCCEEEECCCCC	33.65	28112733
282	Phosphorylation	GSKPIWKYETGPGGT CCCCCEEEECCCCCC	12.06	68854039
289	Phosphorylation	YETGPGGTSRGKPAV EECCCCCCCCCCCCH	22.59	18212344
290	Phosphorylation	ETGPGGTSRGKPAVG ECCCCCCCCCCCCHH	42.16	46155993
291	Methylation	TGPGGTSRGKPAVGD CCCCCCCCCCCCHHH	57.92	24129315
293	Methylation	PGGTSRGKPAVGDML CCCCCCCCCCHHHHH	28.79	-
293	Sumoylation	PGGTSRGKPAVGDML CCCCCCCCCCHHHHH	28.79	28112733
299	Sulfoxidation	GKPAVGDMLRKSSDS CCCCHHHHHHHCCCC	2.99	21406390
301	Methylation	PAVGDMLRKSSDSKP CCHHHHHHHCCCCCC	30.12	-
302	Ubiquitination	AVGDMLRKSSDSKPG CHHHHHHHCCCCCCC	50.80	-
303	Phosphorylation	VGDMLRKSSDSKPGV HHHHHHHCCCCCCCC	32.70	26657352
304	Phosphorylation	GDMLRKSSDSKPGVS HHHHHHCCCCCCCCC	49.27	26055452
306	Phosphorylation	MLRKSSDSKPGVSSK HHHHCCCCCCCCCCC	42.57	29396449
307	Sumoylation	LRKSSDSKPGVSSKK HHHCCCCCCCCCCCC	51.27	28112733
311	Phosphorylation	SDSKPGVSSKKFDDR CCCCCCCCCCCCCCC	42.21	29396449
312	Phosphorylation	DSKPGVSSKKFDDRP CCCCCCCCCCCCCCC	37.14	29396449
313	Acetylation	SKPGVSSKKFDDRPK CCCCCCCCCCCCCCC	50.37	30586609
322	Acetylation	FDDRPKGKHASAVAS CCCCCCCCCCCCCCC	41.97	26051181
330	Acetylation	HASAVASKEDSWTLF CCCCCCCCCCCCCCC	56.66	26051181
333	Phosphorylation	AVASKEDSWTLFKPP CCCCCCCCCCCCCCC	24.05	25159151
338	Acetylation	EDSWTLFKPPPVFPV CCCCCCCCCCCCCCC	60.78	26051181
338	Ubiquitination	EDSWTLFKPPPVFPV CCCCCCCCCCCCCCC	60.78	29967540
348	Phosphorylation	PVFPVDNSSAKIVPK CCCCCCCCCCEECCC	27.49	25627689
349	Phosphorylation	VFPVDNSSAKIVPKI CCCCCCCCCEECCCC	39.57	25627689
355	Ubiquitination	SSAKIVPKISYASKV CCCEECCCCHHHHHH	33.13	29967540
368	Acetylation	KVKENLNKTIQNSSV HHHHHHCHHHHCCCC	50.61	19413330
369	Phosphorylation	VKENLNKTIQNSSVS HHHHHCHHHHCCCCC	27.07	21712546
373	Phosphorylation	LNKTIQNSSVSPTSS HCHHHHCCCCCCCCC	18.75	30631047
374	O-linked_Glycosylation	NKTIQNSSVSPTSSS CHHHHCCCCCCCCCC	33.88	22661428
374	Phosphorylation	NKTIQNSSVSPTSSS CHHHHCCCCCCCCCC	33.88	25159151
376	O-linked_Glycosylation	TIQNSSVSPTSSSSS HHHCCCCCCCCCCCC	25.14	22661428
376	Phosphorylation	TIQNSSVSPTSSSSS HHHCCCCCCCCCCCC	25.14	30278072
378	Phosphorylation	QNSSVSPTSSSSSSS HCCCCCCCCCCCCCC	33.46	30278072
379	Phosphorylation	NSSVSPTSSSSSSSS CCCCCCCCCCCCCCC	31.44	30278072
380	Phosphorylation	SSVSPTSSSSSSSST CCCCCCCCCCCCCCC	36.40	25159151
381	O-linked_Glycosylation	SVSPTSSSSSSSSTG CCCCCCCCCCCCCCC	33.72	22661428
381	Phosphorylation	SVSPTSSSSSSSSTG CCCCCCCCCCCCCCC	33.72	25159151
382	O-linked_Glycosylation	VSPTSSSSSSSSTGE CCCCCCCCCCCCCCC	35.87	22661428
382	Phosphorylation	VSPTSSSSSSSSTGE CCCCCCCCCCCCCCC	35.87	25159151
383	Phosphorylation	SPTSSSSSSSSTGET CCCCCCCCCCCCCCC	35.87	25159151
384	O-linked_Glycosylation	PTSSSSSSSSTGETQ CCCCCCCCCCCCCCC	30.20	22661428
384	Phosphorylation	PTSSSSSSSSTGETQ CCCCCCCCCCCCCCC	30.20	25159151
385	O-linked_Glycosylation	TSSSSSSSSTGETQT CCCCCCCCCCCCCCC	33.59	22661428
385	Phosphorylation	TSSSSSSSSTGETQT CCCCCCCCCCCCCCC	33.59	23663014
386	Phosphorylation	SSSSSSSSTGETQTQ CCCCCCCCCCCCCCC	42.24	23663014
387	O-linked_Glycosylation	SSSSSSSTGETQTQS CCCCCCCCCCCCCCC	40.77	22661428
387	Phosphorylation	SSSSSSSTGETQTQS CCCCCCCCCCCCCCC	40.77	23663014
390	Phosphorylation	SSSSTGETQTQSSSR CCCCCCCCCCCCCHH	37.96	23663014
392	Phosphorylation	SSTGETQTQSSSRLS CCCCCCCCCCCHHHH	37.53	24732914
394	Phosphorylation	TGETQTQSSSRLSQV CCCCCCCCCHHHHHC	33.40	27251789
395	Phosphorylation	GETQTQSSSRLSQVP CCCCCCCCHHHHHCC	15.06	24732914
396	Phosphorylation	ETQTQSSSRLSQVPM CCCCCCCHHHHHCCH	42.35	24732914
399	Phosphorylation	TQSSSRLSQVPMSAL CCCCHHHHHCCHHHH	28.20	28674419
403	Sulfoxidation	SRLSQVPMSALKSVT HHHHHCCHHHHHHHH	3.73	21406390
404	Phosphorylation	RLSQVPMSALKSVTS HHHHCCHHHHHHHHC	25.12	20068231
437	O-linked_Glycosylation	PGGQPLLTTAANTLT CCCCCCCCCCCCCCC	23.28	22661428
510	Phosphorylation	FQNQWGLSFINEPSA HHHCCCCEECCCCCC	21.83	46156005
540	Phosphorylation	EVTFQGEYPATLVSQ EEEECCCCCCEEEEC	12.65	132349
565	Phosphorylation	HPVFPKAYELEKRTS CCCCCCHHHCCCCCC	27.46	24732914
569	Ubiquitination	PKAYELEKRTSPQVL CCHHHCCCCCCHHHH	73.86	-
571	Phosphorylation	AYELEKRTSPQVLGS HHHCCCCCCHHHHHH	56.69	29255136
572	Phosphorylation	YELEKRTSPQVLGSI HHCCCCCCHHHHHHH	19.85	29255136
578	Phosphorylation	TSPQVLGSILKSGTT CCHHHHHHHHHCCCC	22.16	23927012
582	Phosphorylation	VLGSILKSGTTSESG HHHHHHHCCCCCCCC	37.62	25159151
584	Phosphorylation	GSILKSGTTSESGAL HHHHHCCCCCCCCCC	33.95	25159151
585	Phosphorylation	SILKSGTTSESGALS HHHHCCCCCCCCCCC	33.74	25159151
586	Phosphorylation	ILKSGTTSESGALSL HHHCCCCCCCCCCCC	29.60	25159151
588	Phosphorylation	KSGTTSESGALSLEP HCCCCCCCCCCCCCH	29.18	28555341
592	Phosphorylation	TSESGALSLEPSHIG CCCCCCCCCCHHHCC	30.10	28985074
596	Phosphorylation	GALSLEPSHIGDLQK CCCCCCHHHCCCCCC	20.54	28555341
603	Ubiquitination	SHIGDLQKADTSSQG HHCCCCCCCCCCCCC	56.37	29967540
606	Phosphorylation	GDLQKADTSSQGALV CCCCCCCCCCCCEEE	34.83	29255136
607	Phosphorylation	DLQKADTSSQGALVF CCCCCCCCCCCEEEE	22.63	29255136
608	Phosphorylation	LQKADTSSQGALVFL CCCCCCCCCCEEEEE	34.42	17525332
616	Phosphorylation	QGALVFLSKDYEIES CCEEEEECCCCEECC	16.41	21815630
619	Phosphorylation	LVFLSKDYEIESQNP EEEECCCCEECCCCC	23.65	22167270
623	Phosphorylation	SKDYEIESQNPLASP CCCCEECCCCCCCCC	40.70	22167270
629	Phosphorylation	ESQNPLASPTNTLLG CCCCCCCCCCCCHHC	39.68	19664994
631	Phosphorylation	QNPLASPTNTLLGSA CCCCCCCCCCHHCCH	38.04	29255136
633	Phosphorylation	PLASPTNTLLGSAKE CCCCCCCCHHCCHHH	26.32	22167270
637	Phosphorylation	PTNTLLGSAKEQRYQ CCCCHHCCHHHHHHH	35.82	22167270
652	Phosphorylation	RGLERNDSWGSFDLR HHCCCCCCCCCCHHH	36.56	19664994
655	Phosphorylation	ERNDSWGSFDLRAAI CCCCCCCCCHHHHHE	14.88	30266825
667	Acetylation	AAIVYHTKEMESIWN HHEEEEHHHHHHHHC	41.57	26051181
685	Phosphorylation	QDPKRIITYNEAMDS CCCCCEEECHHHCCC	20.23	29449344
686	Phosphorylation	DPKRIITYNEAMDSP CCCCEEECHHHCCCC	10.70	30266825
692	Phosphorylation	TYNEAMDSPDQ---- ECHHHCCCCCC----	19.79	30266825

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 NUFP2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NUFP2_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 NUFP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FMR1_HUMAN	FMR1	physical	12837692
KR412_HUMAN	KRTAP4-12	physical	25416956
KRA32_HUMAN	KRTAP3-2	physical	25416956
KRA92_HUMAN	KRTAP9-2	physical	25416956
KRA94_HUMAN	KRTAP9-4	physical	25416956
KRA42_HUMAN	KRTAP4-2	physical	25416956
KRA33_HUMAN	KRTAP3-3	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
KRA56_HUMAN	KRTAP5-6	physical	25416956
KR411_HUMAN	KRTAP4-11	physical	25416956
ATX2L_HUMAN	ATXN2L	physical	28514442
LSM12_HUMAN	LSM12	physical	28514442
G3BP1_HUMAN	G3BP1	physical	28514442
ATX2_HUMAN	ATXN2	physical	28514442
TF65_HUMAN	RELA	physical	28514442
TRI11_HUMAN	TRIM11	physical	28514442
AGAP3_HUMAN	AGAP3	physical	27173435

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 NUFP2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-140, AND MASS SPECTROMETRY.	19608861 [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-112; SER-212; SER-376;SER-572; SER-629; SER-637 AND SER-652, AND MASS 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-112; SER-212; SER-629AND SER-652, AND MASS SPECTROMETRY.	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-112; SER-212; SER-214;TYR-218; THR-220; SER-376; THR-378; SER-629; THR-631 AND SER-652, ANDMASS 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-112; SER-113; SER-212;SER-214; SER-216; TYR-218; THR-219; THR-220; SER-572; SER-629;SER-637; SER-652 AND SER-692, 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-572; SER-629 ANDSER-652, 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-376; THR-378 ANDSER-652, 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-629, AND MASSSPECTROMETRY.	18187866 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, AND MASSSPECTROMETRY.	17525332 [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 THR-87; SER-572 AND SER-629,AND MASS 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-212 AND THR-220, 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-572 AND SER-652, ANDMASS 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-652, AND MASSSPECTROMETRY.	15144186 [Abstract]