dbPTM

PUR6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PUR6_HUMAN
UniProt AC	P22234
Protein Name	Multifunctional protein ADE2
Gene Name	PAICS
Organism	Homo sapiens (Human).
Sequence Length	425
Subcellular Localization
Protein Description
Protein Sequence	MATAEVLNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTRKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPEGLQMVKKNFEWVAERVELLLKSESQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIPTVFVAVAGRSNGLGPVMSGNTAYPVISCPPLTPDWGVQDVWSSLRLPSGLGCSTVLSPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKIRECNL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATAEVLNI ------CCHHHHHHH	18.60	22223895
3	Phosphorylation	-----MATAEVLNIG -----CCHHHHHHHH	23.27	19651622
11	Acetylation	AEVLNIGKKLYEGKT HHHHHHHHHHHCCCC	35.49	25953088
11	Succinylation	AEVLNIGKKLYEGKT HHHHHHHHHHHCCCC	35.49	23954790
11	Ubiquitination	AEVLNIGKKLYEGKT HHHHHHHHHHHCCCC	35.49	23000965
11 (in isoform 2)	Ubiquitination	-	35.49	-
11	Ubiquitination	AEVLNIGKKLYEGKT HHHHHHHHHHHCCCC	35.49	21890473
12	Ubiquitination	EVLNIGKKLYEGKTK HHHHHHHHHHCCCCH	51.60	23000965
14	Phosphorylation	LNIGKKLYEGKTKEV HHHHHHHHCCCCHHH	31.36	24719451
17	Acetylation	GKKLYEGKTKEVYEL HHHHHCCCCHHHHHH	44.47	25953088
17	Ubiquitination	GKKLYEGKTKEVYEL HHHHHCCCCHHHHHH	44.47	23000965
18	Phosphorylation	KKLYEGKTKEVYELL HHHHCCCCHHHHHHH	43.21	21945579
19	Acetylation	KLYEGKTKEVYELLD HHHCCCCHHHHHHHC	48.98	27452117
19	Ubiquitination	KLYEGKTKEVYELLD HHHCCCCHHHHHHHC	48.98	23000965
19 (in isoform 2)	Ubiquitination	-	48.98	-
22	Nitration	EGKTKEVYELLDSPG CCCCHHHHHHHCCCC	11.27	-
22	Phosphorylation	EGKTKEVYELLDSPG CCCCHHHHHHHCCCC	11.27	21945579
27	Phosphorylation	EVYELLDSPGKVLLQ HHHHHHCCCCCEEEE	35.21	19664994
30	Acetylation	ELLDSPGKVLLQSKD HHHCCCCCEEEEEHH	32.85	23954790
30	Ubiquitination	ELLDSPGKVLLQSKD HHHCCCCCEEEEEHH	32.85	23000965
30 (in isoform 2)	Ubiquitination	-	32.85	-
30	Ubiquitination	ELLDSPGKVLLQSKD HHHCCCCCEEEEEHH	32.85	21890473
35	Phosphorylation	PGKVLLQSKDQITAG CCCEEEEEHHHCCCC	37.86	23927012
36	Acetylation	GKVLLQSKDQITAGN CCEEEEEHHHCCCCH	40.46	-
36	Succinylation	GKVLLQSKDQITAGN CCEEEEEHHHCCCCH	40.46	23954790
36	Ubiquitination	GKVLLQSKDQITAGN CCEEEEEHHHCCCCH	40.46	23000965
36 (in isoform 2)	Ubiquitination	-	40.46	-
36	Ubiquitination	GKVLLQSKDQITAGN CCEEEEEHHHCCCCH	40.46	21890473
40	Phosphorylation	LQSKDQITAGNAARK EEEHHHCCCCHHHHH	23.91	26074081
45	Ubiquitination	QITAGNAARKNHLEG HCCCCHHHHHHCCCH	27.29	21890473
47	Ubiquitination	TAGNAARKNHLEGKA CCCHHHHHHCCCHHH	43.95	29967540
53	Acetylation	RKNHLEGKAAISNKI HHHCCCHHHHHHHHH	25.85	19608861
53	Ubiquitination	RKNHLEGKAAISNKI HHHCCCHHHHHHHHH	25.85	27667366
56	Ubiquitination	HLEGKAAISNKITSC CCCHHHHHHHHHHHH	5.80	21890473
61	Phosphorylation	AAISNKITSCIFQLL HHHHHHHHHHHHHHH	21.11	24043423
62	Phosphorylation	AISNKITSCIFQLLQ HHHHHHHHHHHHHHH	14.53	24043423
62	Ubiquitination	AISNKITSCIFQLLQ HHHHHHHHHHHHHHH	14.53	21890473
63	Glutathionylation	ISNKITSCIFQLLQE HHHHHHHHHHHHHHH	2.43	22555962
63	S-palmitoylation	ISNKITSCIFQLLQE HHHHHHHHHHHHHHH	2.43	29575903
74	Ubiquitination	LLQEAGIKTAFTRKC HHHHCCCCEEEECCC	32.65	21906983
79	Ubiquitination	GIKTAFTRKCGETAF CCCEEEECCCCCEEE	26.30	21890473
80	Ubiquitination	IKTAFTRKCGETAFI CCEEEECCCCCEEEE	43.46	21963094
81	Glutathionylation	KTAFTRKCGETAFIA CEEEECCCCCEEEEC	5.54	22555962
87	Ubiquitination	KCGETAFIAPQCEMI CCCCEEEECCCCEEE	5.18	21963094
100	Ubiquitination	MIPIEWVCRRIATGS EECHHHHHHHHHCCC	2.25	21890473
105	Phosphorylation	WVCRRIATGSFLKRN HHHHHHHCCCHHHCC	30.87	30266825
107	Phosphorylation	CRRIATGSFLKRNPG HHHHHCCCHHHCCCC	24.05	25159151
110	Acetylation	IATGSFLKRNPGVKE HHCCCHHHCCCCCCC	48.39	23749302
110	Ubiquitination	IATGSFLKRNPGVKE HHCCCHHHCCCCCCC	48.39	23000965
114	Phosphorylation	SFLKRNPGVKEGYKF CHHHCCCCCCCCCCC	46.83	24719451
116	Succinylation	LKRNPGVKEGYKFYP HHCCCCCCCCCCCCC	51.87	23954790
116	Ubiquitination	LKRNPGVKEGYKFYP HHCCCCCCCCCCCCC	51.87	23000965
117	Ubiquitination	KRNPGVKEGYKFYPP HCCCCCCCCCCCCCC	66.41	23000965
117 (in isoform 2)	Ubiquitination	-	66.41	-
117	Ubiquitination	KRNPGVKEGYKFYPP HCCCCCCCCCCCCCC	66.41	21890473
120	Acetylation	PGVKEGYKFYPPKVE CCCCCCCCCCCCEEE	49.64	25953088
120	Ubiquitination	PGVKEGYKFYPPKVE CCCCCCCCCCCCEEE	49.64	22817900
122	Phosphorylation	VKEGYKFYPPKVELF CCCCCCCCCCEEEEE	17.93	-
123	Ubiquitination	KEGYKFYPPKVELFF CCCCCCCCCEEEEEE	25.93	23000965
125	Ubiquitination	GYKFYPPKVELFFKD CCCCCCCEEEEEEEC	43.78	22817900
127	Ubiquitination	KFYPPKVELFFKDDA CCCCCEEEEEEECCC	46.08	22817900
131	Acetylation	PKVELFFKDDANNDP CEEEEEEECCCCCCC	47.57	26051181
131	Ubiquitination	PKVELFFKDDANNDP CEEEEEEECCCCCCC	47.57	21906983
132	Ubiquitination	KVELFFKDDANNDPQ EEEEEEECCCCCCCC	55.91	21890473
132	Ubiquitination	KVELFFKDDANNDPQ EEEEEEECCCCCCCC	55.91	21890473
136	Ubiquitination	FFKDDANNDPQWSEE EEECCCCCCCCCCHH	65.15	21890473
138	Ubiquitination	KDDANNDPQWSEEQL ECCCCCCCCCCHHHH	39.40	21963094
138 (in isoform 2)	Ubiquitination	-	39.40	-
142	Ubiquitination	NNDPQWSEEQLIAAK CCCCCCCHHHHHHHH	46.97	21890473
151	Ubiquitination	QLIAAKFCFAGLLIG HHHHHHHHHHHHHCC	1.94	21890473
157	Ubiquitination	FCFAGLLIGQTEVDI HHHHHHHCCCCHHHH	4.64	21890473
179	Phosphorylation	IFEILEKSWLPQNCT HHHHHHHHCCCCCCE	25.19	21712546
213	Phosphorylation	ADVIDNDSWRLWPSG EECCCCCCEEECCCC	21.98	21712546
222	Methylation	RLWPSGDRSQQKDKQ EECCCCCHHHHCCHH	39.63	115486359
223	Phosphorylation	LWPSGDRSQQKDKQS ECCCCCHHHHCCHHH	41.52	25159151
228	Ubiquitination	DRSQQKDKQSYRDLK CHHHHCCHHHHHHHH	48.45	24816145
230	Phosphorylation	SQQKDKQSYRDLKEV HHHCCHHHHHHHHHH	28.07	25849741
231	Phosphorylation	QQKDKQSYRDLKEVT HHCCHHHHHHHHHHC	12.97	30576142
235	Acetylation	KQSYRDLKEVTPEGL HHHHHHHHHHCHHHH	55.20	23236377
235	Neddylation	KQSYRDLKEVTPEGL HHHHHHHHHHCHHHH	55.20	32015554
235	Ubiquitination	KQSYRDLKEVTPEGL HHHHHHHHHHCHHHH	55.20	21906983
237	Phosphorylation	SYRDLKEVTPEGLQM HHHHHHHHCHHHHHH	11.77	27251275
238	Phosphorylation	YRDLKEVTPEGLQMV HHHHHHHCHHHHHHH	19.40	29255136
242	Neddylation	KEVTPEGLQMVKKNF HHHCHHHHHHHHHHH	2.57	32015554
242	Ubiquitination	KEVTPEGLQMVKKNF HHHCHHHHHHHHHHH	2.57	27667366
242 (in isoform 2)	Ubiquitination	-	2.57	-
244	Sulfoxidation	VTPEGLQMVKKNFEW HCHHHHHHHHHHHHH	6.00	21406390
245	Phosphorylation	TPEGLQMVKKNFEWV CHHHHHHHHHHHHHH	5.28	24719451
246	Acetylation	PEGLQMVKKNFEWVA HHHHHHHHHHHHHHH	36.34	23749302
246	Ubiquitination	PEGLQMVKKNFEWVA HHHHHHHHHHHHHHH	36.34	21906983
247	Acetylation	EGLQMVKKNFEWVAE HHHHHHHHHHHHHHH	56.30	19608861
247	Malonylation	EGLQMVKKNFEWVAE HHHHHHHHHHHHHHH	56.30	26320211
247	Ubiquitination	EGLQMVKKNFEWVAE HHHHHHHHHHHHHHH	56.30	22817900
253	Ubiquitination	KKNFEWVAERVELLL HHHHHHHHHHHHHHH	10.43	27667366
253 (in isoform 2)	Ubiquitination	-	10.43	-
254	Acetylation	KNFEWVAERVELLLK HHHHHHHHHHHHHHC	47.87	19608861
254	Ubiquitination	KNFEWVAERVELLLK HHHHHHHHHHHHHHC	47.87	22817900
261	Acetylation	ERVELLLKSESQCRV HHHHHHHCCCCCCEE	52.74	23749302
261	Ubiquitination	ERVELLLKSESQCRV HHHHHHHCCCCCCEE	52.74	21906983
264	Phosphorylation	ELLLKSESQCRVVVL HHHHCCCCCCEEEEE	41.49	19369195
268	Ubiquitination	KSESQCRVVVLMGST CCCCCCEEEEEECCC	4.61	21963094
272	Sulfoxidation	QCRVVVLMGSTSDLG CCEEEEEECCCCHHH	2.42	30846556
272	Ubiquitination	QCRVVVLMGSTSDLG CCEEEEEECCCCHHH	2.42	21890473
273	Ubiquitination	CRVVVLMGSTSDLGH CEEEEEECCCCHHHH	24.50	21890473
274	Phosphorylation	RVVVLMGSTSDLGHC EEEEEECCCCHHHHH	15.69	17224163
275	Phosphorylation	VVVLMGSTSDLGHCE EEEEECCCCHHHHHH	22.11	28450419
276	Phosphorylation	VVLMGSTSDLGHCEK EEEECCCCHHHHHHH	32.32	25159151
281	Phosphorylation	STSDLGHCEKIKKAC CCCHHHHHHHHHHHH	5.59	27251275
283	Acetylation	SDLGHCEKIKKACGN CHHHHHHHHHHHHCC	66.28	23954790
283	Malonylation	SDLGHCEKIKKACGN CHHHHHHHHHHHHCC	66.28	26320211
283	Ubiquitination	SDLGHCEKIKKACGN CHHHHHHHHHHHHCC	66.28	19608861
285	Acetylation	LGHCEKIKKACGNFG HHHHHHHHHHHCCCC	45.44	23749302
285	Ubiquitination	LGHCEKIKKACGNFG HHHHHHHHHHHCCCC	45.44	-
286	Malonylation	GHCEKIKKACGNFGI HHHHHHHHHHCCCCC	53.00	26320211
286	Ubiquitination	GHCEKIKKACGNFGI HHHHHHHHHHCCCCC	53.00	22505724
288	S-palmitoylation	CEKIKKACGNFGIPC HHHHHHHHCCCCCCE	6.68	29575903
290	Acetylation	KIKKACGNFGIPCEL HHHHHHCCCCCCEEE	31.68	19608861
290	Ubiquitination	KIKKACGNFGIPCEL HHHHHHCCCCCCEEE	31.68	29967540
293	Ubiquitination	KACGNFGIPCELRVT HHHCCCCCCEEEEEE	2.86	22505724
295	S-palmitoylation	CGNFGIPCELRVTSA HCCCCCCEEEEEEEC	7.90	29575903
300	Phosphorylation	IPCELRVTSAHKGPD CCEEEEEEECCCCCC	17.48	28122231
301	Phosphorylation	PCELRVTSAHKGPDE CEEEEEEECCCCCCC	26.06	28122231
304	Acetylation	LRVTSAHKGPDETLR EEEEECCCCCCCCEE	72.37	25953088
304	Ubiquitination	LRVTSAHKGPDETLR EEEEECCCCCCCCEE	72.37	23000965
309	Phosphorylation	AHKGPDETLRIKAEY CCCCCCCCEEEEEEE	28.81	20068231
311	Methylation	KGPDETLRIKAEYEG CCCCCCEEEEEEECC	35.46	115486351
311	Ubiquitination	KGPDETLRIKAEYEG CCCCCCEEEEEEECC	35.46	23000965
311 (in isoform 2)	Ubiquitination	-	35.46	-
313	Sumoylation	PDETLRIKAEYEGDG CCCCEEEEEEECCCC	28.82	-
313	Sumoylation	PDETLRIKAEYEGDG CCCCEEEEEEECCCC	28.82	-
313	Ubiquitination	PDETLRIKAEYEGDG CCCCEEEEEEECCCC	28.82	21906983
320	Ubiquitination	KAEYEGDGIPTVFVA EEEECCCCCCEEEEE	38.34	22053931
330	Ubiquitination	TVFVAVAGRSNGLGP EEEEEEECCCCCCCC	27.27	21890473
339	Ubiquitination	SNGLGPVMSGNTAYP CCCCCCCCCCCCCEE	4.83	21890473
345	Phosphorylation	VMSGNTAYPVISCPP CCCCCCCEEEEECCC	8.94	20090780
354	Phosphorylation	VISCPPLTPDWGVQD EEECCCCCCCCCHHH	25.60	27273156
361	Ubiquitination	TPDWGVQDVWSSLRL CCCCCHHHHHHHCCC	41.25	22817900
365	Ubiquitination	GVQDVWSSLRLPSGL CHHHHHHHCCCCCCC	11.20	21963094
366	Ubiquitination	VQDVWSSLRLPSGLG HHHHHHHCCCCCCCC	5.64	22817900
394	Phosphorylation	AAQIFGLSNHLVWSK HHHHHCCCCHHHHHH	23.68	-
400	Phosphorylation	LSNHLVWSKLRASIL CCCHHHHHHHHHHHH	17.84	-
405	Phosphorylation	VWSKLRASILNTWIS HHHHHHHHHHHHHHH	22.60	21406692
409	Phosphorylation	LRASILNTWISLKQA HHHHHHHHHHHHHHH	22.26	21406692
412	Phosphorylation	SILNTWISLKQADKK HHHHHHHHHHHHHHH	22.52	21406692
414	Acetylation	LNTWISLKQADKKIR HHHHHHHHHHHHHHH	36.33	25953088
414	Ubiquitination	LNTWISLKQADKKIR HHHHHHHHHHHHHHH	36.33	22817900
418	Acetylation	ISLKQADKKIRECNL HHHHHHHHHHHHCCC	53.79	25953088
418	Ubiquitination	ISLKQADKKIRECNL HHHHHHHHHHHHCCC	53.79	21963094
419	Ubiquitination	SLKQADKKIRECNL- HHHHHHHHHHHCCC-	47.76	22817900
421	Ubiquitination	KQADKKIRECNL--- HHHHHHHHHCCC---	51.82	22817900
425	Ubiquitination	KKIRECNL------- HHHHHCCC-------	12.88	21963094
426	Ubiquitination	KIRECNL-------- HHHHCCC--------		22817900
440	Ubiquitination	---------------------- ----------------------		21890473

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
27	S	Phosphorylation	Kinase	CDK1	P06493	PSP
27	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PUR6_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 PUR6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CEP76_HUMAN	CEP76	physical	16189514
PUR6_HUMAN	PAICS	physical	16189514
NUD18_HUMAN	NUDT18	physical	16189514
LNX1_HUMAN	LNX1	physical	16189514
CHD3_HUMAN	CHD3	physical	16169070
PUR6_HUMAN	PAICS	physical	16169070
ZPR1_HUMAN	ZPR1	physical	22939629
TTC1_HUMAN	TTC1	physical	22939629
UNK_HUMAN	UNK	physical	22939629
SLD5_HUMAN	GINS4	physical	22939629
CHIP_HUMAN	STUB1	physical	22939629
UBE2B_HUMAN	UBE2B	physical	22939629
RPAP1_HUMAN	RPAP1	physical	22939629
SSA27_HUMAN	SSSCA1	physical	22939629
TACC3_HUMAN	TACC3	physical	22939629
TM177_HUMAN	TMEM177	physical	22939629
AAKG1_HUMAN	PRKAG1	physical	21988832
SMRD1_HUMAN	SMARCD1	physical	21988832
PUR6_HUMAN	PAICS	physical	21988832
QRIC1_HUMAN	QRICH1	physical	22863883
SPT5H_HUMAN	SUPT5H	physical	22863883
SWP70_HUMAN	SWAP70	physical	22863883
PUR6_HUMAN	PAICS	physical	25416956
LMBL2_HUMAN	L3MBTL2	physical	25416956
MRP1_HUMAN	ABCC1	physical	26344197
ASNS_HUMAN	ASNS	physical	26344197
ASSY_HUMAN	ASS1	physical	26344197
PUR9_HUMAN	ATIC	physical	26344197
ETFA_HUMAN	ETFA	physical	26344197
PUR2_HUMAN	GART	physical	26344197
GLOD4_HUMAN	GLOD4	physical	26344197
GLRX5_HUMAN	GLRX5	physical	26344197
HSPB1_HUMAN	HSPB1	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
IMPA2_HUMAN	IMPA2	physical	26344197
MIF_HUMAN	MIF	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PUR4_HUMAN	PFAS	physical	26344197
KPYR_HUMAN	PKLR	physical	26344197
KPYM_HUMAN	PKM	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
RPIA_HUMAN	RPIA	physical	26344197
GLYC_HUMAN	SHMT1	physical	26344197
TKT_HUMAN	TKT	physical	26344197
UGPA_HUMAN	UGP2	physical	26344197

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
DB00128	L-Aspartic Acid

Regulatory Network of PUR6_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-27 AND THR-238, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-53 AND LYS-247, AND MASSSPECTROMETRY.	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-27, 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-27; THR-105; SER-107 ANDTHR-238, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-27 AND THR-238, 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-27; SER-107 AND THR-238,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-27 AND THR-238, AND MASSSPECTROMETRY.	18691976 [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-27, AND MASSSPECTROMETRY.	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-27, AND MASSSPECTROMETRY.	16964243 [Abstract]