dbPTM

TPIS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPIS_HUMAN
UniProt AC	P60174
Protein Name	Triosephosphate isomerase
Gene Name	TPI1
Organism	Homo sapiens (Human).
Sequence Length	286
Subcellular Localization
Protein Description
Protein Sequence	MAEDGEEAEFHFAALYISGQWPRLRADTDLQRLGSSAMAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Ubiquitination	EAEFHFAALYISGQW CCEEEEEEEHHCCCC	10.43	21890473
14	Acetylation	EAEFHFAALYISGQW CCEEEEEEEHHCCCC	10.43	19608861
14 (in isoform 1)	Acetylation	-	10.43	-
16	Phosphorylation	EFHFAALYISGQWPR EEEEEEEHHCCCCHH	6.57	25693802
21	Phosphorylation	ALYISGQWPRLRADT EEHHCCCCHHCCCCC	5.41	19664995
21 (in isoform 1)	Phosphorylation	-	5.41	21406692
28	Phosphorylation	WPRLRADTDLQRLGS CHHCCCCCCHHHHCC	37.31	20068231
28 (in isoform 1)	Phosphorylation	-	37.31	-
35	Phosphorylation	TDLQRLGSSAMAPSR CCHHHHCCCCCCCCC	21.37	30622161
36	Phosphorylation	DLQRLGSSAMAPSRK CHHHHCCCCCCCCCC	21.92	20860994
36 (in isoform 3)	O-linked_Glycosylation	-	21.92	23301498
38 (in isoform 1)	Phosphorylation	-	6.43	21406692
41	Phosphorylation	GSSAMAPSRKFFVGG CCCCCCCCCCEEECC	38.27	20860994
41 (in isoform 3)	O-linked_Glycosylation	-	38.27	23301498
43	2-Hydroxyisobutyrylation	SAMAPSRKFFVGGNW CCCCCCCCEEECCCC	47.71	-
43	Acetylation	SAMAPSRKFFVGGNW CCCCCCCCEEECCCC	47.71	23954790
43	Ubiquitination	SAMAPSRKFFVGGNW CCCCCCCCEEECCCC	47.71	21890473
46 (in isoform 1)	Phosphorylation	-	12.35	21406692
51	Acetylation	FFVGGNWKMNGRKQS EEECCCCCCCCCCCC	26.87	19608861
51	Methylation	FFVGGNWKMNGRKQS EEECCCCCCCCCCCC	26.87	22632985
51	Ubiquitination	FFVGGNWKMNGRKQS EEECCCCCCCCCCCC	26.87	21890473
56	2-Hydroxyisobutyrylation	NWKMNGRKQSLGELI CCCCCCCCCCHHHHH	45.71	-
56	Ubiquitination	NWKMNGRKQSLGELI CCCCCCCCCCHHHHH	45.71	-
58	Phosphorylation	KMNGRKQSLGELIGT CCCCCCCCHHHHHHH	41.18	29255136
59	Ubiquitination	MNGRKQSLGELIGTL CCCCCCCHHHHHHHH	5.98	21890473
59 (in isoform 1)	Ubiquitination	-	5.98	21890473
65	Phosphorylation	SLGELIGTLNAAKVP CHHHHHHHHHHCCCC	15.17	23927012
68	Nitration	ELIGTLNAAKVPADT HHHHHHHHCCCCCCC	16.27	-
69	Ubiquitination	LIGTLNAAKVPADTE HHHHHHHCCCCCCCE	16.59	21890473
69 (in isoform 1)	Ubiquitination	-	16.59	21890473
70	Ubiquitination	IGTLNAAKVPADTEV HHHHHHCCCCCCCEE	46.47	-
71	Phosphorylation	GTLNAAKVPADTEVV HHHHHCCCCCCCEEE	3.97	20068231
71 (in isoform 1)	Phosphorylation	-	3.97	-
75	Phosphorylation	AAKVPADTEVVCAPP HCCCCCCCEEEECCC	32.55	28464451
79	Glutathionylation	PADTEVVCAPPTAYI CCCCEEEECCCCCHH	5.93	22555962
79	S-palmitoylation	PADTEVVCAPPTAYI CCCCEEEECCCCCHH	5.93	29575903
80	Phosphorylation	ADTEVVCAPPTAYID CCCEEEECCCCCHHH	11.07	19413330
80 (in isoform 1)	Phosphorylation	-	11.07	-
83	Phosphorylation	EVVCAPPTAYIDFAR EEEECCCCCHHHHHH	30.91	28796482
85	Phosphorylation	VCAPPTAYIDFARQK EECCCCCHHHHHHHH	11.96	28796482
96	2-Hydroxyisobutyrylation	ARQKLDPKIAVAAQN HHHHCCHHHHHEECC	42.86	-
96	Acetylation	ARQKLDPKIAVAAQN HHHHCCHHHHHEECC	42.86	23236377
96	Ubiquitination	ARQKLDPKIAVAAQN HHHHCCHHHHHEECC	42.86	21890473
104	Glutathionylation	IAVAAQNCYKVTNGA HHHEECCEEEECCCC	2.01	22555962
104	S-palmitoylation	IAVAAQNCYKVTNGA HHHEECCEEEECCCC	2.01	29575903
105	Nitrated tyrosine	AVAAQNCYKVTNGAF HHEECCEEEECCCCC	18.95	-
105	Phosphorylation	AVAAQNCYKVTNGAF HHEECCEEEECCCCC	18.95	28152594
106	Acetylation	VAAQNCYKVTNGAFT HEECCEEEECCCCCC	44.79	25953088
106	Methylation	VAAQNCYKVTNGAFT HEECCEEEECCCCCC	44.79	70215
106	Phosphorylation	VAAQNCYKVTNGAFT HEECCEEEECCCCCC	44.79	-
106	Ubiquitination	VAAQNCYKVTNGAFT HEECCEEEECCCCCC	44.79	21890473
108	Phosphorylation	AQNCYKVTNGAFTGE ECCEEEECCCCCCCC	24.63	21712546
112	Acetylation	YKVTNGAFTGEISPG EEECCCCCCCCCCCC	10.78	19608861
112	Methylation	YKVTNGAFTGEISPG EEECCCCCCCCCCCC	10.78	19608861
112	Ubiquitination	YKVTNGAFTGEISPG EEECCCCCCCCCCCC	10.78	19608861
113	Phosphorylation	KVTNGAFTGEISPGM EECCCCCCCCCCCCC	33.11	25159151
117	Phosphorylation	GAFTGEISPGMIKDC CCCCCCCCCCCEECC	15.88	29255136
120	Sulfoxidation	TGEISPGMIKDCGAT CCCCCCCCEECCCCE	3.80	21406390
122	Acetylation	EISPGMIKDCGATWV CCCCCCEECCCCEEE	37.77	26051181
122	Ubiquitination	EISPGMIKDCGATWV CCCCCCEECCCCEEE	37.77	-
124	Glutathionylation	SPGMIKDCGATWVVL CCCCEECCCCEEEEE	3.20	22555962
124	S-palmitoylation	SPGMIKDCGATWVVL CCCCEECCCCEEEEE	3.20	29575903
127	Phosphorylation	MIKDCGATWVVLGHS CEECCCCEEEEEECC	12.22	28857561
134	Phosphorylation	TWVVLGHSERRHVFG EEEEEECCCCCCCCC	30.88	28857561
137	Methylation	VLGHSERRHVFGESD EEECCCCCCCCCCCH	26.69	115918793
142	Ubiquitination	ERRHVFGESDELIGQ CCCCCCCCCHHHHHH	43.48	21890473
142 (in isoform 1)	Ubiquitination	-	43.48	21890473
143	Phosphorylation	RRHVFGESDELIGQK CCCCCCCCHHHHHHH	36.44	19764811
149	Ubiquitination	ESDELIGQKVAHALA CCHHHHHHHHHHHHH	30.01	21890473
149	Succinylation	ESDELIGQKVAHALA CCHHHHHHHHHHHHH	30.01	-
149 (in isoform 1)	Ubiquitination	-	30.01	21890473
156	Ubiquitination	QKVAHALAEGLGVIA HHHHHHHHHCCCEEE	15.03	21890473
156	Acetylation	QKVAHALAEGLGVIA HHHHHHHHHCCCEEE	15.03	19608861
156	Succinylation	QKVAHALAEGLGVIA HHHHHHHHHCCCEEE	15.03	-
156	Ubiquitination	QKVAHALAEGLGVIA HHHHHHHHHCCCEEE	15.03	19608861
156 (in isoform 1)	Ubiquitination	-	15.03	21890473
159	Phosphorylation	AHALAEGLGVIACIG HHHHHHCCCEEEEEE	3.59	-
160	Ubiquitination	HALAEGLGVIACIGE HHHHHCCCEEEEEEC	21.46	21890473
160 (in isoform 1)	Ubiquitination	-	21.46	21890473
164	Glutathionylation	EGLGVIACIGEKLDE HCCCEEEEEECCCCH	2.56	22555962
164	S-palmitoylation	EGLGVIACIGEKLDE HCCCEEEEEECCCCH	2.56	29575903
168	2-Hydroxyisobutyrylation	VIACIGEKLDEREAG EEEEEECCCCHHCCC	56.90	-
168	Acetylation	VIACIGEKLDEREAG EEEEEECCCCHHCCC	56.90	26051181
168	Ubiquitination	VIACIGEKLDEREAG EEEEEECCCCHHCCC	56.90	-
172	Methylation	IGEKLDEREAGITEK EECCCCHHCCCCCCE	38.44	115918797
173	Phosphorylation	GEKLDEREAGITEKV ECCCCHHCCCCCCEE	49.56	-
175	Ubiquitination	KLDEREAGITEKVVF CCCHHCCCCCCEEEE	23.69	21890473
175	Ubiquitination	KLDEREAGITEKVVF CCCHHCCCCCCEEEE	23.69	21139048
175 (in isoform 1)	Ubiquitination	-	23.69	21890473
177	Phosphorylation	DEREAGITEKVVFEQ CHHCCCCCCEEEEEE	28.92	-
179	2-Hydroxyisobutyrylation	REAGITEKVVFEQTK HCCCCCCEEEEEEEE	34.74	-
179	Acetylation	REAGITEKVVFEQTK HCCCCCCEEEEEEEE	34.74	23954790
179	Sumoylation	REAGITEKVVFEQTK HCCCCCCEEEEEEEE	34.74	25114211
179	Ubiquitination	REAGITEKVVFEQTK HCCCCCCEEEEEEEE	34.74	21890473
186	2-Hydroxyisobutyrylation	KVVFEQTKVIADNVK EEEEEEEEEEECCCC	31.19	-
186	Acetylation	KVVFEQTKVIADNVK EEEEEEEEEEECCCC	31.19	23954790
186	Succinylation	KVVFEQTKVIADNVK EEEEEEEEEEECCCC	31.19	-
186	Succinylation	KVVFEQTKVIADNVK EEEEEEEEEEECCCC	31.19	21890473
186	Ubiquitination	KVVFEQTKVIADNVK EEEEEEEEEEECCCC	31.19	-
188	Ubiquitination	VFEQTKVIADNVKDW EEEEEEEEECCCCCH	4.20	21890473
188	Acetylation	VFEQTKVIADNVKDW EEEEEEEEECCCCCH	4.20	19608861
188 (in isoform 1)	Acetylation	-	4.20	-
188 (in isoform 1)	Ubiquitination	-	4.20	21890473
193	2-Hydroxyisobutyrylation	KVIADNVKDWSKVVL EEEECCCCCHHHEEE	60.79	-
193	Acetylation	KVIADNVKDWSKVVL EEEECCCCCHHHEEE	60.79	23954790
193	Succinylation	KVIADNVKDWSKVVL EEEECCCCCHHHEEE	60.79	-
193	Succinylation	KVIADNVKDWSKVVL EEEECCCCCHHHEEE	60.79	23954790
193	Ubiquitination	KVIADNVKDWSKVVL EEEECCCCCHHHEEE	60.79	-
194	Ubiquitination	VIADNVKDWSKVVLA EEECCCCCHHHEEEE	51.07	21890473
194	Acetylation	VIADNVKDWSKVVLA EEECCCCCHHHEEEE	51.07	19608861
194	Methylation	VIADNVKDWSKVVLA EEECCCCCHHHEEEE	51.07	24129315
194	Succinylation	VIADNVKDWSKVVLA EEECCCCCHHHEEEE	51.07	-
194 (in isoform 1)	Acetylation	-	51.07	-
194 (in isoform 1)	Ubiquitination	-	51.07	21890473
195	Phosphorylation	IADNVKDWSKVVLAY EECCCCCHHHEEEEE	8.37	20068231
195 (in isoform 1)	Phosphorylation	-	8.37	-
196	Phosphorylation	ADNVKDWSKVVLAYE ECCCCCHHHEEEEEE	26.21	28857561
197	Ubiquitination	DNVKDWSKVVLAYEP CCCCCHHHEEEEEEE	31.91	21890473
198	Phosphorylation	NVKDWSKVVLAYEPV CCCCHHHEEEEEEEE	3.39	20068231
198 (in isoform 1)	Phosphorylation	-	3.39	-
202	Phosphorylation	WSKVVLAYEPVWAIG HHHEEEEEEEEEEEC	19.32	28796482
204	Phosphorylation	KVVLAYEPVWAIGTG HEEEEEEEEEEECCC	17.80	20068231
204 (in isoform 1)	Phosphorylation	-	17.80	-
209	Nitration	YEPVWAIGTGKTATP EEEEEEECCCCCCCH	22.22	-
210	Phosphorylation	EPVWAIGTGKTATPQ EEEEEECCCCCCCHH	29.41	28152594
212	Acetylation	VWAIGTGKTATPQQA EEEECCCCCCCHHHH	34.52	25953088
212	Phosphorylation	VWAIGTGKTATPQQA EEEECCCCCCCHHHH	34.52	23186163
212	Ubiquitination	VWAIGTGKTATPQQA EEEECCCCCCCHHHH	34.52	21890473
213	Phosphorylation	WAIGTGKTATPQQAQ EEECCCCCCCHHHHH	36.79	25159151
214	Phosphorylation	AIGTGKTATPQQAQE EECCCCCCCHHHHHH	22.29	24275569
215	Phosphorylation	IGTGKTATPQQAQEV ECCCCCCCHHHHHHH	27.19	28985074
218	S-nitrosylation	GKTATPQQAQEVHEK CCCCCHHHHHHHHHH	46.33	19483679
223	Phosphorylation	PQQAQEVHEKLRGWL HHHHHHHHHHHHHHH	26.22	24275569
225	2-Hydroxyisobutyrylation	QAQEVHEKLRGWLKS HHHHHHHHHHHHHHH	28.71	-
225	Acetylation	QAQEVHEKLRGWLKS HHHHHHHHHHHHHHH	28.71	16916647
225	Ubiquitination	QAQEVHEKLRGWLKS HHHHHHHHHHHHHHH	28.71	21890473
231	Acetylation	EKLRGWLKSNVSDAV HHHHHHHHHCHHHHH	33.21	19608861
231	Malonylation	EKLRGWLKSNVSDAV HHHHHHHHHCHHHHH	33.21	26320211
231	Methylation	EKLRGWLKSNVSDAV HHHHHHHHHCHHHHH	33.21	24129315
231	Succinylation	EKLRGWLKSNVSDAV HHHHHHHHHCHHHHH	33.21	-
231	Ubiquitination	EKLRGWLKSNVSDAV HHHHHHHHHCHHHHH	33.21	-
232	Phosphorylation	KLRGWLKSNVSDAVA HHHHHHHHCHHHHHH	40.05	29255136
235	Phosphorylation	GWLKSNVSDAVAQST HHHHHCHHHHHHHCC	24.89	29255136
238	Ubiquitination	KSNVSDAVAQSTRII HHCHHHHHHHCCEEE	6.30	21890473
238	Acetylation	KSNVSDAVAQSTRII HHCHHHHHHHCCEEE	6.30	19608861
238 (in isoform 1)	Acetylation	-	6.30	-
238 (in isoform 1)	Ubiquitination	-	6.30	21890473
241	Phosphorylation	VSDAVAQSTRIIYGG HHHHHHHCCEEEECC	15.20	20068231
242	Phosphorylation	SDAVAQSTRIIYGGS HHHHHHCCEEEECCC	17.51	20068231
246	Nitrated tyrosine	AQSTRIIYGGSVTGA HHCCEEEECCCCCCH	17.05	-
246	Phosphorylation	AQSTRIIYGGSVTGA HHCCEEEECCCCCCH	17.05	23927012
249	Phosphorylation	TRIIYGGSVTGATCK CEEEECCCCCCHHHH	16.49	23401153
251	Phosphorylation	IIYGGSVTGATCKEL EEECCCCCCHHHHHH	23.85	30266825
254	Phosphorylation	GGSVTGATCKELASQ CCCCCCHHHHHHHCC	26.00	23927012
255	S-nitrosocysteine	GSVTGATCKELASQP CCCCCHHHHHHHCCC	2.98	-
255	Glutathionylation	GSVTGATCKELASQP CCCCCHHHHHHHCCC	2.98	22555962
256	Phosphoglycerylation	SVTGATCKELASQPD CCCCHHHHHHHCCCC	51.94	-
256	Ubiquitination	SVTGATCKELASQPD CCCCHHHHHHHCCCC	51.94	-
260	Phosphorylation	ATCKELASQPDVDGF HHHHHHHCCCCCCCE	55.67	28857561
273	Phosphorylation	GFLVGGASLKPEFVD CEEECCCCCCHHHHH	39.95	28857561
275	Acetylation	LVGGASLKPEFVDII EECCCCCCHHHHHHH	39.75	19608861
275	Malonylation	LVGGASLKPEFVDII EECCCCCCHHHHHHH	39.75	26320211
275	Ubiquitination	LVGGASLKPEFVDII EECCCCCCHHHHHHH	39.75	-
285	Acetylation	FVDIINAKQ------ HHHHHCCCC------	52.64	70211
285	Succinylation	FVDIINAKQ------ HHHHHCCCC------	52.64	23954790
285	Ubiquitination	FVDIINAKQ------ HHHHHCCCC------	52.64	-

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 TPIS_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SETB1_HUMAN	SETDB1	physical	16169070
TPIS_HUMAN	TPI1	physical	8609635
A4_HUMAN	APP	physical	21832049
RL40_HUMAN	UBA52	physical	22939629
VINC_HUMAN	VCL	physical	22939629
ALDR_HUMAN	AKR1B1	physical	26344197
AN32E_HUMAN	ANP32E	physical	26344197
ASSY_HUMAN	ASS1	physical	26344197
CRIP1_HUMAN	CRIP1	physical	26344197
ESTD_HUMAN	ESD	physical	26344197
HNRPR_HUMAN	HNRNPR	physical	26344197
NDUV1_HUMAN	NDUFV1	physical	26344197
PGM2_HUMAN	PGM2	physical	26344197
PGM2L_HUMAN	PGM2L1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615512	Triosephosphate isomerase deficiency (TPID)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TPIS_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-51; LYS-225; LYS-231 ANDLYS-275, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-225, AND MASS SPECTROMETRY.	16916647 [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-58 AND SER-117, AND MASSSPECTROMETRY.	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-58 AND SER-117, 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-58, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASSSPECTROMETRY.	19367720 [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-58, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASSSPECTROMETRY.	17693683 [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-58, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Phosphoproteomic analysis of the human pituitary."; Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; Pituitary 9:109-120(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASSSPECTROMETRY.	16807684 [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-58, AND MASSSPECTROMETRY.	17081983 [Abstract]