dbPTM

TCPG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TCPG_HUMAN
UniProt AC	P49368
Protein Name	T-complex protein 1 subunit gamma
Gene Name	CCT3
Organism	Homo sapiens (Human).
Sequence Length	545
Subcellular Localization	Cytoplasm.
Protein Description	Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin..
Protein Sequence	MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNIINSSITTKAISRWSSLACNIALDAVKMVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANITAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQSRQGGAPDAGQE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MMGHRPVL -------CCCCCCEE	7.01	19413330
5	Methylation	---MMGHRPVLVLSQ ---CCCCCCEEEEEC	19.79	-
11	Phosphorylation	HRPVLVLSQNTKRES CCCEEEEECCCCCCC	17.57	20068231
14	Phosphorylation	VLVLSQNTKRESGRK EEEEECCCCCCCCCC	24.68	20068231
15	2-Hydroxyisobutyrylation	LVLSQNTKRESGRKV EEEECCCCCCCCCCC	62.81	-
15	Acetylation	LVLSQNTKRESGRKV EEEECCCCCCCCCCC	62.81	25953088
15	Malonylation	LVLSQNTKRESGRKV EEEECCCCCCCCCCC	62.81	26320211
15	Sumoylation	LVLSQNTKRESGRKV EEEECCCCCCCCCCC	62.81	28112733
15	Ubiquitination	LVLSQNTKRESGRKV EEEECCCCCCCCCCC	62.81	-
18	Phosphorylation	SQNTKRESGRKVQSG ECCCCCCCCCCCCCC	48.18	26074081
21	Acetylation	TKRESGRKVQSGNIN CCCCCCCCCCCCCCC	48.42	20167786
21	Ubiquitination	TKRESGRKVQSGNIN CCCCCCCCCCCCCCC	48.42	21906983
24	Phosphorylation	ESGRKVQSGNINAAK CCCCCCCCCCCCHHH	36.47	20068231
24 (in isoform 2)	Phosphorylation	-	36.47	20068231
31	Acetylation	SGNINAAKTIADIIR CCCCCHHHHHHHHHH	37.75	20167786
31	Succinylation	SGNINAAKTIADIIR CCCCCHHHHHHHHHH	37.75	23954790
31	Ubiquitination	SGNINAAKTIADIIR CCCCCHHHHHHHHHH	37.75	21890473
32	Phosphorylation	GNINAAKTIADIIRT CCCCHHHHHHHHHHH	19.37	23882029
44	Acetylation	IRTCLGPKSMMKMLL HHHHHCHHHHHHHHH	49.54	20167786
44	Ubiquitination	IRTCLGPKSMMKMLL HHHHHCHHHHHHHHH	49.54	21906983
45	Phosphorylation	RTCLGPKSMMKMLLD HHHHCHHHHHHHHHC	27.52	23532336
49	Sulfoxidation	GPKSMMKMLLDPMGG CHHHHHHHHHCCCCC	2.15	21406390
78	Acetylation	QVQHPAAKSMIEISR EECCHHHHHHEEEEC	42.54	25953088
78	Ubiquitination	QVQHPAAKSMIEISR EECCHHHHHHEEEEC	42.54	21906983
80	Sulfoxidation	QHPAAKSMIEISRTQ CCHHHHHHEEEECCC	2.92	21406390
86	Phosphorylation	SMIEISRTQDEEVGD HHEEEECCCCCCCCC	33.31	-
90	Ubiquitination	ISRTQDEEVGDGTTS EECCCCCCCCCCCEE	61.15	21890473
100	Ubiquitination	DGTTSVIILAGEMLS CCCEEEEEEEHHHHH	1.70	21890473
128	2-Hydroxyisobutyrylation	VVISAYRKALDDMIS HHHHHHHHHHHHHHH	40.39	-
128	Ubiquitination	VVISAYRKALDDMIS HHHHHHHHHHHHHHH	40.39	21906983
133	Sulfoxidation	YRKALDDMISTLKKI HHHHHHHHHHHHHHC	2.32	21406390
135	Phosphorylation	KALDDMISTLKKISI HHHHHHHHHHHHCCC	22.50	21406692
136	Phosphorylation	ALDDMISTLKKISIP HHHHHHHHHHHCCCC	31.50	21406692
138	2-Hydroxyisobutyrylation	DDMISTLKKISIPVD HHHHHHHHHCCCCCC	48.42	-
138	Acetylation	DDMISTLKKISIPVD HHHHHHHHHCCCCCC	48.42	23236377
138	Malonylation	DDMISTLKKISIPVD HHHHHHHHHCCCCCC	48.42	26320211
138	Ubiquitination	DDMISTLKKISIPVD HHHHHHHHHCCCCCC	48.42	21890473
139	Ubiquitination	DMISTLKKISIPVDI HHHHHHHHCCCCCCC	44.81	21906983
141	Phosphorylation	ISTLKKISIPVDISD HHHHHHCCCCCCCCC	29.71	20068231
147	Phosphorylation	ISIPVDISDSDMMLN CCCCCCCCCCHHHHH	26.97	20068231
149	Phosphorylation	IPVDISDSDMMLNII CCCCCCCCHHHHHHH	22.18	20068231
158	Phosphorylation	MMLNIINSSITTKAI HHHHHHCCHHHHHHH	16.83	20068231
159	Phosphorylation	MLNIINSSITTKAIS HHHHHCCHHHHHHHH	21.33	20068231
161	Phosphorylation	NIINSSITTKAISRW HHHCCHHHHHHHHHH	24.96	20068231
162	Phosphorylation	IINSSITTKAISRWS HHCCHHHHHHHHHHH	19.46	20068231
163	Ubiquitination	INSSITTKAISRWSS HCCHHHHHHHHHHHH	34.76	-
169	Phosphorylation	TKAISRWSSLACNIA HHHHHHHHHHHHHHH	17.86	23898821
170	Phosphorylation	KAISRWSSLACNIAL HHHHHHHHHHHHHHH	17.02	27050516
173	S-nitrosocysteine	SRWSSLACNIALDAV HHHHHHHHHHHHHHH	4.61	-
173	Glutathionylation	SRWSSLACNIALDAV HHHHHHHHHHHHHHH	4.61	22555962
173	S-nitrosylation	SRWSSLACNIALDAV HHHHHHHHHHHHHHH	4.61	22178444
181	Ubiquitination	NIALDAVKMVQFEEN HHHHHHHHHEEEHHC	34.77	-
182	Sulfoxidation	IALDAVKMVQFEENG HHHHHHHHEEEHHCC	2.00	21406390
198	Phosphorylation	KEIDIKKYARVEKIP EEEEHHHEEEEEECC	8.47	-
203	Acetylation	KKYARVEKIPGGIIE HHEEEEEECCCCCCC	51.88	25953088
203	Malonylation	KKYARVEKIPGGIIE HHEEEEEECCCCCCC	51.88	26320211
203	Ubiquitination	KKYARVEKIPGGIIE HHEEEEEECCCCCCC	51.88	-
210	Ubiquitination	KIPGGIIEDSCVLRG ECCCCCCCCCCEEEC	41.78	21890473
213	S-nitrosocysteine	GGIIEDSCVLRGVMI CCCCCCCCEEECEEE	5.31	-
213	Glutathionylation	GGIIEDSCVLRGVMI CCCCCCCCEEECEEE	5.31	22555962
213	S-nitrosylation	GGIIEDSCVLRGVMI CCCCCCCCEEECEEE	5.31	22178444
216	Methylation	IEDSCVLRGVMINKD CCCCCEEECEEECCC	18.44	-
222	2-Hydroxyisobutyrylation	LRGVMINKDVTHPRM EECEEECCCCCCHHH	42.52	-
222	Acetylation	LRGVMINKDVTHPRM EECEEECCCCCCHHH	42.52	19608861
222	Malonylation	LRGVMINKDVTHPRM EECEEECCCCCCHHH	42.52	26320211
222	Ubiquitination	LRGVMINKDVTHPRM EECEEECCCCCCHHH	42.52	19608861
225	Phosphorylation	VMINKDVTHPRMRRY EEECCCCCCHHHHHH	35.97	20068231
232	Phosphorylation	THPRMRRYIKNPRIV CCHHHHHHCCCCCEE	13.09	24719451
234	Acetylation	PRMRRYIKNPRIVLL HHHHHHCCCCCEEEE	52.55	25953088
234	Ubiquitination	PRMRRYIKNPRIVLL HHHHHHCCCCCEEEE	52.55	-
243	Phosphorylation	PRIVLLDSSLEYKKG CCEEEEECCCCCCCC	36.47	19664994
244	Phosphorylation	RIVLLDSSLEYKKGE CEEEEECCCCCCCCC	25.53	19664994
247	Nitration	LLDSSLEYKKGESQT EEECCCCCCCCCCCC	24.24	-
247	Phosphorylation	LLDSSLEYKKGESQT EEECCCCCCCCCCCC	24.24	30576142
248	Acetylation	LDSSLEYKKGESQTD EECCCCCCCCCCCCC	44.95	23954790
248	Malonylation	LDSSLEYKKGESQTD EECCCCCCCCCCCCC	44.95	26320211
248	Sumoylation	LDSSLEYKKGESQTD EECCCCCCCCCCCCC	44.95	28112733
248	Ubiquitination	LDSSLEYKKGESQTD EECCCCCCCCCCCCC	44.95	21906983
249	2-Hydroxyisobutyrylation	DSSLEYKKGESQTDI ECCCCCCCCCCCCCC	67.99	-
249	Malonylation	DSSLEYKKGESQTDI ECCCCCCCCCCCCCC	67.99	26320211
249	Sumoylation	DSSLEYKKGESQTDI ECCCCCCCCCCCCCC	67.99	28112733
249	Ubiquitination	DSSLEYKKGESQTDI ECCCCCCCCCCCCCC	67.99	20639865
252	Phosphorylation	LEYKKGESQTDIEIT CCCCCCCCCCCCEEE	47.23	29255136
254	Phosphorylation	YKKGESQTDIEITRE CCCCCCCCCCEEECH	48.50	23927012
259	Phosphorylation	SQTDIEITREEDFTR CCCCCEEECHHHHHH	21.16	29978859
265	Phosphorylation	ITREEDFTRILQMEE EECHHHHHHHHHCCH	29.17	23927012
286	Ubiquitination	CEDIIQLKPDVVITE HHHHHHCCCCEEEEC	23.85	-
297	Phosphorylation	VITEKGISDLAQHYL EEECCCHHHHHHHHH	34.93	20068231
303	Phosphorylation	ISDLAQHYLMRANIT HHHHHHHHHHHCCHH	7.07	20068231
305	Sulfoxidation	DLAQHYLMRANITAI HHHHHHHHHCCHHHH	2.75	30846556
310	Phosphorylation	YLMRANITAIRRVRK HHHHCCHHHHCCHHC	18.81	24719451
313	Methylation	RANITAIRRVRKTDN HCCHHHHCCHHCCCC	28.69	-
317	Acetylation	TAIRRVRKTDNNRIA HHHCCHHCCCCCHHH	58.32	19818619
343	Ubiquitination	EELREDDVGTGAGLL HHHCCCCCCCCCCEE	13.14	21890473
353	2-Hydroxyisobutyrylation	GAGLLEIKKIGDEYF CCCEEEEEEECCEEE	29.03	-
353	Acetylation	GAGLLEIKKIGDEYF CCCEEEEEEECCEEE	29.03	26051181
353	Ubiquitination	GAGLLEIKKIGDEYF CCCEEEEEEECCEEE	29.03	21906983
354	2-Hydroxyisobutyrylation	AGLLEIKKIGDEYFT CCEEEEEEECCEEEE	58.54	-
354	Ubiquitination	AGLLEIKKIGDEYFT CCEEEEEEECCEEEE	58.54	-
359	Nitration	IKKIGDEYFTFITDC EEEECCEEEEEEECC	16.80	-
359	Phosphorylation	IKKIGDEYFTFITDC EEEECCEEEEEEECC	16.80	28152594
361	Phosphorylation	KIGDEYFTFITDCKD EECCEEEEEEECCCC	17.15	28152594
366	Glutathionylation	YFTFITDCKDPKACT EEEEEECCCCHHHHE	3.94	22555962
367	2-Hydroxyisobutyrylation	FTFITDCKDPKACTI EEEEECCCCHHHHEE	78.76	-
367	Acetylation	FTFITDCKDPKACTI EEEEECCCCHHHHEE	78.76	26051181
367	Ubiquitination	FTFITDCKDPKACTI EEEEECCCCHHHHEE	78.76	-
370	2-Hydroxyisobutyrylation	ITDCKDPKACTILLR EECCCCHHHHEEEEC	67.25	-
370	Acetylation	ITDCKDPKACTILLR EECCCCHHHHEEEEC	67.25	26051181
370	Ubiquitination	ITDCKDPKACTILLR EECCCCHHHHEEEEC	67.25	-
372	Glutathionylation	DCKDPKACTILLRGA CCCCHHHHEEEECCC	2.80	22555962
377	Methylation	KACTILLRGASKEIL HHHEEEECCCCHHHH	34.88	-
380	Phosphorylation	TILLRGASKEILSEV EEEECCCCHHHHHHH	33.38	29514088
381	2-Hydroxyisobutyrylation	ILLRGASKEILSEVE EEECCCCHHHHHHHH	48.52	-
381	Acetylation	ILLRGASKEILSEVE EEECCCCHHHHHHHH	48.52	23954790
381	Malonylation	ILLRGASKEILSEVE EEECCCCHHHHHHHH	48.52	26320211
381	Sumoylation	ILLRGASKEILSEVE EEECCCCHHHHHHHH	48.52	25114211
381	Ubiquitination	ILLRGASKEILSEVE EEECCCCHHHHHHHH	48.52	21890473
385	Phosphorylation	GASKEILSEVERNLQ CCCHHHHHHHHHHHH	45.30	21815630
395	Sulfoxidation	ERNLQDAMQVCRNVL HHHHHHHHHHHHHHH	4.06	21406390
398	Glutathionylation	LQDAMQVCRNVLLDP HHHHHHHHHHHHCCC	1.15	22555962
398	S-palmitoylation	LQDAMQVCRNVLLDP HHHHHHHHHHHHCCC	1.15	26865113
414	Phosphorylation	LVPGGGASEMAVAHA CCCCCCHHHHHHHHH	31.05	30622161
416	Sulfoxidation	PGGGASEMAVAHALT CCCCHHHHHHHHHHH	3.17	30846556
423	Phosphorylation	MAVAHALTEKSKAMT HHHHHHHHHHCCCCC	41.99	25693802
425	2-Hydroxyisobutyrylation	VAHALTEKSKAMTGV HHHHHHHHCCCCCCC	52.61	-
425	Ubiquitination	VAHALTEKSKAMTGV HHHHHHHHCCCCCCC	52.61	21906983
427	2-Hydroxyisobutyrylation	HALTEKSKAMTGVEQ HHHHHHCCCCCCCCC	53.93	-
427	Ubiquitination	HALTEKSKAMTGVEQ HHHHHHCCCCCCCCC	53.93	21906983
430	Phosphorylation	TEKSKAMTGVEQWPY HHHCCCCCCCCCCHH	42.82	20068231
437	Phosphorylation	TGVEQWPYRAVAQAL CCCCCCHHHHHHHHH	14.30	20068231
450	Phosphorylation	ALEVIPRTLIQNCGA HHHHCCHHHHHHCCH	23.90	23186163
455	Glutathionylation	PRTLIQNCGASTIRL CHHHHHHCCHHHHHH	2.49	22555962
455	S-palmitoylation	PRTLIQNCGASTIRL CHHHHHHCCHHHHHH	2.49	29575903
458	Phosphorylation	LIQNCGASTIRLLTS HHHHCCHHHHHHHHH	15.06	21712546
459	Phosphorylation	IQNCGASTIRLLTSL HHHCCHHHHHHHHHH	15.02	25072903
464	Ubiquitination	ASTIRLLTSLRAKHT HHHHHHHHHHHHHHC	30.24	21890473
469	Ubiquitination	LLTSLRAKHTQENCE HHHHHHHHHCHHCHH	40.53	21890473
469	Acetylation	LLTSLRAKHTQENCE HHHHHHHHHCHHCHH	40.53	25953088
469	Ubiquitination	LLTSLRAKHTQENCE HHHHHHHHHCHHCHH	40.53	-
477	Phosphorylation	HTQENCETWGVNGET HCHHCHHHCCCCCCC	29.71	-
491	Ubiquitination	TGTLVDMKELGIWEP CCEEEEHHHHCCCCC	45.37	-
502	Ubiquitination	IWEPLAVKLQTYKTA CCCCCHHHHHHHHHH	29.30	21906983
507	Ubiquitination	AVKLQTYKTAVETAV HHHHHHHHHHHHHHH	33.14	21906983
508	Phosphorylation	VKLQTYKTAVETAVL HHHHHHHHHHHHHHH	26.06	21712546
512	Phosphorylation	TYKTAVETAVLLLRI HHHHHHHHHHHHHHH	18.57	-
524	Phosphorylation	LRIDDIVSGHKKKGD HHHHHHHCCCCCCCC	35.20	25159151
527	2-Hydroxyisobutyrylation	DDIVSGHKKKGDDQS HHHHCCCCCCCCCCC	60.76	-
527	Acetylation	DDIVSGHKKKGDDQS HHHHCCCCCCCCCCC	60.76	26051181
527	Succinylation	DDIVSGHKKKGDDQS HHHHCCCCCCCCCCC	60.76	23954790
527	Ubiquitination	DDIVSGHKKKGDDQS HHHHCCCCCCCCCCC	60.76	-
528	Ubiquitination	DIVSGHKKKGDDQSR HHHCCCCCCCCCCCC	57.21	-
529	Ubiquitination	IVSGHKKKGDDQSRQ HHCCCCCCCCCCCCC	72.82	-
534	Phosphorylation	KKKGDDQSRQGGAPD CCCCCCCCCCCCCCC	33.30	30576142

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 TCPG_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SSA27_HUMAN	SSSCA1	physical	16189514
EI2BB_HUMAN	EIF2B2	physical	16169070
TCPH_HUMAN	CCT7	physical	22939629
TCPQ_HUMAN	CCT8	physical	22939629
TCPZ_HUMAN	CCT6A	physical	22939629
TCPW_HUMAN	CCT6B	physical	22939629
ACACA_HUMAN	ACACA	physical	22863883
TCPH_HUMAN	CCT7	physical	22863883
TIF1B_HUMAN	TRIM28	physical	22863883
MIPO1_HUMAN	MIPOL1	physical	25416956
TCPB_HUMAN	CCT2	physical	26344197
TCPD_HUMAN	CCT4	physical	26344197
TCPH_HUMAN	CCT7	physical	26344197
TCPQ_HUMAN	CCT8	physical	26344197
CP27A_HUMAN	CYP27A1	physical	26344197
ENPL_HUMAN	HSP90B1	physical	26344197
IMA3_HUMAN	KPNA4	physical	26344197
SYMC_HUMAN	MARS	physical	26344197
MCM7_HUMAN	MCM7	physical	26344197
PYC_HUMAN	PC	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
STOM_HUMAN	STOM	physical	26344197
TCPA_HUMAN	TCP1	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
TBD_HUMAN	TUBD1	physical	28514442
DCA12_HUMAN	DCAF12	physical	28514442
TCPH_HUMAN	CCT7	physical	28514442
DTL_HUMAN	DTL	physical	28514442
WDR70_HUMAN	WDR70	physical	28514442
DCA13_HUMAN	DCAF13	physical	28514442
JMJD4_HUMAN	JMJD4	physical	28514442
TCPB_HUMAN	CCT2	physical	28514442
TCPW_HUMAN	CCT6B	physical	28514442
TCPD_HUMAN	CCT4	physical	28514442
KLHL8_HUMAN	KLHL8	physical	28514442
MEP50_HUMAN	WDR77	physical	28514442
WDR46_HUMAN	WDR46	physical	28514442
BUB3_HUMAN	BUB3	physical	28514442
TCPA_HUMAN	TCP1	physical	28514442
FBXW8_HUMAN	FBXW8	physical	28514442
TCPZ_HUMAN	CCT6A	physical	28514442
KLD8B_HUMAN	KLHDC8B	physical	28514442
TCPQ_HUMAN	CCT8	physical	28514442
MAP2_HUMAN	METAP2	physical	28514442
TCPE_HUMAN	CCT5	physical	28514442
PHLP_HUMAN	PDCL	physical	28514442
UTP18_HUMAN	UTP18	physical	28514442
HDAC3_HUMAN	HDAC3	physical	28514442
PDCL3_HUMAN	PDCL3	physical	28514442

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 TCPG_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 MET-1, 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-222, 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-244, AND MASSSPECTROMETRY.	19690332 [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-254, AND MASSSPECTROMETRY.	17924679 [Abstract]