dbPTM

TCPA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TCPA_HUMAN
UniProt AC	P17987
Protein Name	T-complex protein 1 subunit alpha
Gene Name	TCP1
Organism	Homo sapiens (Human).
Sequence Length	556
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
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	MEGPLSVFGDRSTGETIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAAKTSMSSKIIGINGDFFANMVVDAVLAIKYTDIRGQPRYPVNSVNILKAHGRSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVEAGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEETFEAAMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLSNGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGSYEDAVHSGALND

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEGPLSVF -------CCCCCEEC	14.00	19413330
1	Sulfoxidation	-------MEGPLSVF -------CCCCCEEC	14.00	28465586
6	Phosphorylation	--MEGPLSVFGDRST --CCCCCEECCCCCC	20.66	21406692
11	Methylation	PLSVFGDRSTGETIR CCEECCCCCCCCCHH	36.18	-
12	Phosphorylation	LSVFGDRSTGETIRS CEECCCCCCCCCHHH	45.57	23186163
13	Phosphorylation	SVFGDRSTGETIRSQ EECCCCCCCCCHHHH	39.67	23186163
19	Phosphorylation	STGETIRSQNVMAAA CCCCCHHHHHHHHHH	23.43	20068231
23	Sulfoxidation	TIRSQNVMAAASIAN CHHHHHHHHHHHHHH	2.49	21406390
27	Phosphorylation	QNVMAAASIANIVKS HHHHHHHHHHHHHHH	19.94	20068231
33	Ubiquitination	ASIANIVKSSLGPVG HHHHHHHHHCCCCCC	30.45	-
34	Phosphorylation	SIANIVKSSLGPVGL HHHHHHHHCCCCCCC	21.65	21712546
35	Phosphorylation	IANIVKSSLGPVGLD HHHHHHHCCCCCCCC	31.46	21712546
43	Ubiquitination	LGPVGLDKMLVDDIG CCCCCCCCCEECCCC	38.89	-
44	Sulfoxidation	GPVGLDKMLVDDIGD CCCCCCCCEECCCCC	4.38	30846556
55	Phosphorylation	DIGDVTITNDGATIL CCCCEEEECCCCHHH	20.21	25690035
60	Phosphorylation	TITNDGATILKLLEV EEECCCCHHHHHHHC	32.16	25690035
63	Ubiquitination	NDGATILKLLEVEHP CCCCHHHHHHHCCCH	47.37	21906983
73	Ubiquitination	EVEHPAAKVLCELAD HCCCHHHHHHHHHHC	37.53	21890473
73	2-Hydroxyisobutyrylation	EVEHPAAKVLCELAD HCCCHHHHHHHHHHC	37.53	-
73	Acetylation	EVEHPAAKVLCELAD HCCCHHHHHHHHHHC	37.53	27452117
76	S-nitrosocysteine	HPAAKVLCELADLQD CHHHHHHHHHHCCCC	4.51	-
76	S-nitrosylation	HPAAKVLCELADLQD CHHHHHHHHHHCCCC	4.51	22178444
84	Acetylation	ELADLQDKEVGDGTT HHHCCCCCCCCCCHH	41.14	7430915
90	Phosphorylation	DKEVGDGTTSVVIIA CCCCCCCHHHHHHHH	22.19	30622161
91	Phosphorylation	KEVGDGTTSVVIIAA CCCCCCHHHHHHHHH	25.67	30622161
92	Phosphorylation	EVGDGTTSVVIIAAE CCCCCHHHHHHHHHH	17.77	30622161
109	Ubiquitination	KNADELVKQKIHPTS HCHHHHHHCCCCCCC	59.50	21906983
109	2-Hydroxyisobutyrylation	KNADELVKQKIHPTS HCHHHHHHCCCCCCC	59.50	-
109	Acetylation	KNADELVKQKIHPTS HCHHHHHHCCCCCCC	59.50	25953088
111	Ubiquitination	ADELVKQKIHPTSVI HHHHHHCCCCCCCHH	36.95	21906983
111	2-Hydroxyisobutyrylation	ADELVKQKIHPTSVI HHHHHHCCCCCCCHH	36.95	-
115	Phosphorylation	VKQKIHPTSVISGYR HHCCCCCCCHHCHHH	22.82	23186163
116	Phosphorylation	KQKIHPTSVISGYRL HCCCCCCCHHCHHHH	23.16	23186163
119	Phosphorylation	IHPTSVISGYRLACK CCCCCHHCHHHHHHH	27.84	20068231
121	Phosphorylation	PTSVISGYRLACKEA CCCHHCHHHHHHHHH	8.82	20068231
126	Ubiquitination	SGYRLACKEAVRYIN CHHHHHHHHHHHHHH	43.00	21906983
126	2-Hydroxyisobutyrylation	SGYRLACKEAVRYIN CHHHHHHHHHHHHHH	43.00	-
131	Phosphorylation	ACKEAVRYINENLIV HHHHHHHHHHHCCEE	11.08	28152594
147	S-nitrosocysteine	TDELGRDCLINAAKT HHHHCHHHHHHHHHH	3.86	-
147	S-nitrosylation	TDELGRDCLINAAKT HHHHCHHHHHHHHHH	3.86	22178444
147	S-palmitoylation	TDELGRDCLINAAKT HHHHCHHHHHHHHHH	3.86	26865113
153	Ubiquitination	DCLINAAKTSMSSKI HHHHHHHHHCCCCCC	38.43	-
153	2-Hydroxyisobutyrylation	DCLINAAKTSMSSKI HHHHHHHHHCCCCCC	38.43	-
153	Acetylation	DCLINAAKTSMSSKI HHHHHHHHHCCCCCC	38.43	25953088
157	Phosphorylation	NAAKTSMSSKIIGIN HHHHHCCCCCCCCCC	28.39	-
158	Phosphorylation	AAKTSMSSKIIGING HHHHCCCCCCCCCCC	21.16	-
181	Phosphorylation	DAVLAIKYTDIRGQP HHHHEEEEECCCCCC	11.97	28152594
182	Phosphorylation	AVLAIKYTDIRGQPR HHHEEEEECCCCCCC	21.68	28152594
185	Methylation	AIKYTDIRGQPRYPV EEEEECCCCCCCCCC	40.27	-
190	Phosphorylation	DIRGQPRYPVNSVNI CCCCCCCCCCCHHHH	20.44	28152594
194	Phosphorylation	QPRYPVNSVNILKAH CCCCCCCHHHHHHHC	19.44	23312004
199	Methylation	VNSVNILKAHGRSQM CCHHHHHHHCCHHHH	34.24	19608861
199	Acetylation	VNSVNILKAHGRSQM CCHHHHHHHCCHHHH	34.24	19608861
199	Ubiquitination	VNSVNILKAHGRSQM CCHHHHHHHCCHHHH	34.24	19608861
199	Malonylation	VNSVNILKAHGRSQM CCHHHHHHHCCHHHH	34.24	26320211
204	Phosphorylation	ILKAHGRSQMESMLI HHHHCCHHHHHHHHH	38.17	25072903
208	Phosphorylation	HGRSQMESMLISGYA CCHHHHHHHHHHHHH	17.34	26126808
212	Phosphorylation	QMESMLISGYALNCV HHHHHHHHHHHHHCC	23.07	25072903
214	Phosphorylation	ESMLISGYALNCVVG HHHHHHHHHHHCCCC	10.92	25072903
218	Glutathionylation	ISGYALNCVVGSQGM HHHHHHHCCCCCCCC	2.46	22555962
222	Phosphorylation	ALNCVVGSQGMPKRI HHHCCCCCCCCCHHH	16.38	25072903
227	Acetylation	VGSQGMPKRIVNAKI CCCCCCCHHHHCCEE	45.95	26051181
233	Ubiquitination	PKRIVNAKIACLDFS CHHHHCCEEEEEEHH	26.15	-
233	Acetylation	PKRIVNAKIACLDFS CHHHHCCEEEEEEHH	26.15	25953088
236	S-nitrosocysteine	IVNAKIACLDFSLQK HHCCEEEEEEHHCHH	4.22	-
236	Glutathionylation	IVNAKIACLDFSLQK HHCCEEEEEEHHCHH	4.22	22555962
236	S-nitrosylation	IVNAKIACLDFSLQK HHCCEEEEEEHHCHH	4.22	19483679
240	Phosphorylation	KIACLDFSLQKTKMK EEEEEEHHCHHCCCC	29.56	25159151
243	Ubiquitination	CLDFSLQKTKMKLGV EEEHHCHHCCCCCCE	56.24	-
243	2-Hydroxyisobutyrylation	CLDFSLQKTKMKLGV EEEHHCHHCCCCCCE	56.24	-
243	Acetylation	CLDFSLQKTKMKLGV EEEHHCHHCCCCCCE	56.24	25953088
245	Acetylation	DFSLQKTKMKLGVQV EHHCHHCCCCCCEEE	40.86	-
245	Ubiquitination	DFSLQKTKMKLGVQV EHHCHHCCCCCCEEE	40.86	-
247	Ubiquitination	SLQKTKMKLGVQVVI HCHHCCCCCCEEEEE	43.58	-
255	Phosphorylation	LGVQVVITDPEKLDQ CCEEEEECCHHHHHH	33.61	23532336
259	Acetylation	VVITDPEKLDQIRQR EEECCHHHHHHHHHH	63.85	25953088
259	Ubiquitination	VVITDPEKLDQIRQR EEECCHHHHHHHHHH	63.85	21906983
268	Phosphorylation	DQIRQRESDITKERI HHHHHHCCHHCHHHH	36.18	22210691
296	Glutathionylation	TGGIDDMCLKYFVEA CCCHHHHHHHHHHHH	3.69	22555962
299	Phosphorylation	IDDMCLKYFVEAGAM HHHHHHHHHHHHHHH	10.42	19534553
306	Sulfoxidation	YFVEAGAMAVRRVLK HHHHHHHHHHHHHHH	3.29	30846556
344	Sulfoxidation	EETFEAAMLGQAEEV HHHHHHHHHCCHHHH	5.79	28183972
357	S-nitrosocysteine	EVVQERICDDELILI HHHHHHCCCCEEEEE	7.26	-
357	Glutathionylation	EVVQERICDDELILI HHHHHHCCCCEEEEE	7.26	22555962
357	S-nitrosylation	EVVQERICDDELILI HHHHHHCCCCEEEEE	7.26	18335467
365	Acetylation	DDELILIKNTKARTS CCEEEEEECCCCCCC	55.93	23749302
365	Ubiquitination	DDELILIKNTKARTS CCEEEEEECCCCCCC	55.93	-
365	2-Hydroxyisobutyrylation	DDELILIKNTKARTS CCEEEEEECCCCCCC	55.93	-
367	Phosphorylation	ELILIKNTKARTSAS EEEEEECCCCCCCCH	22.53	23898821
368	Ubiquitination	LILIKNTKARTSASI EEEEECCCCCCCCHH	45.31	-
371	Phosphorylation	IKNTKARTSASIILR EECCCCCCCCHHHHC	33.24	21406692
372	Phosphorylation	KNTKARTSASIILRG ECCCCCCCCHHHHCC	17.92	21406692
374	Phosphorylation	TKARTSASIILRGAN CCCCCCCHHHHCCCC	15.21	21406692
384	Sulfoxidation	LRGANDFMCDEMERS HCCCCCHHCHHHHHH	2.91	21406390
385	Glutathionylation	RGANDFMCDEMERSL CCCCCHHCHHHHHHH	3.96	22555962
388	Sulfoxidation	NDFMCDEMERSLHDA CCHHCHHHHHHHHHH	3.11	30846556
397	S-nitrosocysteine	RSLHDALCVVKRVLE HHHHHHHHHHHHHHH	3.38	-
397	Glutathionylation	RSLHDALCVVKRVLE HHHHHHHHHHHHHHH	3.38	22555962
397	S-nitrosylation	RSLHDALCVVKRVLE HHHHHHHHHHHHHHH	3.38	19483679
400	Acetylation	HDALCVVKRVLESKS HHHHHHHHHHHHCCC	19.18	19608861
400	Ubiquitination	HDALCVVKRVLESKS HHHHHHHHHHHHCCC	19.18	19608861
400	2-Hydroxyisobutyrylation	HDALCVVKRVLESKS HHHHHHHHHHHHCCC	19.18	-
400	Malonylation	HDALCVVKRVLESKS HHHHHHHHHHHHCCC	19.18	26320211
405	Phosphorylation	VVKRVLESKSVVPGG HHHHHHHCCCCCCCC	26.52	22210691
422	Phosphorylation	VEAALSIYLENYATS HHHHHHHHHHHHHHC	12.46	22210691
428	Phosphorylation	IYLENYATSMGSREQ HHHHHHHHCCCCHHH	14.64	22210691
429	Phosphorylation	YLENYATSMGSREQL HHHHHHHCCCCHHHH	16.99	24275569
443	Methylation	LAIAEFARSLLVIPN HHHHHHHHHHCCCCC	32.91	-
444	Phosphorylation	AIAEFARSLLVIPNT HHHHHHHHHCCCCCH	23.72	21712546
460	Phosphorylation	AVNAAQDSTDLVAKL HHCCCCCCHHHHHHH	16.25	21712546
466	Ubiquitination	DSTDLVAKLRAFHNE CCHHHHHHHHHHHHH	30.90	21906983
466	Acetylation	DSTDLVAKLRAFHNE CCHHHHHHHHHHHHH	30.90	23236377
468	Methylation	TDLVAKLRAFHNEAQ HHHHHHHHHHHHHHC	34.20	-
481	Ubiquitination	AQVNPERKNLKWIGL HCCCCCCCCCEEEEE	66.04	-
484	Acetylation	NPERKNLKWIGLDLS CCCCCCCEEEEEECC	46.27	23749302
484	Ubiquitination	NPERKNLKWIGLDLS CCCCCCCEEEEEECC	46.27	21890473
491	Phosphorylation	KWIGLDLSNGKPRDN EEEEEECCCCCCCCC	43.11	28450419
494	Acetylation	GLDLSNGKPRDNKQA EEECCCCCCCCCCCC	40.92	26051181
494	Ubiquitination	GLDLSNGKPRDNKQA EEECCCCCCCCCCCC	40.92	21890473
494	Malonylation	GLDLSNGKPRDNKQA EEECCCCCCCCCCCC	40.92	26320211
499	Ubiquitination	NGKPRDNKQAGVFEP CCCCCCCCCCCCCCC	45.90	-
499	2-Hydroxyisobutyrylation	NGKPRDNKQAGVFEP CCCCCCCCCCCCCCC	45.90	-
499	Malonylation	NGKPRDNKQAGVFEP CCCCCCCCCCCCCCC	45.90	26320211
499	Acetylation	NGKPRDNKQAGVFEP CCCCCCCCCCCCCCC	45.90	25953088
510	Ubiquitination	VFEPTIVKVKSLKFA CCCCEEEEEECCCCH	39.84	-
510	Acetylation	VFEPTIVKVKSLKFA CCCCEEEEEECCCCH	39.84	25953088
512	Ubiquitination	EPTIVKVKSLKFATE CCEEEEEECCCCHHH	44.33	-
513	Phosphorylation	PTIVKVKSLKFATEA CEEEEEECCCCHHHH	39.52	24719451
515	Ubiquitination	IVKVKSLKFATEAAI EEEEECCCCHHHHHH	39.79	-
532	Acetylation	LRIDDLIKLHPESKD EEHHHHHHHCCCCCC	48.30	23954790
532	Ubiquitination	LRIDDLIKLHPESKD EEHHHHHHHCCCCCC	48.30	21890473
532	2-Hydroxyisobutyrylation	LRIDDLIKLHPESKD EEHHHHHHHCCCCCC	48.30	-
532	Malonylation	LRIDDLIKLHPESKD EEHHHHHHHCCCCCC	48.30	26320211
537	Phosphorylation	LIKLHPESKDDKHGS HHHHCCCCCCCCCCC	45.92	23401153
538	Acetylation	IKLHPESKDDKHGSY HHHCCCCCCCCCCCH	69.18	23749302
538	Ubiquitination	IKLHPESKDDKHGSY HHHCCCCCCCCCCCH	69.18	21906983
541	Acetylation	HPESKDDKHGSYEDA CCCCCCCCCCCHHHH	61.06	23954790
541	Ubiquitination	HPESKDDKHGSYEDA CCCCCCCCCCCHHHH	61.06	21890473
541	2-Hydroxyisobutyrylation	HPESKDDKHGSYEDA CCCCCCCCCCCHHHH	61.06	-
541	Malonylation	HPESKDDKHGSYEDA CCCCCCCCCCCHHHH	61.06	26320211
544	Phosphorylation	SKDDKHGSYEDAVHS CCCCCCCCHHHHHHH	25.68	22167270
545	Phosphorylation	KDDKHGSYEDAVHSG CCCCCCCHHHHHHHC	23.55	22167270
551	Phosphorylation	SYEDAVHSGALND-- CHHHHHHHCCCCC--	21.11	25159151

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 TCPA_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TCPB_HUMAN	CCT2	physical	16085932
TCPG_HUMAN	CCT3	physical	16085932
TCPD_HUMAN	CCT4	physical	16085932
TCPE_HUMAN	CCT5	physical	16085932
TCPZ_HUMAN	CCT6A	physical	16085932
TCPH_HUMAN	CCT7	physical	16085932
TCPQ_HUMAN	CCT8	physical	16085932
GLCM_HUMAN	GBA	physical	21098288
VHL_HUMAN	VHL	physical	14636579
PACRG_HUMAN	PACRG	physical	14532270
TCPB_HUMAN	CCT2	physical	14532270
TCPE_HUMAN	CCT5	physical	22939629
TCPH_HUMAN	CCT7	physical	22939629
TCPB_HUMAN	CCT2	physical	22939629
TCPD_HUMAN	CCT4	physical	22939629
TCPG_HUMAN	CCT3	physical	22939629
TCPZ_HUMAN	CCT6A	physical	22939629
TCPQ_HUMAN	CCT8	physical	22939629
TCPW_HUMAN	CCT6B	physical	22939629
TCPG_HUMAN	CCT3	physical	22863883
PP4C_HUMAN	PPP4C	physical	22863883
VRK2_HUMAN	VRK2	physical	24298020
MTG8R_HUMAN	CBFA2T2	physical	25416956
TCPB_HUMAN	CCT2	physical	26344197
TCPH_HUMAN	CCT7	physical	26344197
TCPQ_HUMAN	CCT8	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
ACTB_HUMAN	ACTB	physical	14532270

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TCPA_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]
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 1-11, AND ACETYLATION AT MET-1.	12665801 [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-199; LYS-400 AND LYS-532,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-400, 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-544 AND SER-551, ANDMASS SPECTROMETRY.	19690332 [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-544, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND MASSSPECTROMETRY.	18088087 [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-544, AND MASSSPECTROMETRY.	17081983 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-299, AND MASSSPECTROMETRY.	19534553 [Abstract]