dbPTM

RLA0_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RLA0_HUMAN
UniProt AC	P05388
Protein Name	60S acidic ribosomal protein P0
Gene Name	RPLP0
Organism	Homo sapiens (Human).
Sequence Length	317
Subcellular Localization	Nucleus . Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:19188445, PubMed:17289661).
Protein Description	Ribosomal protein P0 is the functional equivalent of E.coli protein L10..
Protein Sequence	MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKRVLALSVETDYTFPLAEKVKAFLADPSAFVAAAPVAAATTAAPAAAAAPAKVEAKEESEESDEDMGFGLFD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Methylation	--MPREDRATWKSNY --CCHHHHHHHHHHH	29.21	115492347
8	Phosphorylation	MPREDRATWKSNYFL CCHHHHHHHHHHHHH	34.03	-
10	Ubiquitination	REDRATWKSNYFLKI HHHHHHHHHHHHHHH	25.19	21890473
10	2-Hydroxyisobutyrylation	REDRATWKSNYFLKI HHHHHHHHHHHHHHH	25.19	-
10	Ubiquitination	REDRATWKSNYFLKI HHHHHHHHHHHHHHH	25.19	21890473
10	Methylation	REDRATWKSNYFLKI HHHHHHHHHHHHHHH	25.19	24649263
10	Acetylation	REDRATWKSNYFLKI HHHHHHHHHHHHHHH	25.19	26051181
11	Phosphorylation	EDRATWKSNYFLKII HHHHHHHHHHHHHHH	28.46	23882029
16	Ubiquitination	WKSNYFLKIIQLLDD HHHHHHHHHHHHHHC	28.06	21906983
16	Methylation	WKSNYFLKIIQLLDD HHHHHHHHHHHHHHC	28.06	30793763
16	Ubiquitination	WKSNYFLKIIQLLDD HHHHHHHHHHHHHHC	28.06	21890473
16	Acetylation	WKSNYFLKIIQLLDD HHHHHHHHHHHHHHC	28.06	21466224
24	Phosphorylation	IIQLLDDYPKCFIVG HHHHHHCCCCEEEEC	12.31	25159151
26	Acetylation	QLLDDYPKCFIVGAD HHHHCCCCEEEECCC	35.23	26051181
26	Ubiquitination	QLLDDYPKCFIVGAD HHHHCCCCEEEECCC	35.23	21906983
26	Ubiquitination	QLLDDYPKCFIVGAD HHHHCCCCEEEECCC	35.23	21890473
26	2-Hydroxyisobutyrylation	QLLDDYPKCFIVGAD HHHHCCCCEEEECCC	35.23	-
27	Glutathionylation	LLDDYPKCFIVGADN HHHCCCCEEEECCCC	2.13	22555962
27	S-nitrosylation	LLDDYPKCFIVGADN HHHCCCCEEEECCCC	2.13	22178444
27	S-nitrosocysteine	LLDDYPKCFIVGADN HHHCCCCEEEECCCC	2.13	-
37	Phosphorylation	VGADNVGSKQMQQIR ECCCCCCHHHHHHHH	18.55	28152594
38	Acetylation	GADNVGSKQMQQIRM CCCCCCHHHHHHHHH	43.81	26051181
38	Ubiquitination	GADNVGSKQMQQIRM CCCCCCHHHHHHHHH	43.81	21890473
38	Ubiquitination	GADNVGSKQMQQIRM CCCCCCHHHHHHHHH	43.81	21906983
50	2-Hydroxyisobutyrylation	IRMSLRGKAVVLMGK HHHHHHCCEEEEECC	31.41	-
50	Ubiquitination	IRMSLRGKAVVLMGK HHHHHHCCEEEEECC	31.41	-
57	Ubiquitination	KAVVLMGKNTMMRKA CEEEEECCCHHHHHH	34.97	21890473
57	Ubiquitination	KAVVLMGKNTMMRKA CEEEEECCCHHHHHH	34.97	21906983
59	Phosphorylation	VVLMGKNTMMRKAIR EEEECCCHHHHHHHH	18.81	28857561
66	Methylation	TMMRKAIRGHLENNP HHHHHHHHHHHHCCH	31.19	115492339
77	Ubiquitination	ENNPALEKLLPHIRG HCCHHHHHHHHHHCC	57.06	21890473
77	Acetylation	ENNPALEKLLPHIRG HCCHHHHHHHHHHCC	57.06	19608861
77	Malonylation	ENNPALEKLLPHIRG HCCHHHHHHHHHHCC	57.06	26320211
77	Ubiquitination	ENNPALEKLLPHIRG HCCHHHHHHHHHHCC	57.06	21890473
77	2-Hydroxyisobutyrylation	ENNPALEKLLPHIRG HCCHHHHHHHHHHCC	57.06	-
92	Ubiquitination	NVGFVFTKEDLTEIR CEEEEEEHHHHHHHH	37.45	21890473
92	2-Hydroxyisobutyrylation	NVGFVFTKEDLTEIR CEEEEEEHHHHHHHH	37.45	-
92	Ubiquitination	NVGFVFTKEDLTEIR CEEEEEEHHHHHHHH	37.45	21906983
92	Acetylation	NVGFVFTKEDLTEIR CEEEEEEHHHHHHHH	37.45	26822725
101	Sulfoxidation	DLTEIRDMLLANKVP HHHHHHHHHHHCCCC	2.07	30846556
106	2-Hydroxyisobutyrylation	RDMLLANKVPAAARA HHHHHHCCCCHHHHC	43.94	-
106	Ubiquitination	RDMLLANKVPAAARA HHHHHHCCCCHHHHC	43.94	21906983
106	Ubiquitination	RDMLLANKVPAAARA HHHHHHCCCCHHHHC	43.94	21890473
106	Acetylation	RDMLLANKVPAAARA HHHHHHCCCCHHHHC	43.94	26051181
112	Methylation	NKVPAAARAGAIAPC CCCCHHHHCCCCCCE	28.91	115492355
119	S-palmitoylation	RAGAIAPCEVTVPAQ HCCCCCCEEEEECCC	4.92	29575903
119	S-nitrosylation	RAGAIAPCEVTVPAQ HCCCCCCEEEEECCC	4.92	22178444
119	S-nitrosocysteine	RAGAIAPCEVTVPAQ HCCCCCCEEEEECCC	4.92	-
119	Glutathionylation	RAGAIAPCEVTVPAQ HCCCCCCEEEEECCC	4.92	22555962
122	Phosphorylation	AIAPCEVTVPAQNTG CCCCEEEEECCCCCC	9.85	21712546
128	Phosphorylation	VTVPAQNTGLGPEKT EEECCCCCCCCCCCC	23.00	21712546
134	Acetylation	NTGLGPEKTSFFQAL CCCCCCCCCCHHHHH	53.23	26051181
134	Ubiquitination	NTGLGPEKTSFFQAL CCCCCCCCCCHHHHH	53.23	-
135	Phosphorylation	TGLGPEKTSFFQALG CCCCCCCCCHHHHHC	29.16	21712546
136	Phosphorylation	GLGPEKTSFFQALGI CCCCCCCCHHHHHCC	34.82	21712546
144	Phosphorylation	FFQALGITTKISRGT HHHHHCCEEEECCCE	21.90	21712546
145	Phosphorylation	FQALGITTKISRGTI HHHHCCEEEECCCEE	25.18	21712546
146	Acetylation	QALGITTKISRGTIE HHHCCEEEECCCEEE	29.99	26051181
146	Ubiquitination	QALGITTKISRGTIE HHHCCEEEECCCEEE	29.99	21906983
148	Phosphorylation	LGITTKISRGTIEIL HCCEEEECCCEEEEC	26.64	-
151	Phosphorylation	TTKISRGTIEILSDV EEEECCCEEEECCCC	17.83	20860994
151 (in isoform 2)	Phosphorylation	-	17.83	20068231
156	Phosphorylation	RGTIEILSDVQLIKT CCEEEECCCCEEEEC	41.20	20860994
162	Ubiquitination	LSDVQLIKTGDKVGA CCCCEEEECCCCCCC	55.86	-
162 (in isoform 2)	Phosphorylation	-	55.86	20068231
163	Phosphorylation	SDVQLIKTGDKVGAS CCCEEEECCCCCCCC	43.55	28851738
166	Ubiquitination	QLIKTGDKVGASEAT EEEECCCCCCCCHHH	43.86	-
169 (in isoform 2)	Phosphorylation	-	13.74	20068231
171 (in isoform 2)	Phosphorylation	-	45.18	20068231
174 (in isoform 2)	Phosphorylation	-	4.13	20068231
178 (in isoform 2)	Phosphorylation	-	5.11	20068231
183 (in isoform 2)	Phosphorylation	-	8.25	20068231
224	Phosphorylation	EGVRNVASVCLQIGY HHHHHHHHHHHHCCC	14.74	20068231
233	Phosphorylation	CLQIGYPTVASVPHS HHHCCCCCCCCCCHH	21.88	20068231
245	Phosphorylation	PHSIINGYKRVLALS CHHHHCCCCEEEEEE	7.37	22817901
246	Acetylation	HSIINGYKRVLALSV HHHHCCCCEEEEEEE	37.11	26051181
246	Ubiquitination	HSIINGYKRVLALSV HHHHCCCCEEEEEEE	37.11	-
252	Phosphorylation	YKRVLALSVETDYTF CCEEEEEEEECCCCC	16.58	21712546
257	Phosphorylation	ALSVETDYTFPLAEK EEEEECCCCCCHHHH	20.07	22817900
264	Acetylation	YTFPLAEKVKAFLAD CCCCHHHHHHHHHCC	43.35	26051181
264	Ubiquitination	YTFPLAEKVKAFLAD CCCCHHHHHHHHHCC	43.35	21906983
266	2-Hydroxyisobutyrylation	FPLAEKVKAFLADPS CCHHHHHHHHHCCHH	44.48	-
266	Ubiquitination	FPLAEKVKAFLADPS CCHHHHHHHHHCCHH	44.48	21906983
273	Phosphorylation	KAFLADPSAFVAAAP HHHHCCHHHHHHHHH	34.58	20068231
285	Phosphorylation	AAPVAAATTAAPAAA HHHHHHHHCHHHHHH	16.55	23927012
286	Phosphorylation	APVAAATTAAPAAAA HHHHHHHCHHHHHHH	18.98	23927012
297	Ubiquitination	AAAAAPAKVEAKEES HHHHCCCEEEHHHHC	39.28	21906983
297	Acetylation	AAAAAPAKVEAKEES HHHHCCCEEEHHHHC	39.28	26051181
297	Sumoylation	AAAAAPAKVEAKEES HHHHCCCEEEHHHHC	39.28	25114211
301	Ubiquitination	APAKVEAKEESEESD CCCEEEHHHHCCCCC	48.81	-
304	Phosphorylation	KVEAKEESEESDEDM EEEHHHHCCCCCCCC	47.99	26846344
307	Phosphorylation	AKEESEESDEDMGFG HHHHCCCCCCCCCCC	42.10	26846344

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 RLA0_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RLA0_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 RLA0_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS6_HUMAN	RPS6	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RLA1_HUMAN	RPLP1	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RLA2_HUMAN	RPLP2	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS10_HUMAN	RPS10	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
VASN_HUMAN	VASN	physical	22939629
AIMP1_HUMAN	AIMP1	physical	22863883
SYDC_HUMAN	DARS	physical	22863883
MCA3_HUMAN	EEF1E1	physical	22863883
SYIC_HUMAN	IARS	physical	22863883
IQGA1_HUMAN	IQGAP1	physical	22863883
LRRF1_HUMAN	LRRFIP1	physical	22863883
SYMC_HUMAN	MARS	physical	22863883
SYQ_HUMAN	QARS	physical	22863883
RL13_HUMAN	RPL13	physical	22863883
RL19_HUMAN	RPL19	physical	22863883
RL24_HUMAN	RPL24	physical	22863883
CCDB1_HUMAN	CCNDBP1	physical	25416956
CCDB1_HUMAN	CCNDBP1	physical	26186194
ACOX1_HUMAN	ACOX1	physical	26186194
DDX24_HUMAN	DDX24	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
IF2P_HUMAN	EIF5B	physical	26344197
IF6_HUMAN	EIF6	physical	26344197
RACK1_HUMAN	GNB2L1	physical	26344197
GNL1_HUMAN	GNL1	physical	26344197
HSP7C_HUMAN	HSPA8	physical	26344197
IDH3A_HUMAN	IDH3A	physical	26344197
IPO8_HUMAN	IPO8	physical	26344197
MSH2_HUMAN	MSH2	physical	26344197
C1TC_HUMAN	MTHFD1	physical	26344197
P3C2A_HUMAN	PIK3C2A	physical	26344197
PRP8_HUMAN	PRPF8	physical	26344197
RBP2_HUMAN	RANBP2	physical	26344197
RBBP4_HUMAN	RBBP4	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL19_HUMAN	RPL19	physical	26344197
RL21_HUMAN	RPL21	physical	26344197
RL22_HUMAN	RPL22	physical	26344197
RL23_HUMAN	RPL23	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL24_HUMAN	RPL24	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL28_HUMAN	RPL28	physical	26344197
RL3_HUMAN	RPL3	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL31_HUMAN	RPL31	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL34_HUMAN	RPL34	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RPN2_HUMAN	RPN2	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS12_HUMAN	RPS12	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS2_HUMAN	RPS2	physical	26344197
RS20_HUMAN	RPS20	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
RRP7A_HUMAN	RRP7A	physical	26344197
VAPA_HUMAN	VAPA	physical	26344197
VDAC3_HUMAN	VDAC3	physical	26344197
CCDB1_HUMAN	CCNDBP1	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 RLA0_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-77, 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 TYR-24; SER-304 AND SER-307,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-304 AND SER-307, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASSSPECTROMETRY.	18318008 [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-304 AND SER-307, ANDMASS 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-304 AND SER-307, ANDMASS SPECTROMETRY.	18691976 [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-304 AND SER-307, ANDMASS SPECTROMETRY.	19367720 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, ANDMASS SPECTROMETRY.	19007248 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, ANDMASS SPECTROMETRY.	17487921 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, ANDMASS SPECTROMETRY.	16565220 [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-304 AND SER-307, ANDMASS SPECTROMETRY.	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-304 AND SER-307, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASSSPECTROMETRY.	15302935 [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-24, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, AND MASSSPECTROMETRY.	15592455 [Abstract]