dbPTM

MK03_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MK03_HUMAN
UniProt AC	P27361
Protein Name	Mitogen-activated protein kinase 3
Gene Name	MAPK3
Organism	Homo sapiens (Human).
Sequence Length	379
Subcellular Localization	Cytoplasm. Nucleus. Membrane, caveola . Autophosphorylation at Thr-207 promotes nuclear localization.
Protein Description	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade..
Protein Sequence	MAAAAAQGGGGGEPRRTEGVGPGVPGEVEMVKGQPFDVGPRYTQLQYIGEGAYGMVSSAYDHVRKTRVAIKKISPFEHQTYCQRTLREIQILLRFRHENVIGIRDILRASTLEAMRDVYIVQDLMETDLYKLLKSQQLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLINTTCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINMKARNYLQSLPSKTKVAWAKLFPKSDSKALDLLDRMLTFNPNKRITVEEALAHPYLEQYYDPTDEPVAEEPFTFAMELDDLPKERLKELIFQETARFQPGVLEAP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAAAQGG ------CCHHHHCCC	13.05	22223895
17	Phosphorylation	GGGEPRRTEGVGPGV CCCCCCCCCCCCCCC	38.07	25022875
30	Sulfoxidation	GVPGEVEMVKGQPFD CCCCCEEEECCCCCC	4.57	21406390
32	Ubiquitination	PGEVEMVKGQPFDVG CCCEEEECCCCCCCC	50.98	-
55	Sulfoxidation	IGEGAYGMVSSAYDH EECCCHHCHHHHHHH	1.40	30846556
58	Phosphorylation	GAYGMVSSAYDHVRK CCHHCHHHHHHHHHH	21.31	-
72	Ubiquitination	KTRVAIKKISPFEHQ HHCCEEEECCCCCCH	42.16	-
80	Phosphorylation	ISPFEHQTYCQRTLR CCCCCCHHHHHHHHH	28.33	28152594
81	Phosphorylation	SPFEHQTYCQRTLRE CCCCCHHHHHHHHHH	4.68	28152594
110	Phosphorylation	IRDILRASTLEAMRD HHHHHHHHHHHHHHH	27.39	29438985
119	Nitration	LEAMRDVYIVQDLME HHHHHHHHHHHHHHH	10.32	-
127	Phosphorylation	IVQDLMETDLYKLLK HHHHHHHCCHHHHHH	19.83	29438985
130	Nitration	DLMETDLYKLLKSQQ HHHHCCHHHHHHHCC	11.47	-
130	Phosphorylation	DLMETDLYKLLKSQQ HHHHCCHHHHHHHCC	11.47	29438985
155	Ubiquitination	YQILRGLKYIHSANV HHHHHHCHHHHHCCC	45.01	-
156	Nitration	QILRGLKYIHSANVL HHHHHCHHHHHCCCC	14.65	-
159	Phosphorylation	RGLKYIHSANVLHRD HHCHHHHHCCCCCCC	16.39	-
170	Phosphorylation	LHRDLKPSNLLINTT CCCCCCHHHEEEEEC	38.22	22817900
178	Glutathionylation	NLLINTTCDLKICDF HEEEEECCCEEECCC	5.62	22555962
181	Acetylation	INTTCDLKICDFGLA EEECCCEEECCCCCE	28.21	68741
181	Ubiquitination	INTTCDLKICDFGLA EEECCCEEECCCCCE	28.21	21890473
198	Phosphorylation	ADPEHDHTGFLTEYV CCCCCCCCCHHHHHH	35.37	21945579
202	Phosphorylation	HDHTGFLTEYVATRW CCCCCHHHHHHHHCC	24.02	17591920
203	Phosphorylation	DHTGFLTEYVATRWY CCCCHHHHHHHHCCC	39.91	17016520
204	Phosphorylation	HTGFLTEYVATRWYR CCCHHHHHHHHCCCC	7.08	17591920
207	Phosphorylation	FLTEYVATRWYRAPE HHHHHHHHCCCCCCE	16.22	22322096
210	Phosphorylation	EYVATRWYRAPEIML HHHHHCCCCCCEEHH	8.13	23090842
211	Methylation	YVATRWYRAPEIMLN HHHHCCCCCCEEHHC	36.38	-
216	Sulfoxidation	WYRAPEIMLNSKGYT CCCCCEEHHCCCCCC	2.50	21406390
219	Phosphorylation	APEIMLNSKGYTKSI CCEEHHCCCCCCCCH	24.40	17192257
220	Ubiquitination	PEIMLNSKGYTKSID CEEHHCCCCCCCCHH	55.66	21890473
220	Malonylation	PEIMLNSKGYTKSID CEEHHCCCCCCCCHH	55.66	26320211
220	Ubiquitination	PEIMLNSKGYTKSID CEEHHCCCCCCCCHH	55.66	21890473
220	Ubiquitination	PEIMLNSKGYTKSID CEEHHCCCCCCCCHH	55.66	21890473
220	Ubiquitination	PEIMLNSKGYTKSID CEEHHCCCCCCCCHH	55.66	-
220	Acetylation	PEIMLNSKGYTKSID CEEHHCCCCCCCCHH	55.66	26051181
222	Phosphorylation	IMLNSKGYTKSIDIW EHHCCCCCCCCHHHH	18.09	9124279
223	Phosphorylation	MLNSKGYTKSIDIWS HHCCCCCCCCHHHHH	27.30	-
263	Phosphorylation	HILGILGSPSQEDLN HHHHHCCCCCHHHHH	20.24	25159151
265	Phosphorylation	LGILGSPSQEDLNCI HHHCCCCCHHHHHHH	48.15	22817900
283	Phosphorylation	KARNYLQSLPSKTKV HHHHHHHCCCCCCCE	39.39	20873877
286	Phosphorylation	NYLQSLPSKTKVAWA HHHHCCCCCCCEEHH	59.24	24719451
287	Acetylation	YLQSLPSKTKVAWAK HHHCCCCCCCEEHHH	50.88	25953088
287	Ubiquitination	YLQSLPSKTKVAWAK HHHCCCCCCCEEHHH	50.88	-
289	Ubiquitination	QSLPSKTKVAWAKLF HCCCCCCCEEHHHHC	33.42	-
294	Ubiquitination	KTKVAWAKLFPKSDS CCCEEHHHHCCCCCH	39.70	21890473
294	Acetylation	KTKVAWAKLFPKSDS CCCEEHHHHCCCCCH	39.70	25953088
294	Ubiquitination	KTKVAWAKLFPKSDS CCCEEHHHHCCCCCH	39.70	21890473
294	Ubiquitination	KTKVAWAKLFPKSDS CCCEEHHHHCCCCCH	39.70	21890473
298	Ubiquitination	AWAKLFPKSDSKALD EHHHHCCCCCHHHHH	60.61	-
301	Phosphorylation	KLFPKSDSKALDLLD HHCCCCCHHHHHHHH	27.24	-
302	Ubiquitination	LFPKSDSKALDLLDR HCCCCCHHHHHHHHH	58.94	-
302	Methylation	LFPKSDSKALDLLDR HCCCCCHHHHHHHHH	58.94	-
302	Trimethylation	LFPKSDSKALDLLDR HCCCCCHHHHHHHHH	58.94	-
309	Methylation	KALDLLDRMLTFNPN HHHHHHHHHHHCCCC	23.21	-
317	Ubiquitination	MLTFNPNKRITVEEA HHHCCCCCCCCHHHH	46.57	-
343 (in isoform 3)	Phosphorylation	-	67.45	-
343	Phosphorylation	PTDEPVAEEPFTFAM CCCCCCCCCCCEEEE	67.45	-
357	Ubiquitination	MELDDLPKERLKELI EECCCCCHHHHHHHH	63.86	-
357	Sumoylation	MELDDLPKERLKELI EECCCCCHHHHHHHH	63.86	-
361	Ubiquitination	DLPKERLKELIFQET CCCHHHHHHHHHHHH	57.61	-
361	Methylation	DLPKERLKELIFQET CCCHHHHHHHHHHHH	57.61	-
361	Trimethylation	DLPKERLKELIFQET CCCHHHHHHHHHHHH	57.61	-
368	Phosphorylation	KELIFQETARFQPGV HHHHHHHHHCCCCCC	16.61	25022875

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
202	T	Phosphorylation	Kinase	MAP2K_GROUP	-	PhosphoELM
202	T	Phosphorylation	Kinase	MAP2K-FAMILY	-	GPS
202	T	Phosphorylation	Kinase	MP2K1	Q02750	PhosphoELM
202	T	Phosphorylation	Kinase	MP2K2	P36507	PhosphoELM
202	T	Phosphorylation	Kinase	MAP2K1	P29678	GPS
204	Y	Phosphorylation	Kinase	MAP2K1	P29678	GPS
204	Y	Phosphorylation	Kinase	MAP2K_GROUP	-	PhosphoELM
204	Y	Phosphorylation	Kinase	MAP2K-FAMILY	-	GPS
204	Y	Phosphorylation	Kinase	RET	P07949	PSP
204	Y	Phosphorylation	Kinase	MP2K2	P36507	PhosphoELM
204	Y	Phosphorylation	Kinase	MP2K1	Q02750	PhosphoELM
204	Y	Phosphorylation	Kinase	MAPK3	P27361	GPS
204	Y	Phosphorylation	Kinase	LCK	P06240	PSP
204	Y	Phosphorylation	Kinase	JAK2	O60674	PSP
207	T	Phosphorylation	Kinase	MAP2K1	Q02750	GPS
207	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
210	Y	Phosphorylation	Kinase	MAP2K1	Q02750	GPS
343	S	Phosphorylation	Kinase	CDK1	P06493	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	MAP3K1	Q13233	PMID:12049732

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
202	T	Phosphorylation		18669648
Dually phosphorylated on Thr-202 and Tyr-204, which activates the enzyme.

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 MK03_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AT1A1_HUMAN	ATP1A1	physical	15069082
SPIB_HUMAN	SPIB	physical	8632909
KS6A4_HUMAN	RPS6KA4	physical	9792677
BRAF_HUMAN	BRAF	genetic	10869359
RAF1_HUMAN	RAF1	physical	11409918
INSR_HUMAN	INSR	physical	11409918
LYN_HUMAN	LYN	physical	11131153
KS6B1_MOUSE	Rps6kb1	physical	11279232
IEX1_HUMAN	IER3	physical	12356731
JUN_HUMAN	JUN	physical	1922387
MP2K1_HUMAN	MAP2K1	physical	9733512
MKNK1_HUMAN	MKNK1	physical	9155018
ETV1_HUMAN	ETV1	physical	11551945
MP2K1_HUMAN	MAP2K1	physical	10748187
MP2K1_HUMAN	MAP2K1	physical	8226933
MP2K2_HUMAN	MAP2K2	physical	8226933
C1QBP_HUMAN	C1QBP	physical	11866440
GMFB_HUMAN	GMFB	physical	8639570
HDAC4_HUMAN	HDAC4	physical	11114188
SRBP2_HUMAN	SREBF2	physical	10627507
SRBP1_HUMAN	SREBF1	physical	10627507
P53_HUMAN	TP53	physical	10958792
TY3H_HUMAN	TH	physical	1347949
GTF2I_HUMAN	GTF2I	physical	10648599
VDR_HUMAN	VDR	physical	20371703
HNF4A_HUMAN	HNF4A	physical	20371703
RXRA_HUMAN	RXRA	physical	20371703
ELK1_HUMAN	ELK1	physical	20371703
PP2AA_HUMAN	PPP2CA	physical	12624094
CPXM1_HUMAN	CPXM1	physical	18624398
FKBP2_HUMAN	FKBP2	physical	18624398
ID2_HUMAN	ID2	physical	18624398
F261_HUMAN	PFKFB1	physical	18624398
AK1C1_HUMAN	AKR1C1	physical	18624398
CRP_HUMAN	CRP	physical	18624398
TTYH3_HUMAN	TTYH3	physical	18624398
PFKAM_HUMAN	PFKM	physical	18624398
PEA15_HUMAN	PEA15	physical	21900206
ZN219_HUMAN	ZNF219	physical	21900206
BTBDA_HUMAN	BTBD10	physical	21900206
NUP58_HUMAN	NUPL1	physical	21900206
SCND1_HUMAN	SCAND1	physical	21900206
RN114_HUMAN	RNF114	physical	21900206
KS6A6_HUMAN	RPS6KA6	physical	21900206
ARRB1_HUMAN	ARRB1	physical	10347142
DUS1_HUMAN	DUSP1	physical	10617468
UBF1_HUMAN	UBTF	physical	11741541
SP1_HUMAN	SP1	physical	11904305
USO1_HUMAN	USO1	physical	21147777
PTPRE_HUMAN	PTPRE	physical	12754301
FAS_HUMAN	FASN	physical	19847302
HCDH_HUMAN	HADH	physical	19847302
PRDX3_HUMAN	PRDX3	physical	19847302
ATPB_HUMAN	ATP5B	physical	19847302
VDAC1_HUMAN	VDAC1	physical	19847302
MK03_HUMAN	MAPK3	physical	19847302
CREM_HUMAN	CREM	physical	11466319
SYNE2_HUMAN	SYNE2	physical	19861416
RPTOR_HUMAN	RPTOR	physical	21071439
WDR83_HUMAN	WDR83	physical	15118098
SP1_HUMAN	SP1	physical	17889508
BRCA1_HUMAN	BRCA1	physical	18593910
MAGAB_HUMAN	MAGEA11	physical	19828458
MBP_HUMAN	MBP	physical	17906618
HTRA2_HUMAN	HTRA2	physical	17906618
SCRIB_HUMAN	SCRIB	physical	20622900
GAB2_HUMAN	GAB2	physical	14530346
MBP_HUMAN	MBP	physical	14530346
STAB2_HUMAN	STAB2	physical	18387958
MBP_HUMAN	MBP	physical	19910486
RARA_MOUSE	Rara	physical	10383391
ELK1_HUMAN	ELK1	physical	15782123
SRBP2_HUMAN	SREBF2	physical	14988395
ELK4_HUMAN	ELK4	physical	9020136
MAPK2_HUMAN	MAPKAPK2	physical	14499342
ELK1_HUMAN	ELK1	physical	15967991
GAB2_HUMAN	GAB2	physical	15356145
ELK1_HUMAN	ELK1	physical	14499342
CUED2_HUMAN	CUEDC2	physical	23776205
MBP_HUMAN	MBP	physical	11570821
MK01_HUMAN	MAPK1	physical	23602568
MK03_HUMAN	MAPK3	physical	23602568
KS6A2_HUMAN	RPS6KA2	physical	23602568
PHF3_HUMAN	PHF3	physical	23602568
DHYS_HUMAN	DHPS	physical	23602568
TIE2_HUMAN	TEK	physical	23602568
PGH2_HUMAN	PTGS2	physical	21187340
P53_HUMAN	TP53	physical	21187340
HDAC6_HUMAN	HDAC6	physical	24089523
FOXP2_HUMAN	FOXP2	physical	24722188
AMOT_HUMAN	AMOT	physical	24722188
CDC23_HUMAN	CDC23	physical	24722188
DCP1A_HUMAN	DCP1A	physical	24722188
DHYS_HUMAN	DHPS	physical	24722188
LMBL3_HUMAN	L3MBTL3	physical	24722188
MAGD1_HUMAN	MAGED1	physical	24722188
MYOG_HUMAN	MYOG	physical	24722188
NAB2_HUMAN	NAB2	physical	24722188
TRI54_HUMAN	TRIM54	physical	24722188
VPS52_HUMAN	VPS52	physical	24722188
STAR_HUMAN	STAR	physical	19426868
RAF1_HUMAN	RAF1	physical	19058874
MP2K1_HUMAN	MAP2K1	physical	19058874
MK01_HUMAN	MAPK1	physical	19058874
NIPA_HUMAN	ZC3HC1	physical	22955283
CBP_HUMAN	CREBBP	physical	18443043
DHYS_HUMAN	DHPS	physical	25852190
DUS6_HUMAN	DUSP6	physical	25515236
CHK2_HUMAN	CHEK2	physical	26344197
GALE_HUMAN	GALE	physical	26344197
ILKAP_HUMAN	ILKAP	physical	26344197
MET2B_HUMAN	METTL2B	physical	26344197
MTMRC_HUMAN	MTMR12	physical	26344197
NMD3_HUMAN	NMD3	physical	26344197
PAK2_HUMAN	PAK2	physical	26344197
FBXW7_HUMAN	FBXW7	physical	25753158
DHYS_HUMAN	DHPS	physical	26496610
DC1I2_HUMAN	DYNC1I2	physical	26496610
HD_HUMAN	HTT	physical	26496610
LEG3_HUMAN	LGALS3	physical	26496610
PROF1_HUMAN	PFN1	physical	26496610
RBM4_HUMAN	RBM4	physical	26496610
TAF6_HUMAN	TAF6	physical	26496610
TBX3_HUMAN	TBX3	physical	26496610
TIAR_HUMAN	TIAL1	physical	26496610
TPM2_HUMAN	TPM2	physical	26496610
TRPS1_HUMAN	TRPS1	physical	26496610
BAG6_HUMAN	BAG6	physical	26496610
SYMPK_HUMAN	SYMPK	physical	26496610
UBL4A_HUMAN	UBL4A	physical	26496610
CELF1_HUMAN	CELF1	physical	26496610
CPSF5_HUMAN	NUDT21	physical	26496610
WDR43_HUMAN	WDR43	physical	26496610
GSE1_HUMAN	GSE1	physical	26496610
CSTFT_HUMAN	CSTF2T	physical	26496610
APOL2_HUMAN	APOL2	physical	26496610
GEMI5_HUMAN	GEMIN5	physical	26496610
LTN1_HUMAN	LTN1	physical	26496610
SIR6_HUMAN	SIRT6	physical	26496610
PCF11_HUMAN	PCF11	physical	26496610
MCAF1_HUMAN	ATF7IP	physical	26496610
RBM26_HUMAN	RBM26	physical	26496610
IP6K3_HUMAN	IP6K3	physical	26496610
TTC9C_HUMAN	TTC9C	physical	26496610
TM189_HUMAN	TMEM189	physical	26496610
ELK1_HUMAN	ELK1	physical	25241761
DAPK1_HUMAN	DAPK1	physical	25241761
BRAF_HUMAN	BRAF	physical	25241761
GNDS_HUMAN	RALGDS	physical	25241761
DUS9_HUMAN	DUSP9	physical	25241761
ARRB2_HUMAN	ARRB2	physical	25241761
M3K1_HUMAN	MAP3K1	physical	25241761
DUS1_HUMAN	DUSP1	physical	25241761
KS6A3_HUMAN	RPS6KA3	physical	25241761
KS6A2_HUMAN	RPS6KA2	physical	25241761
RET_HUMAN	RET	physical	25241761
ATF2_HUMAN	ATF2	physical	25241761
ITB3_HUMAN	ITGB3	physical	23640055
ITAV_HUMAN	ITGAV	physical	23640055
ELK1_HUMAN	ELK1	physical	16998585
B2L11_HUMAN	BCL2L11	physical	24269611
MK01_HUMAN	MAPK1	physical	16424009
UBP21_HUMAN	USP21	physical	27886188
IRS1_HUMAN	IRS1	physical	17640984

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
DB01169	Arsenic trioxide
DB00605	Sulindac

Regulatory Network of MK03_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, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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-170; THR-198; THR-202AND TYR-204, AND MASS SPECTROMETRY.	19369195 [Abstract]
"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 THR-202 AND TYR-204, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"A new type of ERK1/2 autophosphorylation causes cardiachypertrophy."; Lorenz K., Schmitt J.P., Schmitteckert E.M., Lohse M.J.; Nat. Med. 15:75-83(2009). Cited for: AUTOPHOSPHORYLATION AT THR-207, ENZYME REGULATION, SUBUNIT, ANDSUBCELLULAR LOCATION.	19060905 [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 THR-202 AND TYR-204, 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 THR-202 AND TYR-204, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, ANDMASS SPECTROMETRY.	17389395 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, ANDMASS SPECTROMETRY.	17192257 [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 THR-202 AND TYR-204, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Crystal structure of human mono-phosphorylated ERK1 at Tyr204."; Kinoshita T., Yoshida I., Nakae S., Okita K., Gouda M., Matsubara M.,Yokota K., Ishiguro H., Tada T.; Biochem. Biophys. Res. Commun. 377:1123-1127(2008). Cited for: X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS), AND PHOSPHORYLATION ATTYR-204.	18983981 [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-204, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits theRAS pathway by direct dephosphorylation of ERK1/2 kinases."; Sacco F., Tinti M., Palma A., Ferrari E., Nardozza A.P.,Hooft van Huijsduijnen R., Takahashi T., Castagnoli L., Cesareni G.; J. Biol. Chem. 284:22048-22058(2009). Cited for: PHOSPHORYLATION AT TYR-204, AND DEPHOSPHORYLATION BY PTPRJ AT TYR-204.	19494114 [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-204, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-204, AND MASSSPECTROMETRY.	15951569 [Abstract]

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