dbPTM

EF2K_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF2K_HUMAN
UniProt AC	O00418
Protein Name	Eukaryotic elongation factor 2 kinase
Gene Name	EEF2K
Organism	Homo sapiens (Human).
Sequence Length	725
Subcellular Localization
Protein Description	Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced..
Protein Sequence	MADEDLIFRLEGVDGGQSPRAGHDGDSDGDSDDEEGYFICPITDDPSSNQNVNSKVNKYYSNLTKSERYSSSGSPANSFHFKEAWKHAIQKAKHMPDPWAEFHLEDIATERATRHRYNAVTGEWLDDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRDVYFEDVRLQMEAKLWGEEYNRHKPPKQVDIMQMCIIELKDRPGKPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTETGTDFGDGNLGVRGMALFFYSHACNRICESMGLAPFDLSPRERDAVNQNTKLLQSAKTILRGTEEKCGSPQVRTLSGSRPPLLRPLSENSGDENMSDVTFDSLPSSPSSATPHSQKLDHLHWPVFSDLDNMASRDHDHLDNHRESENSGDSGYPSEKRGELDDPEPREHGHSYSNRKYESDEDSLGSSGRVCVEKWNLLNSSRLHLPRASAVALEVQRLNALDLEKKIGKSILGKVHLAMVRYHEGGRFCEKGEEWDQESAVFHLEHAANLGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRQSMILVARAFDSGQNLSPDRCQDWLEALHWYNTALEMTDCDEGGEYDGMQDEPRYMMLAREAEMLFTGGYGLEKDPQRSGDLYTQAAEAAMEAMKGRLANQYYQKAEEAWAQMEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADEDLIFR ------CCCCCEEEE	28.97	22223895
18	Phosphorylation	EGVDGGQSPRAGHDG ECCCCCCCCCCCCCC	21.45	19664994
27	Phosphorylation	RAGHDGDSDGDSDDE CCCCCCCCCCCCCCC	49.36	26503892
31	Phosphorylation	DGDSDGDSDDEEGYF CCCCCCCCCCCCCEE	53.11	26503892
37	Phosphorylation	DSDDEEGYFICPITD CCCCCCCEEEEECCC	7.95	23927012
43	Phosphorylation	GYFICPITDDPSSNQ CEEEEECCCCCCCCC	21.35	23927012
47	Phosphorylation	CPITDDPSSNQNVNS EECCCCCCCCCCHHH	49.25	23927012
48	Phosphorylation	PITDDPSSNQNVNSK ECCCCCCCCCCHHHH	48.07	23927012
54	Phosphorylation	SSNQNVNSKVNKYYS CCCCCHHHHHHHHHH	33.43	23927012
58	Ubiquitination	NVNSKVNKYYSNLTK CHHHHHHHHHHCCCH	48.86	29967540
59	Phosphorylation	VNSKVNKYYSNLTKS HHHHHHHHHHCCCHH	13.61	28796482
60	Phosphorylation	NSKVNKYYSNLTKSE HHHHHHHHHCCCHHH	7.84	28796482
61	Phosphorylation	SKVNKYYSNLTKSER HHHHHHHHCCCHHHH	23.44	28796482
65	Ubiquitination	KYYSNLTKSERYSSS HHHHCCCHHHHCCCC	54.18	22817900
66	Phosphorylation	YYSNLTKSERYSSSG HHHCCCHHHHCCCCC	23.28	25159151
69	Phosphorylation	NLTKSERYSSSGSPA CCCHHHHCCCCCCCC	14.62	23927012
70	Phosphorylation	LTKSERYSSSGSPAN CCHHHHCCCCCCCCC	25.01	25463755
71	Phosphorylation	TKSERYSSSGSPANS CHHHHCCCCCCCCCH	29.77	25463755
72	Phosphorylation	KSERYSSSGSPANSF HHHHCCCCCCCCCHH	37.03	22167270
74	Phosphorylation	ERYSSSGSPANSFHF HHCCCCCCCCCHHHH	23.84	22167270
78	Phosphorylation	SSGSPANSFHFKEAW CCCCCCCHHHHHHHH	23.39	15024086
82	Ubiquitination	PANSFHFKEAWKHAI CCCHHHHHHHHHHHH	37.64	29967540
86	Ubiquitination	FHFKEAWKHAIQKAK HHHHHHHHHHHHHHH	30.15	29967540
93	Ubiquitination	KHAIQKAKHMPDPWA HHHHHHHHCCCCCCH	47.69	29967540
132	Ubiquitination	LDDEVLIKMASQPFG CCHHHHHHHHCCCCC	25.01	-
135	Phosphorylation	EVLIKMASQPFGRGA HHHHHHHCCCCCHHH	34.58	22817900
151	Ubiquitination	RECFRTKKLSNFLHA HHHHHHHHHHHHHHH	57.44	29967540
162	Ubiquitination	FLHAQQWKGASNYVA HHHHHHCCCCHHHHH	40.02	21906983
170	Ubiquitination	GASNYVAKRYIEPVD CCHHHHHHHHCCCCC	35.37	29967540
178	Methylation	RYIEPVDRDVYFEDV HHCCCCCCCCCHHHH	35.21	-
202	Ubiquitination	GEEYNRHKPPKQVDI HHHHHCCCCCCCCCE	60.83	29967540
223	Ubiquitination	ELKDRPGKPLFHLEH EECCCCCCCCEEEEE	41.03	29967540
235	Ubiquitination	LEHYIEGKYIKYNSN EEEEECCEEEEECCC	30.89	22817900
236	Phosphorylation	EHYIEGKYIKYNSNS EEEECCEEEEECCCC	17.32	22817900
238	Ubiquitination	YIEGKYIKYNSNSGF EECCEEEEECCCCCC	34.98	21890473
239	Phosphorylation	IEGKYIKYNSNSGFV ECCEEEEECCCCCCC	17.79	23312004
241	Phosphorylation	GKYIKYNSNSGFVRD CEEEEECCCCCCCCC	29.32	29214152
243	Phosphorylation	YIKYNSNSGFVRDDN EEEECCCCCCCCCCC	33.17	29214152
340	Phosphorylation	RDAVNQNTKLLQSAK HHHHHHHHHHHHHHH	17.19	-
341	Ubiquitination	DAVNQNTKLLQSAKT HHHHHHHHHHHHHHH	55.54	21906983
345	Phosphorylation	QNTKLLQSAKTILRG HHHHHHHHHHHHHHC	31.53	26055452
347	Ubiquitination	TKLLQSAKTILRGTE HHHHHHHHHHHHCCH	41.15	22817900
347	Acetylation	TKLLQSAKTILRGTE HHHHHHHHHHHHCCH	41.15	25953088
348	Phosphorylation	KLLQSAKTILRGTEE HHHHHHHHHHHCCHH	25.59	23401153
353	Phosphorylation	AKTILRGTEEKCGSP HHHHHHCCHHHHCCC	34.24	30266825
359	Phosphorylation	GTEEKCGSPQVRTLS CCHHHHCCCCCCCCC	22.94	30266825
364	Phosphorylation	CGSPQVRTLSGSRPP HCCCCCCCCCCCCCC	26.81	23909892
366	Phosphorylation	SPQVRTLSGSRPPLL CCCCCCCCCCCCCCC	33.82	15024086
368	Phosphorylation	QVRTLSGSRPPLLRP CCCCCCCCCCCCCCC	37.93	23312004
377	Phosphorylation	PPLLRPLSENSGDEN CCCCCCCCCCCCCCC	37.10	15024086
380	Phosphorylation	LRPLSENSGDENMSD CCCCCCCCCCCCCCC	43.50	23909892
386	Phosphorylation	NSGDENMSDVTFDSL CCCCCCCCCCCCCCC	40.28	25137130
389	Phosphorylation	DENMSDVTFDSLPSS CCCCCCCCCCCCCCC	27.07	25137130
392	Phosphorylation	MSDVTFDSLPSSPSS CCCCCCCCCCCCCCC	37.68	30576142
395	Phosphorylation	VTFDSLPSSPSSATP CCCCCCCCCCCCCCC	61.24	25137130
396	Phosphorylation	TFDSLPSSPSSATPH CCCCCCCCCCCCCCC	27.19	15024086
398	Phosphorylation	DSLPSSPSSATPHSQ CCCCCCCCCCCCCCC	34.26	15024086
399	Phosphorylation	SLPSSPSSATPHSQK CCCCCCCCCCCCCCC	39.28	30576142
401	Phosphorylation	PSSPSSATPHSQKLD CCCCCCCCCCCCCCC	24.39	26074081
404	Phosphorylation	PSSATPHSQKLDHLH CCCCCCCCCCCCCCC	30.16	27251275
416	Phosphorylation	HLHWPVFSDLDNMAS CCCCCCCCCHHHHHH	37.18	-
435	Phosphorylation	HLDNHRESENSGDSG CHHCCCCCCCCCCCC	41.87	23927012
438	Phosphorylation	NHRESENSGDSGYPS CCCCCCCCCCCCCCC	39.67	23927012
441	Phosphorylation	ESENSGDSGYPSEKR CCCCCCCCCCCCHHC	43.69	23927012
443	Phosphorylation	ENSGDSGYPSEKRGE CCCCCCCCCCHHCCC	13.92	23927012
445	Phosphorylation	SGDSGYPSEKRGELD CCCCCCCCHHCCCCC	47.46	23401153
447	Ubiquitination	DSGYPSEKRGELDDP CCCCCCHHCCCCCCC	70.78	-
462	Phosphorylation	EPREHGHSYSNRKYE CCCCCCCCCCCCCCC	34.54	30242111
464	Ubiquitination	REHGHSYSNRKYESD CCCCCCCCCCCCCCC	32.92	22053931
464	Phosphorylation	REHGHSYSNRKYESD CCCCCCCCCCCCCCC	32.92	27251275
467	Sumoylation	GHSYSNRKYESDEDS CCCCCCCCCCCCCCC	58.58	-
467	Sumoylation	GHSYSNRKYESDEDS CCCCCCCCCCCCCCC	58.58	-
468	Phosphorylation	HSYSNRKYESDEDSL CCCCCCCCCCCCCCC	19.89	22167270
470	Phosphorylation	YSNRKYESDEDSLGS CCCCCCCCCCCCCCC	43.12	22167270
474	Phosphorylation	KYESDEDSLGSSGRV CCCCCCCCCCCCCCC	32.36	22167270
477	Phosphorylation	SDEDSLGSSGRVCVE CCCCCCCCCCCCHHH	34.61	23927012
478	Phosphorylation	DEDSLGSSGRVCVEK CCCCCCCCCCCHHHH	28.90	23927012
485	Ubiquitination	SGRVCVEKWNLLNSS CCCCHHHHHCCCCCC	22.45	23000965
491	Phosphorylation	EKWNLLNSSRLHLPR HHHCCCCCCCCCCCH	19.46	25159151
492	Phosphorylation	KWNLLNSSRLHLPRA HHCCCCCCCCCCCHH	37.48	30576142
500	Phosphorylation	RLHLPRASAVALEVQ CCCCCHHHHHHHHHH	25.26	26329039
516	Ubiquitination	LNALDLEKKIGKSIL HCCCCHHHHHCHHHH	57.92	-
517	Ubiquitination	NALDLEKKIGKSILG CCCCHHHHHCHHHHC	47.52	29967540
520	Ubiquitination	DLEKKIGKSILGKVH CHHHHHCHHHHCCCE	37.48	29967540
521	Phosphorylation	LEKKIGKSILGKVHL HHHHHCHHHHCCCEE	20.17	21712546
582	Ubiquitination	SQLPHHILADVSLKE HCCCHHHHCCCCCCC	2.64	21890473
596	Ubiquitination	ETEENKTKGFDYLLK CCHHHHCCCHHHHHH	60.22	29967540
600	Phosphorylation	NKTKGFDYLLKAAEA HHCCCHHHHHHHHHC	16.21	20068231
603	Ubiquitination	KGFDYLLKAAEAGDR CCHHHHHHHHHCCCC	42.85	21906983
622	Phosphorylation	LVARAFDSGQNLSPD EEEEECCCCCCCCHH	35.51	22468782
627	Phosphorylation	FDSGQNLSPDRCQDW CCCCCCCCHHHHHHH	32.10	21815630
684	Ubiquitination	TGGYGLEKDPQRSGD HCCCCCCCCCCCCCC	78.67	23503661
689	Phosphorylation	LEKDPQRSGDLYTQA CCCCCCCCCCHHHHH	31.26	29759185
693	Phosphorylation	PQRSGDLYTQAAEAA CCCCCCHHHHHHHHH	11.10	29759185
694	Phosphorylation	QRSGDLYTQAAEAAM CCCCCHHHHHHHHHH	21.01	28787133
705	Ubiquitination	EAAMEAMKGRLANQY HHHHHHHHHHHHHHH	48.18	23503661
712	Phosphorylation	KGRLANQYYQKAEEA HHHHHHHHHHHHHHH	13.99	27642862
713	Phosphorylation	GRLANQYYQKAEEAW HHHHHHHHHHHHHHH	8.18	27642862
715	Ubiquitination	LANQYYQKAEEAWAQ HHHHHHHHHHHHHHH	41.46	-
723	Sulfoxidation	AEEAWAQMEE----- HHHHHHHHCC-----	4.89	30846556

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
61	S	Phosphorylation	Kinase	EEF2K	O00418	PSP
66	S	Phosphorylation	Kinase	EEF2K	O00418	PSP
72	S	Phosphorylation	Kinase	MTOR	P42345	PSP
74	S	Phosphorylation	Kinase	MTOR	P42345	PSP
78	S	Phosphorylation	Kinase	AMPK_GROUP	-	PhosphoELM
78	S	Phosphorylation	Kinase	CHAK1	Q96QT4	PSP
78	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
78	S	Phosphorylation	Kinase	EEF2K	O00418	PSP
348	T	Phosphorylation	Kinase	EEF2K	O00418	PSP
353	T	Phosphorylation	Kinase	EEF2K	O00418	PSP
359	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
359	S	Phosphorylation	Kinase	MK13	O15264	PhosphoELM
359	S	Phosphorylation	Kinase	P38D	O15264	PSP
366	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
366	S	Phosphorylation	Kinase	AMPK_GROUP	-	PhosphoELM
366	S	Phosphorylation	Kinase	P70-SUBFAMILY	-	GPS
366	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
366	S	Phosphorylation	Kinase	EEF2K	O00418	PSP
366	S	Phosphorylation	Kinase	P90RSK	Q15418	PSP
366	S	Phosphorylation	Kinase	P70S6K	P23443	PSP
366	S	Phosphorylation	Kinase	RPS6KB2	Q9UBS0	GPS
366	S	Phosphorylation	Kinase	P70S6K_GROUP	-	PhosphoELM
366	S	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
377	S	Phosphorylation	Kinase	MAPKAPK3	Q16644	GPS
377	S	Phosphorylation	Kinase	MAPKAPK5	Q8IW41	GPS
377	S	Phosphorylation	Kinase	MAPK2	P49137	PhosphoELM
396	S	Phosphorylation	Kinase	MAPK13	O15264	GPS
396	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
396	S	Phosphorylation	Kinase	MAPK11	Q15759	GPS
396	S	Phosphorylation	Kinase	EEF2K	O00418	PSP
398	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
398	S	Phosphorylation	Kinase	AMPK_GROUP	-	PhosphoELM
398	S	Phosphorylation	Kinase	PRKAA2	P54646	GPS
398	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
398	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
441	S	Phosphorylation	Kinase	EEF2K	O00418	PSP
445	S	Phosphorylation	Kinase	EEF2K	O00418	PSP
474	S	Phosphorylation	Kinase	EEF2K	O00418	PSP
491	S	Phosphorylation	Kinase	EEF2K	O00418	PSP
500	S	Phosphorylation	Kinase	EEF2K	O00418	PSP
500	S	Phosphorylation	Kinase	PKA	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:22669845

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
78	S	Phosphorylation	21112387
Phosphorylated by TRPM7 at Ser-78 resulting in improved protein stability, higher EE2F phosphorylated and subsequently reduced rate of protein synthesis.
348	T	Phosphorylation	18669648
Autophosphorylated at multiple residues, Thr-348 being the major site.
359	S	Phosphorylation	11500363
Phosphorylation by other kinases such as CDK1 and MAPK13 at Ser-359 or RPS6KA1 and RPS6KB1 at Ser-366 instead decrease EEF2K activity and promote protein synthesis.
366	S	Phosphorylation	11500364
Phosphorylation by other kinases such as CDK1 and MAPK13 at Ser-359 or RPS6KA1 and RPS6KB1 at Ser-366 instead decrease EEF2K activity and promote protein synthesis.
398	S	Phosphorylation	14709557
Phosphorylated by AMP-activated protein kinase AMPK at Ser-398 leading to EEF2K activation and protein synthesis inhibition.

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 EF2K_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FBW1A_HUMAN	BTRC	physical	22669845
SKP1_HUMAN	SKP1	physical	22669845
EF2_HUMAN	EEF2	physical	22669845
CDK1_HUMAN	CDK1	physical	18337751
DENR_HUMAN	DENR	physical	18337751
ALBU_HUMAN	ALB	physical	18337751
ACADV_HUMAN	ACADVL	physical	18337751
MAP2_HUMAN	METAP2	physical	18337751
PA2G4_HUMAN	PA2G4	physical	18337751
IF4A3_HUMAN	EIF4A3	physical	18337751
ARP2_HUMAN	ACTR2	physical	22863883
CALR_HUMAN	CALR	physical	22863883
DPP9_HUMAN	DPP9	physical	22863883
DUS3L_HUMAN	DUS3L	physical	22863883
PANK4_HUMAN	PANK4	physical	22863883
KAP1_HUMAN	PRKAR1B	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
PRPK_HUMAN	TP53RK	physical	22863883
UBE3C_HUMAN	UBE3C	physical	22863883
SRP14_HUMAN	SRP14	physical	23455922
SRP09_HUMAN	SRP9	physical	23455922
RAE1L_HUMAN	RAE1	physical	23455922
ACACA_HUMAN	ACACA	physical	23455922
WDFY3_HUMAN	WDFY3	physical	23455922
FBW1B_HUMAN	FBXW11	physical	23455922
FBW1A_HUMAN	BTRC	physical	23455922

Drug and Disease Associations

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

Regulatory Network of EF2K_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The channel-kinase TRPM7 regulates phosphorylation of thetranslational factor eEF2 via eEF2-k."; Perraud A.L., Zhao X., Ryazanov A.G., Schmitz C.; Cell. Signal. 23:586-593(2011). Cited for: PHOSPHORYLATION AT SER-78.	21112387 [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 SER-18 AND SER-470, 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-18; SER-27; SER-31;SER-470 AND SER-474, AND MASS SPECTROMETRY.	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-18; THR-348; SER-470;SER-474 AND SER-477, AND MASS SPECTROMETRY.	18669648 [Abstract]
"cdc2-cyclin B regulates eEF2 kinase activity in a cell cycle- andamino acid-dependent manner."; Smith E.M., Proud C.G.; EMBO J. 27:1005-1016(2008). Cited for: PHOSPHORYLATION AT SER-359.	18337751 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND MASSSPECTROMETRY.	17287340 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-445, AND MASSSPECTROMETRY.	16964243 [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-18; SER-27; SER-31;TYR-69; SER-70; SER-470 AND SER-474, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Stimulation of the AMP-activated protein kinase leads to activationof eukaryotic elongation factor 2 kinase and to its phosphorylation ata novel site, serine 398."; Browne G.J., Finn S.G., Proud C.G.; J. Biol. Chem. 279:12220-12231(2004). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-398.	14709557 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.	15144186 [Abstract]
"Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6kinase."; Wang X., Li W., Williams M., Terada N., Alessi D.R., Proud C.G.; EMBO J. 20:4370-4379(2001). Cited for: PHOSPHORYLATION AT SER-366 BY RPS6KA1 AND RPS6KB1, AND MUTAGENESIS OFSER-366.	11500364 [Abstract]
"A novel method to identify protein kinase substrates: eEF2 kinase isphosphorylated and inhibited by SAPK4/p38delta."; Knebel A., Morrice N., Cohen P.; EMBO J. 20:4360-4369(2001). Cited for: PHOSPHORYLATION AT SER-359.	11500363 [Abstract]

show

show

show

show

show