dbPTM

EF1D_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF1D_HUMAN
UniProt AC	P29692
Protein Name	Elongation factor 1-delta
Gene Name	EEF1D
Organism	Homo sapiens (Human).
Sequence Length	281
Subcellular Localization	Isoform 2: Nucleus .
Protein Description	Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.; Isoform 2: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE)..
Protein Sequence	MATNFLAHEKIWFDKFKYDDAERRFYEQMNGPVAGASRQENGASVILRDIARARENIQKSLAGSSGPGASSGTSGDHGELVVRIASLEVENQSLRGVVQELQQAISKLEARLNVLEKSSPGHRATAPQTQHVSPMRQVEPPAKKPATPAEDDEDDDIDLFGSDNEEEDKEAAQLREERLRQYAEKKAKKPALVAKSSILLDVKPWDDETDMAQLEACVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEHVQSVDIAAFNKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATNFLAHE ------CCCCCCCCC	15.96	22223895
10	2-Hydroxyisobutyrylation	TNFLAHEKIWFDKFK CCCCCCCCHHHHCCC	35.06	-
10	Acetylation	TNFLAHEKIWFDKFK CCCCCCCCHHHHCCC	35.06	26822725
10	Ubiquitination	TNFLAHEKIWFDKFK CCCCCCCCHHHHCCC	35.06	21890473
10 (in isoform 1)	Ubiquitination	-	35.06	21890473
10	Ubiquitination	TNFLAHEKIWFDKFK CCCCCCCCHHHHCCC	35.06	21890473
12 (in isoform 2)	Phosphorylation	-	13.37	-
15	2-Hydroxyisobutyrylation	HEKIWFDKFKYDDAE CCCHHHHCCCCCHHH	33.99	-
15	Acetylation	HEKIWFDKFKYDDAE CCCHHHHCCCCCHHH	33.99	26051181
15	Ubiquitination	HEKIWFDKFKYDDAE CCCHHHHCCCCCHHH	33.99	21890473
15 (in isoform 1)	Ubiquitination	-	33.99	21890473
15	Ubiquitination	HEKIWFDKFKYDDAE CCCHHHHCCCCCHHH	33.99	21890473
17	Acetylation	KIWFDKFKYDDAERR CHHHHCCCCCHHHHH	54.21	19608861
17	Ubiquitination	KIWFDKFKYDDAERR CHHHHCCCCCHHHHH	54.21	19608861
18	Phosphorylation	IWFDKFKYDDAERRF HHHHCCCCCHHHHHH	23.37	21945579
22	Ubiquitination	KFKYDDAERRFYEQM CCCCCHHHHHHHHHH	51.92	21890473
24	Methylation	KYDDAERRFYEQMNG CCCHHHHHHHHHHCC	29.97	-
26	Nitration	DDAERRFYEQMNGPV CHHHHHHHHHHCCCC	11.93	-
26	Phosphorylation	DDAERRFYEQMNGPV CHHHHHHHHHHCCCC	11.93	21945579
27	Ubiquitination	DAERRFYEQMNGPVA HHHHHHHHHHCCCCC	40.41	21890473
29	Sulfoxidation	ERRFYEQMNGPVAGA HHHHHHHHCCCCCCC	4.12	28465586
37	Phosphorylation	NGPVAGASRQENGAS CCCCCCCCCCCCCCC	33.31	21945579
37 (in isoform 3)	Phosphorylation	-	33.31	22496350
40 (in isoform 3)	Phosphorylation	-	57.43	25159151
41 (in isoform 3)	Phosphorylation	-	42.89	28355574
44	Phosphorylation	SRQENGASVILRDIA CCCCCCCCHHHHHHH	15.87	23401153
46 (in isoform 3)	Phosphorylation	-	2.12	30108239
47 (in isoform 3)	Phosphorylation	-	3.64	20068231
49 (in isoform 3)	Phosphorylation	-	35.14	26552605
50 (in isoform 3)	Phosphorylation	-	1.95	27251275
59	Acetylation	RARENIQKSLAGSSG HHHHHHHHHHCCCCC	43.57	26051181
59	Ubiquitination	RARENIQKSLAGSSG HHHHHHHHHHCCCCC	43.57	21890473
59 (in isoform 1)	Ubiquitination	-	43.57	21890473
60	Phosphorylation	ARENIQKSLAGSSGP HHHHHHHHHCCCCCC	13.69	29255136
64	Phosphorylation	IQKSLAGSSGPGASS HHHHHCCCCCCCCCC	26.89	23401153
64 (in isoform 4)	Phosphorylation	-	26.89	25159151
65	Phosphorylation	QKSLAGSSGPGASSG HHHHCCCCCCCCCCC	48.35	30278072
70	Phosphorylation	GSSGPGASSGTSGDH CCCCCCCCCCCCCCC	34.90	23911959
71	Phosphorylation	SSGPGASSGTSGDHG CCCCCCCCCCCCCCC	45.62	30278072
71 (in isoform 4)	Phosphorylation	-	45.62	25627689
73	Phosphorylation	GPGASSGTSGDHGEL CCCCCCCCCCCCCCE	31.33	21712546
74	Phosphorylation	PGASSGTSGDHGELV CCCCCCCCCCCCCEE	45.83	23898821
77 (in isoform 2)	Phosphorylation	-	34.84	24300666
83	Acetylation	DHGELVVRIASLEVE CCCCEEEEEEEEEEC	15.98	19608861
83	Ubiquitination	DHGELVVRIASLEVE CCCCEEEEEEEEEEC	15.98	19608861
83	Ubiquitination	DHGELVVRIASLEVE CCCCEEEEEEEEEEC	15.98	21890473
86	Phosphorylation	ELVVRIASLEVENQS CEEEEEEEEEECCCH	23.77	30266825
88	Acetylation	VVRIASLEVENQSLR EEEEEEEEECCCHHH	45.34	19608861
88	Ubiquitination	VVRIASLEVENQSLR EEEEEEEEECCCHHH	45.34	19608861
91 (in isoform 2)	Phosphorylation	-	41.75	18669648
93	Acetylation	SLEVENQSLRGVVQE EEEECCCHHHHHHHH	31.45	19608861
93	Phosphorylation	SLEVENQSLRGVVQE EEEECCCHHHHHHHH	31.45	20068231
93	Ubiquitination	SLEVENQSLRGVVQE EEEECCCHHHHHHHH	31.45	19608861
94 (in isoform 2)	Phosphorylation	-	3.88	25159151
95	Methylation	EVENQSLRGVVQELQ EECCCHHHHHHHHHH	40.90	-
98	Acetylation	NQSLRGVVQELQQAI CCHHHHHHHHHHHHH	3.99	19608861
98	Ubiquitination	NQSLRGVVQELQQAI CCHHHHHHHHHHHHH	3.99	19608861
106	Phosphorylation	QELQQAISKLEARLN HHHHHHHHHHHHHHH	33.92	22617229
107	Acetylation	ELQQAISKLEARLNV HHHHHHHHHHHHHHH	44.21	19608861
107	Ubiquitination	ELQQAISKLEARLNV HHHHHHHHHHHHHHH	44.21	21890473
107 (in isoform 1)	Ubiquitination	-	44.21	21890473
107 (in isoform 2)	Phosphorylation	-	44.21	25693802
117	2-Hydroxyisobutyrylation	ARLNVLEKSSPGHRA HHHHHHHHCCCCCCC	52.66	-
117	Acetylation	ARLNVLEKSSPGHRA HHHHHHHHCCCCCCC	52.66	19608861
117	Malonylation	ARLNVLEKSSPGHRA HHHHHHHHCCCCCCC	52.66	26320211
117	Succinylation	ARLNVLEKSSPGHRA HHHHHHHHCCCCCCC	52.66	-
117	Succinylation	ARLNVLEKSSPGHRA HHHHHHHHCCCCCCC	52.66	-
117	Ubiquitination	ARLNVLEKSSPGHRA HHHHHHHHCCCCCCC	52.66	19608861
118	Phosphorylation	RLNVLEKSSPGHRAT HHHHHHHCCCCCCCC	32.18	25159151
119	Phosphorylation	LNVLEKSSPGHRATA HHHHHHCCCCCCCCC	46.07	25159151
125	Phosphorylation	SSPGHRATAPQTQHV CCCCCCCCCCCCCCC	38.54	29255136
129	Phosphorylation	HRATAPQTQHVSPMR CCCCCCCCCCCCCCC	21.42	29255136
133	Phosphorylation	APQTQHVSPMRQVEP CCCCCCCCCCCCCCC	15.74	20201521
135	Sulfoxidation	QTQHVSPMRQVEPPA CCCCCCCCCCCCCCC	3.49	21406390
147	Phosphorylation	PPAKKPATPAEDDED CCCCCCCCCCCCCCC	31.40	19664994
162	Phosphorylation	DDIDLFGSDNEEEDK CCCCCCCCCCHHHHH	29.90	19664994
169	Ubiquitination	SDNEEEDKEAAQLRE CCCHHHHHHHHHHHH	53.16	-
178	Methylation	AAQLREERLRQYAEK HHHHHHHHHHHHHHH	30.34	-
182	Phosphorylation	REERLRQYAEKKAKK HHHHHHHHHHHHCCC	15.42	29341593
185	Acetylation	RLRQYAEKKAKKPAL HHHHHHHHHCCCCCE	50.27	26051181
185	Succinylation	RLRQYAEKKAKKPAL HHHHHHHHHCCCCCE	50.27	23954790
185	Ubiquitination	RLRQYAEKKAKKPAL HHHHHHHHHCCCCCE	50.27	-
186	Ubiquitination	LRQYAEKKAKKPALV HHHHHHHHCCCCCEE	57.87	-
188	Ubiquitination	QYAEKKAKKPALVAK HHHHHHCCCCCEEEC	69.07	-
189	2-Hydroxyisobutyrylation	YAEKKAKKPALVAKS HHHHHCCCCCEEECC	40.14	-
189	Ubiquitination	YAEKKAKKPALVAKS HHHHHCCCCCEEECC	40.14	21906983
196	Phosphorylation	KPALVAKSSILLDVK CCCEEECCEEEECCC	16.93	25627689
197	Phosphorylation	PALVAKSSILLDVKP CCEEECCEEEECCCC	19.29	22985185
203	Acetylation	SSILLDVKPWDDETD CEEEECCCCCCCCCC	39.80	19825591
203	Sumoylation	SSILLDVKPWDDETD CEEEECCCCCCCCCC	39.80	-
208	Ubiquitination	DVKPWDDETDMAQLE CCCCCCCCCCHHHHH	44.21	21890473
209	Phosphorylation	VKPWDDETDMAQLEA CCCCCCCCCHHHHHH	37.76	22817901
211	Sulfoxidation	PWDDETDMAQLEACV CCCCCCCHHHHHHHH	3.14	30846556
220	Phosphorylation	QLEACVRSIQLDGLV HHHHHHHHHCCCCEE	8.35	21712546
225	Ubiquitination	VRSIQLDGLVWGASK HHHHCCCCEEECCCC	30.62	21890473
231	Phosphorylation	DGLVWGASKLVPVGY CCEEECCCCCEEECC	23.68	21712546
232	Ubiquitination	GLVWGASKLVPVGYG CEEECCCCCEEECCC	53.63	2189047
232 (in isoform 1)	Ubiquitination	-	53.63	21890473
238	Phosphorylation	SKLVPVGYGIRKLQI CCCEEECCCEEEEEE	15.04	25394399
242	2-Hydroxyisobutyrylation	PVGYGIRKLQIQCVV EECCCEEEEEEEEEE	42.71	-
242	Ubiquitination	PVGYGIRKLQIQCVV EECCCEEEEEEEEEE	42.71	-
247 (in isoform 2)	Phosphorylation	-	3.85	25884760
265	Ubiquitination	LLEEEITKFEEHVQS HHHHHHHHHHHHHHH	57.34	-
280	2-Hydroxyisobutyrylation	VDIAAFNKI------ CCHHHHCCC------	43.25	-
280	Ubiquitination	VDIAAFNKI------ CCHHHHCCC------	43.25	-
376 (in isoform 2)	Ubiquitination	-		21890473
381 (in isoform 2)	Ubiquitination	-		21890473
403	Phosphorylation	--------------------------------------------------------------------------------------------------------------------------------- ---------------------------------------------------------------------------------------------------------------------------------		27251275
410	Phosphorylation	---------------------------------------------------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------------------------------------------------		24719451
425 (in isoform 2)	Ubiquitination	-		21890473
426	Phosphorylation	-------------------------------------------------------------------------------------------------------------------------------------------------------- --------------------------------------------------------------------------------------------------------------------------------------------------------		27251275
430	Phosphorylation	------------------------------------------------------------------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------------------------------------------------------------------		24719451
431	Phosphorylation	------------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------------		27251275
436	Phosphorylation	------------------------------------------------------------------------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------------------------------------------------------------------------		27251275
437	Phosphorylation	------------------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------------------		24719451
452	Phosphorylation	---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		24719451
473 (in isoform 2)	Ubiquitination	-		21890473
483 (in isoform 2)	Ubiquitination	-		-
484	Phosphorylation	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		27251275
485	Phosphorylation	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		24719451
491	Phosphorylation	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		27251275
495	Phosphorylation	----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- -----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		27251275
499	Phosphorylation	--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		27251275
513	Phosphorylation	----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- -----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		27251275
528	Phosphorylation	-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		24719451
598 (in isoform 2)	Ubiquitination	-		21890473

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
133	S	Phosphorylation	Kinase	CDK1	P06493	PSP
162	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
162	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
162	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EF1D_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 EF1D_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EF1G_HUMAN	EEF1G	physical	16189514
CD48_HUMAN	CD48	physical	16169070
EF1D_HUMAN	EEF1D	physical	16169070
DPYL1_HUMAN	CRMP1	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
GARS_HUMAN	GARS	physical	11829477
RL15_HUMAN	RPL15	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
TPR_HUMAN	TPR	physical	22939629
MCCA_HUMAN	MCCC1	physical	22939629
SF3A3_HUMAN	SF3A3	physical	22939629
FLNC_HUMAN	FLNC	physical	22939629
TF65_HUMAN	RELA	physical	21988832
SIAH1_HUMAN	SIAH1	physical	21988832
SIAH2_HUMAN	SIAH2	physical	21988832
SQSTM_HUMAN	SQSTM1	physical	21988832
CAMP2_HUMAN	CAMSAP2	physical	20195357
RHG21_HUMAN	ARHGAP21	physical	20195357
ATG7_HUMAN	ATG7	physical	20195357
MAP1B_HUMAN	MAP1B	physical	20195357
SYEP_HUMAN	EPRS	physical	20195357
BAG6_HUMAN	BAG6	physical	22863883
OARD1_HUMAN	OARD1	physical	22863883
LMNA_HUMAN	LMNA	physical	22863883
PSD10_HUMAN	PSMD10	physical	22863883
ZW10_HUMAN	ZW10	physical	22863883
EF1D_HUMAN	EEF1D	physical	25416956
EF1G_HUMAN	EEF1G	physical	25416956
SIAH1_HUMAN	SIAH1	physical	25416956
TCTP_HUMAN	TPT1	physical	25416956
ERP27_HUMAN	ERP27	physical	25416956
ACLY_HUMAN	ACLY	physical	26344197
AHNK_HUMAN	AHNAK	physical	26344197
AKAP8_HUMAN	AKAP8	physical	26344197
DDX46_HUMAN	DDX46	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
EF1B_HUMAN	EEF1B2	physical	26344197
EF1G_HUMAN	EEF1G	physical	26344197
T2FA_HUMAN	GTF2F1	physical	26344197
HCFC1_HUMAN	HCFC1	physical	26344197
HNRPK_HUMAN	HNRNPK	physical	26344197
HSPB1_HUMAN	HSPB1	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
RTN4_HUMAN	RTN4	physical	26344197
STMN1_HUMAN	STMN1	physical	26344197
SPT5H_HUMAN	SUPT5H	physical	26344197
SYVC_HUMAN	VARS	physical	26344197
ABTB1_HUMAN	ABTB1	physical	21516116
SYCC_HUMAN	CARS	physical	28514442
MCE1_HUMAN	RNGTT	physical	28514442
ATP23_HUMAN	XRCC6BP1	physical	28514442
SYVC_HUMAN	VARS	physical	28514442
KTN1_HUMAN	KTN1	physical	28514442
EF1B_HUMAN	EEF1B2	physical	28514442
ANGE2_HUMAN	ANGEL2	physical	28514442
RRBP1_HUMAN	RRBP1	physical	28514442
HASP_HUMAN	GSG2	physical	28514442
SAHH3_HUMAN	AHCYL2	physical	28514442
VWA8_HUMAN	VWA8	physical	28514442
C1QBP_HUMAN	C1QBP	physical	28514442
TBB8_HUMAN	TUBB8	physical	28514442
CR025_HUMAN	C18orf25	physical	28514442
MAP1B_HUMAN	MAP1B	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 EF1D_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-133; THR-147 AND SER-162, AND MASSSPECTROMETRY.	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-17; LYS-107 AND LYS-117, ANDMASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Unbiased functional proteomics strategy for protein kinase inhibitorvalidation and identification of bona fide protein kinase substrates:application to identification of as a substrate for CK2."; Gyenis L., Duncan J.S., Turowec J.P., Bretner M., Litchfield D.W.; J. Proteome Res. 10:4887-4901(2011). Cited for: PHOSPHORYLATION AT SER-162 BY CK2.	21936567 [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-162, AND MASSSPECTROMETRY.	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 THR-129; SER-133 ANDSER-162, AND MASS SPECTROMETRY.	19369195 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-133; THR-147 AND SER-162, AND MASSSPECTROMETRY.	19413330 [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-162, 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-133; THR-147 ANDSER-162, AND MASS 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-133; THR-147 ANDSER-162, AND MASS 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-133, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.	18187866 [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-60; SER-119; THR-129;SER-133; THR-147 AND SER-162, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASSSPECTROMETRY.	17693683 [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 SER-133, AND MASSSPECTROMETRY.	17924679 [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-133 AND SER-162, ANDMASS SPECTROMETRY.	17487921 [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-162, AND MASSSPECTROMETRY.	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-133; THR-147 ANDSER-162, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASSSPECTROMETRY.	16097034 [Abstract]