dbPTM

IF2P_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF2P_HUMAN
UniProt AC	O60841
Protein Name	Eukaryotic translation initiation factor 5B
Gene Name	EIF5B
Organism	Homo sapiens (Human).
Sequence Length	1220
Subcellular Localization	Cytoplasm .
Protein Description	Plays a role in translation initiation. Translational GTPase that catalyzes the joining of the 40S and 60S subunits to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon. GTP binding and hydrolysis induces conformational changes in the enzyme that renders it active for productive interactions with the ribosome. The release of the enzyme after formation of the initiation complex is a prerequisite to form elongation-competent ribosomes..
Protein Sequence	MGKKQKNKSEDSTKDDIDLDALAAEIEGAGAAKEQEPQKSKGKKKKEKKKQDFDEDDILKELEELSLEAQGIKADRETVAVKPTENNEEEFTSKDKKKKGQKGKKQSFDDNDSEELEDKDSKSKKTAKPKVEMYSGSDDDDDFNKLPKKAKGKAQKSNKKWDGSEEDEDNSKKIKERSRINSSGESGDESDEFLQSRKGQKKNQKNKPGPNIESGNEDDDASFKIKTVAQKKAEKKERERKKRDEEKAKLRKLKEKEELETGKKDQSKQKESQRKFEEETVKSKVTVDTGVIPASEEKAETPTAAEDDNEGDKKKKDKKKKKGEKEEKEKEKKKGPSKATVKAMQEALAKLKEEEERQKREEEERIKRLEELEAKRKEEERLEQEKRERKKQKEKERKERLKKEGKLLTKSQREARARAEATLKLLQAQGVEVPSKDSLPKKRPIYEDKKRKKIPQQLESKEVSESMELCAAVEVMEQGVPEKEETPPPVEPEEEEDTEDAGLDDWEAMASDEETEKVEGNKVHIEVKENPEEEEEEEEEEEEDEESEEEEEEEGESEGSEGDEEDEKVSDEKDSGKTLDKKPSKEMSSDSEYDSDDDRTKEERAYDKAKRRIEKRRLEHSKNVNTEKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDEFEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKILGKDLEKTLAGLPLLVAYKEDEIPVLKDELIHELKQTLNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVMLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKIKILPQYIFNSRDPIVMGVTVEAGQVKQGTPMCVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIPGESPKMFGRHFEATDILVSKISRQSIDALKDWFRDEMQKSDWQLIVELKKVFEII

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	GKKQKNKSEDSTKDD CCCCCCCCCCCCCCC	56.90	25159151
12	Phosphorylation	QKNKSEDSTKDDIDL CCCCCCCCCCCCCCH	33.05	25159151
13	Phosphorylation	KNKSEDSTKDDIDLD CCCCCCCCCCCCCHH	51.30	25159151
33	Ubiquitination	IEGAGAAKEQEPQKS HCCCCCCHHCCCCCC	60.44	-
50	Ubiquitination	KKKKEKKKQDFDEDD CCHHHHHCCCCCHHH	67.19	-
66	Phosphorylation	LKELEELSLEAQGIK HHHHHHHHHHHCCCC	27.69	19664994
73	Ubiquitination	SLEAQGIKADRETVA HHHHCCCCCCCCEEE	51.57	-
78	Phosphorylation	GIKADRETVAVKPTE CCCCCCCEEEECCCC	18.05	27251789
82	Acetylation	DRETVAVKPTENNEE CCCEEEECCCCCCCC	36.16	26051181
92	Phosphorylation	ENNEEEFTSKDKKKK CCCCCCCCCHHHHHC	37.84	25627689
93	Phosphorylation	NNEEEFTSKDKKKKG CCCCCCCCHHHHHCC	44.15	27251789
107	Phosphorylation	GQKGKKQSFDDNDSE CCCCCCCCCCCCCCH	39.25	29255136
113	Phosphorylation	QSFDDNDSEELEDKD CCCCCCCCHHHCCCC	38.94	29255136
121	Phosphorylation	EELEDKDSKSKKTAK HHHCCCCCCCCCCCC	44.56	23927012
123	Phosphorylation	LEDKDSKSKKTAKPK HCCCCCCCCCCCCCC	43.25	23312004
126	Phosphorylation	KDSKSKKTAKPKVEM CCCCCCCCCCCCEEE	43.58	26074081
133	Sulfoxidation	TAKPKVEMYSGSDDD CCCCCEEECCCCCCC	3.46	21406390
134	Phosphorylation	AKPKVEMYSGSDDDD CCCCEEECCCCCCCC	9.07	29255136
135	Phosphorylation	KPKVEMYSGSDDDDD CCCEEECCCCCCCCC	30.43	29255136
137	Phosphorylation	KVEMYSGSDDDDDFN CEEECCCCCCCCCHH	31.74	29255136
164	Phosphorylation	SNKKWDGSEEDEDNS CCCCCCCCCCCCCHH	35.03	29255136
171	Phosphorylation	SEEDEDNSKKIKERS CCCCCCHHHHHHHHH	47.88	25159151
178	Phosphorylation	SKKIKERSRINSSGE HHHHHHHHHCCCCCC	38.31	23927012
182	Phosphorylation	KERSRINSSGESGDE HHHHHCCCCCCCCCH	37.03	29255136
183	Phosphorylation	ERSRINSSGESGDES HHHHCCCCCCCCCHH	41.93	29255136
186	Phosphorylation	RINSSGESGDESDEF HCCCCCCCCCHHHHH	55.88	29255136
190	Phosphorylation	SGESGDESDEFLQSR CCCCCCHHHHHHHHH	47.37	29255136
196	Phosphorylation	ESDEFLQSRKGQKKN HHHHHHHHHHCCCCC	37.80	22167270
214	Phosphorylation	KPGPNIESGNEDDDA CCCCCCCCCCCCCCC	43.02	19664994
222	Phosphorylation	GNEDDDASFKIKTVA CCCCCCCHHHHHHHH	33.78	22167270
275	Acetylation	KQKESQRKFEEETVK HHHHHHHHHHHHHHH	49.87	25953088
280	Phosphorylation	QRKFEEETVKSKVTV HHHHHHHHHHCCEEE	36.19	30387612
284	2-Hydroxyisobutyrylation	EEETVKSKVTVDTGV HHHHHHCCEEEECCC	35.89	-
284	Ubiquitination	EEETVKSKVTVDTGV HHHHHHCCEEEECCC	35.89	-
286	Phosphorylation	ETVKSKVTVDTGVIP HHHHCCEEEECCCCC	19.19	23403867
289	Phosphorylation	KSKVTVDTGVIPASE HCCEEEECCCCCCCH	29.07	24732914
295	Phosphorylation	DTGVIPASEEKAETP ECCCCCCCHHHCCCC	40.72	23401153
301	Phosphorylation	ASEEKAETPTAAEDD CCHHHCCCCCCCCCC	30.69	30266825
303	Phosphorylation	EEKAETPTAAEDDNE HHHCCCCCCCCCCCC	46.01	30266825
337	Phosphorylation	KEKKKGPSKATVKAM HHHCCCCCHHHHHHH	43.52	25247763
340	Phosphorylation	KKGPSKATVKAMQEA CCCCCHHHHHHHHHH	26.69	25247763
344	Sulfoxidation	SKATVKAMQEALAKL CHHHHHHHHHHHHHH	2.83	30846556
375	Ubiquitination	RLEELEAKRKEEERL HHHHHHHHHHHHHHH	55.41	-
409	Phosphorylation	KKEGKLLTKSQREAR HHHHHHCCHHHHHHH	38.80	23312004
410	Acetylation	KEGKLLTKSQREARA HHHHHCCHHHHHHHH	44.56	25953088
411	Phosphorylation	EGKLLTKSQREARAR HHHHCCHHHHHHHHH	29.27	23312004
424	Ubiquitination	ARAEATLKLLQAQGV HHHHHHHHHHHHCCC	42.68	-
435	Phosphorylation	AQGVEVPSKDSLPKK HCCCCCCCCCCCCCC	55.03	22167270
436	Acetylation	QGVEVPSKDSLPKKR CCCCCCCCCCCCCCC	45.31	26822725
436	Malonylation	QGVEVPSKDSLPKKR CCCCCCCCCCCCCCC	45.31	32601280
438	Phosphorylation	VEVPSKDSLPKKRPI CCCCCCCCCCCCCCC	50.75	22167270
446	Phosphorylation	LPKKRPIYEDKKRKK CCCCCCCCCCHHHCC	22.28	28152594
449	2-Hydroxyisobutyrylation	KRPIYEDKKRKKIPQ CCCCCCCHHHCCCCH	42.40	-
460	Phosphorylation	KIPQQLESKEVSESM CCCHHHHCCCHHHHH	42.58	21815630
486	Phosphorylation	GVPEKEETPPPVEPE CCCCCCCCCCCCCCC	42.03	22199227
498	Phosphorylation	EPEEEEDTEDAGLDD CCCCCCCCCCCCCCH	38.76	30576142
511	Phosphorylation	DDWEAMASDEETEKV CHHHHHCCHHHCCEE	32.25	28355574
515	Phosphorylation	AMASDEETEKVEGNK HHCCHHHCCEECCCE	38.77	30576142
547	Phosphorylation	EEEEDEESEEEEEEE HHHHHHHHHHHHHHH	48.54	25137130
557	Phosphorylation	EEEEEGESEGSEGDE HHHHHCCCCCCCCCH	59.10	25137130
560	Phosphorylation	EEGESEGSEGDEEDE HHCCCCCCCCCHHCC	34.06	25137130
570	Phosphorylation	DEEDEKVSDEKDSGK CHHCCCCCCCCCCCC	51.63	25137130
575	Phosphorylation	KVSDEKDSGKTLDKK CCCCCCCCCCCCCCC	53.94	28985074
584	Phosphorylation	KTLDKKPSKEMSSDS CCCCCCCCCCCCCCC	50.56	20166139
588	Phosphorylation	KKPSKEMSSDSEYDS CCCCCCCCCCCCCCC	31.89	25159151
589	Phosphorylation	KPSKEMSSDSEYDSD CCCCCCCCCCCCCCC	43.79	25159151
591	Phosphorylation	SKEMSSDSEYDSDDD CCCCCCCCCCCCCCC	39.75	23927012
593	Phosphorylation	EMSSDSEYDSDDDRT CCCCCCCCCCCCCCH	25.38	23927012
595	Phosphorylation	SSDSEYDSDDDRTKE CCCCCCCCCCCCHHH	41.88	23927012
600	Phosphorylation	YDSDDDRTKEERAYD CCCCCCCHHHHHHHH	50.21	30108239
606	Phosphorylation	RTKEERAYDKAKRRI CHHHHHHHHHHHHHH	24.97	29083192
622	Acetylation	KRRLEHSKNVNTEKL HHHHHHCCCCCHHHH	67.81	25953088
628	2-Hydroxyisobutyrylation	SKNVNTEKLRAPIIC CCCCCHHHHCCCEEE	41.03	-
628	Acetylation	SKNVNTEKLRAPIIC CCCCCHHHHCCCEEE	41.03	25953088
635	Glutathionylation	KLRAPIICVLGHVDT HHCCCEEEEEECCCC	1.82	22555962
644	2-Hydroxyisobutyrylation	LGHVDTGKTKILDKL EECCCCCCCHHHHHH	49.06	-
646	Acetylation	HVDTGKTKILDKLRH CCCCCCCHHHHHHHC	44.77	26051181
686	Acetylation	NEQTKMIKNFDRENV HHHHHHHHCCCCCCC	48.33	27452117
708	Phosphorylation	IDTPGHESFSNLRNR ECCCCCHHHHHHHHH	28.44	27067055
745	Ubiquitination	IESINLLKSKKCPFI HHHHHCHHCCCCCEE	64.49	-
762	Phosphorylation	LNKIDRLYDWKKSPD ECCHHHHCCCCCCCC	22.20	28064214
765	Acetylation	IDRLYDWKKSPDSDV HHHHCCCCCCCCCHH	40.24	26051181
766	Malonylation	DRLYDWKKSPDSDVA HHHCCCCCCCCCHHH	64.07	26320211
766	Ubiquitination	DRLYDWKKSPDSDVA HHHCCCCCCCCCHHH	64.07	-
767	Phosphorylation	RLYDWKKSPDSDVAA HHCCCCCCCCCHHHH	30.16	21815630
770	Phosphorylation	DWKKSPDSDVAATLK CCCCCCCCHHHHHHH	37.05	22817901
775	Phosphorylation	PDSDVAATLKKQKKN CCCHHHHHHHHHHHC	29.40	-
777	2-Hydroxyisobutyrylation	SDVAATLKKQKKNTK CHHHHHHHHHHHCCH	49.13	-
777	Acetylation	SDVAATLKKQKKNTK CHHHHHHHHHHHCCH	49.13	25953088
777	Malonylation	SDVAATLKKQKKNTK CHHHHHHHHHHHCCH	49.13	26320211
784	Acetylation	KKQKKNTKDEFEERA HHHHHCCHHHHHHHH	65.73	23749302
784	Malonylation	KKQKKNTKDEFEERA HHHHHCCHHHHHHHH	65.73	26320211
861	Sulfoxidation	EELRAQVMEVKALPG HHHHHHHHHHHCCCC	3.05	30846556
871	Phosphorylation	KALPGMGTTIDVILI HCCCCCCCEEEEEEE	16.22	20068231
872	Phosphorylation	ALPGMGTTIDVILIN CCCCCCCEEEEEEEC	14.95	20068231
883	Ubiquitination	ILINGRLKEGDTIIV EEECCEECCCCEEEE	59.29	-
911	Acetylation	LLLPPPMKELRVKNQ EECCCCHHHHHCCCH	60.41	25953088
921	2-Hydroxyisobutyrylation	RVKNQYEKHKEVEAA HCCCHHHHHHHHHHH	55.85	-
921	Acetylation	RVKNQYEKHKEVEAA HCCCHHHHHHHHHHH	55.85	25953088
923	2-Hydroxyisobutyrylation	KNQYEKHKEVEAAQG CCHHHHHHHHHHHHH	74.62	-
923	Acetylation	KNQYEKHKEVEAAQG CCHHHHHHHHHHHHH	74.62	19608861
923	Ubiquitination	KNQYEKHKEVEAAQG CCHHHHHHHHHHHHH	74.62	19608861
932	Ubiquitination	VEAAQGVKILGKDLE HHHHHHCEECCHHHH	38.75	21890473
936	Malonylation	QGVKILGKDLEKTLA HHCEECCHHHHHHHC	56.55	26320211
936	Ubiquitination	QGVKILGKDLEKTLA HHCEECCHHHHHHHC	56.55	-
968	Acetylation	DELIHELKQTLNAIK HHHHHHHHHHHHCCC	37.95	23954790
968	Ubiquitination	DELIHELKQTLNAIK HHHHHHHHHHHHCCC	37.95	-
1000	Phosphorylation	ALLEFLKTSEVPYAG HHHHHHHHCCCCCCC	32.06	28152594
1001	Phosphorylation	LLEFLKTSEVPYAGI HHHHHHHCCCCCCCC	34.70	28152594
1005	Phosphorylation	LKTSEVPYAGINIGP HHHCCCCCCCCEECC	23.72	28152594
1015	2-Hydroxyisobutyrylation	INIGPVHKKDVMKAS CEECCCCHHHHHHHH	51.40	-
1015	Acetylation	INIGPVHKKDVMKAS CEECCCCHHHHHHHH	51.40	25953088
1015	Malonylation	INIGPVHKKDVMKAS CEECCCCHHHHHHHH	51.40	26320211
1048	Sulfoxidation	IERDAQEMADSLGVR ECHHHHHHHHHHCCH	3.14	30846556
1092	S-nitrosylation	KHIAVFPCKIKILPQ HCEEEEEEEEEECCH	4.90	2212679
1093	Ubiquitination	HIAVFPCKIKILPQY CEEEEEEEEEECCHH	47.47	-
1095	Acetylation	AVFPCKIKILPQYIF EEEEEEEEECCHHHH	24.56	26051181
1095	Ubiquitination	AVFPCKIKILPQYIF EEEEEEEEECCHHHH	24.56	-
1100	Phosphorylation	KIKILPQYIFNSRDP EEEECCHHHHCCCCC	12.92	-
1104	Phosphorylation	LPQYIFNSRDPIVMG CCHHHHCCCCCEEEE	27.58	-
1113	Phosphorylation	DPIVMGVTVEAGQVK CCEEEEEEEECCCCC	13.60	29396449
1123	Phosphorylation	AGQVKQGTPMCVPSK CCCCCCCCCCEECCC	12.83	29396449
1129	Phosphorylation	GTPMCVPSKNFVDIG CCCCEECCCCEEEEE	21.60	29396449
1153	Ubiquitination	KQVDVAKKGQEVCVK CEEEHHHCCCEEEEE	56.97	-
1160	Acetylation	KGQEVCVKIEPIPGE CCCEEEEEEEECCCC	35.90	25953088
1168	Phosphorylation	IEPIPGESPKMFGRH EEECCCCCCCHHCCC	35.42	19664994
1170	Acetylation	PIPGESPKMFGRHFE ECCCCCCCHHCCCCC	57.02	27452117
1170	Ubiquitination	PIPGESPKMFGRHFE ECCCCCCCHHCCCCC	57.02	-
1184	Phosphorylation	EATDILVSKISRQSI CHHHHHHHHHHHHHH	22.33	23911959
1185	Ubiquitination	ATDILVSKISRQSID HHHHHHHHHHHHHHH	36.90	-
1190	Phosphorylation	VSKISRQSIDALKDW HHHHHHHHHHHHHHH	22.71	28450419
1195	Acetylation	RQSIDALKDWFRDEM HHHHHHHHHHHHHHH	55.42	23236377
1214	Acetylation	WQLIVELKKVFEII- HHHHHHHHHHHHCC-	33.13	25953088

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 IF2P_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF2P_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 IF2P_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZBTB3_HUMAN	ZBTB3	physical	20211142
YBOX3_HUMAN	YBX3	physical	22863883
NOP53_HUMAN	GLTSCR2	physical	26344197
GNL1_HUMAN	GNL1	physical	26344197
NHP2_HUMAN	NHP2	physical	26344197
PTMA_HUMAN	PTMA	physical	26344197
TSSC4_HUMAN	TSSC4	physical	26344197
TRAP1_HUMAN	TRAP1	physical	27173435
PDIA3_HUMAN	PDIA3	physical	27173435

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 IF2P_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-784 AND LYS-923, AND MASSSPECTROMETRY.	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 SER-113; TYR-134; SER-135;SER-137; SER-164; SER-182; SER-183; SER-186; SER-190 AND SER-214, ANDMASS 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-214, AND MASSSPECTROMETRY.	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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-113; TYR-134;SER-135; SER-137; SER-214 AND SER-1168, AND MASS SPECTROMETRY.	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-107; SER-113 ANDSER-164, AND MASS SPECTROMETRY.	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-66; SER-107; SER-113;TYR-134; SER-135; SER-137; SER-164; SER-182; SER-183; SER-186;SER-190; SER-214; SER-222; THR-301; SER-547; SER-557; SER-560;SER-588; SER-589; SER-591; SER-595 AND SER-1168, AND MASSSPECTROMETRY.	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-214, AND MASSSPECTROMETRY.	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-214, AND MASSSPECTROMETRY.	19367720 [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-135 AND SER-137, ANDMASS SPECTROMETRY.	18088087 [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-190, AND MASSSPECTROMETRY.	18187866 [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-214, 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-137 AND SER-214, ANDMASS SPECTROMETRY.	17487921 [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-1168, 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-107; SER-113; SER-135;SER-137; SER-164; SER-182; SER-183; SER-186; SER-190 AND SER-214, ANDMASS 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-135 AND SER-137, ANDMASS SPECTROMETRY.	16097034 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-182; SER-183;SER-186 AND SER-190, AND MASS SPECTROMETRY.	16083285 [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-107; SER-113; SER-135;SER-164; SER-182; SER-186; SER-190 AND SER-1168, AND MASSSPECTROMETRY.	15302935 [Abstract]