dbPTM

IF4G2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF4G2_HUMAN
UniProt AC	P78344
Protein Name	Eukaryotic translation initiation factor 4 gamma 2
Gene Name	EIF4G2 {ECO:0000312\|HGNC:HGNC:3297}
Organism	Homo sapiens (Human).
Sequence Length	907
Subcellular Localization
Protein Description	Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases..
Protein Sequence	MESAIAEGGASRFSASSGGGGSRGAPQHYPKTAGNSEFLGKTPGQNAQKWIPARSTRRDDNSAANNSANEKERHDAIFRKVRGILNKLTPEKFDKLCLELLNVGVESKLILKGVILLIVDKALEEPKYSSLYAQLCLRLAEDAPNFDGPAAEGQPGQKQSTTFRRLLISKLQDEFENRTRNVDVYDKRENPLLPEEEEQRAIAKIKMLGNIKFIGELGKLDLIHESILHKCIKTLLEKKKRVQLKDMGEDLECLCQIMRTVGPRLDHERAKSLMDQYFARMCSLMLSKELPARIRFLLQDTVELREHHWVPRKAFLDNGPKTINQIRQDAVKDLGVFIPAPMAQGMRSDFFLEGPFMPPRMKMDRDPLGGLADMFGQMPGSGIGTGPGVIQDRFSPTMGRHRSNQLFNGHGGHIMPPTQSQFGEMGGKFMKSQGLSQLYHNQSQGLLSQLQGQSKDMPPRFSKKGQLNADEISLRPAQSFLMNKNQVPKLQPQITMIPPSAQPPRTQTPPLGQTPQLGLKTNPPLIQEKPAKTSKKPPPSKEELLKLTETVVTEYLNSGNANEAVNGVREMRAPKHFLPEMLSKVIILSLDRSDEDKEKASSLISLLKQEGIATSDNFMQAFLNVLDQCPKLEVDIPLVKSYLAQFAARAIISELVSISELAQPLESGTHFPLFLLCLQQLAKLQDREWLTELFQQSKVNMQKMLPEIDQNKDRMLEILEGKGLSFLFPLLKLEKELLKQIKLDPSPQTIYKWIKDNISPKLHVDKGFVNILMTSFLQYISSEVNPPSDETDSSSAPSKEQLEQEKQLLLSFKPVMQKFLHDHVDLQVSALYALQVHCYNSNFPKGMLLRFFVHFYDMEIIEEEAFLAWKEDITQEFPGKGKALFQVNQWLTWLETAEEEESEEEAD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MESAIAEG -------CCCHHHCC	9.18	19413330
1	Sulfoxidation	-------MESAIAEG -------CCCHHHCC	9.18	28465586
3	Phosphorylation	-----MESAIAEGGA -----CCCHHHCCCC	24.55	23186163
11	Phosphorylation	AIAEGGASRFSASSG HHHCCCCCCCCCCCC	36.81	20068231
14	Phosphorylation	EGGASRFSASSGGGG CCCCCCCCCCCCCCC	26.57	29396449
16	Phosphorylation	GASRFSASSGGGGSR CCCCCCCCCCCCCCC	28.46	29255136
17	Phosphorylation	ASRFSASSGGGGSRG CCCCCCCCCCCCCCC	40.97	29255136
22	Phosphorylation	ASSGGGGSRGAPQHY CCCCCCCCCCCCCCC	30.71	29255136
23	Methylation	SSGGGGSRGAPQHYP CCCCCCCCCCCCCCC	48.87	-
29	Phosphorylation	SRGAPQHYPKTAGNS CCCCCCCCCCCCCCC	10.94	28102081
31	Methylation	GAPQHYPKTAGNSEF CCCCCCCCCCCCCCC	43.79	-
31	Ubiquitination	GAPQHYPKTAGNSEF CCCCCCCCCCCCCCC	43.79	-
32	Phosphorylation	APQHYPKTAGNSEFL CCCCCCCCCCCCCCC	34.98	20068231
36	Phosphorylation	YPKTAGNSEFLGKTP CCCCCCCCCCCCCCC	28.89	28857561
41	Acetylation	GNSEFLGKTPGQNAQ CCCCCCCCCCCCCCC	54.41	25953088
41	Methylation	GNSEFLGKTPGQNAQ CCCCCCCCCCCCCCC	54.41	-
41	Ubiquitination	GNSEFLGKTPGQNAQ CCCCCCCCCCCCCCC	54.41	-
42	Phosphorylation	NSEFLGKTPGQNAQK CCCCCCCCCCCCCCC	30.74	29214152
49	Acetylation	TPGQNAQKWIPARST CCCCCCCCCCCCCCC	44.68	25953088
49	Ubiquitination	TPGQNAQKWIPARST CCCCCCCCCCCCCCC	44.68	-
67	Phosphorylation	DNSAANNSANEKERH CCCCCCCCCCHHHHH	32.07	29214152
71	Ubiquitination	ANNSANEKERHDAIF CCCCCCHHHHHHHHH	60.91	21906983
87	Acetylation	KVRGILNKLTPEKFD HHHHHHHHCCHHHHH	50.74	27452117
87	Ubiquitination	KVRGILNKLTPEKFD HHHHHHHHCCHHHHH	50.74	-
89	Phosphorylation	RGILNKLTPEKFDKL HHHHHHCCHHHHHHH	30.89	27067055
92	Acetylation	LNKLTPEKFDKLCLE HHHCCHHHHHHHHHH	61.13	25953088
92	Ubiquitination	LNKLTPEKFDKLCLE HHHCCHHHHHHHHHH	61.13	-
95	Ubiquitination	LTPEKFDKLCLELLN CCHHHHHHHHHHHHC	44.20	-
128	Phosphorylation	KALEEPKYSSLYAQL HHHCCCCCHHHHHHH	17.76	29496907
158	Ubiquitination	AEGQPGQKQSTTFRR CCCCCCCCCCHHHHH	52.73	21906983
158 (in isoform 2)	Ubiquitination	-	52.73	-
170	2-Hydroxyisobutyrylation	FRRLLISKLQDEFEN HHHHHHHHHHHHHHH	43.08	-
170	Acetylation	FRRLLISKLQDEFEN HHHHHHHHHHHHHHH	43.08	25953088
170	Ubiquitination	FRRLLISKLQDEFEN HHHHHHHHHHHHHHH	43.08	21906983
170 (in isoform 2)	Ubiquitination	-	43.08	-
185	Phosphorylation	RTRNVDVYDKRENPL CCCCCCCCCCCCCCC	15.98	28152594
187	2-Hydroxyisobutyrylation	RNVDVYDKRENPLLP CCCCCCCCCCCCCCC	43.88	-
187	Acetylation	RNVDVYDKRENPLLP CCCCCCCCCCCCCCC	43.88	25953088
187	Malonylation	RNVDVYDKRENPLLP CCCCCCCCCCCCCCC	43.88	26320211
187	Ubiquitination	RNVDVYDKRENPLLP CCCCCCCCCCCCCCC	43.88	-
187 (in isoform 2)	Ubiquitination	-	43.88	-
204	Ubiquitination	EEQRAIAKIKMLGNI HHHHHHHHHHHHCCE	36.42	-
206	Ubiquitination	QRAIAKIKMLGNIKF HHHHHHHHHHCCEEE	27.63	-
212	Ubiquitination	IKMLGNIKFIGELGK HHHHCCEEECCCCCC	34.62	-
219	Acetylation	KFIGELGKLDLIHES EECCCCCCHHHHCHH	51.99	26051181
219	Ubiquitination	KFIGELGKLDLIHES EECCCCCCHHHHCHH	51.99	-
226	Phosphorylation	KLDLIHESILHKCIK CHHHHCHHHHHHHHH	19.11	20873877
230	Acetylation	IHESILHKCIKTLLE HCHHHHHHHHHHHHH	33.92	23749302
230	Malonylation	IHESILHKCIKTLLE HCHHHHHHHHHHHHH	33.92	26320211
230	Ubiquitination	IHESILHKCIKTLLE HCHHHHHHHHHHHHH	33.92	-
233	Acetylation	SILHKCIKTLLEKKK HHHHHHHHHHHHHHC	42.46	23749302
233	Ubiquitination	SILHKCIKTLLEKKK HHHHHHHHHHHHHHC	42.46	-
245	Ubiquitination	KKKRVQLKDMGEDLE HHCCCCCHHCHHHHH	28.69	-
247	Sulfoxidation	KRVQLKDMGEDLECL CCCCCHHCHHHHHHH	6.39	21406390
271	2-Hydroxyisobutyrylation	RLDHERAKSLMDQYF CCCHHHHHHHHHHHH	50.79	-
271	Acetylation	RLDHERAKSLMDQYF CCCHHHHHHHHHHHH	50.79	27452117
271	Ubiquitination	RLDHERAKSLMDQYF CCCHHHHHHHHHHHH	50.79	-
272	Phosphorylation	LDHERAKSLMDQYFA CCHHHHHHHHHHHHH	28.13	24043423
274	Sulfoxidation	HERAKSLMDQYFARM HHHHHHHHHHHHHHH	3.78	28183972
277	Phosphorylation	AKSLMDQYFARMCSL HHHHHHHHHHHHHHH	8.57	24043423
283	Phosphorylation	QYFARMCSLMLSKEL HHHHHHHHHHHCCCC	13.89	28857561
287	Phosphorylation	RMCSLMLSKELPARI HHHHHHHCCCCHHHH	15.32	24043423
288	Ubiquitination	MCSLMLSKELPARIR HHHHHHCCCCHHHHH	60.35	-
313	Ubiquitination	EHHWVPRKAFLDNGP HHCCCCCHHHHHCCC	37.10	-
321	Ubiquitination	AFLDNGPKTINQIRQ HHHHCCCCHHHHHHH	64.53	-
332	Ubiquitination	QIRQDAVKDLGVFIP HHHHHHHHHHCCEEE	49.29	-
360	Methylation	EGPFMPPRMKMDRDP CCCCCCCCCCCCCCC	31.33	24129315
362	Ubiquitination	PFMPPRMKMDRDPLG CCCCCCCCCCCCCCC	38.64	-
381	Phosphorylation	MFGQMPGSGIGTGPG HHCCCCCCCCCCCCC	22.74	26846344
385	Phosphorylation	MPGSGIGTGPGVIQD CCCCCCCCCCCCCCC	37.98	26846344
393	Methylation	GPGVIQDRFSPTMGR CCCCCCCCCCCCCCC	19.98	-
395	Phosphorylation	GVIQDRFSPTMGRHR CCCCCCCCCCCCCCC	21.98	29255136
397	Phosphorylation	IQDRFSPTMGRHRSN CCCCCCCCCCCCCCC	30.93	30266825
400	Methylation	RFSPTMGRHRSNQLF CCCCCCCCCCCCCCC	15.95	-
402	Methylation	SPTMGRHRSNQLFNG CCCCCCCCCCCCCCC	35.62	-
428	Acetylation	QFGEMGGKFMKSQGL HHHHHCHHHHHHHCH	36.23	25953088
428	Ubiquitination	QFGEMGGKFMKSQGL HHHHHCHHHHHHHCH	36.23	21890473
431	Methylation	EMGGKFMKSQGLSQL HHCHHHHHHHCHHHH	42.64	24129315
431	Ubiquitination	EMGGKFMKSQGLSQL HHCHHHHHHHCHHHH	42.64	21890473
432	Phosphorylation	MGGKFMKSQGLSQLY HCHHHHHHHCHHHHH	20.07	21945579
435 (in isoform 2)	Phosphorylation	-	1.98	28348404
436	Phosphorylation	FMKSQGLSQLYHNQS HHHHHCHHHHHCHHH	25.60	21945579
439	Phosphorylation	SQGLSQLYHNQSQGL HHCHHHHHCHHHHHH	7.35	21945579
441 (in isoform 2)	Phosphorylation	-	29.64	28348404
443	Phosphorylation	SQLYHNQSQGLLSQL HHHHCHHHHHHHHHH	31.37	21945579
448	Phosphorylation	NQSQGLLSQLQGQSK HHHHHHHHHHHCCCC	33.61	21945579
454	Phosphorylation	LSQLQGQSKDMPPRF HHHHHCCCCCCCCCC	37.13	21945579
460	Methylation	QSKDMPPRFSKKGQL CCCCCCCCCCCCCCC	42.47	-
463	Methylation	DMPPRFSKKGQLNAD CCCCCCCCCCCCCHH	59.20	-
464	Methylation	MPPRFSKKGQLNADE CCCCCCCCCCCCHHH	51.17	-
464	Ubiquitination	MPPRFSKKGQLNADE CCCCCCCCCCCCHHH	51.17	-
473	Phosphorylation	QLNADEISLRPAQSF CCCHHHHCCCHHHHH	19.11	29514088
475	Methylation	NADEISLRPAQSFLM CHHHHCCCHHHHHHH	20.09	-
479	Phosphorylation	ISLRPAQSFLMNKNQ HCCCHHHHHHHCCCC	23.58	25159151
482	Sulfoxidation	RPAQSFLMNKNQVPK CHHHHHHHCCCCCCC	6.72	21406390
484	Ubiquitination	AQSFLMNKNQVPKLQ HHHHHHCCCCCCCCC	34.49	-
495	Phosphorylation	PKLQPQITMIPPSAQ CCCCCCCEECCCCCC	12.10	24732914
496	Sulfoxidation	KLQPQITMIPPSAQP CCCCCCEECCCCCCC	4.65	21406390
500	Phosphorylation	QITMIPPSAQPPRTQ CCEECCCCCCCCCCC	33.89	26846344
501	Ubiquitination	ITMIPPSAQPPRTQT CEECCCCCCCCCCCC	31.50	21890473
501	Ubiquitination	ITMIPPSAQPPRTQT CEECCCCCCCCCCCC	31.50	21890473
504	Ubiquitination	IPPSAQPPRTQTPPL CCCCCCCCCCCCCCC	39.61	21890473
504	Ubiquitination	IPPSAQPPRTQTPPL CCCCCCCCCCCCCCC	39.61	21890473
505	Methylation	PPSAQPPRTQTPPLG CCCCCCCCCCCCCCC	46.26	24129315
506	O-linked_Glycosylation	PSAQPPRTQTPPLGQ CCCCCCCCCCCCCCC	42.44	30059200
506	Phosphorylation	PSAQPPRTQTPPLGQ CCCCCCCCCCCCCCC	42.44	19664994
508	Phosphorylation	AQPPRTQTPPLGQTP CCCCCCCCCCCCCCC	26.68	19664994
514	Phosphorylation	QTPPLGQTPQLGLKT CCCCCCCCCCCCCCC	15.94	30266825
520	Ubiquitination	QTPQLGLKTNPPLIQ CCCCCCCCCCCCCCC	44.45	-
529	Acetylation	NPPLIQEKPAKTSKK CCCCCCCCCCCCCCC	33.62	23749302
529	Ubiquitination	NPPLIQEKPAKTSKK CCCCCCCCCCCCCCC	33.62	-
537	Ubiquitination	PAKTSKKPPPSKEEL CCCCCCCCCCCHHHH	50.17	21890473
541	Acetylation	SKKPPPSKEELLKLT CCCCCCCHHHHHHHH	62.07	23236377
541	Malonylation	SKKPPPSKEELLKLT CCCCCCCHHHHHHHH	62.07	30639696
541	Ubiquitination	SKKPPPSKEELLKLT CCCCCCCHHHHHHHH	62.07	-
546	Ubiquitination	PSKEELLKLTETVVT CCHHHHHHHHHHHHH	67.02	-
575	Acetylation	VREMRAPKHFLPEML HHHHCCCCCHHHHHH	46.10	25953088
575	Sumoylation	VREMRAPKHFLPEML HHHHCCCCCHHHHHH	46.10	28112733
575	Ubiquitination	VREMRAPKHFLPEML HHHHCCCCCHHHHHH	46.10	21890473
584	Ubiquitination	FLPEMLSKVIILSLD HHHHHHHHHHHHHCC	33.23	-
592	Methylation	VIILSLDRSDEDKEK HHHHHCCCCHHHHHH	51.83	-
599	Ubiquitination	RSDEDKEKASSLISL CCHHHHHHHHHHHHH	60.35	-
601	Phosphorylation	DEDKEKASSLISLLK HHHHHHHHHHHHHHH	36.42	23186163
602	Phosphorylation	EDKEKASSLISLLKQ HHHHHHHHHHHHHHH	34.28	20873877
605	Phosphorylation	EKASSLISLLKQEGI HHHHHHHHHHHHCCC	32.70	20873877
640	Ubiquitination	EVDIPLVKSYLAQFA CCCHHHHHHHHHHHH	40.86	-
641	Phosphorylation	VDIPLVKSYLAQFAA CCHHHHHHHHHHHHH	20.21	28152594
642	Phosphorylation	DIPLVKSYLAQFAAR CHHHHHHHHHHHHHH	10.59	28152594
648	Ubiquitination	SYLAQFAARAIISEL HHHHHHHHHHHHHHH	11.61	21890473
648	Ubiquitination	SYLAQFAARAIISEL HHHHHHHHHHHHHHH	11.61	21890473
687	Methylation	QLAKLQDREWLTELF HHHHCCCHHHHHHHH	24.83	-
691	Phosphorylation	LQDREWLTELFQQSK CCCHHHHHHHHHHHC	31.54	29888752
697	Phosphorylation	LTELFQQSKVNMQKM HHHHHHHHCCHHHHH	27.99	29888752
698	Ubiquitination	TELFQQSKVNMQKML HHHHHHHCCHHHHHC	33.03	-
701	Ubiquitination	FQQSKVNMQKMLPEI HHHHCCHHHHHCCHH	4.54	21890473
703	Ubiquitination	QSKVNMQKMLPEIDQ HHCCHHHHHCCHHHC	31.47	-
704	Sulfoxidation	SKVNMQKMLPEIDQN HCCHHHHHCCHHHCC	4.20	21406390
712	2-Hydroxyisobutyrylation	LPEIDQNKDRMLEIL CCHHHCCHHHHHHHH	40.87	-
712	Acetylation	LPEIDQNKDRMLEIL CCHHHCCHHHHHHHH	40.87	26051181
712	Ubiquitination	LPEIDQNKDRMLEIL CCHHHCCHHHHHHHH	40.87	-
732	Ubiquitination	SFLFPLLKLEKELLK HHHHHHHHHHHHHHH	63.38	-
735	2-Hydroxyisobutyrylation	FPLLKLEKELLKQIK HHHHHHHHHHHHHCC	65.19	-
735	Ubiquitination	FPLLKLEKELLKQIK HHHHHHHHHHHHHCC	65.19	-
739	Ubiquitination	KLEKELLKQIKLDPS HHHHHHHHHCCCCCC	63.70	2189047
742	Ubiquitination	KELLKQIKLDPSPQT HHHHHHCCCCCCHHH	44.32	-
751	Nitration	DPSPQTIYKWIKDNI CCCHHHHHHHHHHCC	12.03	-
751	Phosphorylation	DPSPQTIYKWIKDNI CCCHHHHHHHHHHCC	12.03	23917254
755	Acetylation	QTIYKWIKDNISPKL HHHHHHHHHCCCCCC	43.54	27452117
755	Ubiquitination	QTIYKWIKDNISPKL HHHHHHHHHCCCCCC	43.54	-
759	Phosphorylation	KWIKDNISPKLHVDK HHHHHCCCCCCCCCH	23.41	24719451
761	2-Hydroxyisobutyrylation	IKDNISPKLHVDKGF HHHCCCCCCCCCHHH	44.42	-
761	Acetylation	IKDNISPKLHVDKGF HHHCCCCCCCCCHHH	44.42	25953088
761	Ubiquitination	IKDNISPKLHVDKGF HHHCCCCCCCCCHHH	44.42	-
806	Ubiquitination	KEQLEQEKQLLLSFK HHHHHHHHHHHHHCH	46.04	-
811	Phosphorylation	QEKQLLLSFKPVMQK HHHHHHHHCHHHHHH	31.06	21406692
812	Ubiquitination	EKQLLLSFKPVMQKF HHHHHHHCHHHHHHH	11.92	21890473
812	Ubiquitination	EKQLLLSFKPVMQKF HHHHHHHCHHHHHHH	11.92	21890473
813	Acetylation	KQLLLSFKPVMQKFL HHHHHHCHHHHHHHH	33.07	26051181
813	Ubiquitination	KQLLLSFKPVMQKFL HHHHHHCHHHHHHHH	33.07	-
880	Ubiquitination	ITQEFPGKGKALFQV CHHHCCCCCCHHEEH	58.43	-
892	Phosphorylation	FQVNQWLTWLETAEE EEHHHHHHHHHHHHH	25.66	20068231
896	Phosphorylation	QWLTWLETAEEEESE HHHHHHHHHHHHHHH	36.88	20068231
902	Phosphorylation	ETAEEEESEEEAD-- HHHHHHHHHHHCC--	54.29	25159151

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
508	T	Phosphorylation	Kinase	CDK1	P06493	PSP
902	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF4G2_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 IF4G2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EIF3A_HUMAN	EIF3A	physical	10611228
IF4A1_HUMAN	EIF4A1	physical	10611228
IF4G3_HUMAN	EIF4G3	physical	22939629
IF4H_HUMAN	EIF4H	physical	22939629
RAB7A_HUMAN	RAB7A	physical	22939629
SLIRP_HUMAN	SLIRP	physical	22939629
PDIP3_HUMAN	POLDIP3	physical	22939629
RFA2_HUMAN	RPA2	physical	21988832

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 IF4G2_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-508, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 1-12, AND ACETYLATION AT MET-1.	12665801 [Abstract]
Phosphorylation
Reference	PubMed
"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-395 AND THR-508, ANDMASS SPECTROMETRY.	17924679 [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-508, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-508, 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 THR-508 AND THR-514, ANDMASS SPECTROMETRY.	18669648 [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 THR-508, AND MASSSPECTROMETRY.	18088087 [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 THR-508, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Suppression of cap-dependent translation in mitosis."; Pyronnet S., Dostie J., Sonenberg N.; Genes Dev. 15:2083-2093(2001). Cited for: FUNCTION, AND PHOSPHORYLATION.	11511540 [Abstract]