dbPTM

EF2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF2_MOUSE
UniProt AC	P58252
Protein Name	Elongation factor 2
Gene Name	Eef2
Organism	Mus musculus (Mouse).
Sequence Length	858
Subcellular Localization	Cytoplasm . Nucleus . Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product.
Protein Description	Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome..
Protein Sequence	MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLSAAERAKKVEDMMKKLWGDRYFDPANGKFSKSANSPDGKKLPRTFCQLILDPIFKVFDAIMNFRKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKARARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Phosphorylation	KANIRNMSVIAHVDH CCCCCCEEEEEEECC	17.58	27841257
33	Phosphorylation	AHVDHGKSTLTDSLV EEECCCCCCCCHHHH	32.99	22324799
34	Phosphorylation	HVDHGKSTLTDSLVC EECCCCCCCCHHHHH	36.84	22324799
36	Phosphorylation	DHGKSTLTDSLVCKA CCCCCCCCHHHHHHH	24.51	22324799
38	Phosphorylation	GKSTLTDSLVCKAGI CCCCCCHHHHHHHHH	19.91	22324799
41	S-nitrosocysteine	TLTDSLVCKAGIIAS CCCHHHHHHHHHHHH	2.79	-
41	Glutathionylation	TLTDSLVCKAGIIAS CCCHHHHHHHHHHHH	2.79	24333276
41	S-nitrosylation	TLTDSLVCKAGIIAS CCCHHHHHHHHHHHH	2.79	24895380
41	S-palmitoylation	TLTDSLVCKAGIIAS CCCHHHHHHHHHHHH	2.79	28526873
42	Acetylation	LTDSLVCKAGIIASA CCHHHHHHHHHHHHC	42.01	23806337
42	Succinylation	LTDSLVCKAGIIASA CCHHHHHHHHHHHHC	42.01	23806337
42	Ubiquitination	LTDSLVCKAGIIASA CCHHHHHHHHHHHHC	42.01	-
48	Phosphorylation	CKAGIIASARAGETR HHHHHHHHCCCCCCC	14.10	22817900
54	Phosphorylation	ASARAGETRFTDTRK HHCCCCCCCCCCCCH	30.11	25521595
57	Phosphorylation	RAGETRFTDTRKDEQ CCCCCCCCCCCHHHH	32.92	27087446
59	Phosphorylation	GETRFTDTRKDEQER CCCCCCCCCHHHHHH	36.24	25521595
67	Glutathionylation	RKDEQERCITIKSTA CHHHHHHEEEEEHHH	2.95	24333276
69	Phosphorylation	DEQERCITIKSTAIS HHHHHEEEEEHHHHH	26.44	23375375
93	Ubiquitination	LNFIKQSKDGSGFLI CCHHHHCCCCCCEEE	64.71	-
152	Acetylation	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	23806337
152	Succinylation	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	-
152	Succinylation	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	23806337
152	Ubiquitination	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	27667366
159	Ubiquitination	KPVLMMNKMDRALLE HHHHCCCHHHHHHHH	25.04	22790023
235	Acetylation	FAEMYVAKFAAKGEG HHHHHHHHHHHCCCC	26.03	22826441
235	Ubiquitination	FAEMYVAKFAAKGEG HHHHHHHHHHHCCCC	26.03	22790023
239	Acetylation	YVAKFAAKGEGQLSA HHHHHHHCCCCCCCH	54.81	23806337
239	Malonylation	YVAKFAAKGEGQLSA HHHHHHHCCCCCCCH	54.81	26320211
239	Ubiquitination	YVAKFAAKGEGQLSA HHHHHHHCCCCCCCH	54.81	27667366
252	Acetylation	SAAERAKKVEDMMKK CHHHHHHHHHHHHHH	50.28	22826441
252	Ubiquitination	SAAERAKKVEDMMKK CHHHHHHHHHHHHHH	50.28	27667366
258	Acetylation	KKVEDMMKKLWGDRY HHHHHHHHHHHCCCC	37.77	7495505
258	Malonylation	KKVEDMMKKLWGDRY HHHHHHHHHHHCCCC	37.77	26320211
259	Acetylation	KVEDMMKKLWGDRYF HHHHHHHHHHCCCCC	31.41	22826441
259	Ubiquitination	KVEDMMKKLWGDRYF HHHHHHHHHHCCCCC	31.41	22790023
265	Phosphorylation	KKLWGDRYFDPANGK HHHHCCCCCCCCCCC	19.64	-
272	Acetylation	YFDPANGKFSKSANS CCCCCCCCCCCCCCC	46.39	23806337
272	Malonylation	YFDPANGKFSKSANS CCCCCCCCCCCCCCC	46.39	26320211
272	Succinylation	YFDPANGKFSKSANS CCCCCCCCCCCCCCC	46.39	-
272	Succinylation	YFDPANGKFSKSANS CCCCCCCCCCCCCCC	46.39	23806337
272	Ubiquitination	YFDPANGKFSKSANS CCCCCCCCCCCCCCC	46.39	27667366
275	Acetylation	PANGKFSKSANSPDG CCCCCCCCCCCCCCC	57.64	23806337
275	Malonylation	PANGKFSKSANSPDG CCCCCCCCCCCCCCC	57.64	26320211
275	Succinylation	PANGKFSKSANSPDG CCCCCCCCCCCCCCC	57.64	-
275	Ubiquitination	PANGKFSKSANSPDG CCCCCCCCCCCCCCC	57.64	27667366
279	Phosphorylation	KFSKSANSPDGKKLP CCCCCCCCCCCCCCC	24.88	29895711
283	Acetylation	SANSPDGKKLPRTFC CCCCCCCCCCCHHHH	59.52	30985869
283	Ubiquitination	SANSPDGKKLPRTFC CCCCCCCCCCCHHHH	59.52	22790023
288	Phosphorylation	DGKKLPRTFCQLILD CCCCCCHHHHHHHHH	27.16	23984901
290	S-nitrosocysteine	KKLPRTFCQLILDPI CCCCHHHHHHHHHHH	2.96	-
290	Glutathionylation	KKLPRTFCQLILDPI CCCCHHHHHHHHHHH	2.96	24333276
290	S-nitrosylation	KKLPRTFCQLILDPI CCCCHHHHHHHHHHH	2.96	22588120
290	S-palmitoylation	KKLPRTFCQLILDPI CCCCHHHHHHHHHHH	2.96	28526873
305	Sulfoxidation	FKVFDAIMNFRKEET HHHHHHHHCCCHHHH	4.09	21406390
314	Acetylation	FRKEETAKLIEKLDI CCHHHHHHHHHHCCC	58.37	23236377
314	Malonylation	FRKEETAKLIEKLDI CCHHHHHHHHHHCCC	58.37	26320211
314	Ubiquitination	FRKEETAKLIEKLDI CCHHHHHHHHHHCCC	58.37	27667366
318	Acetylation	ETAKLIEKLDIKLDS HHHHHHHHCCCCCCC	44.45	23806337
318	Malonylation	ETAKLIEKLDIKLDS HHHHHHHHCCCCCCC	44.45	26320211
318	Succinylation	ETAKLIEKLDIKLDS HHHHHHHHCCCCCCC	44.45	-
318	Ubiquitination	ETAKLIEKLDIKLDS HHHHHHHHCCCCCCC	44.45	27667366
322	Succinylation	LIEKLDIKLDSEDKD HHHHCCCCCCCCCCC	46.00	23954790
322	Ubiquitination	LIEKLDIKLDSEDKD HHHHCCCCCCCCCCC	46.00	27667366
325	Phosphorylation	KLDIKLDSEDKDKEG HCCCCCCCCCCCCCC	59.12	26824392
333	Ubiquitination	EDKDKEGKPLLKAVM CCCCCCCHHHHHHHH	33.32	27667366
337	Acetylation	KEGKPLLKAVMRRWL CCCHHHHHHHHHHHC	46.77	23236377
337	Ubiquitination	KEGKPLLKAVMRRWL CCCHHHHHHHHHHHC	46.77	-
360	Phosphorylation	MITIHLPSPVTAQKY HHEEECCCCCCCCCE	38.06	26745281
363	Phosphorylation	IHLPSPVTAQKYRCE EECCCCCCCCCEEEE	27.10	26745281
366	Acetylation	PSPVTAQKYRCELLY CCCCCCCCEEEEEEE	32.00	23954790
369	S-nitrosocysteine	VTAQKYRCELLYEGP CCCCCEEEEEEECCC	3.81	-
369	Glutathionylation	VTAQKYRCELLYEGP CCCCCEEEEEEECCC	3.81	24333276
369	S-nitrosylation	VTAQKYRCELLYEGP CCCCCEEEEEEECCC	3.81	20925432
373	Phosphorylation	KYRCELLYEGPPDDE CEEEEEEECCCCCCH	31.31	-
388	Glutathionylation	AAMGIKSCDPKGPLM HHHCCCCCCCCCCEE	9.85	24333276
391	Acetylation	GIKSCDPKGPLMMYI CCCCCCCCCCEEEEE	60.97	22826441
399	Phosphorylation	GPLMMYISKMVPTSD CCEEEEEEEEECCCC	9.37	22817900
400	Acetylation	PLMMYISKMVPTSDK CEEEEEEEEECCCCC	34.07	22826441
400	Ubiquitination	PLMMYISKMVPTSDK CEEEEEEEEECCCCC	34.07	22790023
407	Ubiquitination	KMVPTSDKGRFYAFG EEECCCCCCCEEEEC	52.32	27667366
411	Phosphorylation	TSDKGRFYAFGRVFS CCCCCCEEEECCEEC	10.32	25367039
418	Phosphorylation	YAFGRVFSGVVSTGL EEECCEECCCCCCCC	28.02	29514104
426	Acetylation	GVVSTGLKVRIMGPN CCCCCCCEEEEECCC	30.71	23236377
426	Malonylation	GVVSTGLKVRIMGPN CCCCCCCEEEEECCC	30.71	26320211
426	Ubiquitination	GVVSTGLKVRIMGPN CCCCCCCEEEEECCC	30.71	27667366
434	Phosphorylation	VRIMGPNYTPGKKED EEEECCCCCCCCHHH	19.90	21149613
435	Phosphorylation	RIMGPNYTPGKKEDL EEECCCCCCCCHHHC	32.00	26824392
438	Malonylation	GPNYTPGKKEDLYLK CCCCCCCCHHHCCCH	54.94	26320211
438	Ubiquitination	GPNYTPGKKEDLYLK CCCCCCCCHHHCCCH	54.94	27667366
439	Acetylation	PNYTPGKKEDLYLKP CCCCCCCHHHCCCHH	63.48	23806337
439	Malonylation	PNYTPGKKEDLYLKP CCCCCCCHHHCCCHH	63.48	26320211
439	Ubiquitination	PNYTPGKKEDLYLKP CCCCCCCHHHCCCHH	63.48	27667366
443	Phosphorylation	PGKKEDLYLKPIQRT CCCHHHCCCHHHHHH	25.63	25263469
445	Acetylation	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	23806337
445	Malonylation	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	26320211
445	Succinylation	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	23954790
445	Ubiquitination	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	27667366
466	S-nitrosocysteine	EPIEDVPCGNIVGLV CCCCCCCCCCEEEEE	7.00	-
466	Glutathionylation	EPIEDVPCGNIVGLV CCCCCCCCCCEEEEE	7.00	24333276
466	S-nitrosylation	EPIEDVPCGNIVGLV CCCCCCCCCCEEEEE	7.00	21278135
466	S-palmitoylation	EPIEDVPCGNIVGLV CCCCCCCCCCEEEEE	7.00	28526873
498	Acetylation	AHNMRVMKFSVSPVV CCCCEEEEEEECCEE	31.46	23806337
498	Ubiquitination	AHNMRVMKFSVSPVV CCCCEEEEEEECCEE	31.46	22790023
500	Phosphorylation	NMRVMKFSVSPVVRV CCEEEEEEECCEEEE	19.03	29472430
502	Phosphorylation	RVMKFSVSPVVRVAV EEEEEEECCEEEEEE	15.69	26824392
512	Acetylation	VRVAVEAKNPADLPK EEEEEEECCHHHHHH	50.38	23806337
512	Malonylation	VRVAVEAKNPADLPK EEEEEEECCHHHHHH	50.38	26320211
512	Succinylation	VRVAVEAKNPADLPK EEEEEEECCHHHHHH	50.38	-
512	Ubiquitination	VRVAVEAKNPADLPK EEEEEEECCHHHHHH	50.38	27667366
525	"N6,N6,N6-trimethyllysine"	PKLVEGLKRLAKSDP HHHHHHHHHHHHCCC	57.11	-
525	Methylation	PKLVEGLKRLAKSDP HHHHHHHHHHHHCCC	57.11	-
567	S-nitrosocysteine	DLEEDHACIPIKKSD HHHHCCCEEEECCCC	3.22	-
567	Glutathionylation	DLEEDHACIPIKKSD HHHHCCCEEEECCCC	3.22	24333276
567	S-nitrosylation	DLEEDHACIPIKKSD HHHHCCCEEEECCCC	3.22	20925432
567	S-palmitoylation	DLEEDHACIPIKKSD HHHHCCCEEEECCCC	3.22	28526873
571	Acetylation	DHACIPIKKSDPVVS CCCEEEECCCCCCEE	40.65	22826441
571	Malonylation	DHACIPIKKSDPVVS CCCEEEECCCCCCEE	40.65	26320211
571	Ubiquitination	DHACIPIKKSDPVVS CCCEEEECCCCCCEE	40.65	-
572	Acetylation	HACIPIKKSDPVVSY CCEEEECCCCCCEEE	61.89	23806337
572	Succinylation	HACIPIKKSDPVVSY CCEEEECCCCCCEEE	61.89	-
572	Succinylation	HACIPIKKSDPVVSY CCEEEECCCCCCEEE	61.89	23806337
572	Ubiquitination	HACIPIKKSDPVVSY CCEEEECCCCCCEEE	61.89	-
573	Phosphorylation	ACIPIKKSDPVVSYR CEEEECCCCCCEEEE	41.99	24899341
578	Phosphorylation	KKSDPVVSYRETVSE CCCCCCEEEEEECCC	20.78	19060867
579	Phosphorylation	KSDPVVSYRETVSEE CCCCCEEEEEECCCC	10.81	28066266
582	Phosphorylation	PVVSYRETVSEESNV CCEEEEEECCCCCCE	21.97	30635358
584	Phosphorylation	VSYRETVSEESNVLC EEEEEECCCCCCEEE	42.96	30635358
587	Phosphorylation	RETVSEESNVLCLSK EEECCCCCCEEEEEC	28.34	30635358
591	S-nitrosocysteine	SEESNVLCLSKSPNK CCCCCEEEEECCCCC	3.34	-
591	Glutathionylation	SEESNVLCLSKSPNK CCCCCEEEEECCCCC	3.34	24333276
591	S-nitrosylation	SEESNVLCLSKSPNK CCCCCEEEEECCCCC	3.34	24895380
591	S-palmitoylation	SEESNVLCLSKSPNK CCCCCEEEEECCCCC	3.34	28526873
593	Phosphorylation	ESNVLCLSKSPNKHN CCCEEEEECCCCCCC	30.05	25263469
594	Acetylation	SNVLCLSKSPNKHNR CCEEEEECCCCCCCC	57.91	23806337
594	Succinylation	SNVLCLSKSPNKHNR CCEEEEECCCCCCCC	57.91	23806337
594	Ubiquitination	SNVLCLSKSPNKHNR CCEEEEECCCCCCCC	57.91	-
595	Phosphorylation	NVLCLSKSPNKHNRL CEEEEECCCCCCCCE	30.26	25263469
604	Sulfoxidation	NKHNRLYMKARPFPD CCCCCEEEEEECCCC	3.03	21406390
605	Ubiquitination	KHNRLYMKARPFPDG CCCCEEEEEECCCCC	27.90	22790023
619	Acetylation	GLAEDIDKGEVSARQ CCHHCCCCCCCCHHH	58.25	23806337
629	Malonylation	VSARQELKARARYLA CCHHHHHHHHHHHHH	34.77	26073543
629	Ubiquitination	VSARQELKARARYLA CCHHHHHHHHHHHHH	34.77	27667366
634	Phosphorylation	ELKARARYLAEKYEW HHHHHHHHHHHHCCC	14.85	25168779
638	Acetylation	RARYLAEKYEWDVAE HHHHHHHHCCCCHHH	42.75	23806337
638	Ubiquitination	RARYLAEKYEWDVAE HHHHHHHHCCCCHHH	42.75	22790023
639	Phosphorylation	ARYLAEKYEWDVAEA HHHHHHHCCCCHHHH	17.48	25168779
648	Acetylation	WDVAEARKIWCFGPD CCHHHHHEEEEECCC	47.83	22733758
648	Ubiquitination	WDVAEARKIWCFGPD CCHHHHHEEEEECCC	47.83	22790023
651	S-nitrosocysteine	AEARKIWCFGPDGTG HHHHEEEEECCCCCC	3.00	-
651	Glutathionylation	AEARKIWCFGPDGTG HHHHEEEEECCCCCC	3.00	24333276
651	S-nitrosylation	AEARKIWCFGPDGTG HHHHEEEEECCCCCC	3.00	20925432
651	S-palmitoylation	AEARKIWCFGPDGTG HHHHEEEEECCCCCC	3.00	28526873
657	Phosphorylation	WCFGPDGTGPNILTD EEECCCCCCCCHHHH	57.77	23984901
663	Phosphorylation	GTGPNILTDITKGVQ CCCCCHHHHHHHHHH	22.89	23984901
666	Phosphorylation	PNILTDITKGVQYLN CCHHHHHHHHHHHHH	25.26	22817900
676	Ubiquitination	VQYLNEIKDSVVAGF HHHHHHHCHHHEEEC	37.46	-
693	S-nitrosocysteine	ATKEGALCEENMRGV CCCCCCCCCCCCCCC	6.46	-
693	S-nitrosylation	ATKEGALCEENMRGV CCCCCCCCCCCCCCC	6.46	24926564
693	S-palmitoylation	ATKEGALCEENMRGV CCCCCCCCCCCCCCC	6.46	28526873
715	Diphthamide	TLHADAIHRGGGQII EEEHHHEECCCCCCC	24.85	-
715	Amidation	TLHADAIHRGGGQII EEEHHHEECCCCCCC	24.85	-
728	S-nitrosocysteine	IIPTARRCLYASVLT CCCCHHHHHHHHHHH	2.58	-
728	Glutathionylation	IIPTARRCLYASVLT CCCCHHHHHHHHHHH	2.58	24333276
728	S-nitrosylation	IIPTARRCLYASVLT CCCCHHHHHHHHHHH	2.58	21278135
728	S-palmitoylation	IIPTARRCLYASVLT CCCCHHHHHHHHHHH	2.58	28526873
730	Phosphorylation	PTARRCLYASVLTAQ CCHHHHHHHHHHHCC	10.64	22802335
751	S-nitrosocysteine	IYLVEIQCPEQVVGG EEEEEEECCHHHHHH	5.00	-
751	Glutathionylation	IYLVEIQCPEQVVGG EEEEEEECCHHHHHH	5.00	24333276
751	S-nitrosylation	IYLVEIQCPEQVVGG EEEEEEECCHHHHHH	5.00	21278135
751	S-palmitoylation	IYLVEIQCPEQVVGG EEEEEEECCHHHHHH	5.00	28526873
760	Phosphorylation	EQVVGGIYGVLNRKR HHHHHHHHHHHCCCC	12.40	24224561
812	Glutathionylation	GGQAFPQCVFDHWQI CCCCCCCCEECCCEE	3.16	24333276
842	Ubiquitination	VAETRKRKGLKEGIP HHHHHHHCCHHHCCH	72.18	-
845	Acetylation	TRKRKGLKEGIPALD HHHHCCHHHCCHHHH	63.66	23954790
845	Ubiquitination	TRKRKGLKEGIPALD HHHHCCHHHCCHHHH	63.66	22790023
857	Acetylation	ALDNFLDKL------ HHHHHHHHC------	59.24	23806337
857	Ubiquitination	ALDNFLDKL------ HHHHHHHHC------	59.24	-

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
57	T	Phosphorylation	Kinase	EEF2K	O08796	Uniprot
265	Y	Phosphorylation	Kinase	CSK	P41241	Uniprot
373	Y	Phosphorylation	Kinase	CSK	P41241	Uniprot
595	S	Phosphorylation	Kinase	CDK2	P97377	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
595	S	Phosphorylation		-
Phosphorylation by EF-2 kinase completely inactivates EF-2; it requires prior phosphorylation by CDK2 at Ser-595 during mitotic prometaphase.

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 EF2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of EF2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of EF2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57 AND THR-59, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54 AND THR-57, AND MASSSPECTROMETRY.	17242355 [Abstract]

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