dbPTM

EI2BE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EI2BE_HUMAN
UniProt AC	Q13144
Protein Name	Translation initiation factor eIF-2B subunit epsilon
Gene Name	EIF2B5
Organism	Homo sapiens (Human).
Sequence Length	721
Subcellular Localization
Protein Description	Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP..
Protein Sequence	MAAPVVAPPGVVVSRANKRSGAGPGGSGGGGARGAEEEPPPPLQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTSLNVVRIITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVSVMTMIFKESSPSHPTRCHEDNVVVAVDSTTNRVLHFQKTQGLRRFAFPLSLFQGSSDGVEVRYDLLDCHISICSPQVAQLFTDNFDYQTRDDFVRGLLVNEEILGNQIHMHVTAKEYGARVSNLHMYSAVCADVIRRWVYPLTPEANFTDSTTQSCTHSRHNIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVISLHPPDAEEDEDDGEFSDDSGADQEKDKVKMKGYNPAEVGAAGKGYLWKAAGMNMEEEEELQQNLWGLKINMEEESESESEQSMDSEEPDSRGGSPQMDDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQMDSPLDSSRYCALLLPLLKAWSPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFIQWLKEAEEESSEDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAPVVAPP ------CCCCEECCC	22.07	22223895
14	Phosphorylation	APPGVVVSRANKRSG CCCCEEEECCCCCCC	17.67	21406692
19	Methylation	VVSRANKRSGAGPGG EEECCCCCCCCCCCC	39.88	-
20	Phosphorylation	VSRANKRSGAGPGGS EECCCCCCCCCCCCC	34.31	21406692
27	Phosphorylation	SGAGPGGSGGGGARG CCCCCCCCCCCCCCC	39.93	21406692
51	Phosphorylation	QAVLVADSFDRRFFP EEEEEECCCCCCCCC	21.22	11500362
61	Ubiquitination	RRFFPISKDQPRVLL CCCCCCCCCCCCCHH	62.19	33845483
103	Ubiquitination	CWKAAQIKEHLLKSK HHHHHHHHHHHHHCC	27.31	29967540
108	Ubiquitination	QIKEHLLKSKWCRPT HHHHHHHHCCCCCCC	57.24	27667366
124	Phosphorylation	LNVVRIITSELYRSL CCHHHHHHHHHHHHH	17.49	22167270
125	Phosphorylation	NVVRIITSELYRSLG CHHHHHHHHHHHHHH	18.39	22167270
128	Phosphorylation	RIITSELYRSLGDVL HHHHHHHHHHHHHHH	8.29	22167270
130	Phosphorylation	ITSELYRSLGDVLRD HHHHHHHHHHHHHHC	24.13	-
141	Ubiquitination	VLRDVDAKALVRSDF HHHCCCHHHHHCCCE	37.48	21906983
147	Ubiquitination	AKALVRSDFLLVYGD HHHHHCCCEEEEECH	27.87	27667366
176	Ubiquitination	RLRRKLEKNVSVMTM HHHHHHHHCCEEEEE	73.43	27667366
182	Phosphorylation	EKNVSVMTMIFKESS HHCCEEEEEEEECCC	12.64	-
186	Ubiquitination	SVMTMIFKESSPSHP EEEEEEEECCCCCCC	45.84	-
202	Ubiquitination	RCHEDNVVVAVDSTT CCCCCCEEEEEECCC	2.61	27667366
214	Ubiquitination	STTNRVLHFQKTQGL CCCCCEEEEECCCCC	21.89	21890473
217	Ubiquitination	NRVLHFQKTQGLRRF CCEEEEECCCCCCHH	41.70	27667366
219	Ubiquitination	VLHFQKTQGLRRFAF EEEEECCCCCCHHEE	56.83	22817900
231	Ubiquitination	FAFPLSLFQGSSDGV HEEEEHHHCCCCCCC	7.50	27667366
243	Ubiquitination	DGVEVRYDLLDCHIS CCCEEEEEEHHHEEE	30.14	21890473
248	Ubiquitination	RYDLLDCHISICSPQ EEEEHHHEEEECCHH	19.25	22817900
319	Phosphorylation	DVIRRWVYPLTPEAN HHHHHHHCCCCCCCC	5.88	20090780
322	Phosphorylation	RRWVYPLTPEANFTD HHHHCCCCCCCCCCC	17.99	-
334	Phosphorylation	FTDSTTQSCTHSRHN CCCCCCCCCCCCCCC	20.91	27080861
336	Phosphorylation	DSTTQSCTHSRHNIY CCCCCCCCCCCCCCC	28.29	27080861
338	Phosphorylation	TTQSCTHSRHNIYRG CCCCCCCCCCCCCCC	19.65	27080861
414	Ubiquitination	QIHQSLLCDNAEVKE CHHHHHCCCCCCCCC	4.62	24816145
420	Ubiquitination	LCDNAEVKERVTLKP CCCCCCCCCCCCCCC	31.16	-
420	Acetylation	LCDNAEVKERVTLKP CCCCCCCCCCCCCCC	31.16	26051181
426	Ubiquitination	VKERVTLKPRSVLTS CCCCCCCCCCCEEEE	29.08	27667366
442	Phosphorylation	VVVGPNITLPEGSVI EEECCCCCCCCCCEE	42.79	28348404
443	Ubiquitination	VVGPNITLPEGSVIS EECCCCCCCCCCEEE	3.00	24816145
447	Phosphorylation	NITLPEGSVISLHPP CCCCCCCCEEEECCC	18.02	27251275
450	Phosphorylation	LPEGSVISLHPPDAE CCCCCEEEECCCCCC	20.61	27251275
466	Phosphorylation	DEDDGEFSDDSGADQ CCCCCCCCCCCCCCH	35.88	26657352
469	Phosphorylation	DGEFSDDSGADQEKD CCCCCCCCCCCHHHH	40.65	11500362
481	Ubiquitination	EKDKVKMKGYNPAEV HHHHCCCCCCCHHHC	53.15	27667366
483	Phosphorylation	DKVKMKGYNPAEVGA HHCCCCCCCHHHCCC	16.68	-
493	Ubiquitination	AEVGAAGKGYLWKAA HHCCCCCCHHHHHHC	39.39	22817900
498	Ubiquitination	AGKGYLWKAAGMNME CCCHHHHHHCCCCHH	26.26	22817900
525	Phosphorylation	KINMEEESESESEQS CCCCCCCCCCHHCCC	50.10	25137130
527	Phosphorylation	NMEEESESESEQSMD CCCCCCCCHHCCCCC	56.56	25137130
529	Phosphorylation	EEESESESEQSMDSE CCCCCCHHCCCCCCC	50.65	25137130
532	Phosphorylation	SESESEQSMDSEEPD CCCHHCCCCCCCCCC	22.09	25137130
535	Phosphorylation	ESEQSMDSEEPDSRG HHCCCCCCCCCCCCC	34.91	25137130
540	Dephosphorylation	MDSEEPDSRGGSPQM CCCCCCCCCCCCCCH	43.47	9468292
540	Phosphorylation	MDSEEPDSRGGSPQM CCCCCCCCCCCCCCH	43.47	11500362
544	Phosphorylation	EPDSRGGSPQMDDIK CCCCCCCCCCHHHHH	18.12	19664994
560	Phosphorylation	FQNEVLGTLQRGKEE HHHHHHHHHHCCCCC	18.63	28857561
565	Ubiquitination	LGTLQRGKEENISCD HHHHHCCCCCCCCCC	65.13	29967540
570	Phosphorylation	RGKEENISCDNLVLE CCCCCCCCCCCEEEE	27.31	30622161
583	Phosphorylation	LEINSLKYAYNISLK EEEHHHHHHHCCCHH	21.44	28152594
585	Phosphorylation	INSLKYAYNISLKEV EHHHHHHHCCCHHHH	15.22	28442448
588	Phosphorylation	LKYAYNISLKEVMQV HHHHHCCCHHHHHHH	29.74	24719451
597	Phosphorylation	KEVMQVLSHVVLEFP HHHHHHHHHHHHHCC	18.51	27080861
610	Phosphorylation	FPLQQMDSPLDSSRY CCHHHCCCCCCHHHH	23.24	25159151
614	Phosphorylation	QMDSPLDSSRYCALL HCCCCCCHHHHHHHH	25.13	27732954
615	Phosphorylation	MDSPLDSSRYCALLL CCCCCCHHHHHHHHH	27.25	27732954
617	Phosphorylation	SPLDSSRYCALLLPL CCCCHHHHHHHHHHH	5.52	20068231
618	S-nitrosocysteine	PLDSSRYCALLLPLL CCCHHHHHHHHHHHH	1.77	-
618	S-nitrosylation	PLDSSRYCALLLPLL CCCHHHHHHHHHHHH	1.77	19483679
693	Ubiquitination	SQRDTTDKGQQLRKN HCCCCCCHHHHHHHH	57.43	24816145
717	Phosphorylation	LKEAEEESSEDD--- HHHHHHHHCCCC---	42.16	23927012
718	Phosphorylation	KEAEEESSEDD---- HHHHHHHCCCC----	48.61	23927012

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
535	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
535	S	Phosphorylation	Kinase	GSK-3_GROUP	-	PhosphoELM
544	S	Phosphorylation	Kinase	DYRK2	Q92630	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
544	S	Phosphorylation		18088087
Phosphorylated at Ser-544 by DYRK2; this is required for subsequent phosphorylation by GSK3B (By similarity).

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 EI2BE_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EI2BB_HUMAN	EIF2B2	physical	10858531
A4_HUMAN	APP	physical	21832049
EI2BG_HUMAN	EIF2B3	physical	22939629
EI2BB_HUMAN	EIF2B2	physical	26344197
EI2BG_HUMAN	EIF2B3	physical	26344197
EI2BD_HUMAN	EIF2B4	physical	26344197
EIF3K_HUMAN	EIF3K	physical	26344197
EIF3L_HUMAN	EIF3L	physical	26344197
IF4G3_HUMAN	EIF4G3	physical	26344197
EI2BA_HUMAN	EIF2B1	physical	27173435
EI2BB_HUMAN	EIF2B2	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603896	Leukodystrophy with vanishing white matter (VWM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EI2BE_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-544, AND MASS SPECTROMETRY.	19413330 [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-717 AND SER-718, ANDMASS SPECTROMETRY.	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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-544, 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-544; SER-717 ANDSER-718, 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-544, AND MASSSPECTROMETRY.	18691976 [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-544, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND MASSSPECTROMETRY.	19007248 [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-525; SER-527; SER-529;SER-532; SER-535; SER-540 AND SER-544, 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-544, AND MASSSPECTROMETRY.	16097034 [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-544, AND MASSSPECTROMETRY.	15302935 [Abstract]

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