dbPTM

EIF2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EIF2A_HUMAN
UniProt AC	Q9BY44
Protein Name	Eukaryotic translation initiation factor 2A
Gene Name	EIF2A
Organism	Homo sapiens (Human).
Sequence Length	585
Subcellular Localization
Protein Description	Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner..
Protein Sequence	MAPSTPLLTVRGSEGLYMVNGPPHFTESTVFPRESGKNCKVCIFSKDGTLFAWGNGEKVNIISVTNKGLLHSFDLLKAVCLEFSPKNTVLATWQPYTTSKDGTAGIPNLQLYDVKTGTCLKSFIQKKMQNWCPSWSEDETLCARNVNNEVHFFENNNFNTIANKLHLQKINDFVLSPGPQPYKVAVYVPGSKGAPSFVRLYQYPNFAGPHAALANKSFFKADKVTMLWNKKATAVLVIASTDVDKTGASYYGEQTLHYIATNGESAVVQLPKNGPIYDVVWNSSSTEFCAVYGFMPAKATIFNLKCDPVFDFGTGPRNAAYYSPHGHILVLAGFGNLRGQMEVWDVKNYKLISKPVASDSTYFAWCPDGEHILTATCAPRLRVNNGYKIWHYTGSILHKYDVPSNAELWQVSWQPFLDGIFPAKTITYQAVPSEVPNEEPKVATAYRPPALRNKPITNSKLHEEEPPQNMKPQSGNDKPLSKTALKNQRKHEAKKAAKQEARSDKSPDLAPTPAPQSTPRNTVSQSISGDPEIDKKIKNLKKKLKAIEQLKEQAATGKQLEKNQLEKIQKETALLQELEDLELGI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MAPSTPLL -------CCCCCCEE	12.81	22814378
2	Acetylation	------MAPSTPLLT ------CCCCCCEEE	13.52	-
4	Phosphorylation	----MAPSTPLLTVR ----CCCCCCEEEEE	32.87	29396449
5	Phosphorylation	---MAPSTPLLTVRG ---CCCCCCEEEEEC	19.52	25159151
9	Phosphorylation	APSTPLLTVRGSEGL CCCCCEEEEECCCCE	18.81	29396449
17	Phosphorylation	VRGSEGLYMVNGPPH EECCCCEEEECCCCC	15.18	23403867
26	Phosphorylation	VNGPPHFTESTVFPR ECCCCCCCCCCCCCC	26.45	28857561
28	Phosphorylation	GPPHFTESTVFPRES CCCCCCCCCCCCCCC	27.15	28857561
35	Phosphorylation	STVFPRESGKNCKVC CCCCCCCCCCCCEEE	57.24	23403867
40	Acetylation	RESGKNCKVCIFSKD CCCCCCCEEEEEECC	49.92	25953088
40	Ubiquitination	RESGKNCKVCIFSKD CCCCCCCEEEEEECC	49.92	-
45	Phosphorylation	NCKVCIFSKDGTLFA CCEEEEEECCCCEEE	15.21	24719451
46	Acetylation	CKVCIFSKDGTLFAW CEEEEEECCCCEEEE	49.80	26051181
67	Ubiquitination	NIISVTNKGLLHSFD EEEEECCCCHHHHHH	41.38	-
67	Ubiquitination	NIISVTNKGLLHSFD EEEEECCCCHHHHHH	41.38	-
75	Ubiquitination	GLLHSFDLLKAVCLE CHHHHHHHHHHHHHH	5.07	-
84	Phosphorylation	KAVCLEFSPKNTVLA HHHHHHCCCCCCEEE	26.11	24719451
86	Acetylation	VCLEFSPKNTVLATW HHHHCCCCCCEEEEE	65.14	26051181
88	Phosphorylation	LEFSPKNTVLATWQP HHCCCCCCEEEEEEE	24.03	23898821
90	Ubiquitination	FSPKNTVLATWQPYT CCCCCCEEEEEEEEE	3.10	-
92	Phosphorylation	PKNTVLATWQPYTTS CCCCEEEEEEEEECC	22.07	23898821
96	Ubiquitination	VLATWQPYTTSKDGT EEEEEEEEECCCCCC	13.93	-
96	Phosphorylation	VLATWQPYTTSKDGT EEEEEEEEECCCCCC	13.93	28152594
97	Phosphorylation	LATWQPYTTSKDGTA EEEEEEEECCCCCCC	31.14	28152594
98	Phosphorylation	ATWQPYTTSKDGTAG EEEEEEECCCCCCCC	28.12	28152594
99	Phosphorylation	TWQPYTTSKDGTAGI EEEEEECCCCCCCCC	22.43	28152594
100	Ubiquitination	WQPYTTSKDGTAGIP EEEEECCCCCCCCCC	59.07	21906983
100 (in isoform 1)	Ubiquitination	-	59.07	21906983
102	Ubiquitination	PYTTSKDGTAGIPNL EEECCCCCCCCCCCE	22.62	-
103	Phosphorylation	YTTSKDGTAGIPNLQ EECCCCCCCCCCCEE	31.66	30576142
108	Ubiquitination	DGTAGIPNLQLYDVK CCCCCCCCEEEEECC	38.20	-
108 (in isoform 2)	Ubiquitination	-	38.20	21906983
112	Phosphorylation	GIPNLQLYDVKTGTC CCCCEEEEECCCCCH	13.01	23898821
115	Acetylation	NLQLYDVKTGTCLKS CEEEEECCCCCHHHH	38.04	25953088
115	Ubiquitination	NLQLYDVKTGTCLKS CEEEEECCCCCHHHH	38.04	-
116	Phosphorylation	LQLYDVKTGTCLKSF EEEEECCCCCHHHHH	37.26	23898821
118	Phosphorylation	LYDVKTGTCLKSFIQ EEECCCCCHHHHHHH	21.64	23898821
119	S-nitrosocysteine	YDVKTGTCLKSFIQK EECCCCCHHHHHHHH	4.82	-
119	S-nitrosylation	YDVKTGTCLKSFIQK EECCCCCHHHHHHHH	4.82	19483679
121	Acetylation	VKTGTCLKSFIQKKM CCCCCHHHHHHHHHH	45.53	25953088
121	Ubiquitination	VKTGTCLKSFIQKKM CCCCCHHHHHHHHHH	45.53	-
122	Ubiquitination	KTGTCLKSFIQKKMQ CCCCHHHHHHHHHHH	18.03	-
122 (in isoform 2)	Ubiquitination	-	18.03	21906983
126	Acetylation	CLKSFIQKKMQNWCP HHHHHHHHHHHHCCC	45.45	26051181
127	Ubiquitination	LKSFIQKKMQNWCPS HHHHHHHHHHHCCCC	29.37	-
131	Ubiquitination	IQKKMQNWCPSWSED HHHHHHHCCCCCCCC	4.40	-
131 (in isoform 2)	Ubiquitination	-	4.40	21906983
136	Phosphorylation	QNWCPSWSEDETLCA HHCCCCCCCCCCEEE	39.24	27134283
139	Ubiquitination	CPSWSEDETLCARNV CCCCCCCCCEEECCC	39.36	-
155	Ubiquitination	NEVHFFENNNFNTIA CCEEEEECCCHHHHH	43.52	-
155 (in isoform 2)	Ubiquitination	-	43.52	21906983
160	Phosphorylation	FENNNFNTIANKLHL EECCCHHHHHHHHHH	19.82	20873877
164	Acetylation	NFNTIANKLHLQKIN CHHHHHHHHHHHEEC	28.41	25953088
164	Ubiquitination	NFNTIANKLHLQKIN CHHHHHHHHHHHEEC	28.41	21906983
164 (in isoform 1)	Ubiquitination	-	28.41	21906983
169	Acetylation	ANKLHLQKINDFVLS HHHHHHHEECCEECC	50.25	25953088
169	Malonylation	ANKLHLQKINDFVLS HHHHHHHEECCEECC	50.25	26320211
169	Ubiquitination	ANKLHLQKINDFVLS HHHHHHHEECCEECC	50.25	-
169 (in isoform 1)	Ubiquitination	-	50.25	21906983
176	Phosphorylation	KINDFVLSPGPQPYK EECCEECCCCCCCEE	23.62	-
183	Acetylation	SPGPQPYKVAVYVPG CCCCCCEEEEEEECC	30.33	25953088
183	Ubiquitination	SPGPQPYKVAVYVPG CCCCCCEEEEEEECC	30.33	21906983
183 (in isoform 1)	Ubiquitination	-	30.33	21906983
191	Phosphorylation	VAVYVPGSKGAPSFV EEEEECCCCCCCCEE	23.11	20068231
192	Malonylation	AVYVPGSKGAPSFVR EEEECCCCCCCCEEE	66.07	26320211
192	Ubiquitination	AVYVPGSKGAPSFVR EEEECCCCCCCCEEE	66.07	-
192 (in isoform 1)	Ubiquitination	-	66.07	21906983
201	Phosphorylation	APSFVRLYQYPNFAG CCCEEEEECCCCCCC	8.74	28152594
216	Acetylation	PHAALANKSFFKADK CCHHHCCCCHHCCCC	42.93	26051181
216	Ubiquitination	PHAALANKSFFKADK CCHHHCCCCHHCCCC	42.93	21906983
216 (in isoform 1)	Ubiquitination	-	42.93	21906983
220	Ubiquitination	LANKSFFKADKVTML HCCCCHHCCCCEEEC	54.38	-
241	Phosphorylation	AVLVIASTDVDKTGA EEEEEEECCCCCCCC	30.90	-
244	Ubiquitination	VIASTDVDKTGASYY EEEECCCCCCCCCCC	45.68	-
249	Phosphorylation	DVDKTGASYYGEQTL CCCCCCCCCCCEEEE	21.89	-
250	Phosphorylation	VDKTGASYYGEQTLH CCCCCCCCCCEEEEE	18.24	27155012
251	Phosphorylation	DKTGASYYGEQTLHY CCCCCCCCCEEEEEE	16.22	-
258	Phosphorylation	YGEQTLHYIATNGES CCEEEEEEEEECCCC	8.72	-
286	Ubiquitination	VVWNSSSTEFCAVYG EEEECCCCCCEEEEC	34.72	-
286 (in isoform 2)	Ubiquitination	-	34.72	21906983
289	Ubiquitination	NSSSTEFCAVYGFMP ECCCCCCEEEECEEC	1.72	-
293	Ubiquitination	TEFCAVYGFMPAKAT CCCEEEECEECCEEE	13.04	-
305	Acetylation	KATIFNLKCDPVFDF EEEEEEEECCCCEEC	37.38	26051181
305	Ubiquitination	KATIFNLKCDPVFDF EEEEEEEECCCCEEC	37.38	-
314	Phosphorylation	DPVFDFGTGPRNAAY CCCEECCCCCCCCEE	43.96	28634120
347	Acetylation	QMEVWDVKNYKLISK EEEEEECCCCEEECC	52.68	26051181
347	Ubiquitination	QMEVWDVKNYKLISK EEEEEECCCCEEECC	52.68	21906983
347 (in isoform 1)	Ubiquitination	-	52.68	21906983
349	Phosphorylation	EVWDVKNYKLISKPV EEEECCCCEEECCCC	11.06	18452278
350	Ubiquitination	VWDVKNYKLISKPVA EEECCCCEEECCCCC	49.06	-
354	Acetylation	KNYKLISKPVASDST CCCEEECCCCCCCCC	36.20	26051181
354	Ubiquitination	KNYKLISKPVASDST CCCEEECCCCCCCCC	36.20	-
361	Phosphorylation	KPVASDSTYFAWCPD CCCCCCCCEEEECCC	27.87	-
362	Phosphorylation	PVASDSTYFAWCPDG CCCCCCCEEEECCCC	8.68	-
380	Ubiquitination	LTATCAPRLRVNNGY EEEEECCEEEECCCE	19.32	-
380 (in isoform 2)	Ubiquitination	-	19.32	21906983
392	Phosphorylation	NGYKIWHYTGSILHK CCEEEEEEECCEEEC	9.59	20068231
393	Phosphorylation	GYKIWHYTGSILHKY CEEEEEEECCEEECC	16.15	20068231
395	Phosphorylation	KIWHYTGSILHKYDV EEEEEECCEEECCCC	17.74	20068231
425	Phosphorylation	DGIFPAKTITYQAVP CCCCCCEEEEEEECC	22.21	21945579
427	Phosphorylation	IFPAKTITYQAVPSE CCCCEEEEEEECCCC	18.14	21945579
428	Phosphorylation	FPAKTITYQAVPSEV CCCEEEEEEECCCCC	7.22	21945579
441	Ubiquitination	EVPNEEPKVATAYRP CCCCCCCCCEECCCC	48.02	2190698
441 (in isoform 1)	Ubiquitination	-	48.02	21906983
446	Phosphorylation	EPKVATAYRPPALRN CCCCEECCCCHHHHC	21.21	21945579
471	Methylation	EEPPQNMKPQSGNDK CCCCCCCCCCCCCCC	47.67	-
474	Acetylation	PQNMKPQSGNDKPLS CCCCCCCCCCCCCCC	48.36	-
474	Phosphorylation	PQNMKPQSGNDKPLS CCCCCCCCCCCCCCC	48.36	29214152
478	Methylation	KPQSGNDKPLSKTAL CCCCCCCCCCCHHHH	52.43	-
503	Phosphorylation	AAKQEARSDKSPDLA HHHHHHHHCCCCCCC	57.34	29255136
506	Phosphorylation	QEARSDKSPDLAPTP HHHHHCCCCCCCCCC	28.74	29255136
512	Phosphorylation	KSPDLAPTPAPQSTP CCCCCCCCCCCCCCC	26.86	23927012
517	Phosphorylation	APTPAPQSTPRNTVS CCCCCCCCCCCCCCC	39.04	23927012
518	Phosphorylation	PTPAPQSTPRNTVSQ CCCCCCCCCCCCCCH	22.48	23927012
522	Phosphorylation	PQSTPRNTVSQSISG CCCCCCCCCCHHCCC	23.86	25159151
524	Phosphorylation	STPRNTVSQSISGDP CCCCCCCCHHCCCCH	19.03	25159151
526	Phosphorylation	PRNTVSQSISGDPEI CCCCCCHHCCCCHHH	15.94	12133843
528	Phosphorylation	NTVSQSISGDPEIDK CCCCHHCCCCHHHHH	42.25	25159151
535	Acetylation	SGDPEIDKKIKNLKK CCCHHHHHHHHHHHH	63.16	23954790
535	Malonylation	SGDPEIDKKIKNLKK CCCHHHHHHHHHHHH	63.16	26320211
551	2-Hydroxyisobutyrylation	LKAIEQLKEQAATGK HHHHHHHHHHHHHCH	47.69	-
551	Acetylation	LKAIEQLKEQAATGK HHHHHHHHHHHHHCH	47.69	26051181
567	Acetylation	LEKNQLEKIQKETAL HHHHHHHHHHHHHHH	60.06	25953088
567	Malonylation	LEKNQLEKIQKETAL HHHHHHHHHHHHHHH	60.06	26320211

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 EIF2A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EIF2A_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 EIF2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
PA2G4_HUMAN	PA2G4	physical	22939629
NXF1_HUMAN	NXF1	physical	18337511
ILF3_HUMAN	ILF3	physical	18337511
EIF3K_HUMAN	EIF3K	physical	22863883
RS10_HUMAN	RPS10	physical	22863883
RS16_HUMAN	RPS16	physical	22863883
RS19_HUMAN	RPS19	physical	22863883
RS23_HUMAN	RPS23	physical	22863883
RS24_HUMAN	RPS24	physical	22863883
RS29_HUMAN	RPS29	physical	22863883
RS5_HUMAN	RPS5	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
PAIRB_HUMAN	SERBP1	physical	22863883
RS6_HUMAN	RPS6	physical	21745818
CHRD1_HUMAN	CHORDC1	physical	26344197
ERCC2_HUMAN	ERCC2	physical	26344197
PNCB_HUMAN	NAPRT	physical	26344197
TBL1R_HUMAN	TBL1XR1	physical	26344197

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 EIF2A_HUMAN

Related Literatures of Post-Translational Modification

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-503, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND MASSSPECTROMETRY.	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-506; SER-517 ANDTHR-518, AND MASS SPECTROMETRY.	18669648 [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-506, 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-506; THR-512 ANDTHR-522, AND MASS SPECTROMETRY.	17287340 [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-506, AND MASSSPECTROMETRY.	17081983 [Abstract]