dbPTM

IF2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF2B_HUMAN
UniProt AC	P20042
Protein Name	Eukaryotic translation initiation factor 2 subunit 2
Gene Name	EIF2S2
Organism	Homo sapiens (Human).
Sequence Length	333
Subcellular Localization
Protein Description	eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B..
Protein Sequence	MSGDEMIFDPTMSKKKKKKKKPFMLDEEGDTQTEETQPSETKEVEPEPTEDKDLEADEEDTRKKDASDDLDDLNFFNQKKKKKKTKKIFDIDEAEEGVKDLKIESDVQEPTEPEDDLDIMLGNKKKKKKNVKFPDEDEILEKDEALEDEDNKKDDGISFSNQTGPAWAGSERDYTYEELLNRVFNIMREKNPDMVAGEKRKFVMKPPQVVRVGTKKTSFVNFTDICKLLHRQPKHLLAFLLAELGTSGSIDGNNQLVIKGRFQQKQIENVLRRYIKEYVTCHTCRSPDTILQKDTRLYFLQCETCHSRCSVASIKTGFQAVTGKRAQLRAKAN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGDEMIFD ------CCCCCCCCC	55.76	29255136
2	Acetylation	------MSGDEMIFD ------CCCCCCCCC	55.76	19413330
11	Phosphorylation	DEMIFDPTMSKKKKK CCCCCCCCCCCCCCC	35.60	23401153
13	Phosphorylation	MIFDPTMSKKKKKKK CCCCCCCCCCCCCCC	43.75	23401153
21	Acetylation	KKKKKKKKPFMLDEE CCCCCCCCCCCCCCC	52.98	26051181
24	Sulfoxidation	KKKKKPFMLDEEGDT CCCCCCCCCCCCCCC	6.64	30846556
31	Phosphorylation	MLDEEGDTQTEETQP CCCCCCCCCCCCCCC	48.52	25159151
33	Phosphorylation	DEEGDTQTEETQPSE CCCCCCCCCCCCCCC	37.57	25159151
36	Phosphorylation	GDTQTEETQPSETKE CCCCCCCCCCCCCCC	39.28	23403867
39	Phosphorylation	QTEETQPSETKEVEP CCCCCCCCCCCCCCC	48.34	23403867
41	Phosphorylation	EETQPSETKEVEPEP CCCCCCCCCCCCCCC	36.52	25627689
52	Acetylation	EPEPTEDKDLEADEE CCCCCCCCCCCCCHH	58.96	26051181
52	Ubiquitination	EPEPTEDKDLEADEE CCCCCCCCCCCCCHH	58.96	21890473
64	Ubiquitination	DEEDTRKKDASDDLD CHHHHHHCCCCCCHH	56.06	-
67	Phosphorylation	DTRKKDASDDLDDLN HHHHCCCCCCHHHHH	41.62	20201521
79	Succinylation	DLNFFNQKKKKKKTK HHHHCCHHHCCCCCC	68.60	23954790
79	Ubiquitination	DLNFFNQKKKKKKTK HHHHCCHHHCCCCCC	68.60	-
79	Acetylation	DLNFFNQKKKKKKTK HHHHCCHHHCCCCCC	68.60	23236377
79	2-Hydroxyisobutyrylation	DLNFFNQKKKKKKTK HHHHCCHHHCCCCCC	68.60	-
87	2-Hydroxyisobutyrylation	KKKKKTKKIFDIDEA HCCCCCCCCCCHHHH	54.56	-
87	Ubiquitination	KKKKKTKKIFDIDEA HCCCCCCCCCCHHHH	54.56	-
99	Acetylation	DEAEEGVKDLKIESD HHHHHHHCCCEEECC	69.10	25953088
99	2-Hydroxyisobutyrylation	DEAEEGVKDLKIESD HHHHHHHCCCEEECC	69.10	-
99	Ubiquitination	DEAEEGVKDLKIESD HHHHHHHCCCEEECC	69.10	21906983
102	Sumoylation	EEGVKDLKIESDVQE HHHHCCCEEECCCCC	55.34	28112733
105	Phosphorylation	VKDLKIESDVQEPTE HCCCEEECCCCCCCC	46.70	29255136
111	Phosphorylation	ESDVQEPTEPEDDLD ECCCCCCCCCCCHHH	64.52	29255136
124	2-Hydroxyisobutyrylation	LDIMLGNKKKKKKNV HHHHCCCCCCCCCCC	65.26	-
124	Methylation	LDIMLGNKKKKKKNV HHHHCCCCCCCCCCC	65.26	-
124	Ubiquitination	LDIMLGNKKKKKKNV HHHHCCCCCCCCCCC	65.26	21890473
124	Acetylation	LDIMLGNKKKKKKNV HHHHCCCCCCCCCCC	65.26	26051181
125	Ubiquitination	DIMLGNKKKKKKNVK HHHCCCCCCCCCCCC	74.05	21906983
132	Ubiquitination	KKKKKNVKFPDEDEI CCCCCCCCCCCHHHH	61.65	21890473
142	Ubiquitination	DEDEILEKDEALEDE CHHHHHHHHHHHCCC	58.38	21906983
142	2-Hydroxyisobutyrylation	DEDEILEKDEALEDE CHHHHHHHHHHHCCC	58.38	-
142	Acetylation	DEDEILEKDEALEDE CHHHHHHHHHHHCCC	58.38	26051181
153	Ubiquitination	LEDEDNKKDDGISFS HCCCCCCCCCCCCCC	68.27	-
153	Acetylation	LEDEDNKKDDGISFS HCCCCCCCCCCCCCC	68.27	26051181
158	Phosphorylation	NKKDDGISFSNQTGP CCCCCCCCCCCCCCC	28.31	21815630
160	Phosphorylation	KDDGISFSNQTGPAW CCCCCCCCCCCCCCC	22.65	28555341
163	Phosphorylation	GISFSNQTGPAWAGS CCCCCCCCCCCCCCC	49.75	28555341
172	Methylation	PAWAGSERDYTYEEL CCCCCCCCCCCHHHH	43.89	-
174	Phosphorylation	WAGSERDYTYEELLN CCCCCCCCCHHHHHH	19.90	28152594
175	Phosphorylation	AGSERDYTYEELLNR CCCCCCCCHHHHHHH	28.84	28152594
176	Phosphorylation	GSERDYTYEELLNRV CCCCCCCHHHHHHHH	10.94	28796482
190	Ubiquitination	VFNIMREKNPDMVAG HHHHHHHHCCCCCCC	64.51	-
190	Acetylation	VFNIMREKNPDMVAG HHHHHHHHCCCCCCC	64.51	23749302
194	Sulfoxidation	MREKNPDMVAGEKRK HHHHCCCCCCCCCCE	2.04	30846556
199	2-Hydroxyisobutyrylation	PDMVAGEKRKFVMKP CCCCCCCCCEECCCC	61.03	-
199	Ubiquitination	PDMVAGEKRKFVMKP CCCCCCCCCEECCCC	61.03	-
201	Malonylation	MVAGEKRKFVMKPPQ CCCCCCCEECCCCCE	54.07	26320211
204	Sulfoxidation	GEKRKFVMKPPQVVR CCCCEECCCCCEEEE	6.41	28183972
205	Malonylation	EKRKFVMKPPQVVRV CCCEECCCCCEEEEE	48.52	30639696
205	Ubiquitination	EKRKFVMKPPQVVRV CCCEECCCCCEEEEE	48.52	-
205	Acetylation	EKRKFVMKPPQVVRV CCCEECCCCCEEEEE	48.52	25953088
216	Ubiquitination	VVRVGTKKTSFVNFT EEEECCCCCCCCCHH	49.60	-
216	2-Hydroxyisobutyrylation	VVRVGTKKTSFVNFT EEEECCCCCCCCCHH	49.60	-
216	Malonylation	VVRVGTKKTSFVNFT EEEECCCCCCCCCHH	49.60	26320211
216	Acetylation	VVRVGTKKTSFVNFT EEEECCCCCCCCCHH	49.60	26051181
217	Phosphorylation	VRVGTKKTSFVNFTD EEECCCCCCCCCHHH	29.02	26434776
218	Phosphorylation	RVGTKKTSFVNFTDI EECCCCCCCCCHHHH	35.76	26434776
223	Phosphorylation	KTSFVNFTDICKLLH CCCCCCHHHHHHHHH	21.17	26434776
226	Glutathionylation	FVNFTDICKLLHRQP CCCHHHHHHHHHCCH	2.57	22555962
227	2-Hydroxyisobutyrylation	VNFTDICKLLHRQPK CCHHHHHHHHHCCHH	55.18	-
227	Acetylation	VNFTDICKLLHRQPK CCHHHHHHHHHCCHH	55.18	25825284
227	Ubiquitination	VNFTDICKLLHRQPK CCHHHHHHHHHCCHH	55.18	21890473
265	Acetylation	IKGRFQQKQIENVLR ECEECCHHHHHHHHH	42.32	19608861
265	Malonylation	IKGRFQQKQIENVLR ECEECCHHHHHHHHH	42.32	26320211
265	Ubiquitination	IKGRFQQKQIENVLR ECEECCHHHHHHHHH	42.32	19608861
274	Phosphorylation	IENVLRRYIKEYVTC HHHHHHHHHHHHHCC	15.20	26074081
276	Acetylation	NVLRRYIKEYVTCHT HHHHHHHHHHHCCCC	33.77	23749302
276	Ubiquitination	NVLRRYIKEYVTCHT HHHHHHHHHHHCCCC	33.77	-
278	Phosphorylation	LRRYIKEYVTCHTCR HHHHHHHHHCCCCCC	8.96	28152594
280	Phosphorylation	RYIKEYVTCHTCRSP HHHHHHHCCCCCCCC	9.54	26074081
283	Phosphorylation	KEYVTCHTCRSPDTI HHHHCCCCCCCCCCC	16.26	25159151
286	Phosphorylation	VTCHTCRSPDTILQK HCCCCCCCCCCCCCC	29.31	21815630
293	Ubiquitination	SPDTILQKDTRLYFL CCCCCCCCCCEEEEE	58.59	19608861
293	2-Hydroxyisobutyrylation	SPDTILQKDTRLYFL CCCCCCCCCCEEEEE	58.59	-
293	Malonylation	SPDTILQKDTRLYFL CCCCCCCCCCEEEEE	58.59	26320211
293	Acetylation	SPDTILQKDTRLYFL CCCCCCCCCCEEEEE	58.59	19608861
295	Phosphorylation	DTILQKDTRLYFLQC CCCCCCCCEEEEEEE	29.61	28152594
296	Methylation	TILQKDTRLYFLQCE CCCCCCCEEEEEEEH	37.21	-
298	Phosphorylation	LQKDTRLYFLQCETC CCCCCEEEEEEEHHC	10.04	28152594
310	Phosphorylation	ETCHSRCSVASIKTG HHCCCCCCHHHHHHC	21.43	28857561
315	Ubiquitination	RCSVASIKTGFQAVT CCCHHHHHHCHHHHH	39.85	-
315	Acetylation	RCSVASIKTGFQAVT CCCHHHHHHCHHHHH	39.85	26051181
324	Ubiquitination	GFQAVTGKRAQLRAK CHHHHHCCHHHHHHH	34.88	-
324	Malonylation	GFQAVTGKRAQLRAK CHHHHHCCHHHHHHH	34.88	26320211
324	Acetylation	GFQAVTGKRAQLRAK CHHHHHCCHHHHHHH	34.88	25953088
324	2-Hydroxyisobutyrylation	GFQAVTGKRAQLRAK CHHHHHCCHHHHHHH	34.88	-

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
2	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
2	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
67	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
67	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF2B_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 IF2B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PKHM1_HUMAN	PLEKHM1	physical	16169070
DPYL1_HUMAN	CRMP1	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
ZBT16_HUMAN	ZBTB16	physical	16169070
APLP1_HUMAN	APLP1	physical	16169070
CC90B_HUMAN	CCDC90B	physical	16169070
TLE1_HUMAN	TLE1	physical	16169070
P53_HUMAN	TP53	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
IF5_RAT	Eif5	physical	9395514
A4_HUMAN	APP	physical	21832049
CSK21_HUMAN	CSNK2A1	physical	12901717
CSK2B_HUMAN	CSNK2B	physical	12901717
HMGA1_HUMAN	HMGA1	physical	18850631
IF2A_HUMAN	EIF2S1	physical	22863883
IF2G_HUMAN	EIF2S3	physical	26186194
ANM7_HUMAN	PRMT7	physical	26186194
IF2A_HUMAN	EIF2S1	physical	26186194
CD123_HUMAN	CDC123	physical	26186194
DDX56_HUMAN	DDX56	physical	26344197
IF2A_HUMAN	EIF2S1	physical	26344197
IF2G_HUMAN	EIF2S3	physical	26344197
KIF23_HUMAN	KIF23	physical	26344197
CNDD3_HUMAN	NCAPD3	physical	26344197
NOP56_HUMAN	NOP56	physical	26344197
NOP58_HUMAN	NOP58	physical	26344197
NSA2_HUMAN	NSA2	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
UBIM_HUMAN	FAU	physical	27082860
RL40_HUMAN	UBA52	physical	27082860
IF5A1_HUMAN	EIF5A	physical	27082860
RS19_HUMAN	RPS19	physical	27082860
RS12_HUMAN	RPS12	physical	27082860
RS10_HUMAN	RPS10	physical	27082860
NPM_HUMAN	NPM1	physical	27082860
RAN_HUMAN	RAN	physical	27082860
ATPG_HUMAN	ATP5C1	physical	27082860
HDGF_HUMAN	HDGF	physical	27082860
VAT1_HUMAN	VAT1	physical	27082860
PA2G4_HUMAN	PA2G4	physical	27082860
STIP1_HUMAN	STIP1	physical	27082860
ANM7_HUMAN	PRMT7	physical	28514442
IF2A_HUMAN	EIF2S1	physical	28514442
CD123_HUMAN	CDC123	physical	28514442
IF2G_HUMAN	EIF2S3	physical	28514442

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 IF2B_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-265 AND LYS-293, 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-105 AND THR-111, 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-2, AND MASSSPECTROMETRY.	19369195 [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-67; SER-105 AND THR-111,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-2, AND MASSSPECTROMETRY.	18691976 [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-2, AND MASSSPECTROMETRY.	17081983 [Abstract]