dbPTM

IF2B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF2B_MOUSE
UniProt AC	Q99L45
Protein Name	Eukaryotic translation initiation factor 2 subunit 2
Gene Name	Eif2s2
Organism	Mus musculus (Mouse).
Sequence Length	331
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 (By similarity)..
Protein Sequence	MSGDEMIFDPTMSKKKKKKKKPFMLDEEGDAQTEETQPSETKEVEPEPTEEKDVDADEEDSRKKDASDDLDDLNFFNQKKKKKKTKKIFDIDEAEEAIKDVKIESDAQEPAEPEDDLDIMLGNKKKKKKNVKFPEEDEILEKDEALEDEDSKKDDGISFSSQTAWAGSERDYTYEELLNRVFNIMREKNPDMVAGEKRKFVMKPPQVVRVGTKKTSFVNFTDICKLLHRQPKHLLAFLLAELGTSGSIDGNNQLVIKGRFQQKQIENVLRRYIKEYVTCHTCRSPDTILQKDTRLYFLQCETCHSRCSVASIKTGFQAVTGKRAQLRAKAN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSGDEMIFD ------CCCCCCCCC	55.76	-
2	Phosphorylation	------MSGDEMIFD ------CCCCCCCCC	55.76	18388127
11	Phosphorylation	DEMIFDPTMSKKKKK CCCCCCCCCCCCCCC	35.60	23684622
13	Phosphorylation	MIFDPTMSKKKKKKK CCCCCCCCCCCCCCC	43.75	23684622
20	Acetylation	SKKKKKKKKPFMLDE CCCCCCCCCCCCCCC	74.65	22826441
36	Phosphorylation	GDAQTEETQPSETKE CCCCCCCCCCCCCCC	39.28	-
39	Phosphorylation	QTEETQPSETKEVEP CCCCCCCCCCCCCCC	48.34	25338131
52	Acetylation	EPEPTEEKDVDADEE CCCCCCCCCCCCCHH	57.74	23954790
52	Ubiquitination	EPEPTEEKDVDADEE CCCCCCCCCCCCCHH	57.74	-
61	Phosphorylation	VDADEEDSRKKDASD CCCCHHHHHCCCCCC	49.64	24899341
67	Phosphorylation	DSRKKDASDDLDDLN HHHCCCCCCCHHHHH	41.62	27087446
80	Acetylation	LNFFNQKKKKKKTKK HHHHCHHHCCCCCCC	61.12	19861659
99	Ubiquitination	DEAEEAIKDVKIESD HHHHHHHHHCCCCCC	64.61	-
105	Phosphorylation	IKDVKIESDAQEPAE HHHCCCCCCCCCCCC	41.54	27087446
151	Phosphorylation	EALEDEDSKKDDGIS HHHCCCCCCCCCCCC	39.29	25521595
158	Phosphorylation	SKKDDGISFSSQTAW CCCCCCCCCCCCCCC	25.30	-
161	Phosphorylation	DDGISFSSQTAWAGS CCCCCCCCCCCCCCC	29.55	26370283
168	Phosphorylation	SQTAWAGSERDYTYE CCCCCCCCCCCCCHH	23.01	-
172	Phosphorylation	WAGSERDYTYEELLN CCCCCCCCCHHHHHH	19.90	-
199	Ubiquitination	MVAGEKRKFVMKPPQ CCCCCCCEECCCCCE	54.07	-
203	Ubiquitination	EKRKFVMKPPQVVRV CCCEECCCCCEEEEE	48.52	-
216	Phosphorylation	RVGTKKTSFVNFTDI EECCCCCCCCCHHHH	35.76	-
224	S-palmitoylation	FVNFTDICKLLHRQP CCCHHHHHHHHHCCH	2.57	28526873
224	S-nitrosocysteine	FVNFTDICKLLHRQP CCCHHHHHHHHHCCH	2.57	-
224	S-nitrosylation	FVNFTDICKLLHRQP CCCHHHHHHHHHCCH	2.57	21278135
225	Ubiquitination	VNFTDICKLLHRQPK CCHHHHHHHHHCCHH	55.18	-
225	Acetylation	VNFTDICKLLHRQPK CCHHHHHHHHHCCHH	55.18	22826441
263	Acetylation	IKGRFQQKQIENVLR ECEECCHHHHHHHHH	42.32	22826441
263	Malonylation	IKGRFQQKQIENVLR ECEECCHHHHHHHHH	42.32	26320211
263	Ubiquitination	IKGRFQQKQIENVLR ECEECCHHHHHHHHH	42.32	-
274	Acetylation	NVLRRYIKEYVTCHT HHHHHHHHHHHCCCC	33.77	22826441
274	Malonylation	NVLRRYIKEYVTCHT HHHHHHHHHHHCCCC	33.77	26320211
291	Malonylation	SPDTILQKDTRLYFL CCCCCCCCCCEEEEE	58.59	26320211
291	Acetylation	SPDTILQKDTRLYFL CCCCCCCCCCEEEEE	58.59	22826441
296	Phosphorylation	LQKDTRLYFLQCETC CCCCCEEEEEEEHHC	10.04	25367039
307	Glutathionylation	CETCHSRCSVASIKT EHHCCCCCCHHHHHH	4.26	24333276
313	Ubiquitination	RCSVASIKTGFQAVT CCCHHHHHHCHHHHH	39.85	-
322	Malonylation	GFQAVTGKRAQLRAK CHHHHHCCHHHHHHH	34.88	26320211
322	Ubiquitination	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
Oops, there are no upstream regulatory protein records of IF2B_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF2B_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of IF2B_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of IF2B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND MASSSPECTROMETRY.	17203969 [Abstract]