UniProt Accession

 IF2G_HUMAN; P41091; B5BTZ4 

Genbank Protein ID

 L19161; AB451230; AB451353; CH471074; BC019906 

Genbank Nucleotide ID

 AAA19696.1; BAG70044.1; BAG70167.1; EAW99010.1; AAH19906.1 

Protein Name

 Eukaryotic translation initiation factor 2 subunit 3 

Protein Synonyms/Alias

 Eukaryotic translation initiation factor 2 subunit gamma X; eIF-2-gamma X; eIF-2gX 

Gene Name

 EIF2S3 

Gene Synonyms/Alias

 EIF2G 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
27	LTTLDVTKLTPLSHE	ubiquitination	[1, 2, 3, 4, 5, 6]
59	HGKSTVVKAISGVHT	ubiquitination	[1, 3, 4, 6]
70	GVHTVRFKNELERNI	ubiquitination	[1, 4, 6]
87	KLGYANAKIYKLDDP	ubiquitination	[2, 3, 4]
90	YANAKIYKLDDPSCP	ubiquitination	[1, 4, 6, 7]
121	PTDIPGTKGNFKLVR	ubiquitination	[4, 5, 7]
125	PGTKGNFKLVRHVSF	ubiquitination	[3, 4]
191	HILILQNKIDLVKES	ubiquitination	[2, 3, 4, 8]
196	QNKIDLVKESQAKEQ	ubiquitination	[1, 2, 3, 6, 8, 9]
242	VCEYIVKKIPVPPRD	ubiquitination	[4]
266	IRSFDVNKPGCEVDD	ubiquitination	[4, 7]
275	GCEVDDLKGGVAGGS	ubiquitination	[4, 7]
285	VAGGSILKGVLKVGQ	ubiquitination	[2, 5]
289	SILKGVLKVGQEIEV	ubiquitination	[1, 3, 4, 6, 8, 9]
303	VRPGIVSKDSEGKLM	ubiquitination	[2, 4, 5, 8, 9]
308	VSKDSEGKLMCKPIF	ubiquitination	[4, 8, 9]
312	SEGKLMCKPIFSKIV	ubiquitination	[4, 8, 9]
317	MCKPIFSKIVSLFAE	ubiquitination	[8]
342	GLIGVGTKIDPTLCR	ubiquitination	[3, 4, 8]
400	AKVQKLSKNEVLMVN	ubiquitination	[3]
421	GGRVSAVKADLGKIV	ubiquitination	[1, 2, 3, 4, 6, 8]
426	AVKADLGKIVLTNPV	ubiquitination	[4, 8, 9]
440	VCTEVGEKIALSRRV	ubiquitination	[3, 4, 8, 9]
449	ALSRRVEKHWRLIGW	ubiquitination	[8]
466	IRRGVTIKPTVDDD*	ubiquitination	[2, 3, 4, 5, 8]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional 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. 

Sequence Annotation

 NP_BIND 48 55 GTP (By similarity).
 NP_BIND 134 138 GTP (By similarity).
 NP_BIND 190 193 GTP (By similarity).
 MOD_RES 2 2 N-acetylalanine; partial.
 MOD_RES 22 22 Phosphothreonine (By similarity).  

Keyword

 Acetylation; Complete proteome; Direct protein sequencing; GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 472 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; TAS:ProtInc.
 GO:0003743; F:translation initiation factor activity; IDA:UniProtKB. 

Interpro

 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR015256; TIF2_gsu_C.
 IPR009001; Transl_elong_EF1A/Init_IF2_C.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 

Pfam

 PF09173; eIF2_C
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 

SMART

  

PROSITE

  

PRINTS

 PR00315; ELONGATNFCT.