UniProt Accession

 IF2B_HUMAN; P20042; Q9BVU0; Q9UJE4 

Genbank Protein ID

 M29536; AL031668; BC000461; BC000934 

Genbank Nucleotide ID

 AAA52383.1; CAB43741.1; AAH00461.1; AAH00934.1 

Protein Name

 Eukaryotic translation initiation factor 2 subunit 2 

Protein Synonyms/Alias

 Eukaryotic translation initiation factor 2 subunit beta; eIF-2-beta 

Gene Name

 EIF2S2 

Gene Synonyms/Alias

 EIF2B 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
52	EPEPTEDKDLEADEE	ubiquitination	[1, 2]
79	DLNFFNQKKKKKKTK	acetylation	[3]
79	DLNFFNQKKKKKKTK	ubiquitination	[2]
99	DEAEEGVKDLKIESD	ubiquitination	[2, 4]
124	LDIMLGNKKKKKKNV	ubiquitination	[2]
125	DIMLGNKKKKKKNVK	ubiquitination	[2]
132	KKKKKNVKFPDEDEI	ubiquitination	[5, 6]
142	DEDEILEKDEALEDE	ubiquitination	[2]
190	VFNIMREKNPDMVAG	acetylation	[4]
216	VVRVGTKKTSFVNFT	ubiquitination	[7]
227	VNFTDICKLLHRQPK	acetylation	[4]
227	VNFTDICKLLHRQPK	ubiquitination	[4, 5, 6, 7]
265	IKGRFQQKQIENVLR	acetylation	[3, 8]
265	IKGRFQQKQIENVLR	ubiquitination	[4, 7]
276	NVLRRYIKEYVTCHT	acetylation	[4]
276	NVLRRYIKEYVTCHT	ubiquitination	[7]
293	SPDTILQKDTRLYFL	acetylation	[3, 4, 8, 9]
315	RCSVASIKTGFQAVT	ubiquitination	[7]
324	GFQAVTGKRAQLRAK	ubiquitination	[2, 4, 7]

Reference

 [1] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [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] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] 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]
 [5] 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]
 [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] 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]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 

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

 ZN_FING 281 305 C4-type (Potential).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 13 13 Phosphoserine (By similarity).
 MOD_RES 67 67 Phosphoserine.
 MOD_RES 105 105 Phosphoserine.
 MOD_RES 111 111 Phosphothreonine.
 MOD_RES 158 158 Phosphoserine.
 MOD_RES 218 218 Phosphoserine (By similarity).
 MOD_RES 265 265 N6-acetyllysine.
 MOD_RES 293 293 N6-acetyllysine.  

Keyword

 Acetylation; Complete proteome; Initiation factor; Metal-binding; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 333 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005850; C:eukaryotic translation initiation factor 2 complex; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003743; F:translation initiation factor activity; IDA:UniProtKB. 

Interpro

 IPR002735; Transl_init_fac_IF2/IF5.
 IPR016189; Transl_init_fac_IF2/IF5_N.
 IPR016190; Transl_init_fac_IF2/IF5_Zn-bd. 

Pfam

 PF01873; eIF-5_eIF-2B 

SMART

 SM00653; eIF2B_5 

PROSITE

  

PRINTS