UniProt Accession

 EF1B_YEAST; P32471; D6VPL3 

Genbank Protein ID

 D14080; L22015; BK006935 

Genbank Nucleotide ID

 BAA03165.1; AAC04954.1; DAA06983.1 

Protein Name

 Elongation factor 1-beta 

Protein Synonyms/Alias

 EF-1-beta; Eukaryotic elongation factor 1Balpha; eEF1Balpha; Translation elongation factor 1B alpha 

Gene Name

 EFB1 

Gene Synonyms/Alias

 TEF5; YAL003W 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
8	MASTDFSKIETLKQL	acetylation	[1]
13	FSKIETLKQLNASLA	acetylation	[1]
13	FSKIETLKQLNASLA	ubiquitination	[2, 3]
22	LNASLADKSYIEGTA	ubiquitination	[3]
39	QADVTVFKAFQSAYP	ubiquitination	[4]
109	RIAAYNAKKAAKPAK	ubiquitination	[3]
128	SIVTLDVKPWDDETN	ubiquitination	[3]
166	IPIGFGIKKLQINCV	ubiquitination	[2, 3]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [4] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269] 

Functional Description

 Catalytic subunit of the guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A), probably by displacing GDP from the nucleotide binding pocket in eEF1A. The 30-fold higher concentration of GTP compared to GDP in cells favors the formation of eEF1A-GTP, which rapidly forms a ternary complex with aminoacyl-tRNA that in turn displaces eEF1B from the complex. 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 4 4 Phosphothreonine.
 MOD_RES 31 31 Phosphoserine.
 MOD_RES 43 43 Phosphoserine.
 MOD_RES 86 86 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Elongation factor; Phosphoprotein; Protein biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 206 AA 

Protein Sequence

Gene Ontology

 GO:0005853; C:eukaryotic translation elongation factor 1 complex; IMP:SGD.
 GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
 GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
 GO:0006414; P:translational elongation; TAS:SGD. 

Interpro

 IPR018940; EF-1_beta_acid_region_euk.
 IPR014717; Transl_elong_EF1B/ribosomal_S6.
 IPR001326; Transl_elong_EF1B_B/D_CS.
 IPR014038; Transl_elong_fac_EF1B_bsu/dsu. 

Pfam

 PF10587; EF-1_beta_acid
 PF00736; EF1_GNE 

SMART

 SM00888; EF1_GNE 

PROSITE

 PS00824; EF1BD_1
 PS00825; EF1BD_2 

PRINTS