EEF1B2

Eukaryotic translation elongation factor 1 beta 2

PDB rendering based on 1b64.

Available structures
PDB	1b64

Identifiers

Symbols

EEF1B2; EEF1B; EEF1B1; EF1B

External IDs

OMIM: 600655 MGI: 1929520 HomoloGene: 1480 GeneCards: EEF1B2 Gene

Gene Ontology
Molecular function	• translation elongation factor activity • protein binding
Cellular component	• cytosol • cytosol • eukaryotic translation elongation factor 1 complex
Biological process	• translation • translational elongation • translational elongation • gene expression • cellular protein metabolic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
207.02 – 207.03 Mb

Chr 1:
63.22 – 63.23 Mb

PubMed search

[1]

[2]

Elongation factor 1-beta is a protein that in humans is encoded by the EEF1B2 gene.^[1]^[2]

This gene encodes a translation elongation factor. The protein is a guanine nucleotide exchange factor involved in the transfer of aminoacylated tRNAs to the ribosome. Alternative splicing results in three transcript variants which differ only in the 5' UTR.^[2]

Interactions

EEF1B2 has been shown to interact with EEF1G^[3]^[4] and HARS.^[5]

References

^ Pizzuti A, Gennarelli M, Novelli G, Colosimo A, Lo Cicero S, Caskey CT, Dallapiccola B (Jan 1994). "Human elongation factor EF-1 beta: cloning and characterization of the EF1 beta 5a gene and assignment of EF-1 beta isoforms to chromosomes 2,5,15 and X". Biochem Biophys Res Commun 197 (1): 154–62. doi:10.1006/bbrc.1993.2454. PMID 8250921.
^ ^a ^b "Entrez Gene: EEF1B2 eukaryotic translation elongation factor 1 beta 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1933.
^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
^ Stelzl, Ulrich; Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E (Sep. 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell (United States) 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. ISSN 0092-8674. PMID 16169070.
^ Sang Lee, Jong; Gyu Park Sang, Park Heonyong, Seol Wongi, Lee Sangwon, Kim Sunghoon (Feb. 2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys. Res. Commun. (United States) 291 (1): 158–64. doi:10.1006/bbrc.2002.6398. ISSN 0006-291X. PMID 11829477.

Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667.
Hochstrasser DF, Frutiger S, Paquet N, et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis 13 (12): 992–1001. doi:10.1002/elps.11501301201. PMID 1286669.
von der Kammer H, Klaudiny J, Zimmer M, Scheit KH (1991). "Human elongation factor 1 beta: cDNA and derived amino acid sequence". Biochem. Biophys. Res. Commun. 177 (1): 312–7. doi:10.1016/0006-291X(91)91984-K. PMID 1710449.
Sanders J, Maassen JA, Amons R, Möller W (1991). "Nucleotide sequence of human elongation factor-1 beta cDNA". Nucleic Acids Res. 19 (16): 4551. doi:10.1093/nar/19.16.4551. PMC 328648. PMID 1886777. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=328648.
Bec G, Kerjan P, Zha XD, Waller JP (1990). "Valyl-tRNA synthetase from rabbit liver. I. Purification as a heterotypic complex in association with elongation factor 1". J. Biol. Chem. 264 (35): 21131–7. PMID 2556394.
Motorin YuA , Wolfson AD, Orlovsky AF, Gladilin KL (1988). "Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor". FEBS Lett. 238 (2): 262–4. doi:10.1016/0014-5793(88)80492-7. PMID 3169261.
Chen CJ, Traugh JA (1996). "Expression of recombinant elongation factor 1 beta from rabbit in Escherichia coli. Phosphorylation by casein kinase II". Biochim. Biophys. Acta 1264 (3): 303–11. PMID 8547318.
Béhar G, Coleclough C, Houlgatte R, et al. (1996). "Human lymphocyte cDNA ordered library analyzed by 2D gel electrophoresis. 3. Analysis of individual clones". Appl. Theor. Electrophor. 5 (2): 99–105. PMID 8573604.
Sanders J, Brandsma M, Janssen GM, et al. (1996). "Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum". J. Cell. Sci. 109 ( Pt 5): 1113–7. PMID 8743958.
Sheu GT, Traugh JA (1998). "Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli. Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII". J. Biol. Chem. 272 (52): 33290–7. doi:10.1074/jbc.272.52.33290. PMID 9407120.
Sheu GT, Traugh JA (1999). "A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII". Mol. Cell. Biochem. 191 (1–2): 181–6. doi:10.1023/A:1006802125856. PMID 10094407.
Pérez JM, Siegal G, Kriek J, et al. (1999). "The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli". Structure 7 (2): 217–26. doi:10.1016/S0969-2126(99)80027-6. PMID 10368288.
Chambers DM, Rouleau GA, Abbott CM (2001). "Comparative genomic analysis of genes encoding translation elongation factor 1B(alpha) in human and mouse shows EEF1B1 to be a recent retrotransposition event". Genomics 77 (3): 145–8. doi:10.1006/geno.2001.6626. PMID 11597139.
Sang Lee J, Gyu Park S, Park H, et al. (2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys. Res. Commun. 291 (1): 158–64. doi:10.1006/bbrc.2002.6398. PMID 11829477.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Cans C, Passer BJ, Shalak V, et al. (2004). "Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A". Proc. Natl. Acad. Sci. U.S.A. 100 (24): 13892–7. doi:10.1073/pnas.2335950100. PMC 283517. PMID 14623968. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=283517.
Shu H, Chen S, Bi Q, et al. (2004). "Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line". Mol. Cell Proteomics 3 (3): 279–86. doi:10.1074/mcp.D300003-MCP200. PMID 14729942.
Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446.
Ito T, Marintchev A, Wagner G (2005). "Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B". Structure 12 (9): 1693–704. doi:10.1016/j.str.2004.07.010. PMID 15341733.

PDB gallery

1b64: SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES

Protein biosynthesis: translation (prokaryotic, eukaryotic)

Ribosomal proteins

Initiation factor

Prokaryotic	PIF-1 · PIF-2 · PIF-3

Archaeal	aIF1 · aIF2 · aIF5 · aIF6

Eukaryotic	eIF1 (EIF1AX, AY, 1B) eIF2 (EIF2S1, EIF2S2, EIF2S3) · EIF2B1, EIF2B2, EIF2B3, EIF2B4, EIF2B5 · EIF-2 kinase eIF3 (EIF3A, B, C, D, F, G, H, I, J, K, M, S6) eIF4 (EIF4A2, A3, B, E1, E2, G1, G2, G3, H) eIF5 (EIF5A, A2, B) eIF6 (EIF6)

Elongation factor

Prokaryotic	EF-Tu, EF-Ts, EF-G

Archaeal	aEF-1, aEF-2

Eukaryotic	EEF-1 (EEF1A1, EEF1A2, EEF1A3, EEF1B1, EEF1B2, EEF1B3, EEF1B4, EEF1D, EEF1E1, EEF1G) · EEF2

Release factor

Prokaryotic · Archaeal · Eukaryotic (ETF1)

Other

RPS1 · RPS2 · RPS3 · RPS4 · RPS5 · RPS6 · RPS7 · RPS8 · RPS9 · RPS10 · RPS11 · RPS12 · RPS13 · RPS14 · RPS15 · RPS16 · RPS17 · RPS18 · RPS19 · RPS20 · RPS21 · RPS22 · RPS23 · RPS24 · RPS25 · RPS26 · RPS27 · RPS28 · RPS29

Other concepts

Aminoacyl tRNA synthetase · Reading frame · Start codon · Stop codon · Shine-Dalgarno sequence/Kozak consensus sequence

see also disorders of translation and posttranslational modification
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

EEF1B2

Interactions

References

Further reading