EIF2B5

Eukaryotic translation initiation factor 2B, subunit 5 epsilon, 82kDa

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
3JUI

Identifiers

Symbols

EIF2B5 ; CACH; CLE; EIF-2B; EIF2Bepsilon; LVWM

External IDs

OMIM: 603945 MGI: 2446176 HomoloGene: 2903 GeneCards: EIF2B5 Gene

Gene ontology
Molecular function	• translation initiation factor activity • guanyl-nucleotide exchange factor activity • protein binding • translation initiation factor binding
Cellular component	• nucleus • cytoplasm • cytosol • eukaryotic translation initiation factor 2B complex
Biological process	• ovarian follicle development • translation • translational initiation • response to heat • response to glucose • gene expression • astrocyte development • oligodendrocyte development • negative regulation of translational initiation in response to stress • response to endoplasmic reticulum stress • cellular response to drug • myelination • response to peptide hormone • positive regulation of GTPase activity • cellular protein metabolic process • positive regulation of translational initiation • astrocyte differentiation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
183.85 – 184.4 Mb

Chr 16:
20.5 – 20.51 Mb

PubMed search

Translation initiation factor eIF-2B subunit epsilon is a protein that in humans is encoded by the EIF2B5 gene.^[1]^[2]

Interactions

EIF2B5 has been shown to interact with EIF2B2^[3] and EIF2B1.^[3]^[4]

References

↑ Asuru AI, Mellor H, Thomas NS, Yu L, Chen JJ, Crosby JS, Hartson SD, Kimball SR, Jefferson LS, Matts RL (August 1996). "Cloning and characterization of cDNAs encoding the epsilon-subunit of eukaryotic initiation factor-2B from rabbit and human". Biochim Biophys Acta 1307 (3): 309–17. doi:10.1016/0167-4781(96)00054-1. PMID 8688466.
↑ "Entrez Gene: EIF2B5 eukaryotic translation initiation factor 2B, subunit 5 epsilon, 82kDa".
↑ 3.0 3.1 Anthony, T G; Fabian J R; Kimball S R; Jefferson L S (June 2000). "Identification of domains within the epsilon-subunit of the translation initiation factor eIF2B that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation". Biochim. Biophys. Acta (NETHERLANDS) 1492 (1): 56–62. doi:10.1016/S0167-4781(00)00062-2. ISSN 0006-3002. PMID 10858531.
↑ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Leegwater PA, Pronk JC, van der Knaap MS (2003). "Leukoencephalopathy with vanishing white matter: from magnetic resonance imaging pattern to five genes.". J. Child Neurol. 18 (9): 639–45. doi:10.1177/08830738030180091101. PMID 14572143.
Chaudhri MA, Crawford AC (1991). "Carbon determination in human teeth by activation with He-3 ions.". Biological trace element research. 26-27: 521–7. doi:10.1007/BF02992708. PMID 1704758.
Welsh GI, Miyamoto S, Price NT et al. (1996). "T-cell activation leads to rapid stimulation of translation initiation factor eIF2B and inactivation of glycogen synthase kinase-3.". J. Biol. Chem. 271 (19): 11410–3. doi:10.1074/jbc.271.19.11410. PMID 8626696.
Kimball SR, Heinzinger NK, Horetsky RL, Jefferson LS (1998). "Identification of interprotein interactions between the subunits of eukaryotic initiation factors eIF2 and eIF2B.". J. Biol. Chem. 273 (5): 3039–44. doi:10.1074/jbc.273.5.3039. PMID 9446619.
Welsh GI, Miller CM, Loughlin AJ et al. (1998). "Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin.". FEBS Lett. 421 (2): 125–30. doi:10.1016/S0014-5793(97)01548-2. PMID 9468292.
Leegwater PA, Könst AA, Kuyt B et al. (1999). "The gene for leukoencephalopathy with vanishing white matter is located on chromosome 3q27.". Am. J. Hum. Genet. 65 (3): 728–34. doi:10.1086/302548. PMC 1377979. PMID 10441579.
Gomez E, Pavitt GD (2000). "Identification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2Bepsilon) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation.". Mol. Cell. Biol. 20 (11): 3965–76. doi:10.1128/MCB.20.11.3965-3976.2000. PMC 85753. PMID 10805739.
Anthony TG, Fabian JR, Kimball SR, Jefferson LS (2000). "Identification of domains within the epsilon-subunit of the translation initiation factor eIF2B that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation.". Biochim. Biophys. Acta 1492 (1): 56–62. doi:10.1016/S0167-4781(00)00062-2. PMID 10858531.
Williams DD, Price NT, Loughlin AJ, Proud CG (2001). "Characterization of the mammalian initiation factor eIF2B complex as a GDP dissociation stimulator protein.". J. Biol. Chem. 276 (27): 24697–703. doi:10.1074/jbc.M011788200. PMID 11323413.
Wang X, Paulin FE, Campbell LE et al. (2001). "Eukaryotic initiation factor 2B: identification of multiple phosphorylation sites in the epsilon-subunit and their functions in vivo.". EMBO J. 20 (16): 4349–59. doi:10.1093/emboj/20.16.4349. PMC 125262. PMID 11500362.
Leegwater PA, Vermeulen G, Könst AA et al. (2001). "Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter.". Nat. Genet. 29 (4): 383–8. doi:10.1038/ng764. PMID 11704758.
Wang X, Janmaat M, Beugnet A et al. (2002). "Evidence that the dephosphorylation of Ser(535) in the epsilon-subunit of eukaryotic initiation factor (eIF) 2B is insufficient for the activation of eIF2B by insulin.". Biochem. J. 367 (Pt 2): 475–81. doi:10.1042/BJ20020677. PMC 1222905. PMID 12133000.
Fogli A, Wong K, Eymard-Pierre E et al. (2002). "Cree leukoencephalopathy and CACH/VWM disease are allelic at the EIF2B5 locus.". Ann. Neurol. 52 (4): 506–10. doi:10.1002/ana.10339. PMID 12325082.
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.
Fogli A, Dionisi-Vici C, Deodato F et al. (2003). "A severe variant of childhood ataxia with central hypomyelination/vanishing white matter leukoencephalopathy related to EIF21B5 mutation.". Neurology 59 (12): 1966–8. doi:10.1212/01.wnl.0000041666.76863.47. PMID 12499492.
Fogli A, Rodriguez D, Eymard-Pierre E et al. (2003). "Ovarian failure related to eukaryotic initiation factor 2B mutations.". Am. J. Hum. Genet. 72 (6): 1544–50. doi:10.1086/375404. PMC 1180314. PMID 12707859.
van der Knaap MS, van Berkel CG, Herms J et al. (2004). "eIF2B-related disorders: antenatal onset and involvement of multiple organs.". Am. J. Hum. Genet. 73 (5): 1199–207. doi:10.1086/379524. PMC 1180499. PMID 14566705.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.

Protein biosynthesis: translation (prokaryotic, eukaryotic)

Ribosomal proteins

Initiation factor

Prokaryotic

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

Other

Other concepts

Index of genetics

Description	Gene expression DNA replication cycle recombination repair binding proteins Transcription factors regulators nucleic acids RNA RNA binding proteins ribonucleoproteins repeated sequence modification Translation ribosome modification nexins Proteins domains Structure primary secondary tertiary quaternary

Disease	Replication and repair Transcription factor Transcription Translation

EIF2B5

Interactions

References

Further reading