EIF2B4

Identifiers

EIF2B4, EIF-2B, EIF2B, EIF2Bdelta, eukaryotic translation initiation factor 2B subunit delta

External IDs

MGI: 95300 HomoloGene: 5976 GeneCards: EIF2B4

Gene ontology
Molecular function	• S-methyl-5-thioribose-1-phosphate isomerase activity • guanyl-nucleotide exchange factor activity • protein binding • translation initiation factor binding • translation initiation factor activity
Cellular component	• cytoplasm • cytosol • eukaryotic translation initiation factor 2B complex
Biological process	• L-methionine biosynthetic process from methylthioadenosine • negative regulation of translational initiation in response to stress • negative regulation of translational initiation • response to peptide hormone • response to heat • response to glucose • cellular response to stimulus • cellular metabolic process • ovarian follicle development • myelination • oligodendrocyte development • regulation of translation • translational initiation • positive regulation of GTPase activity • translation
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


8890


13667

Ensembl


ENSG00000115211


ENSMUSG00000029145

UniProt


Q9UI10


Q61749

RefSeq (mRNA)

NM_001034116 NM_015636 NM_172195 NM_001318965 NM_001318966
NM_001318967 NM_001318968 NM_001318969


NM_001127355 NM_001127356 NM_010122

RefSeq (protein)

NP_001029288.1 NP_056451.3 NP_751945.2 NP_001305894.1 NP_001305895.1
NP_001305896.1 NP_001305897.1 NP_001305896.1


NP_001120827.1 NP_001120828.1 NP_034252.2

Location (UCSC)

Chr 2: 27.36 – 27.37 Mb

Chr 5: 31.19 – 31.19 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Translation initiation factor eIF-2B subunit delta is a protein that in humans is encoded by the EIF2B4 gene.^[3]^[4]^[5]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Price NT, Mellor H, Craddock BL, Flowers KM, Kimball SR, Wilmer T, Jefferson LS, Proud CG (Nov 1996). "eIF2B, the guanine nucleotide-exchange factor for eukaryotic initiation factor 2. Sequence conservation between the alpha, beta and delta subunits of eIF2B from mammals and yeast". Biochem J. 318 (2): 637–43. PMC 1217679. PMID 8929216.
↑ Henderson RA, Krissansen GW, Yong RY, Leung E, Watson JD, Dholakia JN (Dec 1994). "The delta-subunit of murine guanine nucleotide exchange factor eIF-2B. Characterization of cDNAs predicts isoforms differing at the amino-terminal end". J Biol Chem. 269 (48): 30517–23. PMID 7982969.
↑ "Entrez Gene: EIF2B4 eukaryotic translation initiation factor 2B, subunit 4 delta, 67kDa".

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.
Yang W, Hinnebusch AG (1996). "Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2.". Mol. Cell. Biol. 16 (11): 6603–16. PMC 231662. PMID 8887689.
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.
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.
Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
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.
van der Knaap MS, Leegwater PA, Könst AA, et al. (2002). "Mutations in each of the five subunits of translation initiation factor eIF2B can cause leukoencephalopathy with vanishing white matter.". Ann. Neurol. 51 (2): 264–70. doi:10.1002/ana.10112. PMID 11835386.
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.
Kobayashi H, Børsheim E, Anthony TG, et al. (2003). "Reduced amino acid availability inhibits muscle protein synthesis and decreases activity of initiation factor eIF2B.". Am. J. Physiol. Endocrinol. Metab. 284 (3): E488–98. doi:10.1152/ajpendo.00094.2002. PMID 12556349.
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.
Fogli A, Schiffmann R, Hugendubler L, et al. (2005). "Decreased guanine nucleotide exchange factor activity in eIF2B-mutated patients.". Eur. J. Hum. Genet. 12 (7): 561–6. doi:10.1038/sj.ejhg.5201189. PMID 15054402.
Li W, Wang X, Van Der Knaap MS, Proud CG (2004). "Mutations linked to leukoencephalopathy with vanishing white matter impair the function of the eukaryotic initiation factor 2B complex in diverse ways.". Mol. Cell. Biol. 24 (8): 3295–306. doi:10.1128/MCB.24.8.3295-3306.2004. PMC 381664. PMID 15060152.
Van Haren K, van der Voorn JP, Peterson DR, et al. (2004). "The life and death of oligodendrocytes in vanishing white matter disease.". J. Neuropathol. Exp. Neurol. 63 (6): 618–30. PMID 15217090.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Fogli A, Gauthier-Barichard F, Schiffmann R, et al. (2004). "Screening for known mutations in EIF2B genes in a large panel of patients with premature ovarian failure.". BMC women's health [electronic resource]. 4 (1): 8. doi:10.1186/1472-6874-4-8. PMC 529454. PMID 15507143.

Protein biosynthesis: translation (prokaryotic, eukaryotic)

Proteins

Initiation factor

Prokaryotic

Archaeal

aIF1
aIF2
aIF5
aIF6

Eukaryotic

eIF1	eIF1 EIF1AX AY 1B

eIF2	EIF2S1 EIF2S2 EIF2S3 EIF2B1 EIF2B2 EIF2B3 EIF2B4 EIF2B5 EIF-2 kinase eIF2A eIF2D

eIF3	EIF3A B C D E F G H I J K L M

eIF4	EIF4A2 A3 B E1 E2 E3 G1 G2 G3 H

eIF5	EIF5 EIF5A A2 5B

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

Ribosomal Proteins

Other concepts

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EIF2B4

References

Further reading