EIF2B4

Protein-coding gene in the species Homo sapiens

EIF2B4

Identifiers

Aliases

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

External IDs

OMIM: 606687; MGI: 95300; HomoloGene: 5976; GeneCards: EIF2B4; OMA:EIF2B4 - orthologs

Gene location (Human)

Chr.	Chromosome 2 (human)^[1]

Band	2p23.3	Start	27,364,352 bp^[1]
Band	2p23.3	End	27,370,338 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5\|5 B1	Start	31,344,902 bp^[2]
Band	5\|5 B1	End	31,350,774 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

body of pancreas

left testis

right testis

muscle layer of sigmoid colon

sural nerve

gingival epithelium

anterior pituitary

skin of abdomen

mucosa of transverse colon

skin of leg

Top expressed in

primitive streak

temporal muscle

primary oocyte

digastric muscle

hair follicle

sternocleidomastoid muscle

triceps brachii muscle

muscle of thigh

vastus lateralis muscle

motor neuron

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	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	response to peptide hormone response to heat response to glucose cell metabolism ovarian follicle development myelination oligodendrocyte development regulation of translation translational initiation protein biosynthesis T cell receptor signaling pathway
Sources:Amigo / QuickGO

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 NP_001305894 NP_001305895 NP_001305896 NP_001305897
NP_001305898 NP_056451 NP_751945 NP_001305896.1


NP_001120827 NP_001120828 NP_034252

Location (UCSC)

Chr 2: 27.36 – 27.37 Mb

Chr 5: 31.34 – 31.35 Mb

PubMed search

^[3]

^[4]

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.^[5]^[6]^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000115211 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000029145 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. doi:10.1042/bj3180637. 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. doi:10.1016/S0021-9258(18)43844-6. 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. doi:10.1128/MCB.16.11.6603. 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. Bibcode:2000PNAS...97.9543H. 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. S2CID 1849575.
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. Bibcode:2002PNAS...9916899M. 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. S2CID 13129517.
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. doi:10.1093/jnen/63.6.618. 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. 4 (1): 8. doi:10.1186/1472-6874-4-8. PMC 529454. PMID 15507143.

Protein biosynthesis: translation (bacterial, archaeal, eukaryotic)

Proteins

Initiation factor

Bacterial

Mitochondrial

MTIF1
MTIF2
MTIF3

Archaeal

aIF1
aIF2
aIF5
aIF6

Eukaryotic

eIF1	eIF1 B SUI1 family eIF1A Y
eIF2	α kinase β γ eIF2A eIF2B 1 2 3 4 5 eIF2D
eIF3	A B C D E F G H I J K L M
eIF4	A 1 2 3 E1 2 3 G 1 2 3 B H
eIF5	EIF5 EIF5A 2 5B
eIF6	EIF6

Elongation factor

Bacterial/Mitochondrial	EF-Tu EF-Ts EF-G EF-4 EF-P TSFM GFM1 GFM2
Archaeal/Eukaryotic	a/eEF-1 A1 2 3 B P1 P2 P3 D E G a/eEF-2

Release factor

Class 1
- eRF1
Class 2/RF3
- GSPT1
- GSPT2

Ribosomal Proteins

Cytoplasmic

60S subunit	RPL3 RPL4 RPL5 RPL6 RPL7 RPL7A RPL8 RPL9 RPL10 RPL10A RPL10-like RPL11 RPL12 RPL13 RPL13A RPL14 RPL15 RPL17 RPL18 RPL18A RPL19 RPL21 RPL22 RPL23 RPL23A RPL24 RPL26 RPL27 RPL27A RPL28 RPL29 RPL30 RPL31 RPL32 RPL34 RPL35 RPL35A RPL36 RPL36A RPL37 RPL37A RPL38 RPL39 RPL40 RPL41 RPLP0 RPLP1 RPLP2 RRP15-like RSL24D1
40S subunit	RPSA RPS2 RPS3 RPS3A RPS4 (RPS4X, RPS4Y1, RPS4Y2) RPS5 RPS6 RPS7 RPS8 RPS9 RPS10 RPS11 RPS12 RPS13 RPS14 RPS15 RPS15A RPS16 RPS17 RPS18 RPS19 RPS20 RPS21 RPS23 RPS24 RPS25 RPS26 RPS27 RPS27A RPS28 RPS29 RPS30 RACK1

Mitochondrial

39S subunit	MRPL1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42
28S subunit	MRPS1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35