EIF2B2

Identifiers

EIF2B2, EIF-2Bbeta, EIF2B, eukaryotic translation initiation factor 2B subunit beta, EIF2Bbeta

External IDs

OMIM: 606454 MGI: 2145118 HomoloGene: 6507 GeneCards: EIF2B2

Gene location (Human)

Chr.	Chromosome 14 (human)^[1]

Band	14q24.3	Start	75,002,921 bp^[1]
Band	14q24.3	End	75,012,366 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 12 (mouse)^[2]

Band	12\|12 D1	Start	85,266,255 bp^[2]
Band	12\|12 D1	End	85,273,402 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

left lobe of thyroid gland

right lobe of thyroid gland

gastrocnemius muscle

left adrenal gland

popliteal artery

right coronary artery

left coronary artery

anterior pituitary

ascending aorta

right lung

Top expressed in

condyle

fossa

renal corpuscle

internal carotid artery

external carotid artery

endocardial cushion

saccule

yolk sac

substantia nigra

medullary collecting duct

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	translation initiation factor activity guanyl-nucleotide exchange factor activity GTP binding protein binding ATP binding
Cellular component	cytoplasm cytosol eukaryotic translation initiation factor 2B complex
Biological process	response to peptide hormone response to heat response to glucose central nervous system development cell metabolism ovarian follicle development myelination oligodendrocyte development regulation of translational initiation protein biosynthesis translational initiation T cell receptor signaling pathway
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


8892


217715

Ensembl


ENSG00000119718


ENSMUSG00000004788

UniProt


P49770


Q99LD9

RefSeq (mRNA)


NM_014239


NM_145445

RefSeq (protein)


NP_055054


NP_663420

Location (UCSC)

Chr 14: 75 – 75.01 Mb

Chr 12: 85.27 – 85.27 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Translation initiation factor eIF-2B subunit beta is a protein that in humans is encoded by the EIF2B2 gene.^[5]^[6]

Function

Eukaryotic initiation factor-2B (EIF2B) is a GTP exchange protein essential for protein synthesis. It consists of alpha (EIF2B1; MIM 606686), beta (EIF2B2), gamma (EIF2B3; MIM 606273), delta (EIF2B4; MIM 606687), and epsilon (EIF2B5; MIM 603945) subunits. EIF2B activates its EIF2 (see MIM 603907) substrate by exchanging EIF2-bound GDP for GTP.^[6]

Interactions

EIF2B2 has been shown to interact with EIF2B5^[7] and NCK1.^[8]

References

Labauge P, Fogli A, Niel F, Rodriguez D, Boespflug-Tanguy O (2007). "[CACH/VWM syndrome and leucodystrophies related to EIF2B mutations]". Rev. Neurol. (Paris). 163 (8–9): 793–9. doi:10.1016/s0035-3787(07)91461-7. PMID 17878805.
Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, Tsuda T, Mar L, Foncin JF, Bruni AC, Montesi MP, Sorbi S, Rainero I, Pinessi L, Nee L, Chumakov I, Pollen D, Brookes A, Sanseau P, Polinsky RJ, Wasco W, Da Silva HA, Haines JL, Perkicak-Vance MA, Tanzi RE, Roses AD, Fraser PE, Rommens JM, St George-Hyslop PH (1995). "Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease". Nature. 375 (6534): 754–760. Bibcode:1995Natur.375..754S. doi:10.1038/375754a0. PMID 7596406. S2CID 4308372.
Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–113. doi:10.1006/abio.1996.0138. PMID 8619474.
Welsh GI, Miyamoto S, Price NT, Safer B, Proud CG (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): 11410–11413. doi:10.1074/jbc.271.19.11410. PMID 8626696.
Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
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): 3039–3044. 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): 3965–3976. 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): 24697–24703. doi:10.1074/jbc.M011788200. PMID 11323413.
Leegwater PA, Vermeulen G, Könst AA, Naidu S, Mulders J, Visser A, Kersbergen P, Mobach D, Fonds D, van Berkel CG, Lemmers RJ, Frants RR, Oudejans CB, Schutgens RB, Pronk JC, van der Knaap MS (2001). "Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter". Nat. Genet. 29 (4): 383–388. doi:10.1038/ng764. PMID 11704758. S2CID 20313523.
Kebache S, Zuo D, Chevet E, Larose L (2002). "Modulation of protein translation by Nck-1". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5406–5411. Bibcode:2002PNAS...99.5406K. doi:10.1073/pnas.082483399. PMC 122782. PMID 11959995.
Fogli A, Dionisi-Vici C, Deodato F, Bartuli A, Boespflug-Tanguy O, Bertini E (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.
Fogli A, Rodriguez D, Eymard-Pierre E, Bouhour F, Labauge P, Meaney BF, Zeesman S, Kaneski CR, Schiffmann R, Boespflug-Tanguy O (2003). "Ovarian failure related to eukaryotic initiation factor 2B mutations". Am. J. Hum. Genet. 72 (6): 1544–1550. doi:10.1086/375404. PMC 1180314. PMID 12707859.
van der Knaap MS, van Berkel CG, Herms J, van Coster R, Baethmann M, Naidu S, Boltshauser E, Willemsen MA, Plecko B, Hoffmann GF, Proud CG, Scheper GC, Pronk JC (2004). "eIF2B-related disorders: antenatal onset and involvement of multiple organs". Am. J. Hum. Genet. 73 (5): 1199–1207. doi:10.1086/379524. PMC 1180499. PMID 14566705.
Richardson JP, Mohammad SS, Pavitt GD (2004). "Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity". Mol. Cell. Biol. 24 (6): 2352–2363. doi:10.1128/MCB.24.6.2352-2363.2004. PMC 355856. PMID 14993275.
Fogli A, Schiffmann R, Hugendubler L, Combes P, Bertini E, Rodriguez D, Kimball SR, Boespflug-Tanguy O (2005). "Decreased guanine nucleotide exchange factor activity in eIF2B-mutated patients". Eur. J. Hum. Genet. 12 (7): 561–566. 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): 3295–3306. doi:10.1128/MCB.24.8.3295-3306.2004. PMC 381664. PMID 15060152.

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

Other concepts

Function

Interactions

References

Further reading