EIF2B2

From Wikipedia, the free encyclopedia

Eukaryotic translation initiation factor 2B, subunit 2 beta, 39kDa

Identifiers

EIF2B2; EIF-2Bbeta; EIF2B

External IDs

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

Gene Ontology
Molecular function	• translation initiation factor activity • guanyl-nucleotide exchange factor activity • protein binding • ATP binding • GTP binding • S-methyl-5-thioribose-1-phosphate isomerase activity
Cellular component	• cytoplasm • cytosol • eukaryotic translation initiation factor 2B complex
Biological process	• ovarian follicle development • translation • translational initiation • regulation of translational initiation • central nervous system development • response to heat • response to glucose stimulus • gene expression • oligodendrocyte development • L-methionine salvage from methylthioadenosine • myelination • response to peptide hormone stimulus • cellular protein metabolic process • cellular response to stimulus
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
75.47 – 75.48 Mb

Chr 12:
85.22 – 85.23 Mb

PubMed search

Translation initiation factor eIF-2B subunit beta is a protein that in humans is encoded by the EIF2B2 gene.^[1]^[2]

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.[supplied by OMIM]^[2]

Interactions

EIF2B2 has been shown to interact with EIF2B5^[3] and NCK1.^[4]

References

↑ Yang W, Hinnebusch AG (December 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.
↑ 2.0 2.1 "Entrez Gene: EIF2B2 eukaryotic translation initiation factor 2B, subunit 2 beta, 39kDa".
↑ 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. Cite uses deprecated parameters (help)
↑ Kebache, Sem; Zuo Dongmei, Chevet Eric, Larose Louise (April 2002). "Modulation of protein translation by Nck-1". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (8): 5406–5411. doi:10.1073/pnas.082483399. ISSN 0027-8424. PMC 122782. PMID 11959995. Cite uses deprecated parameters (help)

Labauge P, Fogli A, Niel F et al. (2007). "[CACH/VWM syndrome and leucodystrophies related to EIF2B mutations]". Rev. Neurol. (Paris) 163 (8–9): 793–9. PMID 17878805.
Sherrington R, Rogaev EI, Liang Y et al. (1995). "Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease". Nature 375 (6534): 754–760. doi:10.1038/375754a0. PMID 7596406.
Andersson B, Wentland MA, Ricafrente JY et al. (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 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): 11410–11413. doi:10.1074/jbc.271.19.11410. PMID 8626696.
Yu W, Andersson B, Worley KC et al. (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 et al. (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.
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. doi:10.1073/pnas.082483399. PMC 122782. PMID 11959995.
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): 16899–16903. 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. PMID 12499492.
Heilig R, Eckenberg R, Petit JL et al. (2003). "The DNA sequence and analysis of human chromosome 14". Nature 421 (6923): 601–607. doi:10.1038/nature01348. PMID 12508121.
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): 1544–1550. doi:10.1086/375404. PMC 1180314. PMID 12707859.
van der Knaap MS (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 et al. (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 (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

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°)

This article is issued from Wikipedia. The text is available under the Creative Commons Attribution/Share Alike; additional terms may apply for the media files.

EIF2B2

Interactions

References

Further reading