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EIF2B3

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

EIF2B3

Identifiers

Aliases

EIF2B3, EIF-2B, EIF2Bgamma, eukaryotic translation initiation factor 2B subunit gamma

External IDs

OMIM:606273;MGI:1313286;HomoloGene:7005;GeneCards:EIF2B3;OMA:EIF2B3 - orthologs

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1p34.1	Start	44,850,522bp^[1]
Band	1p34.1	End	44,986,722bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4\|4 D1	Start	116,876,599bp^[2]
Band	4\|4 D1	End	116,944,503bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

triceps brachii muscle

glutes

gastrocnemius muscle

muscle of thigh

Skeletal muscle tissue of biceps brachii

deltoid muscle

vastus lateralis muscle

islet of Langerhans

parotid gland

Skeletal muscle tissue of rectus abdominis

Top expressed in

morula

superior cervical ganglion

embryo

embryo

epiblast

autopod region

hand

foot

yolk sac

blastocyst

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	nucleotidyltransferase activity translation factor activity, RNA binding protein binding translation initiation factor activity guanyl-nucleotide exchange factor activity
Cellular component	cytoplasm cytosol eukaryotic translation initiation factor 2B complex
Biological process	oligodendrocyte development response to peptide hormone response to heat response to glucose biosynthesis hippocampus development protein biosynthesis translational initiation T cell receptor signaling pathway
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


8891


108067

Ensembl


ENSG00000070785


ENSMUSG00000028683

UniProt


Q9NR50


n/a

RefSeq (mRNA)


NM_001166588 NM_001261418 NM_020365


NM_001111277 NM_175135 NM_001355225

RefSeq (protein)


NP_001160060 NP_001248347 NP_065098


n/a

Location (UCSC)

Chr 1: 44.85 – 44.99 Mb

Chr 4: 116.88 – 116.94 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Translation initiation factor eIF-2B subunit gamma is aprotein that in humans is encoded by theEIF2B3gene.^[5]^[6]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000070785 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000028683 –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.
^Kruger M, Beger C, Li QX, Welch PJ, Tritz R, Leavitt M, Barber JR, Wong-Staal F (Aug 2000)."Identification of eIF2Bgamma and eIF2gamma as cofactors of hepatitis C virus internal ribosome entry site-mediated translation using a functional genomics approach".Proc Natl Acad Sci U S A.97 (15):8566–71.Bibcode:2000PNAS...97.8566K.doi:10.1073/pnas.97.15.8566.PMC 26988.PMID 10900014.
^"Entrez Gene: EIF2B3 eukaryotic translation initiation factor 2B, subunit 3 gamma, 58kDa".

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.
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.
Hartley JL, Temple GF, Brasch MA (2001)."DNA cloning using in vitro site-specific recombination".Genome Res.10 (11):1788–95.doi:10.1101/gr.143000.PMC 310948.PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, et al. (2001)."Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs".Genome Res.11 (3):422–35.doi:10.1101/gr.GR1547R.PMC 311072.PMID 11230166.
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.
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.
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.
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.
Wiemann S, Arlt D, Huber W, et al. (2004)."From ORFeome to biology: a functional genomics pipeline".Genome Res.14 (10B):2136–44.doi:10.1101/gr.2576704.PMC 528930.PMID 15489336.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network".Nature.437 (7062):1173–8.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.
Suragani RN, Kamindla R, Ehtesham NZ, Ramaiah KV (2006). "Interaction of recombinant human eIF2 subunits with eIF2B and eIF2alpha kinases".Biochem. Biophys. Res. Commun.338 (4):1766–72.doi:10.1016/j.bbrc.2005.10.150.PMID 16288713.
Mikami S, Masutani M, Sonenberg N, et al. (2006)."An efficient mammalian cell-free translation system supplemented with translation factors".Protein Expr. Purif.46 (2):348–57.doi:10.1016/j.pep.2005.09.021.PMID 16289705.

Protein biosynthesis:translation (bacterial,archaeal,eukaryotic)

Proteins

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

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