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EIF2B1

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From Wikipedia, the free encyclopedia

Protein-coding gene in humans

EIF2B1

Available structures

PDB

Ortholog search:PDBe RCSB

List of PDB id codes
3ECS

Identifiers

Aliases

EIF2B1, EIF2B, EIF2BA, eukaryotic translation initiation factor 2B subunit alpha, EIF2Balpha

External IDs

OMIM:606686;MGI:2384802;HomoloGene:1080;GeneCards:EIF2B1;OMA:EIF2B1 - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12q24.31	Start	123,620,406bp^[1]
Band	12q24.31	End	123,633,766bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5 F\|5 63.67 cM	Start	124,708,276bp^[2]
Band	5 F\|5 63.67 cM	End	124,717,194bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

oocyte

secondary oocyte

monocyte

Achilles tendon

body of uterus

skin of hip

skin of thigh

right coronary artery

granulocyte

tibial arteries

Top expressed in

zygote

secondary oocyte

morula

morula

primary oocyte

yolk sac

primitive streak

embryo

epiblast

blastocyst

More reference expression data

BioGPS


More reference expression data

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

Orthologs

Species

Human

Mouse

Entrez


1967


209354

Ensembl


ENSG00000111361


ENSMUSG00000029388

UniProt


Q14232


Q99LC8

RefSeq (mRNA)


NM_001414


NM_145371

RefSeq (protein)


NP_001405


NP_663346

Location (UCSC)

Chr 12: 123.62 – 123.63 Mb

Chr 5: 124.71 – 124.72 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Translation initiation factor eIF-2B subunit alpha is aprotein that in humans is encoded by theEIF2B1gene.^[5]

Interactions

[edit]

EIF2B1 has been shown tointeract withEIF2B5.^[6]^[7]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000111361 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000029388 –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.
^"Entrez Gene: EIF2B1 eukaryotic translation initiation factor 2B, subunit 1 alpha, 26kDa".
^Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007)."Large-scale mapping of human protein–protein interactions by mass spectrometry".Mol. Syst. Biol.3 (1): 89.doi:10.1038/msb4100134.PMC 1847948.PMID 17353931.
^Anthony TG, Fabian JR, Kimball SR, Jefferson LS (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.1492 (1):56–62.doi:10.1016/S0167-4781(00)00062-2.PMID 10858531.

Hershey JW (1991). "Translational control in mammalian cells".Annu. Rev. Biochem.60:717–55.doi:10.1146/annurev.bi.60.070191.003441.PMID 1883206.
Flowers KM, Mellor H, Kimball SR, Jefferson LS (1996). "Structure and sequence of the gene encoding the alpha-subunit of rat translation initiation factor-2B".Biochim. Biophys. Acta.1264 (2):163–7.doi:10.1016/0167-4781(95)00160-i.PMID 7495858.
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):11410–3.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.
Klein U, Ramirez MT, Kobilka BK, von Zastrow M (1997)."A novel interaction between adrenergic receptors and the alpha-subunit of eukaryotic initiation factor 2B".J. Biol. Chem.272 (31):19099–102.doi:10.1074/jbc.272.31.19099.PMID 9235896.
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 ɛ Subunit of Eukaryotic Translation Initiation Factor 2B (eIF2Bɛ) 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.
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, Visser A, Naidu S, Oudejans CB, Schutgens RB, Pronk JC (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.
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):1544–50.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):1199–207.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):2352–63.doi:10.1128/MCB.24.6.2352-2363.2004.PMC 355856.PMID 14993275.
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, van der Knaap MS, Powers JM (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.
Yin X, Warner DR, Roberts EA, Pisano MM, Greene RM (2005). "Identification of novel CBP interacting proteins in embryonic orofacial tissue".Biochem. Biophys. Res. Commun.329 (3):1010–7.doi:10.1016/j.bbrc.2005.02.075.PMID 15752756.

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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