EIF2B5

Last updated
EIF2B5
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases EIF2B5 , CACH, CLE, EIF-2B, EIF2Bepsilon, LVWM, eukaryotic translation initiation factor 2B subunit epsilon
External IDs OMIM: 603945 MGI: 2446176 HomoloGene: 2903 GeneCards: EIF2B5
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003907

NM_172265

RefSeq (protein)

NP_003898

NP_758469

Location (UCSC) Chr 3: 184.14 – 184.15 Mb Chr 16: 20.32 – 20.33 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Translation initiation factor eIF-2B subunit epsilon is a protein that in humans is encoded by the EIF2B5 gene. [5] [6]

Contents

Interactions

EIF2B5 has been shown to interact with EIF2B2 [7] and EIF2B1. [7] [8]

Related Research Articles

Eukaryotic initiation factors (eIFs) are proteins or protein complexes involved in the initiation phase of eukaryotic translation. These proteins help stabilize the formation of ribosomal preinitiation complexes around the start codon and are an important input for post-transcription gene regulation. Several initiation factors form a complex with the small 40S ribosomal subunit and Met-tRNAiMet called the 43S preinitiation complex. Additional factors of the eIF4F complex recruit the 43S PIC to the five-prime cap structure of the mRNA, from which the 43S particle scans 5'-->3' along the mRNA to reach an AUG start codon. Recognition of the start codon by the Met-tRNAiMet promotes gated phosphate and eIF1 release to form the 48S preinitiation complex, followed by large 60S ribosomal subunit recruitment to form the 80S ribosome. There exist many more eukaryotic initiation factors than prokaryotic initiation factors, reflecting the greater biological complexity of eukaryotic translation. There are at least twelve eukaryotic initiation factors, composed of many more polypeptides, and these are described below.

<span class="mw-page-title-main">Leukoencephalopathy with vanishing white matter</span> Neurological disease

Leukoencephalopathy with vanishing white matter is an autosomal recessive neurological disease. The cause of the disease are mutations in any of the 5 genes encoding subunits of the translation initiation factor eIF2B: EIF2B1, EIF2B2, EIF2B3, EIF2B4, or EIF2B5. The disease belongs to a family of conditions called the Leukodystrophies.

<span class="mw-page-title-main">Eukaryotic translation initiation factor 4 gamma 1</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 4 gamma 1 is a protein that in humans is encoded by the EIF4G1 gene.

<span class="mw-page-title-main">EIF2S1</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 2 subunit 1 (eIF2α) is a protein that in humans is encoded by the EIF2S1 gene.

<span class="mw-page-title-main">EIF2B2</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">EIF2AK3</span> Human protein and coding gene

Eukaryotic translation initiation factor 2-alpha kinase 3, also known as protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK), is an enzyme that in humans is encoded by the EIF2AK3 gene.

<span class="mw-page-title-main">EIF2S2</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 2 subunit 2 (eIF2β) is a protein that in humans is encoded by the EIF2S2 gene.

<span class="mw-page-title-main">EIF2B1</span> Protein-coding gene in humans

Translation initiation factor eIF-2B subunit alpha is a protein that in humans is encoded by the EIF2B1 gene.

<span class="mw-page-title-main">EIF2B4</span> Protein-coding gene in the species Homo sapiens

Translation initiation factor eIF-2B subunit delta is a protein that in humans is encoded by the EIF2B4 gene.

<span class="mw-page-title-main">EIF2B3</span> Protein-coding gene in the species Homo sapiens

Translation initiation factor eIF-2B subunit gamma is a protein that in humans is encoded by the EIF2B3 gene.

<span class="mw-page-title-main">EIF2S3</span> Protein-coding gene in humans

Eukaryotic translation initiation factor 2 subunit 3 (eIF2γ) is a protein that in humans is encoded by the EIF2S3 gene.

<span class="mw-page-title-main">EIF3H</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 3 subunit H (eIF3h) is a protein that in humans is encoded by the EIF3H gene.

<span class="mw-page-title-main">EIF5</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 5 is a protein that in humans is encoded by the EIF5 gene.

<span class="mw-page-title-main">EIF3EIP</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 3 subunit L (eIF3l), less commonly known as EIF3EIP, is a protein that in humans is encoded by the EIF3L gene.

<span class="mw-page-title-main">EIF3J</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 3 subunit J (eIF3j) is a protein that in humans is encoded by the EIF3J gene.

<span class="mw-page-title-main">EIF5B</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 5B is a protein that in humans is encoded by the EIF5B gene.

<span class="mw-page-title-main">EIF1</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 1 (eIF1) is a protein that in humans is encoded by the EIF1 gene. It is related to yeast SUI1.

eIF2B is a protein complex found in eukaryotes. It is the guanine nucleotide exchange factor for the eukaryotic initiation factor 2 and therefore converts the inactive eIF2-GDP to the active eIF2-GTP. This activation is hindered by phosphorylation of the alpha subunit of eIF2, which leads to a stable eIF2α-P-GDP-eIF2B complex and therefore inhibits translation initiation.

Eukaryotic Initiation Factor 2 (eIF2) is an eukaryotic initiation factor. It is required for most forms of eukaryotic translation initiation. eIF2 mediates the binding of tRNAiMet to the ribosome in a GTP-dependent manner. eIF2 is a heterotrimer consisting of an alpha, a beta, and a gamma subunit.

<span class="mw-page-title-main">EIF-W2 protein domain</span>

In molecular biology, the protein domain eIF4-gamma/eIF5/eIF2-epsilon is a family of evolutionarily related proteins. This domain is found at the C-terminus of several translation Initiation factors. It was first detected at the very C-termini of the yeast protein GCD6, eIF-2B epsilon, and two other eukaryotic translation initiation factors, eIF-4 gamma and eIF-5 and it may be involved in the interaction of eIF-2B, eIF-4 gamma, and eIF-5 with eIF-2.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000145191 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000003235 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Asuru AI, Mellor H, Thomas NS, Yu L, Chen JJ, Crosby JS, Hartson SD, Kimball SR, Jefferson LS, Matts RL (Jul 1996). "Cloning and characterization of cDNAs encoding the epsilon-subunit of eukaryotic initiation factor-2B from rabbit and human". Biochimica et Biophysica Acta. 1307 (3): 309–17. doi:10.1016/0167-4781(96)00054-1. PMID   8688466.
  6. "Entrez Gene: EIF2B5 eukaryotic translation initiation factor 2B, subunit 5 epsilon, 82kDa".
  7. 1 2 Anthony TG, Fabian JR, Kimball SR, Jefferson LS (Jun 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". Biochimica et Biophysica Acta. 1492 (1): 56–62. doi:10.1016/S0167-4781(00)00062-2. PMID   10858531.
  8. 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". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.

Further reading