EIF2AK3

From Wikipedia, the free encyclopedia

Eukaryotic translation initiation factor 2-alpha kinase 3

Identifiers

EIF2AK3; WRS; DKFZp781H1925; PEK; PERK

External IDs

OMIM: 604032 MGI: 1341830 HomoloGene: 3557

Gene ontology
Molecular Function:	• nucleotide binding • eukaryotic translation initiation factor 2alpha kinase activity • ATP binding • transferase activity • identical protein binding
Cellular Component:	• cytoplasm • endoplasmic reticulum • endoplasmic reticulum membrane • membrane • integral to membrane
Biological Process:	• chondrocyte development • caspase activation • virus-infected cell apoptosis • ER overload response • endoplasmic reticulum organization and biogenesis • negative regulation of protein biosynthetic process • calcium-mediated signaling • insulin secretion • bone mineralization • unfolded protein response • endocrine pancreas development • negative regulation of myelination • negative regulation of translation initiation in response to stress • positive regulation of protein binding • protein amino acid autophosphorylation • insulin-like growth factor receptor signaling pathway • protein homooligomerization

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004836 (mRNA)
NP_004827 (protein)

XM_988416 (mRNA)
XP_993510 (protein)

Location

Chr 2: 88.64 - 88.71 Mb

Chr 6: 70.77 - 70.83 Mb

Pubmed search

[1]

[2]

Eukaryotic translation initiation factor 2-alpha kinase 3, also known as EIF2AK3, is a human gene.^[1]

[edit] References

^ Entrez Gene: EIF2AK3 eukaryotic translation initiation factor 2-alpha kinase 3.

[edit] Further reading

Mellor H, Proud CG (1991). "A synthetic peptide substrate for initiation factor-2 kinases.". Biochem. Biophys. Res. Commun. 178 (2): 430-7. PMID 1677563.
Dever TE, Chen JJ, Barber GN, et al. (1993). "Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast.". Proc. Natl. Acad. Sci. U.S.A. 90 (10): 4616-20. PMID 8099443.
Shi Y, Vattem KM, Sood R, et al. (1998). "Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control.". Mol. Cell. Biol. 18 (12): 7499-509. PMID 9819435.
Shi Y, An J, Liang J, et al. (1999). "Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and co-localization with somatostatin in islet delta cells.". J. Biol. Chem. 274 (9): 5723-30. PMID 10026192.
Hayes SE, Conner LJ, Stramm LE, Shi Y (2000). "Assignment of pancreatic eIF-2alpha kinase (EIF2AK3) to human chromosome band 2p12 by radiation hybrid mapping and in situ hybridization.". Cytogenet. Cell Genet. 86 (3-4): 327-8. PMID 10575235.
Sood R, Porter AC, Ma K, et al. (2000). "Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress.". Biochem. J. 346 Pt 2: 281-93. PMID 10677345.
Delépine M, Nicolino M, Barrett T, et al. (2000). "EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome.". Nat. Genet. 25 (4): 406-9. doi:10.1038/78085. PMID 10932183.
Saelens X, Kalai M, Vandenabeele P (2001). "Translation inhibition in apoptosis: caspase-dependent PKR activation and eIF2-alpha phosphorylation.". J. Biol. Chem. 276 (45): 41620-8. doi:10.1074/jbc.M103674200. PMID 11555640.
Ma K, Vattem KM, Wek RC (2002). "Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress.". J. Biol. Chem. 277 (21): 18728-35. doi:10.1074/jbc.M200903200. PMID 11907036.
Okada T, Yoshida H, Akazawa R, et al. (2002). "Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response.". Biochem. J. 366 (Pt 2): 585-94. doi:10.1042/BJ20020391. PMID 12014989.
Biason-Lauber A, Lang-Muritano M, Vaccaro T, Schoenle EJ (2002). "Loss of kinase activity in a patient with Wolcott-Rallison syndrome caused by a novel mutation in the EIF2AK3 gene.". Diabetes 51 (7): 2301-5. PMID 12086964.
Koumenis C, Naczki C, Koritzinsky M, et al. (2002). "Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha.". Mol. Cell. Biol. 22 (21): 7405-16. PMID 12370288.
Marcu MG, Doyle M, Bertolotti A, et al. (2003). "Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.". Mol. Cell. Biol. 22 (24): 8506-13. PMID 12446770.
Yan W, Frank CL, Korth MJ, et al. (2003). "Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK.". Proc. Natl. Acad. Sci. U.S.A. 99 (25): 15920-5. doi:10.1073/pnas.252341799. PMID 12446838.
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. doi:10.1073/pnas.242603899. PMID 12477932.
Pavio N, Romano PR, Graczyk TM, et al. (2003). "Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK.". J. Virol. 77 (6): 3578-85. PMID 12610133.
Cullinan SB, Zhang D, Hannink M, et al. (2003). "Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival.". Mol. Cell. Biol. 23 (20): 7198-209. PMID 14517290.
Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707-16. doi:10.1038/nbt971. PMID 15146197.
Senée V, Vattem KM, Delépine M, et al. (2004). "Wolcott-Rallison Syndrome: clinical, genetic, and functional study of EIF2AK3 mutations and suggestion of genetic heterogeneity.". Diabetes 53 (7): 1876-83. PMID 15220213.
Allotey RA, Mohan V, McDermott MF, et al. (2005). "The EIF2AK3 gene region and type I diabetes in subjects from South India.". Genes Immun. 5 (8): 648-52. doi:10.1038/sj.gene.6364139. PMID 15483661.