Sequence Detail

ID/Version

Q9Z2B5 Q9CWT5 Q9CTK8 (UniProt | EBI)

Last sequence update: 1999-05-01
Last annotation update: 2025-02-05

Sequence description from provider

RecName: Full=Eukaryotic translation initiation factor 2-alpha kinase 3 {ECO:0000305}; EC=2.7.11.1 {ECO:0000269|PubMed:16418533, ECO:0000269|PubMed:21543844, ECO:0000269|PubMed:21954288, ECO:0000269|PubMed:9930704};AltName: Full=PRKR-like endoplas

Provider

SWISS-PROT

Sequence

Polypeptide 1114 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Eif2ak3	eukaryotic translation initiation factor 2 alpha kinase 3	132	108	3	17

Sequence references in MGI

J:51759 Harding HP, et al., Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase [published erratum appears in Nature 1999 Mar 4;398(6722):90] [see comments]. Nature. 1999 Jan 21;397(6716):271-4
J:62257 Harding HP, et al., Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell. 2000 May;5(5):897-904
J:70005 Harding HP, et al., Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. Mol Cell. 2001 Jun;7(6):1153-63
J:76661 Zhang P, et al., The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas. Mol Cell Biol. 2002 Jun;22(11):3864-74
J:85958 Cullinan SB, et al., Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival. Mol Cell Biol. 2003 Oct;23(20):7198-209
J:99455 Harding HP, et al., Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell. 2000 Nov;6(5):1099-108
J:99680 The FANTOM Consortium and RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group), The Transcriptional Landscape of the Mammalian Genome. Science. 2005;309(5740):1559-1563
J:200066 Munoz JP, et al., Mfn2 modulates the UPR and mitochondrial function via repression of PERK. EMBO J. 2013 Aug 28;32(17):2348-61
J:218003 Cullinan SB, et al., PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress. J Biol Chem. 2004 May 7;279(19):20108-17
J:222776 Carrara M, et al., Crystal structures reveal transient PERK luminal domain tetramerization in endoplasmic reticulum stress signaling. EMBO J. 2015 Jun 3;34(11):1589-600
J:260006 Mounir Z, et al., Akt determines cell fate through inhibition of the PERK-eIF2alpha phosphorylation pathway. Sci Signal. 2011 Sep 27;4(192):ra62
J:278383 Balsa E, et al., ER and Nutrient Stress Promote Assembly of Respiratory Chain Supercomplexes through the PERK-eIF2alpha Axis. Mol Cell. 2019 Jun 6;74(5):877-890.e6
J:292518 Huttlin EL, et al., A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89
J:355657 Marciniak SJ, et al., Activation-dependent substrate recruitment by the eukaryotic translation initiation factor 2 kinase PERK. J Cell Biol. 2006 Jan 16;172(2):201-9
J:355658 Su Q, et al., Modulation of the eukaryotic initiation factor 2 alpha-subunit kinase PERK by tyrosine phosphorylation. J Biol Chem. 2008 Jan 4;283(1):469-475
J:355667 Wang P, et al., The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization. J Biol Chem. 2018 Mar 16;293(11):4110-4121