PRKRA

Protein kinase, interferon-inducible double stranded RNA dependent activator

PDB rendering based on 2dix.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2DIX

Identifiers

Symbols

PRKRA ; DYT16; HSD14; PACT; RAX

External IDs

OMIM: 603424 MGI: 1344375 HomoloGene: 2738 GeneCards: PRKRA Gene

Gene ontology
Molecular function	• double-stranded RNA binding • protein binding • enzyme activator activity • enzyme binding • identical protein binding • protein homodimerization activity • poly(A) RNA binding
Cellular component	• nucleoplasm • cytoplasm • cytosol • membrane • perinuclear region of cytoplasm
Biological process	• protein phosphorylation • immune response • negative regulation of cell proliferation • response to virus • gene expression • production of siRNA involved in RNA interference • pre-miRNA processing • cellular response to oxidative stress • production of miRNAs involved in gene silencing by miRNA • outer ear morphogenesis • middle ear morphogenesis • positive regulation of catalytic activity • skeletal system morphogenesis • positive regulation of intrinsic apoptotic signaling pathway
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
178.43 – 178.45 Mb

Chr 2:
76.63 – 76.65 Mb

PubMed search

Protein kinase, interferon-inducible double stranded RNA dependent activator, also known as interferon-inducible double stranded RNA-dependent protein kinase activator A or Protein ACTivator of the interferon-induced protein kinase (PACT) is a protein that in humans is encoded by the PRKRA gene.^[1]^[2]^[3] PACT heterodimerizes with and activates protein kinase R.^[2]^[4] PRKRA mutations have been linked to a rare form of dystonia parkinsonism. ^[5]

References

↑ "Entrez Gene: PRKRA protein kinase, interferon-inducible double stranded RNA dependent activator".
1 2 Patel RC, Sen GC (August 1998). "PACT, a protein activator of the interferon-induced protein kinase, PKR". EMBO J. 17 (15): 4379–90. doi:10.1093/emboj/17.15.4379. PMC 1170771. PMID 9687506.
↑ Ito T, Yang M, May WS (May 1999). "RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling". J. Biol. Chem. 274 (22): 15427–32. doi:10.1074/jbc.274.22.15427. PMID 10336432.
↑ Huang X, Hutchins B, Patel RC (August 2002). "The C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase (PKR)". Biochem. J. 366 (Pt 1): 175–86. doi:10.1042/BJ20020204. PMC 1222748. PMID 11985496.
↑ Camargos S, Scholz S, Simón-Sánchez J, Paisán-Ruiz C, Lewis P, Hernandez D, Ding J, Gibbs JR, Cookson MR, Bras J, Guerreiro R, Oliveira CR, Lees A, Hardy J, Cardoso F, Singleton AB (March 2008). "DYT16, a novel young-onset dystonia-parkinsonism disorder: identification of a segregating mutation in the stress-response protein PRKRA". Lancet Neurology 7 (3): 207–215. doi:10.1016/S1474-4422(08)70022-X. PMID 18243799.

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Peters GA, Hartmann R, Qin J, et al. (2001). "Modular structure of PACT: distinct domains for binding and activating PKR". Mol Cell Biol 21 (6): 1908–20. doi:10.1128/MCB.21.6.1908-1920.2001. PMC 86773. PMID 11238927.
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.
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Huang X, Hutchins B, Patel RC (2002). "The C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase (PKR)". Biochem. J. 366 (Pt 1): 175–86. doi:10.1042/BJ20020204. PMC 1222748. PMID 11985496.
Peters GA, Khoo D, Mohr I, Sen GC (2002). "Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein". J. Virol. 76 (21): 11054–64. doi:10.1128/JVI.76.21.11054-11064.2002. PMC 136652. PMID 12368348.
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. PMC 139241. PMID 12477932.
Yang M, Ito T, May WS (2003). "A novel role for RAX, the cellular activator of PKR, in synergistically stimulating SV40 large T antigen-dependent gene expression". J. Biol. Chem. 278 (40): 38325–32. doi:10.1074/jbc.M303420200. PMID 12874289.
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.
Bennett RL, Blalock WL, May WS (2004). "Serine 18 phosphorylation of RAX, the PKR activator, is required for PKR activation and consequent translation inhibition". J. Biol. Chem. 279 (41): 42687–93. doi:10.1074/jbc.M403321200. PMID 15299031.
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.
Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
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. doi:10.1038/nature04209. PMID 16189514.
Peters GA, Li S, Sen GC (2006). "Phosphorylation of specific serine residues in the PKR-activation domain of PACT is essential for its ability to mediate apoptosis". J Biol Chem 281 (46): 35129–36. doi:10.1074/jbc.M607714200. PMID 16982605.
Rowe TM, Rizzi M, Hirose K, Peters GA, et al. (2006). "A role of the double-stranded RNA-binding protein PACT in mouse ear development and hearing". Proc Natl Acad Sci USA 103 (15): 5823–8. doi:10.1073/pnas.0601287103. PMC 1458657. PMID 16571658.
Li S, Peters GA, Ding K, et al. (2006). "Molecular basis for PKR activation by PACT or dsRNA". Proc Natl Acad Sci USA 103 (26): 10005–10. doi:10.1073/pnas.0602317103. PMC 1502496. PMID 16785445.
Lee Y, Hur I, Park SY, et al. (2006). "The role of PACT in the RNA silencing pathway". EMBO J. 25 (3): 522–32. doi:10.1038/sj.emboj.7600942. PMC 1383527. PMID 16424907.
Bennett RL, Blalock WL, Abtahi DM, et al. (2006). "RAX, the PKR activator, sensitizes cells to inflammatory cytokines, serum withdrawal, chemotherapy, and viral infection". Blood 108 (3): 821–9. doi:10.1182/blood-2005-11-006817. PMC 1617065. PMID 16861340.
Peters GA, Seachrist DD, Keri RA, et al. (2009). "The double-stranded RNA-binding protein, PACT, is required for postnatal anterior pituitary proliferation". Proc Natl Acad Sci USA 106 (26): 10696–701. doi:10.1073/pnas.0900735106. PMC 2705576. PMID 19541653.

PDB gallery

2dix: Solution structure of the DSRM domain of Protein activator of the interferon-induced protein kinase

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PRKRA

References

Further reading