- DNAJC3
-
DnaJ (Hsp40) homolog, subfamily C, member 3 Identifiers Symbols DNAJC3; FLJ21288; HP58; P58; P58IPK; PRKRI External IDs OMIM: 601184 MGI: 107373 HomoloGene: 2486 GeneCards: DNAJC3 Gene Gene Ontology Molecular function • protein kinase inhibitor activity
• binding
• heat shock protein binding
• unfolded protein binding
• chaperone binding
• misfolded protein bindingCellular component • cytoplasm
• endoplasmic reticulum
• endoplasmic reticulum lumen
• endoplasmic reticulum Sec complexBiological process • protein folding
• response to unfolded protein
• response to virus
• proteolysis involved in cellular protein catabolic processSources: Amigo / QuickGO Orthologs Species Human Mouse Entrez 5611 100037258 Ensembl ENSG00000102580 ENSMUSG00000022136 UniProt Q13217 Q3UFV9 RefSeq (mRNA) NM_006260 NM_008929.3 RefSeq (protein) NP_006251 NP_032955.2 Location (UCSC) Chr 13:
96.33 – 96.44 MbChr 14:
119.34 – 119.38 MbPubMed search [1] [2] DnaJ homolog subfamily C member 3 is a protein that in humans is encoded by the DNAJC3 gene.[1][2][3]
The protein encoded by this gene contains multiple tetratricopeptide repeat (TPR) motifs as well as the highly conserved J domain found in DNAJ chaperone family members. It is a member of the tetratricopeptide repeat family of proteins and acts as an inhibitor of the interferon-induced, dsRNA-activated protein kinase (PKR).[3]
Interactions
DNAJC3 has been shown to interact with Protein kinase R,[4][5] PRKRIR[5] and EIF2AK3.[6]
References
- ^ Lee TG, Tang N, Thompson S, Miller J, Katze MG (Apr 1994). "The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins". Mol Cell Biol 14 (4): 2331–42. PMC 358600. PMID 7511204. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=358600.
- ^ Scherer SW, Duvoisin RM, Kuhn R, Heng HH, Belloni E, Tsui LC (Mar 1997). "Localization of two metabotropic glutamate receptor genes, GRM3 and GRM8, to human chromosome 7q". Genomics 31 (2): 230–3. doi:10.1006/geno.1996.0036. PMID 8824806.
- ^ a b "Entrez Gene: DNAJC3 DnaJ (Hsp40) homolog, subfamily C, member 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5611.
- ^ Polyak, S J; Tang N, Wambach M, Barber G N, Katze M G (Jan. 1996). "The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity". J. Biol. Chem. (UNITED STATES) 271 (3): 1702–7. doi:10.1074/jbc.271.3.1702. ISSN 0021-9258. PMID 8576172.
- ^ a b Gale, M; Blakely C M, Hopkins D A, Melville M W, Wambach M, Romano P R, Katze M G (Feb. 1998). "Regulation of Interferon-Induced Protein Kinase PKR: Modulation of P58IPK Inhibitory Function by a Novel Protein, P52rIPK". Mol. Cell. Biol. (UNITED STATES) 18 (2): 859–71. ISSN 0270-7306. PMC 108797. PMID 9447982. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=108797.
- ^ Yan, Wei; Frank Christopher L, Korth Marcus J, Sopher Bryce L, Novoa Isabel, Ron David, Katze Michael G (Dec. 2002). "Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (25): 15920–5. doi:10.1073/pnas.252341799. ISSN 0027-8424. PMC 138540. PMID 12446838. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=138540.
Further reading
- Polyak SJ, Tang N, Wambach M, et al. (1996). "The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity". J. Biol. Chem. 271 (3): 1702–7. doi:10.1074/jbc.271.3.1702. PMID 8576172.
- Korth MJ, Lyons CN, Wambach M, Katze MG (1996). "Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase". Gene 170 (2): 181–8. doi:10.1016/0378-1119(95)00883-7. PMID 8666242.
- Korth MJ, Edelhoff S, Disteche CM, Katze MG (1997). "Chromosomal assignment of the gene encoding the human 58-kDa inhibitor (PRKRI) of the interferon-induced dsRNA-activated protein kinase to chromosome 13q32". Genomics 31 (2): 238–9. doi:10.1006/geno.1996.0038. PMID 8824808.
- Gale M, Blakely CM, Hopkins DA, et al. (1998). "Regulation of Interferon-Induced Protein Kinase PKR: Modulation of P58IPK Inhibitory Function by a Novel Protein, P52rIPK". Mol. Cell. Biol. 18 (2): 859–71. PMC 108797. PMID 9447982. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=108797.
- Melville MW, Tan SL, Wambach M, et al. (1999). "The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity". J. Biol. Chem. 274 (6): 3797–803. doi:10.1074/jbc.274.6.3797. PMID 9920933.
- Ohtsuka K, Hata M (2001). "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature". Cell Stress Chaperones 5 (2): 98–112. doi:10.1379/1466-1268(2000)005<0098:MHDHCO>2.0.CO;2. ISSN 1466-1268. PMC 312896. PMID 11147971. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=312896.
- Horng T, Barton GM, Medzhitov R (2001). "TIRAP: an adapter molecule in the Toll signaling pathway". Nat. Immunol. 2 (9): 835–41. doi:10.1038/ni0901-835. PMID 11526399.
- Yan W, Gale MJ, Tan SL, Katze MG; Gale (2002). "Inactivation of the PKR protein kinase and stimulation of mRNA translation by the cellular co-chaperone P58(IPK) does not require J domain function". Biochemistry 41 (15): 4938–45. doi:10.1021/bi0121499. PMID 11939789.
- Ladiges W, Morton J, Hopkins H, et al. (2003). "Expression of human PKR protein kinase in transgenic mice". J. Interferon Cytokine Res. 22 (3): 329–34. doi:10.1089/107999002753675758. PMID 12034040.
- Yan W, Frank CL, Korth MJ, et al. (2003). "Control of PERK eIF2α 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. PMC 138540. PMID 12446838. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=138540.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- van Huizen R, Martindale JL, Gorospe M, Holbrook NJ (2003). "P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling". J. Biol. Chem. 278 (18): 15558–64. doi:10.1074/jbc.M212074200. PMID 12601012.
- Dunham A, Matthews LH, Burton J, et al. (2004). "The DNA sequence and analysis of human chromosome 13". Nature 428 (6982): 522–8. doi:10.1038/nature02379. PMC 2665288. PMID 15057823. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2665288.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- 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.
Chaperones/
protein foldingOtherProtein targeting Ubiquitin E1 Ubiquitin-activating enzyme (UBA1, UBA2, UBA3, UBA5, UBA6, UBA7, ATG7, NAE1, SAE1)
E2 Ubiquitin-conjugating enzyme (A • B • C • D1, D2, D3 • E1, E2, E3 • G1, G2 • H • I • J1, J2 • K • L1, L2, L3, L4, L6 • M • N • O • Q1, Q2 • R1 (CDC34), R2 • S • V1, V2 • Z)
E3 Ubiquitin ligase (VHL, Cullin, CBL, MDM2, FANCL, UBR1)
Deubiquitinating enzyme: Ataxin 3 • USP6 • CYLD
ATG3 • BIRC6 • UFC1Other see also posttranslational modification disorders
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)Categories:- Human proteins
- Chromosome 13 gene stubs
- Heat shock proteins
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