RIPK3

Receptor-interacting serine-threonine kinase 3
Identifiers
Symbols	RIPK3 ; RIP3
External IDs	OMIM: 605817 MGI: 2154952 HomoloGene: 31410 ChEMBL: 1795199 GeneCards: RIPK3 Gene
EC number	2.7.11.1
Gene ontology Molecular function • transcription coactivator activity • protein kinase activity • protein serine/threonine kinase activity • NF-kappaB-inducing kinase activity • protein binding • ATP binding • protein complex binding • identical protein binding Cellular component • mitochondrion • cytosol • plasma membrane • ripoptosome Biological process • regulation of T cell mediated cytotoxicity • toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • regulation of adaptive immune response • cellular protein modification process • signal transduction • I-kappaB kinase/NF-kappaB signaling • positive regulation of phosphatase activity • programmed cell death • activation of protein kinase activity • positive regulation of type I interferon production • regulation of interferon-gamma production • T cell differentiation in thymus • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • TRIF-dependent toll-like receptor signaling pathway • NIK/NF-kappaB signaling • T cell homeostasis • innate immune response • regulation of activated T cell proliferation • protein autophosphorylation • lymph node development • spleen development • thymus development • positive regulation of NF-kappaB transcription factor activity • protein homooligomerization • protein heterooligomerization • positive regulation of ligase activity • positive regulation of oxidoreductase activity • positive regulation of necroptotic process • regulation of activation-induced cell death of T cells • necroptotic process • positive regulation of protein deacetylation • apoptotic signaling pathway • programmed necrotic cell death • amyloid fibril formation • positive regulation of reactive oxygen species metabolic process • regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation • positive regulation of intrinsic apoptotic signaling pathway Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11035	56532
Ensembl	ENSG00000129465	ENSMUSG00000022221
UniProt	Q9Y572	Q9QZL0
RefSeq (mRNA)	NM_006871	NM_001164107
RefSeq (protein)	NP_006862	NP_001157579
Location (UCSC)	Chr 14: 24.34 – 24.34 Mb	Chr 14: 55.78 – 55.79 Mb
PubMed search

Receptor-interacting serine/threonine-protein kinase 3 is an enzyme that in humans is encoded by the RIPK3 gene.^[1][2][3][4]

The product of this gene is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases, and contains a C-terminal domain unique from other RIP family members. The encoded protein is predominantly localized to the cytoplasm, and can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. It is a component of the tumor necrosis factor (TNF) receptor-I signaling complex, and can induce apoptosis and weakly activate the NF-kappaB transcription factor.^[3]

Interactions

RIPK3 has been shown to interact with RIPK1.^[1][4]

References

1. Yu PW, Huang BC, Shen M, Quast J, Chan E, Xu X, Nolan GP, Payan DG, Luo Y (Jun 1999). "Identification of RIP3, a RIP-like kinase that activates apoptosis and NFkappaB". Curr Biol 9 (10): 539–42. doi:10.1016/S0960-9822(99)80239-5. PMID 10339433.
2. Sun X, Lee J, Navas T, Baldwin DT, Stewart TA, Dixit VM (Jul 1999). "RIP3, a novel apoptosis-inducing kinase". J Biol Chem 274 (24): 16871–5. doi:10.1074/jbc.274.24.16871. PMID 10358032.
3. "Entrez Gene: RIPK3 receptor-interacting serine-threonine kinase 3".
4. Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. (July 2012) The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell 150 (2):339-50.doi: 10.1016/j.cell.2012.06.019. PMID 22817896

Further reading

• Kasof GM, Prosser JC, Liu D, et al. (2000). "The RIP-like kinase, RIP3, induces apoptosis and NF-kappaB nuclear translocation and localizes to mitochondria". FEBS Lett. 473 (3): 285–91. doi:10.1016/S0014-5793(00)01473-3. PMID 10818227.
• Sun X, Yin J, Starovasnik MA, et al. (2002). "Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3". J. Biol. Chem. 277 (11): 9505–11. doi:10.1074/jbc.M109488200. PMID 11734559.
• 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.
• Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
• Meylan E, Burns K, Hofmann K, et al. (2004). "RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation". Nat. Immunol. 5 (5): 503–7. doi:10.1038/ni1061. PMID 15064760.
• Yang Y, Ma J, Chen Y, Wu M (2004). "Nucleocytoplasmic shuttling of receptor-interacting protein 3 (RIP3): identification of novel nuclear export and import signals in RIP3". J. Biol. Chem. 279 (37): 38820–9. doi:10.1074/jbc.M401663200. PMID 15208320.
• Yang Y, Hu W, Feng S, et al. (2005). "RIP3 beta and RIP3 gamma, two novel splice variants of receptor-interacting protein 3 (RIP3), downregulate RIP3-induced apoptosis". Biochem. Biophys. Res. Commun. 332 (1): 181–7. doi:10.1016/j.bbrc.2005.04.114. PMID 15896315.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Zhao L, Wang G, Lu D, et al. (2006). "Homocysteine, hRIP3 and congenital cardiovascular malformations". Anat. Embryol. 211 (3): 203–12. doi:10.1007/s00429-005-0074-9. PMID 16429275.
• Feng S, Ma L, Yang Y, Wu M (2006). "Truncated RIP3 (tRIP3) acts upstream of FADD to induce apoptosis in the human hepatocellular carcinoma cell line QGY-7703". Biochem. Biophys. Res. Commun. 347 (3): 558–65. doi:10.1016/j.bbrc.2006.06.118. PMID 16844082.
• Ahn KS, Sethi G, Krishnan K, Aggarwal BB (2007). "Gamma-tocotrienol inhibits nuclear factor-kappaB signaling pathway through inhibition of receptor-interacting protein and TAK1 leading to suppression of antiapoptotic gene products and potentiation of apoptosis". J. Biol. Chem. 282 (1): 809–20. doi:10.1074/jbc.M610028200. PMID 17114179.