RIPK3

Receptor-interacting serine/threonine-protein kinase 3 is an enzyme that in humans is encoded by the RIPK3 gene.[5][6][7][8]

RIPK3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4M66, 4M69
Identifiers
Aliases	RIPK3, RIP3, receptor interacting serine/threonine kinase 3
External IDs	OMIM: 605817 MGI: 2154952 HomoloGene: 31410 GeneCards: RIPK3
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q12 Start 24,336,025 bp[1] End 24,340,022 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14|14 C3 Start 55,784,995 bp[2] End 55,788,865 bp[2]
Gene ontology Molecular function • transferase activity • protein kinase activity • nucleotide binding • GO:0001105 transcription coactivator activity • kinase activity • protein serine/threonine kinase activity • NF-kappaB-inducing kinase activity • GO:0001948 protein binding • identical protein binding • ATP binding • GO:0032403 macromolecular complex binding Cellular component • cytoplasm • cytosol • membrane • cell membrane • intracellular • mitochondrion Biological process • regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation • amyloid fibril formation • T cell differentiation in thymus • protein heterooligomerization • phosphorylation • thymus development • regulation of interferon-gamma production • positive regulation of oxidoreductase activity • regulation of adaptive immune response • spleen development • regulation of reactive oxygen species metabolic process • regulation of activation-induced cell death of T cells • T cell homeostasis • positive regulation of phosphatase activity • positive regulation of necroptotic process • protein phosphorylation • regulation of activated T cell proliferation • positive regulation of reactive oxygen species metabolic process • cellular protein modification process • NIK/NF-kappaB signaling • positive regulation of NF-kappaB transcription factor activity • apoptotic signaling pathway • autophosphorylation • positive regulation of ligase activity • GO:0060554, GO:0060555 necroptosis • regulation of T cell mediated cytotoxicity • I-kappaB kinase/NF-kappaB signaling • lymph node development • protein homooligomerization • activation of protein kinase activity • positive regulation of intrinsic apoptotic signaling pathway • signal transduction • programmed cell death • positive regulation of necrotic cell death • positive regulation of nucleic acid-templated transcription • cellular response to hydrogen peroxide • programmed necrotic cell death Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11035	56532
Ensembl	ENSG00000129465 ENSG00000285379	ENSMUSG00000022221
UniProt	Q9Y572	Q9QZL0
RefSeq (mRNA)	NM_006871	NM_001164107 NM_001164108 NM_019955
RefSeq (protein)	NP_006862	NP_001157579 NP_001157580 NP_064339
Location (UCSC)	Chr 14: 24.34 – 24.34 Mb	Chr 14: 55.78 – 55.79 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[7]

Interactions

RIPK3 has been shown to interact with RIPK1 to form an amyloid spine [5][8]

References

1. ENSG00000285379 GRCh38: Ensembl release 89: ENSG00000129465, ENSG00000285379 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022221 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: RIPK3 receptor-interacting serine-threonine kinase 3".
8. Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H (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. PMC 3664196. 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.