RIPK2

Receptor-interacting serine/threonine-protein kinase 2 is an enzyme that in humans is encoded by the RIPK2 gene.[5][6][7]

RIPK2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4C8B, 2N7Z, 5AR3, 5AR2, 5AR7, 5AR8, 5AR5, 5AR4, 2N83, 5J7B, 5J79
Identifiers
Aliases	RIPK2, CARD3, CARDIAK, CCK, GIG30, RICK, RIP2, receptor interacting serine/threonine kinase 2
External IDs	OMIM: 603455 MGI: 1891456 HomoloGene: 37856 GeneCards: RIPK2
EC number	2.7.10.2
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8q21.3 Start 89,757,806 bp[1] End 89,791,064 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 A2|4 6.7 cM Start 16,122,733 bp[2] End 16,163,647 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • LIM domain binding • kinase activity • CARD domain binding • receptor binding • ATP binding • protein kinase activity • non-membrane spanning protein tyrosine kinase activity • transferase activity • protein homodimerization activity • GO:0001948 protein binding • nucleotide binding • signal transducer activity • protein serine/threonine kinase activity • identical protein binding • caspase binding • JUN kinase kinase kinase activity Cellular component • cytoplasm • cytoskeleton • vesicle • cytosol • macromolecular complex Biological process • response to interleukin-1 • positive regulation of cytokine-mediated signaling pathway • response to exogenous dsRNA • positive regulation of JNK cascade • positive regulation of xenophagy • cellular response to muramyl dipeptide • protein phosphorylation • positive regulation of ERK1 and ERK2 cascade • cellular response to peptidoglycan • positive regulation of stress-activated MAPK cascade • defense response to Gram-positive bacterium • apoptotic process • regulation of apoptotic process • positive regulation of immature T cell proliferation • positive regulation of interleukin-12 production • positive regulation of interferon-alpha production • positive regulation of peptidyl-serine phosphorylation • JNK cascade • response to interleukin-12 • nucleotide-binding oligomerization domain containing 2 signaling pathway • positive regulation of T-helper 1 type immune response • positive regulation of alpha-beta T cell proliferation • positive regulation of interleukin-6 production • positive regulation of tumor necrosis factor production • positive regulation of peptidyl-tyrosine phosphorylation • inflammatory response • I-kappaB kinase/NF-kappaB signaling • nucleotide-binding oligomerization domain containing 1 signaling pathway • positive regulation of interferon-beta production • phosphorylation • immune system process • positive regulation of T-helper 1 cell differentiation • negative regulation of apoptotic process • activation of MAPK activity • cellular response to lipoteichoic acid • positive regulation of interleukin-2 production • positive regulation of chemokine production • nucleotide-binding oligomerization domain containing signaling pathway • positive regulation of protein ubiquitination • lipopolysaccharide-mediated signaling pathway • positive regulation of interferon-gamma production • T cell proliferation • positive regulation of peptidyl-threonine phosphorylation • positive regulation of apoptotic process • positive regulation of I-kappaB kinase/NF-kappaB signaling • peptidyl-tyrosine phosphorylation • cellular response to lipopolysaccharide • T cell receptor signaling pathway • response to interleukin-18 • signal transduction • positive regulation of transcription from RNA polymerase II promoter • toll-like receptor 4 signaling pathway • toll-like receptor 2 signaling pathway • innate immune system • MAPK cascade • adaptive immune response • positive regulation of protein binding • positive regulation of NF-kappaB transcription factor activity • activation of cysteine-type endopeptidase activity • positive regulation of cell death • interleukin-1-mediated signaling pathway • activation of JNKK activity • activation of JUN kinase activity Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8767	192656
Ensembl	ENSG00000104312	ENSMUSG00000041135
UniProt	O43353	P58801
RefSeq (mRNA)	NM_003821 NM_001375360	NM_138952 NM_001329751
RefSeq (protein)	NP_003812 NP_001362289	NP_001316680 NP_620402
Location (UCSC)	Chr 8: 89.76 – 89.79 Mb	Chr 4: 16.12 – 16.16 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases. The encoded protein contains a C-terminal caspase recruitment domain (CARD), and is a component of signaling complexes in both the innate and adaptive immune pathways. It is a potent activator of NF-κB and inducer of apoptosis in response to various stimuli.[7]

Interactions

RIPK2 has been shown to interact with BIRC2.[6][8]

References

1. GRCh38: Ensembl release 89: ENSG00000104312 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000041135 - 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. Inohara N, del Peso L, Koseki T, Chen S, Nunez G (Jun 1998). "RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis". J Biol Chem. 273 (20): 12296–300. doi:10.1074/jbc.273.20.12296. PMID 9575181.
6. Thome M, Hofmann K, Burns K, Martinon F, Bodmer JL, Mattmann C, Tschopp J (Nov 1998). "Identification of CARDIAK, a RIP-like kinase that associates with caspase-1". Curr Biol. 8 (15): 885–8. doi:10.1016/S0960-9822(07)00352-1. PMID 9705938. S2CID 1235278.
7. "Entrez Gene: RIPK2 receptor-interacting serine-threonine kinase 2".
8. McCarthy, J V; Ni J; Dixit V M (Jul 1998). "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase". J. Biol. Chem. UNITED STATES. 273 (27): 16968–75. doi:10.1074/jbc.273.27.16968. ISSN 0021-9258. PMID 9642260.

Further reading

• Medzhitov R, Janeway C (2000). "Innate immune recognition: mechanisms and pathways". Immunol. Rev. 173: 89–97. doi:10.1034/j.1600-065X.2000.917309.x. PMID 10719670. S2CID 20844121.
• Dufner A, Mak TW (2006). "CARD tricks: controlling the interactions of CARD6 with RICK and microtubules". Cell Cycle. 5 (8): 797–800. doi:10.4161/cc.5.8.2635. PMID 16582588.
• McCarthy JV, Ni J, Dixit VM (1998). "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase". J. Biol. Chem. 273 (27): 16968–75. doi:10.1074/jbc.273.27.16968. PMID 9642260.
• Bertin J, Nir WJ, Fischer CM, et al. (1999). "Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-kappaB". J. Biol. Chem. 274 (19): 12955–8. doi:10.1074/jbc.274.19.12955. PMID 10224040.
• Inohara N, Koseki T, del Peso L, et al. (1999). "Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB". J. Biol. Chem. 274 (21): 14560–7. doi:10.1074/jbc.274.21.14560. PMID 10329646.
• Navas TA, Baldwin DT, Stewart TA (1999). "RIP2 is a Raf1-activated mitogen-activated protein kinase kinase". J. Biol. Chem. 274 (47): 33684–90. doi:10.1074/jbc.274.47.33684. PMID 10559258.
• Inohara N, Koseki T, Lin J, et al. (2000). "An induced proximity model for NF-kappa B activation in the Nod1/RICK and RIP signaling pathways". J. Biol. Chem. 275 (36): 27823–31. doi:10.1074/jbc.M003415200. PMID 10880512.
• Ogura Y, Inohara N, Benito A, et al. (2001). "Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-kappaB". J. Biol. Chem. 276 (7): 4812–8. doi:10.1074/jbc.M008072200. PMID 11087742.
• Lee SH, Stehlik C, Reed JC (2001). "Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing". J. Biol. Chem. 276 (37): 34495–500. doi:10.1074/jbc.M101415200. PMID 11432859.
• Khursigara G, Bertin J, Yano H, et al. (2001). "A prosurvival function for the p75 receptor death domain mediated via the caspase recruitment domain receptor-interacting protein 2". J. Neurosci. 21 (16): 5854–63. doi:10.1523/JNEUROSCI.21-16-05854.2001. PMC 6763175. PMID 11487608.
• Andersson L, Scharin Tang M (2015). "Rip2 modifies VEGF-induced signalling and vascular permeability in myocardial ischaemia". Cardiovasc. Res. 107 (4): 478–86. doi:10.1093/cvr/cvv186. PMID 26130752.
• Druilhe A, Srinivasula SM, Razmara M, et al. (2001). "Regulation of IL-1beta generation by Pseudo-ICE and ICEBERG, two dominant negative caspase recruitment domain proteins". Cell Death Differ. 8 (6): 649–57. doi:10.1038/sj.cdd.4400881. PMID 11536016.
• Chin AI, Dempsey PW, Bruhn K, et al. (2002). "Involvement of receptor-interacting protein 2 in innate and adaptive immune responses". Nature. 416 (6877): 190–4. Bibcode:2002Natur.416..190C. doi:10.1038/416190a. PMID 11894097. S2CID 4405035.
• Kobayashi K, Inohara N, Hernandez LD, et al. (2002). "RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems" (PDF). Nature. 416 (6877): 194–9. Bibcode:2002Natur.416..194K. doi:10.1038/416194a. hdl:2027.42/62842. PMID 11894098. S2CID 4363636.
• Munz B, Hildt E, Springer ML, Blau HM (2002). "RIP2, a Checkpoint in Myogenic Differentiation". Mol. Cell. Biol. 22 (16): 5879–86. doi:10.1128/MCB.22.16.5879-5886.2002. PMC 133983. PMID 12138198.
• Yoo NJ, Park WS, Kim SY, et al. (2003). "Nod1, a CARD protein, enhances pro-interleukin-1beta processing through the interaction with pro-caspase-1". Biochem. Biophys. Res. Commun. 299 (4): 652–8. doi:10.1016/S0006-291X(02)02714-6. PMID 12459189.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Chen YR, Clark AC (2003). "Equilibrium and kinetic folding of an alpha-helical Greek key protein domain: caspase recruitment domain (CARD) of RICK". Biochemistry. 42 (20): 6310–20. doi:10.1021/bi0340752. PMID 12755636.