RIPK2

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; OMA:RIPK2 - orthologs
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 Bgee Human Mouse (ortholog) Top expressed in cartilage tissue monocyte gonad vena cava bone marrow stromal cell of endometrium granulocyte gallbladder skin of arm oocyte Top expressed in zygote esophagus genital tubercle secondary oocyte tibiofemoral joint tail of embryo embryo lens granulocyte primary oocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function LIM domain binding kinase activity CARD domain binding signaling receptor binding ATP binding protein kinase activity non-membrane spanning protein tyrosine kinase activity transferase activity protein homodimerization activity 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 protein-containing 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 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 by RNA polymerase II toll-like receptor 4 signaling pathway toll-like receptor 2 signaling pathway innate immune response 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 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

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

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. Bibcode:1998CBio....8..885T. doi:10.1016/S0960-9822(07)00352-1. PMID 9705938. S2CID 1235278.
7. "Entrez Gene: RIPK2 receptor-interacting serine-threonine kinase 2".
8. McCarthy JV, Ni J, Dixit V M (Jul 1998). "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase". J. Biol. Chem. 273 (27). UNITED STATES: 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.