RNF216

RNF216
Identifiers
Aliases	RNF216 , CAHH, TRIAD3, U7I1, UBCE7IP1, ZIN, ring finger protein 216
External IDs	OMIM: 609948 MGI: 1344349 HomoloGene: 19442 GeneCards: RNF216
Gene location (Human) Chr. Chromosome 7 (human) [1] Band 7p22.1 Start 5,620,047 bp [1] End 5,781,696 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5|5 G2 Start 142,976,648 bp [2] End 143,098,749 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in saphenous vein sperm stromal cell of endometrium oocyte Achilles tendon secondary oocyte gastric mucosa lymph node popliteal artery blood Top expressed in spermatid hand spermatocyte secondary oocyte morula interventricular septum foot otolith organ yolk sac utricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding metal ion binding ubiquitin protein ligase activity transferase activity Cellular component cytoplasm nucleus nucleoplasm cytosol Schaffer collateral - CA1 synapse postsynaptic endocytic zone glutamatergic synapse Biological process protein K48-linked ubiquitination negative regulation of type I interferon production viral process regulation of interferon-beta production protein ubiquitination regulation of defense response to virus by host proteasome-mediated ubiquitin-dependent protein catabolic process apoptotic process protein catabolic process, modulating synaptic transmission Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 54476 108086 Ensembl ENSG00000011275 ENSMUSG00000045078 UniProt Q9NWF9 P58283 RefSeq (mRNA) NM_019011 NM_207111 NM_207116 NM_001377156 NM_080561 NM_207110 NM_001359851 RefSeq (protein) NP_996994 NP_996999 NP_001364085 NP_542128 NP_996993 NP_001346780 Location (UCSC) Chr 7: 5.62 – 5.78 Mb Chr 5: 142.98 – 143.1 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

E3 ubiquitin-protein ligase RNF216 is an enzyme that in humans is encoded by the RNF216 gene. ^[5]

This gene encodes a cytoplasmic protein which specifically colocalizes and interacts with the serine/threonine protein kinase, receptor-interacting protein (RIP). Zinc finger domains of the encoded protein are required for its interaction with RIP and for inhibition of TNF- and IL1-induced NF-kappa B activation pathways. The encoded protein may also function as an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes and transfers it to substrates. Several alternatively spliced transcript variants have been described for this locus but the full-length natures of only some are known. ^[5]

See also

• RING finger domain

Interactions

RNF216 has been shown to interact with TLR9 ^[6] and RIPK1. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000011275 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000045078 - 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. "Entrez Gene: TRIAD3 TRIAD3 protein".
6. Chuang, Tsung-Hsien; Ulevitch Richard J (May 2004). "Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors". Nat. Immunol. 5 (5): 495–502. doi:10.1038/ni1066. ISSN   1529-2908. PMID   15107846. S2CID   39773935.
7. Chen, Danying; Li Xiaoyan; Zhai Zhonghe; Shu Hong-Bing (May 2002). "A novel zinc finger protein interacts with receptor-interacting protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-induced NF-kappa B activation". J. Biol. Chem. 277 (18): 15985–91. doi: 10.1074/jbc.M108675200 . ISSN   0021-9258. PMID   11854271.

Further reading

• Lake JA, Carr J, Feng F, et al. (2003). "The role of Vif during HIV-1 infection: interaction with novel host cellular factors". J. Clin. Virol. 26 (2): 143–52. doi:10.1016/S1386-6532(02)00113-0. PMID   12600646.
• Matoba R, Okubo K, Hori N, et al. (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene. 146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID   8076819.
• van der Reijden BA, Erpelinck-Verschueren CA, Löwenberg B, Jansen JH (1999). "TRIADs: a new class of proteins with a novel cysteine-rich signature". Protein Sci. 8 (7): 1557–61. doi:10.1110/ps.8.7.1557. PMC   2144383 . PMID   10422847.
• Wang X, Stollar BD (1999). "Immunoglobulin VH gene expression in human aging". Clin. Immunol. 93 (2): 132–42. doi:10.1006/clim.1999.4781. PMID   10527689.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC   310948 . PMID   11076863.
• Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC   311072 . PMID   11230166.
• Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC   1083732 . PMID   11256614.
• Chen D, Li X, Zhai Z, Shu HB (2002). "A novel zinc finger protein interacts with receptor-interacting protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-induced NF-kappa B activation". J. Biol. Chem. 277 (18): 15985–91. doi: 10.1074/jbc.M108675200 . PMID   11854271.
• 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.
• Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi: 10.1038/nature01782 . PMID   12853948.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• Chuang TH, Ulevitch RJ (2004). "Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors". Nat. Immunol. 5 (5): 495–502. doi:10.1038/ni1066. PMID   15107846. S2CID   39773935.
• Feng F, Davis A, Lake JA, et al. (2004). "Ring finger protein ZIN interacts with human immunodeficiency virus type 1 Vif". J. Virol. 78 (19): 10574–81. doi:10.1128/JVI.78.19.10574-10581.2004. PMC   516435 . PMID   15367624.
• 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.
• Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC   528930 . PMID   15489336.
• Oh JH, Yang JO, Hahn Y, et al. (2006). "Transcriptome analysis of human gastric cancer". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID   16341674. S2CID   69278.
• Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC   1347501 . PMID   16381901.
• Fearns C, Pan Q, Mathison JC, Chuang TH (2006). "Triad3A regulates ubiquitination and proteasomal degradation of RIP1 following disruption of Hsp90 binding". J. Biol. Chem. 281 (45): 34592–600. doi: 10.1074/jbc.M604019200 . PMID   16968706.

External links

• RNF216+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)