RNF5

Ring finger protein 5, E3 ubiquitin protein ligase
Identifiers
Symbols	RNF5 ; RING5; RMA1
External IDs	OMIM: 602677 MGI: 1860076 HomoloGene: 56004 GeneCards: RNF5 Gene
Gene ontology Molecular function • ubiquitin-protein transferase activity • protein binding • zinc ion binding • ligase activity • ubiquitin protein ligase activity involved in ERAD pathway Cellular component • endoplasmic reticulum membrane • integral component of membrane • mitochondrial membrane Biological process • response to bacterium • negative regulation of autophagy • protein destabilization • ERAD pathway • cellular protein catabolic process • protein K63-linked ubiquitination • protein K48-linked ubiquitination • ER-associated misfolded protein catabolic process • regulation of autophagosome assembly Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6048	54197
Ensembl	ENSG00000183574	ENSMUSG00000015478
UniProt	Q99942	O35445
RefSeq (mRNA)	NM_006913	NM_019403
RefSeq (protein)	NP_008844	NP_062276
Location (UCSC)	Chr 6: 32.18 – 32.18 Mb	Chr 17: 34.6 – 34.6 Mb
PubMed search

E3 ubiquitin-protein ligase RNF5 is an enzyme that in humans is encoded by the RNF5 gene.^[1][2]

The protein encoded by this gene contains a RING finger, which is a motif known to be involved in protein-protein interactions. This protein is a membrane-bound ubiquitin ligase. It can regulate cell motility by targeting paxillin ubiquitination and altering the distribution and localization of paxillin in cytoplasm and cell focal adhesions.^[2]

See also

• RING finger domain

References

1. Kyushiki H, Kuga Y, Suzuki M, Takahashi E, Horie M (Apr 1998). "Cloning, expression and mapping of a novel RING-finger gene (RNF5), a human homologue of a putative zinc-finger gene from Caenorhabditis elegans". Cytogenet Cell Genet 79 (1–2): 114–7. doi:10.1159/000134695. PMID 9533025.
2. "Entrez Gene: RNF5 ring finger protein 5".

Further reading

• Kendall E, Sargent CA, Campbell RD (1991). "Human major histocompatibility complex contains a new cluster of genes between the HLA-D and complement C4 loci". Nucleic Acids Res. 18 (24): 7251–7. doi:10.1093/nar/18.24.7251. PMC 332860. PMID 2259622.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Barritt DS, Pearn MT, Zisch AH, et al. (2000). "The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the membrane-spanning proteoglycan NG2". J. Cell. Biochem. 79 (2): 213–24. doi:10.1002/1097-4644(20001101)79:2<213::AID-JCB50>3.0.CO;2-G. PMC 3501957. PMID 10967549.
• Matsuda N, Suzuki T, Tanaka K, Nakano A (2001). "Rma1, a novel type of RING finger protein conserved from Arabidopsis to human, is a membrane-bound ubiquitin ligase". J. Cell. Sci. 114 (Pt 10): 1949–57. PMID 11329381.
• Pouly S, Prat A, Blain M, et al. (2002). "NG2 immunoreactivity on human brain endothelial cells". Acta Neuropathol. 102 (4): 313–20. doi:10.1007/s004010000350. PMID 11603805.
• 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.
• Didier C, Broday L, Bhoumik A, et al. (2003). "RNF5, a RING Finger Protein That Regulates Cell Motility by Targeting Paxillin Ubiquitination and Altered Localization". Mol. Cell. Biol. 23 (15): 5331–45. doi:10.1128/MCB.23.15.5331-5345.2003. PMC 165736. PMID 12861019.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
• Xie T, Rowen L, Aguado B, et al. (2004). "Analysis of the Gene-Dense Major Histocompatibility Complex Class III Region and Its Comparison to Mouse". Genome Res. 13 (12): 2621–36. doi:10.1101/gr.1736803. PMC 403804. PMID 14656967.
• Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• Liu AM, Wong YH (2005). "G16-mediated activation of nuclear factor kappaB by the adenosine A1 receptor involves c-Src, protein kinase C, and ERK signaling". J. Biol. Chem. 279 (51): 53196–204. doi:10.1074/jbc.M410196200. PMID 15485865.
• 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.
• Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153.
• Zhang Y, Higashide W, Dai S, et al. (2006). "Recognition and ubiquitination of Salmonella type III effector SopA by a ubiquitin E3 ligase, HsRMA1". J. Biol. Chem. 280 (46): 38682–8. doi:10.1074/jbc.M506309200. PMID 16176924.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Younger JM, Chen L, Ren HY, et al. (2006). "Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator". Cell 126 (3): 571–82. doi:10.1016/j.cell.2006.06.041. PMID 16901789.
• Bromberg KD, Kluger HM, Delaunay A, et al. (2007). "Increased Expression of the E3 Ubiquitin Ligase RNF5 Is Associated with Decreased Survival in Breast Cancer". Cancer Res. 67 (17): 8172–9. doi:10.1158/0008-5472.CAN-07-0045. PMC 2962863. PMID 17804730.

External links

• RNF5 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)