RNF5

RNF5
Identifiers
Aliases	RNF5 , RING5, RMA1, ring finger protein 5
External IDs	OMIM: 602677 MGI: 1860076 HomoloGene: 56004 GeneCards: RNF5
Gene location (Human) Chr. Chromosome 6 (human) [1] Band 6p21.32 Start 32,178,405 bp [1] End 32,180,793 bp [1]
Gene location (Mouse) Chr. Chromosome 17 (mouse) [2] Band 17 B1|17 18.18 cM Start 34,820,065 bp [2] End 34,822,664 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence kidney right adrenal gland monocyte left ventricle duodenum right lobe of liver left adrenal gland putamen rectum Top expressed in proximal tubule neural tube yolk sac ganglionic eminence kidney pons brown adipose tissue olfactory bulb stomach medulla oblongata More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metal ion binding ubiquitin-protein transferase activity protein binding ubiquitin-like protein conjugating enzyme binding transferase activity identical protein binding zinc ion binding ubiquitin protein ligase activity protein-containing complex binding Cellular component integral component of membrane mitochondrial membranes membrane mitochondrion Derlin-1 retrotranslocation complex endoplasmic reticulum endoplasmic reticulum membrane endoplasmic reticulum quality control compartment Biological process response to bacterium protein K63-linked ubiquitination ER-associated misfolded protein catabolic process regulation of autophagosome assembly protein K48-linked ubiquitination protein destabilization protein ubiquitination negative regulation of autophagy transmembrane transport endoplasmic reticulum mannose trimming ubiquitin-dependent ERAD pathway ERAD pathway ubiquitin-dependent protein catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6048 54197 Ensembl ENSG00000227277 ENSG00000223767 ENSG00000228907 ENSG00000183574 ENSG00000204308 ENSG00000225452 ENSG00000228405 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: 34.82 – 34.82 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

E3 ubiquitin-protein ligase RNF5 is an enzyme that in humans is encoded by the RNF5 gene. ^{[5] [6]}

Function

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. ^[6]

References

1. ENSG00000223767, ENSG00000228907, ENSG00000183574, ENSG00000204308, ENSG00000225452, ENSG00000228405 GRCh38: Ensembl release 89: ENSG00000227277, ENSG00000223767, ENSG00000228907, ENSG00000183574, ENSG00000204308, ENSG00000225452, ENSG00000228405 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000015478 - 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. 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". Cytogenetics and Cell Genetics. 79 (1–2): 114–7. doi:10.1159/000134695. PMID   9533025.
6. "Entrez Gene: RNF5 ring finger protein 5".

Further reading

• Kendall E, Sargent CA, Campbell RD (December 1990). "Human major histocompatibility complex contains a new cluster of genes between the HLA-D and complement C4 loci". Nucleic Acids Research. 18 (24): 7251–7. doi:10.1093/nar/18.24.7251. PMC   332860 . PMID   2259622.
• Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi: 10.1101/gr.6.9.791 . PMID   8889548.
• Barritt DS, Pearn MT, Zisch AH, Lee SS, Javier RT, Pasquale EB, Stallcup WB (August 2000). "The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the membrane-spanning proteoglycan NG2". Journal of Cellular Biochemistry. 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 (May 2001). "Rma1, a novel type of RING finger protein conserved from Arabidopsis to human, is a membrane-bound ubiquitin ligase". Journal of Cell Science. 114 (Pt 10): 1949–57. doi:10.1242/jcs.114.10.1949. PMID   11329381.
• Pouly S, Prat A, Blain M, Olivier A, Antel J (October 2001). "NG2 immunoreactivity on human brain endothelial cells". Acta Neuropathologica. 102 (4): 313–20. doi:10.1007/s004010000350. PMID   11603805. S2CID   1353236.
• Didier C, Broday L, Bhoumik A, Israeli S, Takahashi S, Nakayama K, Thomas SM, Turner CE, Henderson S, Sabe H, Ronai Z (August 2003). "RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization". Molecular and Cellular Biology. 23 (15): 5331–45. doi:10.1128/MCB.23.15.5331-5345.2003. PMC   165736 . PMID   12861019.
• Xie T, Rowen L, Aguado B, Ahearn ME, Madan A, Qin S, Campbell RD, Hood L (December 2003). "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse". Genome Research. 13 (12): 2621–36. doi:10.1101/gr.1736803. PMC   403804 . PMID   14656967.
• Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (January 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 (December 2004). "G16-mediated activation of nuclear factor kappaB by the adenosine A1 receptor involves c-Src, protein kinase C, and ERK signaling" (PDF). The Journal of Biological Chemistry. 279 (51): 53196–204. doi: 10.1074/jbc.M410196200 . PMID   15485865.
• Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (March 2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID   15761153. S2CID   39457788.
• Zhang Y, Higashide W, Dai S, Sherman DM, Zhou D (November 2005). "Recognition and ubiquitination of Salmonella type III effector SopA by a ubiquitin E3 ligase, HsRMA1". The Journal of Biological Chemistry. 280 (46): 38682–8. doi: 10.1074/jbc.M506309200 . PMID   16176924.
• Younger JM, Chen L, Ren HY, Rosser MF, Turnbull EL, Fan CY, Patterson C, Cyr DM (August 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. S2CID   51698.
• Bromberg KD, Kluger HM, Delaunay A, Abbas S, DiVito KA, Krajewski S, Ronai Z (September 2007). "Increased expression of the E3 ubiquitin ligase RNF5 is associated with decreased survival in breast cancer". Cancer Research. 67 (17): 8172–9. doi:10.1158/0008-5472.CAN-07-0045. PMC   2962863 . PMID   17804730.
• Fujita Y, Khateb A, Li Y, Tinoco R, Zhang T, Bar-Yoseph H, Tam MA, Chowers Y, Sabo E, Gerassy-Vainberg S, Starosvetsky E, James B, Brown K, Shen-Orr SS, Bradley LM, Tessier PA, Ronai ZA (September 2018). "Regulation of S100A8 Stability by RNF5 in Intestinal Epithelial Cells Determines Intestinal Inflammation and Severity of Colitis". Cell Reports. 24 (12): 3296–3311.e6. doi:10.1016/j.celrep.2018.08.057. PMC   6185744 . PMID   30232010.

External links

• RNF5+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)