RNF5

Protein-coding gene in the species Homo sapiens
RNF5
Identifiers
AliasesRNF5, RING5, RMA1, ring finger protein 5
External IDsOMIM: 602677; MGI: 1860076; HomoloGene: 56004; GeneCards: RNF5; OMA:RNF5 - orthologs
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for RNF5
Genomic location for RNF5
Band6p21.32Start32,178,405 bp[1]
End32,180,793 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for RNF5
Genomic location for RNF5
Band17 B1|17 18.18 cMStart34,820,065 bp[2]
End34,822,664 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ganglionic eminence

  • human kidney

  • ventricular zone

  • right adrenal gland

  • mucosa of transverse colon

  • right adrenal cortex

  • monocyte

  • apex of heart

  • left ventricle

  • duodenum
Top expressed in
  • proximal tubule

  • right kidney

  • neural tube

  • neural layer of retina

  • yolk sac

  • ganglionic eminence

  • human kidney

  • pons

  • brown adipose tissue

  • olfactory bulb
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
SpeciesHumanMouse
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 MbChr 17: 34.82 – 34.82 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c ENSG00000223767, ENSG00000228907, ENSG00000183574, ENSG00000204308, ENSG00000225452, ENSG00000228405 GRCh38: Ensembl release 89: ENSG00000227277, ENSG00000223767, ENSG00000228907, ENSG00000183574, ENSG00000204308, ENSG00000225452, ENSG00000228405 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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.
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