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Ring Finger Protein 5 (RNF5)

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RING5; RMA1; NG2; G16; E3 ubiquitin-protein ligase RNF5

Ring Finger Protein 5 (RNF5)
CCC E958
HGNC 10068
MGI 1860076
PubMed 12861019
UniProt Q99942
Wiki RNF5
E3 ubiquitin-protein ligase RNF5 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.
Derlin-1 retained CFTR in the ER membrane and interacted with RMA1 and UBC6E to promote proteasomal degradation of CFTR. RMA1 could recognize folding defects in delF508 coincident with translation, whereas CHIP appeared to act posttranslationally. A folding defect in delF508 detected by RMA1 involved the inability of the second membrane-spanning domain of CFTR to productively interact with N-terminal domains.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Ring Finger Protein 5 (RNF5) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Ring Finger Protein 5 (RNF5) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Ring Finger Protein 5 (RNF5) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Ring Finger Protein 5 (RNF5) CLIA Kit Customized Service Offer
n/a ELISA Kit for Ring Finger Protein 5 (RNF5) ELISA Kit Customized Service Offer

Organism species: Mus musculus (Mouse)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Ring Finger Protein 5 (RNF5) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Ring Finger Protein 5 (RNF5) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Ring Finger Protein 5 (RNF5) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Ring Finger Protein 5 (RNF5) CLIA Kit Customized Service Offer
n/a ELISA Kit for Ring Finger Protein 5 (RNF5) ELISA Kit Customized Service Offer
  1. "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. 79:114-117(1997) [PubMed] [Europe PMC] [Abstract]
  2. "Rma1, a novel type of RING finger protein conserved from Arabidopsis to human, is a membrane-bound ubiquitin ligase."J. Cell Sci. 114:1949-1957(2001) [PubMed] [Europe PMC] [Abstract]
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs." Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
  4. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
  5. "The DNA sequence and analysis of human chromosome 6." Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
  7. "RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization."Mol. Cell. Biol. 23:5331-5345(2003) [PubMed] [Europe PMC] [Abstract]
  8. "Recognition and ubiquitination of Salmonella type III effector SopA by a ubiquitin E3 ligase, HsRMA1."J. Biol. Chem. 280:38682-38688(2005) [PubMed] [Europe PMC] [Abstract]
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
  10. "The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA."Immunity 30:397-407(2009) [PubMed] [Europe PMC] [Abstract]
  11. "Regulation of endoplasmic reticulum-associated degradation by RNF5-dependent ubiquitination of JNK-associated membrane protein (JAMP)."J. Biol. Chem. 284:12099-12109(2009) [PubMed] [Europe PMC] [Abstract]
  12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
  13. "N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]