The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Ring1  -  ring finger protein 1

Mus musculus

Synonyms: E3 ubiquitin-protein ligase RING1, Polycomb complex protein RING1, RING finger protein 1, Ring1A, Rnf1, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Ring1

  • An oncogenic form of Cbl was recently identified in the 70Z/3 pre-B cell lymphoma which has a small deletion at the N-terminus of the Ring finger domain [1].

High impact information on Ring1

  • Ring1A and Ring1B display blocks of similarity throughout their sequences, including an N-terminal RING finger domain [2].
  • Ring1A represses transcription through sequences not involved in M33 binding [2].
  • Within the neural tube, Ring1A RNA is located at the rhombomere boundaries of the hindbrain [2].
  • Both Ring1A(-/-)and Ring1A(+/-) mice show anterior transformations and other abnormalities of the axial skeleton, which indicates an unusual sensitivity of axial skeleton patterning to Ring1A gene dosage [3].
  • These are either dependent on the phosphotyrosine binding domain of c-Cbl that directly binds to the EGFR or on the region C-terminal of the Ring finger, which allows for indirect binding to an alternative site on the receptor [4].

Biological context of Ring1

  • We find that the penetrance of some of these alterations was reduced in mice that are deficient in the class II PcG gene Ring1/Ring1A, indicating a genetic interaction between those two genes [5].
  • On the inactive X chromosome, uH2A was maintained in Ring1A or Ring1B null cells, but not in double knockout cells, demonstrating an overlapping function for these proteins in development [6].
  • Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation [6].
  • RING finger (C3HC4-type zinc finger) is a variant zinc finger motif present in a large family of functionally distinct proteins [7].
  • It comprises 12 exons and encodes a putative protein of 496 amino acid residues which shares an overall 67% identity with its human ortholog; it also shares 70% of amino acid identity with mouse CBL over their conserved SH2 and Ring finger domains [8].

Co-localisations of Ring1

  • Immunofluorescent staining by the antibodies has shown that endogenous Ring1B proteins clearly co-localize with Ring1A at the pattern of diffuse nuclear speckles [9].

Other interactions of Ring1

  • Homeotic transformations of the axial skeleton of YY1 mutant mice and genetic interaction with the Polycomb group gene Ring1/Ring1A [5].
  • The expression of Ring1A at early stages of development is restricted to the neural tube, whereas M33 is expressed ubiquitously [2].


  1. Tyrosine kinase activity of the EGF receptor is enhanced by the expression of oncogenic 70Z-Cbl. Thien, C.B., Langdon, W.Y. Oncogene (1997) [Pubmed]
  2. Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain. Schoorlemmer, J., Marcos-Gutiérrez, C., Were, F., Martínez, R., García, E., Satijn, D.P., Otte, A.P., Vidal, M. EMBO J. (1997) [Pubmed]
  3. Loss- and gain-of-function mutations show a polycomb group function for Ring1A in mice. del Mar Lorente, M., Marcos-Gutiérrez, C., Pérez, C., Schoorlemmer, J., Ramírez, A., Magin, T., Vidal, M. Development (2000) [Pubmed]
  4. Ubiquitin ligase activity of c-Cbl guides the epidermal growth factor receptor into clathrin-coated pits by two distinct modes of Eps15 recruitment. de Melker, A.A., van der Horst, G., Borst, J. J. Biol. Chem. (2004) [Pubmed]
  5. Homeotic transformations of the axial skeleton of YY1 mutant mice and genetic interaction with the Polycomb group gene Ring1/Ring1A. Lorente, M., Pérez, C., Sánchez, C., Donohoe, M., Shi, Y., Vidal, M. Mech. Dev. (2006) [Pubmed]
  6. Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation. de Napoles, M., Mermoud, J.E., Wakao, R., Tang, Y.A., Endoh, M., Appanah, R., Nesterova, T.B., Silva, J., Otte, A.P., Vidal, M., Koseki, H., Brockdorff, N. Dev. Cell (2004) [Pubmed]
  7. Cloning and characterization of a novel human gene RNF38 encoding a conserved putative protein with a RING finger domain. Eisenberg, I., Hochner, H., Levi, T., Yelin, R., Kahan, T., Mitrani-Rosenbaum, S. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  8. Characterization of the mouse Cblc/Cbl3 gene. Fiore, F., Ollendorff, V., Birnbaum, D. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  9. Production of monoclonal antibodies against mammalian Ring1B proteins. Atsuta, T., Fujimura, S., Moriya, H., Vidal, M., Akasaka, T., Koseki, H. Hybridoma (2001) [Pubmed]
WikiGenes - Universities