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Gene Review

RBX1  -  ring-box 1, E3 ubiquitin protein ligase

Homo sapiens

Synonyms: BA554C12.1, E3 ubiquitin-protein ligase RBX1, Protein ZYP, RING finger protein 75, RING-box protein 1, ...
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Disease relevance of RBX1


High impact information on RBX1

  • Functional studies indicated that the 3-M-associated CUL7 nonsense and missense mutations R1445X and H1464P, respectively, render CUL7 deficient in recruiting ROC1 [2].
  • Cand1, a 120 kDa HEAT repeat protein, forms a tight complex with the Cul1-Roc1 SCF catalytic core, inhibiting the assembly of the multisubunit E3 complex [3].
  • Both complexes contain cullin 4A and Roc1 and display ubiquitin ligase activity [4].
  • ROC1 plays a unique role in the ubiquitination reaction by heterodimerizing with cullin 1 to catalyze ubiquitin polymerization [5].
  • CUL7 is a large polypeptide containing a cullin domain, which is responsible for ROC1 binding, and a DOC domain, which is also present in the anaphase-promoting complex [6].

Biological context of RBX1

  • Furthermore, endogenous levels of pro-caspase-3 were decreased by overexpression of SAG/ROC-SCF(beta-TrCP) E3 Ub ligases, but increased on siRNA silencing of SAG, regulator of cullin-1 (ROC1), or beta-TrCPs, leading to increased apoptosis by etoposide and TNF-related apoptosis-inducing ligand through increased activation of caspase-3 [7].
  • The SCF-ROC1 ubiquitin-protein isopeptide ligase (E3) ubiquitin ligase complex targets the ubiquitination and subsequent degradation of protein substrates required for the regulation of cell cycle progression and signal transduction pathways [8].
  • The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1 [9].

Anatomical context of RBX1

  • Here we show that in primary human T lymphocytes, the SCF(skp2) core components Roc1, Cul1 and Skp1 are constitutively expressed, and their levels remain unchanged upon TCR/CD3-plus-CD28 costimulation [10].

Associations of RBX1 with chemical compounds

  • The cDNA codes for a 21-kDa protein, salmon hyperosmotic protein 21 (Shop21), with 98% identity to Rbx1, an E3 ubiquitin ligase; the protein also contains a novel 81-amino acid domain at the NH(2) terminus not found in Rbx1 [11].

Physical interactions of RBX1

  • Ligand-dependent degradation of Smad3 by a ubiquitin ligase complex of ROC1 and associated proteins [12].

Regulatory relationships of RBX1

  • Replacement of each of the six residues with the corresponding amino acid in ubiquitin decreases the ability of Nedd8 to activate the ubiquitin ligase activity of ROC1-CUL1 [13].

Other interactions of RBX1

  • RING finger mutations of ROC1 eliminated the Ub ligase activity toward cyclin D1 [14].
  • An E3 ubiquitin ligase complex ROC1-SCF(Fbw1a) consisting of ROC1, Skp1, Cullin1, and Fbw1a (also termed betaTrCP1) induces ubiquitination of Smad3 [12].
  • Smad3 interacts with a RING finger protein, ROC1, through its C-terminal MH2 domain in a ligand-dependent manner [12].
  • In productively infected cells, E1B-55K and E4orf6 assemble a ubiquitin ligase with cellular proteins Elongins B and C, Cullin 5 and RBX1 that polyubiquitinates p53 and one or more subunits of the MRN complex involved in DNA double-strand break repair, directing them to proteosomal degradation [15].
  • No coding region sequence variations were detected for the elongin B, elongin C or Rbx1 genes [16].


  1. A model for compression trauma: pressure-induced injury in cell cultures. Murphy, E.J., Horrocks, L.A. J. Neurotrauma (1993) [Pubmed]
  2. Identification of mutations in CUL7 in 3-M syndrome. Huber, C., Dias-Santagata, D., Glaser, A., O'Sullivan, J., Brauner, R., Wu, K., Xu, X., Pearce, K., Wang, R., Uzielli, M.L., Dagoneau, N., Chemaitilly, W., Superti-Furga, A., Dos Santos, H., Mégarbané, A., Morin, G., Gillessen-Kaesbach, G., Hennekam, R., Van der Burgt, I., Black, G.C., Clayton, P.E., Read, A., Le Merrer, M., Scambler, P.J., Munnich, A., Pan, Z.Q., Winter, R., Cormier-Daire, V. Nat. Genet. (2005) [Pubmed]
  3. Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases. Goldenberg, S.J., Cascio, T.C., Shumway, S.D., Garbutt, K.C., Liu, J., Xiong, Y., Zheng, N. Cell (2004) [Pubmed]
  4. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Groisman, R., Polanowska, J., Kuraoka, I., Sawada, J., Saijo, M., Drapkin, R., Kisselev, A.F., Tanaka, K., Nakatani, Y. Cell (2003) [Pubmed]
  5. Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha. Tan, P., Fuchs, S.Y., Chen, A., Wu, K., Gomez, C., Ronai, Z., Pan, Z.Q. Mol. Cell (1999) [Pubmed]
  6. CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex. Dias, D.C., Dolios, G., Wang, R., Pan, Z.Q. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  7. SAG/ROC-SCFbeta-TrCP E3 ubiquitin ligase promotes pro-caspase-3 degradation as a mechanism of apoptosis protection. Tan, M., Gallegos, J.R., Gu, Q., Huang, Y., Li, J., Jin, Y., Lu, H., Sun, Y. Neoplasia (2006) [Pubmed]
  8. Conjugation of Nedd8 to CUL1 enhances the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization. Wu, K., Chen, A., Pan, Z.Q. J. Biol. Chem. (2000) [Pubmed]
  9. The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1. Hetfeld, B.K., Helfrich, A., Kapelari, B., Scheel, H., Hofmann, K., Guterman, A., Glickman, M., Schade, R., Kloetzel, P.M., Dubiel, W. Curr. Biol. (2005) [Pubmed]
  10. CD28 costimulation mediates transcription of SKP2 and CKS1, the substrate recognition components of SCFSkp2 ubiquitin ligase that leads p27kip1 to degradation. Appleman, L.J., Chernova, I., Li, L., Boussiotis, V.A. Cell Cycle (2006) [Pubmed]
  11. A homolog of the E3 ubiquitin ligase Rbx1 is induced during hyperosmotic stress of salmon. Pan, F., Zarate, J., Bradley, T.M. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2002) [Pubmed]
  12. Ligand-dependent degradation of Smad3 by a ubiquitin ligase complex of ROC1 and associated proteins. Fukuchi, M., Imamura, T., Chiba, T., Ebisawa, T., Kawabata, M., Tanaka, K., Miyazono, K. Mol. Biol. Cell (2001) [Pubmed]
  13. The Nedd8-conjugated ROC1-CUL1 core ubiquitin ligase utilizes Nedd8 charged surface residues for efficient polyubiquitin chain assembly catalyzed by Cdc34. Wu, K., Chen, A., Tan, P., Pan, Z.Q. J. Biol. Chem. (2002) [Pubmed]
  14. In vitro ubiquitination of cyclin D1 by ROC1-CUL1 and ROC1-CUL3. Maeda, I., Ohta, T., Koizumi, H., Fukuda, M. FEBS Lett. (2001) [Pubmed]
  15. Recent lessons in gene expression, cell cycle control, and cell biology from adenovirus. Berk, A.J. Oncogene (2005) [Pubmed]
  16. The pVHL-associated SCF ubiquitin ligase complex: molecular genetic analysis of elongin B and C, Rbx1 and HIF-1alpha in renal cell carcinoma. Clifford, S.C., Astuti, D., Hooper, L., Maxwell, P.H., Ratcliffe, P.J., Maher, E.R. Oncogene (2001) [Pubmed]
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