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Protein RBX1 PDB 1ldj.png
Available structures
PDB Human UniProt search: PDBe RCSB
Aliases RBX1, BA554C12.1, RNF75, ROC1, ring-box 1
External IDs MGI: 3710517 HomoloGene: 6872 GeneCards: RBX1
Gene location (Human)
Chromosome 22 (human)
Chr. Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for RBX1
Genomic location for RBX1
Band 22q13.2 Start 40,951,347 bp[1]
End 40,973,309 bp[1]
RNA expression pattern
PBB GE RBX1 218117 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 22: 40.95 – 40.97 Mb Chr 15: 81.47 – 81.48 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

RING-box protein 1 is a protein that in humans is encoded by the RBX1 gene.[5][6]


This gene encodes an evolutionarily conserved protein that interacts with cullins. The protein plays a unique role in the ubiquitination reaction by heterodimerizing with cullin-1 to catalyze ubiquitin polymerization. It also may be involved in the regulation of protein turn-over.[7]


RBX1 has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100387 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022400 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Kamura T, Koepp DM, Conrad MN, Skowyra D, Moreland RJ, Iliopoulos O, Lane WS, Kaelin WG, Elledge SJ, Conaway RC, Harper JW, Conaway JW (Apr 1999). "Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase". Science. 284 (5414): 657–61. doi:10.1126/science.284.5414.657. PMID 10213691. 
  6. ^ a b c d e Ohta T, Michel JJ, Schottelius AJ, Xiong Y (Apr 1999). "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity". Molecular Cell. 3 (4): 535–41. doi:10.1016/S1097-2765(00)80482-7. PMID 10230407. 
  7. ^ "Entrez Gene: RBX1 ring-box 1". 
  8. ^ a b Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB (May 2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". The Journal of Biological Chemistry. 278 (18): 15905–10. doi:10.1074/jbc.M213070200. PMID 12609982. 
  9. ^ a b c Kim AY, Bommeljé CC, Lee BE, Yonekawa Y, Choi L, Morris LG, Huang G, Kaufman A, Ryan RJ, Hao B, Ramanathan Y, Singh B (Nov 2008). "SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation". The Journal of Biological Chemistry. 283 (48): 33211–20. doi:10.1074/jbc.M804440200. PMC 2586271Freely accessible. PMID 18826954. 
  10. ^ a b c d Dias DC, Dolios G, Wang R, Pan ZQ (Dec 2002). "CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16601–6. doi:10.1073/pnas.252646399. PMC 139190Freely accessible. PMID 12481031. 
  11. ^ Kim J, Kim JH, Lee SH, Kim DH, Kang HY, Bae SH, Pan ZQ, Seo YS (Jul 2002). "The novel human DNA helicase hFBH1 is an F-box protein". The Journal of Biological Chemistry. 277 (27): 24530–7. doi:10.1074/jbc.M201612200. PMID 11956208. 
  12. ^ Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP (Apr 2002). "Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex". Nature. 416 (6882): 703–9. doi:10.1038/416703a. PMID 11961546. 
  13. ^ Guerrero-Santoro J, Kapetanaki MG, Hsieh CL, Gorbachinsky I, Levine AS, Rapić-Otrin V (Jul 2008). "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A". Cancer Research. 68 (13): 5014–22. doi:10.1158/0008-5472.CAN-07-6162. PMID 18593899. 
  14. ^ Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA (Sep 2008). "Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation". Cell. 134 (6): 995–1006. doi:10.1016/j.cell.2008.07.022. PMC 2628631Freely accessible. PMID 18805092. 
  15. ^ Panasyuk G, Nemazanyy I, Filonenko V, Gout I (May 2008). "Ribosomal protein S6 kinase 1 interacts with and is ubiquitinated by ubiquitin ligase ROC1". Biochemical and Biophysical Research Communications. 369 (2): 339–43. doi:10.1016/j.bbrc.2008.02.016. PMID 18279656. 

Further reading[edit]