From Wikipedia, the free encyclopedia
Jump to: navigation, search
Ring-box 1, E3 ubiquitin protein ligase
Protein RBX1 PDB 1ldj.png
PDB rendering based on 1ldj.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols RBX1 ; BA554C12.1; RNF75; ROC1
External IDs OMIM603814 MGI1891829 HomoloGene6872 GeneCards: RBX1 Gene
RNA expression pattern
PBB GE RBX1 218117 at tn.png
More reference expression data
Species Human Mouse
Entrez 9978 100043674
Ensembl ENSG00000100387 ENSMUSG00000022400
UniProt P62877 P62878
RefSeq (mRNA) NM_014248 n/a
RefSeq (protein) NP_055063 n/a
Location (UCSC) Chr 22:
41.35 – 41.37 Mb
Chr 15:
81.47 – 81.48 Mb
PubMed search [1] [2]

RING-box protein 1 is a protein that in humans is encoded by the RBX1 gene.[1][2]

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.[3]


RBX1 has been shown to interact with CUL4A,[2][4][5] CAND1,[6][7] CUL1,[2][4][6][7][8][9] CUL2,[2][4] P70-S6 Kinase 1,[10] DCUN1D1,[7] CUL5[2][11] and CUL7.[4]


  1. ^ Kamura T, Koepp DM, Conrad MN, Skowyra D, Moreland RJ, Iliopoulos O, Lane WS, Kaelin WG Jr, Elledge SJ, Conaway RC, Harper JW, Conaway JW (May 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. 
  2. ^ a b c d e Ohta T, Michel JJ, Schottelius AJ, Xiong Y (May 1999). "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity". Mol Cell 3 (4): 535–41. doi:10.1016/S1097-2765(00)80482-7. PMID 10230407. 
  3. ^ "Entrez Gene: RBX1 ring-box 1". 
  4. ^ a b c d Dias, Dora C; Dolios Georgia; Wang Rong; Pan Zhen-Qiang (Dec 2002). "CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (26): 16601–6. doi:10.1073/pnas.252646399. ISSN 0027-8424. PMC 139190. PMID 12481031. 
  5. ^ Guerrero-Santoro, Jennifer; Kapetanaki Maria G, Hsieh Ching L, Gorbachinsky Ilya, Levine Arthur S, Rapić-Otrin Vesna (Jul 2008). "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A". Cancer Res. (United States) 68 (13): 5014–22. doi:10.1158/0008-5472.CAN-07-6162. PMID 18593899. 
  6. ^ a b Min, Kyoeng-Woo; Hwang Ji-Won; Lee Jong-Sik; Park Yoon; Tamura Taka-aki; Yoon Jong-Bok (May 2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". J. Biol. Chem. (United States) 278 (18): 15905–10. doi:10.1074/jbc.M213070200. ISSN 0021-9258. PMID 12609982. 
  7. ^ a b c Kim, Alexander Y; Bommeljé Claire C, Lee Benjamin E, Yonekawa Yoshihiro, Choi Lydia, Morris Luc G, Huang Guochang, Kaufman Andrew, Ryan Russel J H, Hao Bing, Ramanathan Y, Singh Bhuvanesh (Nov 2008). "SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation". J. Biol. Chem. (United States) 283 (48): 33211–20. doi:10.1074/jbc.M804440200. ISSN 0021-9258. PMC 2586271. PMID 18826954. 
  8. ^ Kim, Jaehoon; Kim Jeong-Hoon; Lee Sung-Hak; Kim Do-Hyung; Kang Ho-Young; Bae Sung-Ho; Pan Zhen-Qiang; Seo Yeon-Soo (Jul 2002). "The novel human DNA helicase hFBH1 is an F-box protein". J. Biol. Chem. (United States) 277 (27): 24530–7. doi:10.1074/jbc.M201612200. ISSN 0021-9258. PMID 11956208. 
  9. ^ Zheng, Ning; Schulman Brenda A, Song Langzhou, Miller Julie J, Jeffrey Philip D, Wang Ping, Chu Claire, Koepp Deanna M, Elledge Stephen J, Pagano Michele, Conaway Ronald C, Conaway Joan W, Harper J Wade, Pavletich Nikola P (Apr 2002). "Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex". Nature (England) 416 (6882): 703–9. doi:10.1038/416703a. ISSN 0028-0836. PMID 11961546. 
  10. ^ Panasyuk, Ganna; Nemazanyy Ivan; Filonenko Valeriy; Gout Ivan (May 2008). "Ribosomal protein S6 kinase 1 interacts with and is ubiquitinated by ubiquitin ligase ROC1". Biochem. Biophys. Res. Commun. (United States) 369 (2): 339–43. doi:10.1016/j.bbrc.2008.02.016. PMID 18279656. 
  11. ^ Duda, David M; Borg Laura A; Scott Daniel C; Hunt Harold W; Hammel Michal; Schulman Brenda A (Sep 2008). "Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation". Cell (United States) 134 (6): 995–1006. doi:10.1016/j.cell.2008.07.022. PMC 2628631. PMID 18805092. 

Further reading[edit]