RBX1

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Ring-box 1, E3 ubiquitin protein ligase
Protein RBX1 PDB 1ldj.png
PDB rendering based on 1ldj.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
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
Orthologs
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]

Interactions[edit]

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]

References[edit]

  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]