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RBX1
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	1LDJ, 1LDK, 1U6G, 2HYE, 2LGV, 3DPL, 3DQV, 3RTR, 4F52, 4P5O
Identifiers
Aliases	RBX1, BA554C12.1, RNF75, ROC1, ring-box 1
External IDs	OMIM: 603814; MGI: 3710517; HomoloGene: 6872; GeneCards: RBX1; OMA:RBX1 - orthologs
Gene location (Human)
Chr.	Chromosome 22 (human)
End	40,973,309 bp
RNA expression pattern
	Top expressed in
	periodontal fiber; ; trabecular bone; ; Skeletal muscle tissue of rectus abdominis; ; right ventricle; ; monocyte; ; palpebral conjunctiva; ; beta cell; ; C1 segment; ; olfactory bulb; ; oral cavity;
	n/a
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	cullin family protein binding; ubiquitin protein ligase activity; zinc ion binding; metal ion binding; ubiquitin-ubiquitin ligase activity; protein binding; ubiquitin protein ligase binding; ubiquitin-protein transferase activity; NEDD8 transferase activity; transcription factor binding; transferase activity; protein-containing complex binding;
Cellular component	cytoplasm; cullin-RING ubiquitin ligase complex; cytosol; SCF ubiquitin ligase complex; VCB complex; Cul2-RING ubiquitin ligase complex; Cul3-RING ubiquitin ligase complex; Cul5-RING ubiquitin ligase complex; Cul7-RING ubiquitin ligase complex; Cul4A-RING E3 ubiquitin ligase complex; Cul4B-RING E3 ubiquitin ligase complex; nucleus; nucleoplasm; nuclear SCF ubiquitin ligase complex; Cul4-RING E3 ubiquitin ligase complex;
Biological process	nucleotide-excision repair, DNA damage recognition; protein monoubiquitination; MAPK cascade; cellular response to DNA damage stimulus; protein neddylation; global genome nucleotide-excision repair; protein catabolic process; regulation of transcription from RNA polymerase II promoter in response to hypoxia; transcription-coupled nucleotide-excision repair; nucleotide-excision repair, DNA incision; negative regulation of canonical Wnt signaling pathway; nucleotide-excision repair, preincision complex stabilization; DNA repair; viral process; protein polyubiquitination; nucleotide-excision repair, preincision complex assembly; nucleotide-excision repair, DNA incision, 5'-to lesion; Wnt signaling pathway; SCF complex assembly; negative regulation of G2/M transition of mitotic cell cycle; post-translational protein modification; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; interleukin-1-mediated signaling pathway; protein ubiquitination; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; proteasome-mediated ubiquitin-dependent protein catabolic process; ubiquitin-dependent protein catabolic process; nucleotide-excision repair, DNA duplex unwinding; nucleotide-excision repair, DNA incision, 3'-to lesion;
	Sources:Amigo / QuickGO
Orthologs
	9978
	100043674
	ENSG00000100387
	n/a
	P62877
	n/a
	NM_014248
	XM_006525232; XM_006536722; XM_006537452
	NP_055063
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

RING-box protein 1 is a protein that in humans is encoded by the RBX1 gene.^[4]^[5]

Function

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.^[6]

Interactions

RBX1 has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100387 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. Bibcode:1999Sci...284..657K. doi:10.1126/science.284.5414.657. PMID 10213691.
^ ^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. S2CID 19371828.
^ "Entrez Gene: RBX1 ring-box 1".
^ ^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.
^ ^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 2586271. PMID 18826954.
^ ^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 139190. PMID 12481031.
^ 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.
^ 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. Bibcode:2002Natur.416..703Z. doi:10.1038/416703a. PMID 11961546. S2CID 4423882.
^ 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.
^ 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 2628631. PMID 18805092.
^ 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.