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RBX1 (ring-box 1)

Written2008-07Lijun Jia, Yi Sun
Division of Cancer Biology, Dept. of Radiation Oncology, University of Michigan, 4424B Medical Science I, 1301 Catherine Street, Ann Arbor, MI 48109-5637, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesring-box 1
ring-box 1, E3 ubiquitin protein ligase
Alias_symbol (synonym)ROC1
RNF75
BA554C12.1
Other aliasMGC13357
MGC1481
Rbx1
HGNC (Hugo) RBX1
LocusID (NCBI) 9978
Atlas_Id 42075
Location 22q13.2  [Link to chromosome band 22q13]
Location_base_pair Starts at 40951347 and ends at 40973015 bp from pter ( according to hg19-Feb_2009)  [Mapping RBX1.png]

DNA/RNA

 
Description RBX1 gene is evolutionarily conserved from plants to mammals with multiple family members in each species (Sun Y et al., 2001; Kamura T et al., 1999; Ohta T et al., 1999). Both Homo sapiens and Mus musculus genes are composed of five exons and four introns.
Transcription About 0.5 kb mRNA; regulated in mouse embryonic development with the strongest expression at 7 day-old followed by progressively decrease; ubiquitously distributed in adult mouse tissue and prevalent in the genital tract (ovary, testis, prostate and uterus) (Perin JP et al., 1999). RBX1 is also ubiquitously expressed in human tissues with the highest expression in heart, muscle, kidney and placenta (Swaroop M et al., 2001).

Protein

 
Description The RBX1 family of proteins from different organisms have 108-121 amino acids with molecular weight about 12-16 kDa (Sun Y et al., 2001; Kamura T et al., 1999; Ohta T et al., 1999; Tan P et al., 1999). Human RBX1 contains a RING-H2 finger domain (Cys42 -X2- Cys45-X29- Cys75-X1- His77 -X2 - His80 -X2 - Cys83 -X10 - Cys94 -X2 - Asp97, see drawing above), which is required for zinc ion binding and ubiquitin ligation (Sun Y et al., 2001; Kamura T et al., 1999; Ohta T et al., 1999; Tan P et al., 1999; Chen A et al., 2000).
Expression Ubiquitously expressed in human and mouse tissues and cell lines.
Localisation Both cytoplasm and nucleus.
Function RBX1, as an essential subunit of SCF, (Skp-1, cullins, F-box proteins) and VHL (von Hippel-Lindau) E3 ubiquitin ligases, interacts with different cullins and E2 ubiquitin-conjugating enzymes to catalyze ubiquitin polymerization of diverse substrates for proteasome-dependent degradation in numerous organisms (Kamura T et al., 1999; Nakayama KI et al., 2006; Petroski MD et al., 2005). Crystal structure study showed that RBX1, on one hand, complexes with cullin-F-box proteins which recognize a variety of protein substrates, and on the other hand, binds to E2 and transfers ubiquitin from E2 to substrates for proteasome-targeted degradation (Zheng N et al.,2002).
1) Binding with cullin family members for targeted protein degradation.
(A) Complexing with cullin1 in F-box protein/ SKP1/ Cullin 1/ RBX1, which is responsible for the degradation of a variety of substrates, including cell cycle regulators (e.g. cell cycle inhibitor p21/ p27/ p57 and cyclin A/ D/ E) , transcription factors (e.g. E2F1, FOXO1, Myc and c-Jun), signal transducers (e.g. Notch1/ 4 and BETA-catenin) and others (Nakayama KI et al., 2006; Petroski MD et al., 2005).
(B) Complexing with cullin 2 in VHL/ elongin BC/ Cullin 2/ RBX1, which is responsible for degradation of hypoxia-inducible factor-a (HIF-a) (Maxwell PH et al.,1999).
(C) Complexing with cullin 3 in BTB-domain protein/ Cullin 3/ RBX1, which is responsible for degradation of microtubule-severing protein MEI-1, Dishevelled (Dsh) and antioxidative transcription factor Nrf2 (Furukawa M et al., 2003; Furukawa M et al., 2005; Pintard L et al., 2003; Angers S et al., 2006).
(D) Complexing with cullin 4A in DDB1/ Cullin 4A/ RBX1, which is responsible for degradation of p53, TSC2, CDT1 and Merlin (Nag A et al., 2004; Banks D et al., 2006; Hu J et al., 2004; Hu J et al., 2008; Huang J et al., 2008).
(E) Complexing with cullin 5 in SOCS/ BC-box protein/ elongin BC/ Cullin 5/ RBX1, which is responsible for degradation of Disabled-1 (Dab1) (Feng L et al., 200721).
(F) Complexing with cullin 7 in Fbw8/ SKP1/ Cullin 7/ RBX1, which is responsible for degradation of insulin receptor substrate 1 ( IRS-1 ) (Xu X et al., 2008)
2) RBX1 activates Rub1 (also known as NEDD8) modification of cullin-1 and cullin-2 by E1 Rub1-activating enzyme Uba3/Ula1, and E2 Rub1-conjugating enzyme Ubc12, which is crucial for the activation of SCF ubiquitin ligase (Kamura T et al., 1999; Yamaguchi Y et al.,2007).
3) In yeast, RBX1 is a subunit of the Cdc53-containing SCF ubiquitin ligase required for ubiquitination of the cyclin-dependent kinase inhibitor Sic1 for the G1 to S cell cycle transition (Seol JH et al., 1999). RBX1 deletion causes yeast death, which can be rescued by human RBX1 and RBX2 (Ohta T et al., 1999; Swaroop M et al., 2000). Mutation of predicted zinc-binding residues in the conserved RING domain of RBX1 is lethal in S.cerevisiae and interferes with RBX1 activity in Rub1 conjugation and in ubiquitination of Cln2 (Ohta T et al., 1999; Kamura T et al., 1999; Swaroop M et al., 2000).
4) In Caenorhabditis elegans, RBX1 is essential for cell cycle progression and chromosome metabolism. Depletion of RBX1 by RNA-mediated interference (RNAi) causes pronounced defects in meiosis, mitotic chromosomal condensation and segregation, and cytokinesis (Sasagawa Y et al., 2005; Sasagawa Y et al., 2003).
5) In Drosophila, RBX1a is required for cell proliferation and embryo development. Deletion of RBX1a results in animal death, which cannot be rescued by overexpression of RBX1b, indicating a non-redundant function between the family members (Noureddine MA et al., 2003).
6) In mammalian cells, RBX1 is essential for normal cell cycle progression. Depletion of RBX1 by RNAi inhibits the proliferation of both normal and cancerous cells (Schlabach MR et al., 2008).
 

Mutations

Germinal Not known
Somatic Not known

Implicated in

Note
  
Entity Various cancers
Disease RBX1 is ubiquitously expressed in many human cancer cells (Swaroop M et al., 2001; Schlabach MR et al., 2008).
Prognosis Not known
Oncogenesis Not known
  

To be noted

Therapeutic potential:
RBX1 deletion by RNAi inhibits cancer cell proliferation and induces cancer cell death (Schlabach MR et al., 2008).

Bibliography

The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation.
Angers S, Thorpe CJ, Biechele TL, Goldenberg SJ, Zheng N, MacCoss MJ, Moon RT.
Nat Cell Biol 2006; 8(4): 348-357.
PMID 16547521
 
L2DTL/CDT2 and PCNA interact with p53 and regulate p53 polyubiquitination and protein stability through MDM2 and CUL4A/DDB1 complexes.
Banks D, Wu M, Higa LA, Gavrilova N, Quan J, Ye T, Kobayashi R, Sun H, Zhang H.
Cell Cycle 2006; 5(15): 1719-1729.
PMID 16861890
 
The conserved RING-H2 finger of ROC1 is required for ubiquitin ligation.
Chen A, Wu K, Fuchs SY, Tan P, Gomez C, Pan ZQ.
J Biol Chem 2000; 275(20): 15432-15439.
PMID 10748083
 
Cullin 5 regulates Dab1 protein levels and neuron positioning during cortical development.
Feng L, Allen NS, Simo S, Cooper JA.
Genes Dev 2007; 21(21): 2717-2730.
PMID 17974915
 
BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase.
Furukawa M, Xiong Y.
Mol Cell Biol 2005; 25(1): 162-171.
PMID 15601839
 
Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage.
Hu J, McCall CM, Ohta T, Xiong Y.
Nat Cell Biol 2004; 6(10): 1003-1009.
PMID 15448697
 
WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by DDB1-CUL4-ROC1 ligase.
Hu J, Zacharek S, He YJ, Lee H, Shumway S, Duronio RJ, Xiong Y.
Genes Dev 2008; 22(7): 866-871.
PMID 18381890
 
VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for degradation.
Huang J, Chen J.
Oncogene 2008; 27(29): 4056-4064
PMID 18332868
 
The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2.
Kamura T, Conrad MN, Yan Q, Conaway RC, Conaway JW.
Genes Dev 1999; 13(22): 2928-2933.
PMID 10579999
 
Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase.
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.
Science 1999; 284: 657-661.
PMID 10213691
 
The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis.
Maxwell PH, Wiesener MS, Chang GW, Clifford SC, Vaux EC, Cockman ME, Wykoff CC, Pugh CW, Maher ER, Ratcliffe PJ.
Nature 1999; 399(6733): 271-275.
PMID 10353251
 
Cul4A physically associates with MDM2 and participates in the proteolysis of p53.
Nag A, Bagchi S, Raychaudhuri P.
Cancer Res 2004; 64(22): 8152-8155.
PMID 15548678
 
Ubiquitin ligases: cell-cycle control and cancer.
Nakayama KI, Nakayama K.
Nat Rev Cancer 2006; 6(5): 369-381.
PMID 16633365
 
Drosophila Roc1a encodes a RING-H2 protein with a unique function in processing the Hh signal transducer Ci by the SCF E3 ubiquitin ligase.
Noureddine MA, Donaldson TD, Thacker SA, Duronio RJ.
Dev Cell 2002; 2(6): 757-770.
PMID 12062088
 
ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity.
Ohta T, Michel JJ, Schottelius AJ, Xiong Y.
Mol Cell 1999; 3: 535-541.
PMID 10230407
 
Genomic organization and expression of the ubiquitin-proteasome complex-associated protein Rbx1/ROC1/Hrt1.
Perin J-P, Seddiqi N, Charbonnier F, Goudou D, Belkadi L, Rieger F, Alliel PM.
Cell Mol Biol 1999; 45(8): 1131-1137.
PMID 10643962
 
Function and regulation of cullin-RING ubiquitin ligases.
Petroski MD, Deshaies RJ.
Nat Rev Mol Cell Biol 2005; 6(1): 9-20.
PMID 15688063
 
The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase.
Pintard L, Willis JH, Willems A, Johnson JL, Srayko M, Kurz T, Glaser S, Mains PE, Tyers M, Bowerman B, Peter M.
Nature 2003; 425(6955): 311-316.
PMID 13679921
 
Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity.
Sakata E, Yamaguchi Y, Miyauchi Y, Iwai K, Chiba T, Saeki Y, Matsuda N, Tanaka K, Kato K.
Nat Struct Mol Biol 2007; 14(2): 167-168.
PMID 17206147
 
Caenorhabditis elegans Elongin BC complex is essential for cell proliferation and chromosome condensation and segregation during mitosis and meiotic division II.
Sasagawa Y, Kikuchi K, Dazai K, Higashitani A.
Chromosome Res 2005; 13(4): 357-375.
PMID 15973501
 
Cancer proliferation gene discovery through functional genomics.
Schlabach MR, Luo J, Solimini NL, Hu G, Xu Q, Li MZ, Zhao Z, Smogorzewska A, Sowa ME, Ang XL, Westbrook TF, Liang AC, Chang K, Hackett JA, Harper JW, Hannon GJ, Elledge SJ.
Science 2008; 319(5863): 620-624.
PMID 18239126
 
Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34.
Seol JH, Feldman RM, Zachariae W, Shevchenko A, Correll CC, Lyapina S, Chi Y, Galova M, Claypool J, Sandmeyer S, Nasmyth K, Deshaies RJ, Shevchenko A, Deshaies RJ.
Genes & Dev 1999; 13: 1614-1626.
PMID 10385629
 
SAG/ROC/Rbx/Hrt, a zinc RING finger gene family: molecular cloning, biochemical properties, and biological functions.
Sun Y, Tan M, Duan H, Swaroop M.
Antioxid Redox Signal 2001; 3(4): 635-650.
PMID 11554450
 
SAG/ROC2/Rbx2/Hrt2, a component of SCF E3 ubiquitin ligase: genomic structure, a splicing variant, and two family pseudogenes.
Swaroop M, Gosink M, Sun Y. DNA
Cell Biol 2001; 20(7): 425-434.
PMID 11506706
 
Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth, but not for germination: Chip profiling implicates its role in cell cycle regulation.
Swaroop M, Wang Y, Miller P, Duan H, Jatkoe T, Madore SJ, Sun Y.
Oncogene 2000; 19: 2855-2866.
PMID 10851089
 
Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of IkBa.
Tan P, Fuchs SY, Chen A, Wu K, Gomez C, Ronai Z, Pan ZQ.
Mol Cell 1999; 3: 527-533.
PMID 10230406
 
The CUL7 E3 ubiquitin ligase targets insulin receptor substrate 1 for ubiquitin-dependent degradation.
Xu X, Sarikas A, Dias-Santagata DC, Dolios G, Lafontant PJ, Tsai SC, Zhu W, Nakajima H, Nakajima HO, Field LJ, Wang R, Pan ZQ.
Mol Cell 2008; 30(4): 403-414.
PMID 18498745
 
Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex.
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.
Nature 2002; 416(6882): 703-709.
PMID 11961546
 

Citation

This paper should be referenced as such :
Jia, L ; Sun, Y
RBX1 (ring-box 1)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(6):422-425.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/RBX1ID42075ch22q13.html


Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 2 ]
  Head and Neck: Ear: Endolymphatic Sac Tumor (ELST)
Nervous system: Astrocytoma with t(1;17)(p36;q21) SPOP/PRDM16


External links

Nomenclature
HGNC (Hugo)RBX1   9928
Cards
AtlasRBX1ID42075ch22q13
Entrez_Gene (NCBI)RBX1  9978  ring-box 1
AliasesBA554C12.1; RNF75; ROC1
GeneCards (Weizmann)RBX1
Ensembl hg19 (Hinxton)ENSG00000100387 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000100387 [Gene_View]  chr22:40951347-40973015 [Contig_View]  RBX1 [Vega]
ICGC DataPortalENSG00000100387
TCGA cBioPortalRBX1
AceView (NCBI)RBX1
Genatlas (Paris)RBX1
WikiGenes9978
SOURCE (Princeton)RBX1
Genetics Home Reference (NIH)RBX1
Genomic and cartography
GoldenPath hg38 (UCSC)RBX1  -     chr22:40951347-40973015 +  22q13.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)RBX1  -     22q13.2   [Description]    (hg19-Feb_2009)
EnsemblRBX1 - 22q13.2 [CytoView hg19]  RBX1 - 22q13.2 [CytoView hg38]
Mapping of homologs : NCBIRBX1 [Mapview hg19]  RBX1 [Mapview hg38]
OMIM603814   
Gene and transcription
Genbank (Entrez)AF085906 AF140598 AF142059 AK090764 AK315722
RefSeq transcript (Entrez)NM_014248
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)RBX1
Cluster EST : UnigeneHs.474949 [ NCBI ]
CGAP (NCI)Hs.474949
Alternative Splicing GalleryENSG00000100387
Gene ExpressionRBX1 [ NCBI-GEO ]   RBX1 [ EBI - ARRAY_EXPRESS ]   RBX1 [ SEEK ]   RBX1 [ MEM ]
Gene Expression Viewer (FireBrowse)RBX1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)9978
GTEX Portal (Tissue expression)RBX1
Protein : pattern, domain, 3D structure
UniProt/SwissProtP62877   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP62877  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP62877
Splice isoforms : SwissVarP62877
Catalytic activity : Enzyme6.3.2.- [ Enzyme-Expasy ]   6.3.2.-6.3.2.- [ IntEnz-EBI ]   6.3.2.- [ BRENDA ]   6.3.2.- [ KEGG ]   
PhosPhoSitePlusP62877
Domaine pattern : Prosite (Expaxy)ZF_RING_2 (PS50089)   
Domains : Interpro (EBI)Znf_RING    Znf_RING/FYVE/PHD    Znf_RING_H2   
Domain families : Pfam (Sanger)zf-rbx1 (PF12678)   
Domain families : Pfam (NCBI)pfam12678   
Conserved Domain (NCBI)RBX1
DMDM Disease mutations9978
Blocks (Seattle)RBX1
PDB (SRS)1LDJ    1LDK    1U6G    2HYE    2LGV    3DPL    3DQV    3RTR    4F52    4P5O   
PDB (PDBSum)1LDJ    1LDK    1U6G    2HYE    2LGV    3DPL    3DQV    3RTR    4F52    4P5O   
PDB (IMB)1LDJ    1LDK    1U6G    2HYE    2LGV    3DPL    3DQV    3RTR    4F52    4P5O   
PDB (RSDB)1LDJ    1LDK    1U6G    2HYE    2LGV    3DPL    3DQV    3RTR    4F52    4P5O   
Structural Biology KnowledgeBase1LDJ    1LDK    1U6G    2HYE    2LGV    3DPL    3DQV    3RTR    4F52    4P5O   
SCOP (Structural Classification of Proteins)1LDJ    1LDK    1U6G    2HYE    2LGV    3DPL    3DQV    3RTR    4F52    4P5O   
CATH (Classification of proteins structures)1LDJ    1LDK    1U6G    2HYE    2LGV    3DPL    3DQV    3RTR    4F52    4P5O   
SuperfamilyP62877
Human Protein AtlasENSG00000100387
Peptide AtlasP62877
HPRD06794
IPIIPI00003386   IPI00921133   
Protein Interaction databases
DIP (DOE-UCLA)P62877
IntAct (EBI)P62877
FunCoupENSG00000100387
BioGRIDRBX1
STRING (EMBL)RBX1
ZODIACRBX1
Ontologies - Pathways
QuickGOP62877
Ontology : AmiGOMAPK cascade  protein polyubiquitination  nucleotide-excision repair, DNA damage recognition  nucleotide-excision repair, DNA duplex unwinding  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleoplasm  nucleoplasm  cytosol  cytosol  transcription-coupled nucleotide-excision repair  nucleotide-excision repair, preincision complex stabilization  nucleotide-excision repair, preincision complex assembly  nucleotide-excision repair, DNA incision, 3'-to lesion  nucleotide-excision repair, DNA incision, 5'-to lesion  protein monoubiquitination  zinc ion binding  SCF complex assembly  negative regulation of G2/M transition of mitotic cell cycle  viral process  Wnt signaling pathway  protein ubiquitination  ligase activity  SCF ubiquitin ligase complex  SCF ubiquitin ligase complex  NEDD8 transferase activity  VCB complex  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  cullin-RING ubiquitin ligase complex  Cul2-RING ubiquitin ligase complex  Cul3-RING ubiquitin ligase complex  Cul4A-RING E3 ubiquitin ligase complex  Cul4B-RING E3 ubiquitin ligase complex  Cul5-RING ubiquitin ligase complex  Cul7-RING ubiquitin ligase complex  ubiquitin protein ligase binding  protein complex binding  nucleotide-excision repair, DNA incision  ubiquitin-ubiquitin ligase activity  DNA damage response, detection of DNA damage  proteasome-mediated ubiquitin-dependent protein catabolic process  proteasome-mediated ubiquitin-dependent protein catabolic process  protein neddylation  regulation of transcription from RNA polymerase II promoter in response to hypoxia  ubiquitin protein ligase activity  ubiquitin protein ligase activity  global genome nucleotide-excision repair  negative regulation of canonical Wnt signaling pathway  cullin family protein binding  
Ontology : EGO-EBIMAPK cascade  protein polyubiquitination  nucleotide-excision repair, DNA damage recognition  nucleotide-excision repair, DNA duplex unwinding  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleoplasm  nucleoplasm  cytosol  cytosol  transcription-coupled nucleotide-excision repair  nucleotide-excision repair, preincision complex stabilization  nucleotide-excision repair, preincision complex assembly  nucleotide-excision repair, DNA incision, 3'-to lesion  nucleotide-excision repair, DNA incision, 5'-to lesion  protein monoubiquitination  zinc ion binding  SCF complex assembly  negative regulation of G2/M transition of mitotic cell cycle  viral process  Wnt signaling pathway  protein ubiquitination  ligase activity  SCF ubiquitin ligase complex  SCF ubiquitin ligase complex  NEDD8 transferase activity  VCB complex  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  SCF-dependent proteasomal ubiquitin-dependent protein catabolic process  cullin-RING ubiquitin ligase complex  Cul2-RING ubiquitin ligase complex  Cul3-RING ubiquitin ligase complex  Cul4A-RING E3 ubiquitin ligase complex  Cul4B-RING E3 ubiquitin ligase complex  Cul5-RING ubiquitin ligase complex  Cul7-RING ubiquitin ligase complex  ubiquitin protein ligase binding  protein complex binding  nucleotide-excision repair, DNA incision  ubiquitin-ubiquitin ligase activity  DNA damage response, detection of DNA damage  proteasome-mediated ubiquitin-dependent protein catabolic process  proteasome-mediated ubiquitin-dependent protein catabolic process  protein neddylation  regulation of transcription from RNA polymerase II promoter in response to hypoxia  ubiquitin protein ligase activity  ubiquitin protein ligase activity  global genome nucleotide-excision repair  negative regulation of canonical Wnt signaling pathway  cullin family protein binding  
Pathways : BIOCARTARegulation of p27 Phosphorylation during Cell Cycle Progression [Genes]    ER?associated degradation (ERAD) Pathway [Genes]   
Pathways : KEGG   
REACTOMEP62877 [protein]
REACTOME PathwaysR-HSA-983168 [pathway]   
NDEx NetworkRBX1
Atlas of Cancer Signalling NetworkRBX1
Wikipedia pathwaysRBX1
Orthology - Evolution
OrthoDB9978
GeneTree (enSembl)ENSG00000100387
Phylogenetic Trees/Animal Genes : TreeFamRBX1
HOVERGENP62877
HOGENOMP62877
Homologs : HomoloGeneRBX1
Homology/Alignments : Family Browser (UCSC)RBX1
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerRBX1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)RBX1
dbVarRBX1
ClinVarRBX1
1000_GenomesRBX1 
Exome Variant ServerRBX1
ExAC (Exome Aggregation Consortium)RBX1 (select the gene name)
Genetic variants : HAPMAP9978
Genomic Variants (DGV)RBX1 [DGVbeta]
DECIPHERRBX1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisRBX1 
Mutations
ICGC Data PortalRBX1 
TCGA Data PortalRBX1 
Broad Tumor PortalRBX1
OASIS PortalRBX1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICRBX1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDRBX1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch RBX1
DgiDB (Drug Gene Interaction Database)RBX1
DoCM (Curated mutations)RBX1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)RBX1 (select a term)
intoGenRBX1
NCG5 (London)RBX1
Cancer3DRBX1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM603814   
Orphanet
MedgenRBX1
Genetic Testing Registry RBX1
NextProtP62877 [Medical]
TSGene9978
GENETestsRBX1
Target ValidationRBX1
Huge Navigator RBX1 [HugePedia]
snp3D : Map Gene to Disease9978
BioCentury BCIQRBX1
ClinGenRBX1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD9978
Chemical/Pharm GKB GenePA34299
Clinical trialRBX1
Miscellaneous
canSAR (ICR)RBX1 (select the gene name)
Probes
Litterature
PubMed364 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineRBX1
EVEXRBX1
GoPubMedRBX1
iHOPRBX1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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