RBX2

Domain Architecture (From InterPro) ▾

Protein functions ▾

Start	End	Type	Name	InterPro	Source
17	113	Homologous_superfamily	Zinc finger, RING/FYVE/PHD-type	IPR013083	G3DSA:3.30.40.10
48	103	Domain	Zinc finger, RING-H2-type	IPR024766	PF12678
61	103	Domain	Zinc finger, RING-type	IPR001841	PS50089

GO term	Name	Ontology	Evidence	Reference
GO:0038026	reelin-mediated signaling pathway	Biological Process	ISS	GO_REF:0000024
GO:0001837	epithelial to mesenchymal transition	Biological Process	IDA	PMID:16096638
GO:0010498	proteasomal protein catabolic process	Biological Process	IDA	PMID:29033132
GO:0021819	layer formation in cerebral cortex	Biological Process	ISS	GO_REF:0000024
GO:0031146	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	Biological Process	IDA	PMID:22017875
GO:0038162	erythropoietin-mediated signaling pathway	Biological Process	IDA	PMID:2163696
GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	Biological Process	IDA	PMID:11781573
GO:0045087	innate immune response	Biological Process	IDA	PMID:22915799
GO:0046314	phosphocreatine biosynthetic process	Biological Process	IDA	PMID:8186255
GO:0051607	defense response to virus	Biological Process	IDA	PMID:22915799
GO:0051894	positive regulation of focal adhesion assembly	Biological Process	IMP	PMID:35512830
GO:0060396	growth hormone receptor signaling pathway	Biological Process	IDA	PMID:2825030
GO:0060397	growth hormone receptor signaling pathway via JAK-STAT	Biological Process	IDA	PMID:12552091
GO:0060400	negative regulation of growth hormone receptor signaling pathway	Biological Process	IDA	PMID:21980433
GO:0140896	cGAS/STING signaling pathway	Biological Process	IDA	PMID:30842659
GO:0006511	ubiquitin-dependent protein catabolic process	Biological Process	IBA	GO_REF:0000033
GO:0016567	protein ubiquitination	Biological Process	IBA	GO_REF:0000033
GO:0030335	positive regulation of cell migration	Biological Process	NAS	PMID:33999101
GO:0030968	endoplasmic reticulum unfolded protein response	Biological Process	IDA	PMID:31387940
GO:0035556	intracellular signal transduction	Biological Process	IEA	GO_REF:0000117
GO:0043687	post-translational protein modification	Biological Process	TAS	Reactome:R-HSA-597592
GO:0045116	protein neddylation	Biological Process	IDA	PMID:19250909
GO:0051775	response to redox state	Biological Process	TAS	PMID:10082581
GO:0051895	negative regulation of focal adhesion assembly	Biological Process	IDA	PMID:35512830
GO:0070979	protein K11-linked ubiquitination	Biological Process	IDA	PMID:27910872
GO:0120184	negative regulation of focal adhesion disassembly	Biological Process	NAS	PMID:26598620
GO:2001222	regulation of neuron migration	Biological Process	ISS	GO_REF:0000024
GO:0005634	nucleus	Cellular Component	IBA	GO_REF:0000033
GO:0005737	cytoplasm	Cellular Component	IDA	PMID:16874460
GO:0005654	nucleoplasm	Cellular Component	IDA	GO_REF:0000052
GO:0005829	cytosol	Cellular Component	IDA	GO_REF:0000052
GO:0031466	Cul5-RING ubiquitin ligase complex	Cellular Component	IBA	GO_REF:0000033
GO:0005507	copper ion binding	Molecular Function	TAS	PMID:10082581
GO:0005515	protein binding	Molecular Function	IPI	PMID:16325183
GO:0008270	zinc ion binding	Molecular Function	IEA	GO_REF:0000120
GO:0016740	transferase activity	Molecular Function	IEA	GO_REF:0000043
GO:0019788	NEDD8 transferase activity	Molecular Function	TAS	Reactome:R-HSA-8952044
GO:0046872	metal ion binding	Molecular Function	IEA	GO_REF:0000043
GO:0061630	ubiquitin protein ligase activity	Molecular Function	IBA	GO_REF:0000033
GO:0061663	NEDD8 ligase activity	Molecular Function	IDA	PMID:19250909
GO:0097602	cullin family protein binding	Molecular Function	IBA	GO_REF:0000033

Enzyme–Substrate Interactions ▾

Data Usage Statement and License Agreement

Ownership and Copyright

The E3 Ligome database, including all associated data, metadata, and documentation, is the intellectual property of Goethe University (PROXIDRUGs consortium) under the InnoDATA project.
The contents of this Database are protected under applicable copyright and database protection laws.

Prohibited Use

Use of the Database or any derivative works for commercial purposes without prior written consent from Dr. Ramachandra M. Bhaskara (Goethe University, Frankfurt and the PROXIDRUGs consortia).
Redistribute or republish the Database (or substantial parts of it) without proper credit and adherence to the license terms.
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The sale, lease, license, or other transfer of DATA or MODIFICATIONS to a for-profit organization. COMMERCIAL PURPOSES shall also include uses of DATA or MODIFICATIONS by any other organization, including RECIPIENT, to perform contract research to screen E3–substrate networks and compound libraries, to manufacture products for general sale or to conduct research activities that result in any sale, lease, license, or transfer of DATA or MODIFICATIONS for-profit organization.

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The Database is provided for research, academic, and non-commercial purposes only, unless explicitly stated otherwise.
Users are permitted to:
- Access, download, and use the data.
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Licensing

Unless otherwise stated, the Human E3 Ligome Database and all associated data are licensed under the Creative Commons Attribution 4.0 International License ( CC BY-NC-SA 4.0).
Contributors must agree to license their contributions under the same CC BY-NC-SA 4.0 license.

Citation Requirements

If you use or refer to the Database in your publications, reports, or presentations, you must cite the paper: Dutta, A., Cristiani, A., Nikte, S.V. et al. Multi-scale classification decodes the complexity of the human E3 ligome. Nat Commun 16, 11382 (2025).

Contact and Support

For inquiries, permissions, or support regarding the Database, please contact: Dr. Ramachandra M. Bhaskara, Goethe University Frankfurt.
Email: bhaskara@med.uni-frankfurt.de.
Website maintained by Alberto Cristiani, Arghya Dutta, and Siddhanta V. Nikte.

RBX2

Details:

Protein Sequence ▾

Domain Architecture (From InterPro) ▾

Protein functions ▾

Enzyme–Substrate Interactions ▾