SPOPL

Details:

UniProt Entry: Q6IQ16
Gene: SPOPL
Class: Other E3 Components
Family: Adaptor
Protein length: 392
Database confidence: 0.5
InterPro: InterPro Entry
Mode of Action: unknown
AlphaFold Model: Link

Protein Sequence ▾

>Q6IQ16
MSREPTPPLP GDMSTGPIAE SWCYTQVKVV KFSYMWTINN FSFCREEMGE VLKSSTFSSG
PSDKMKWCLR VNPKGLDDES KDYLSLYLLL VSCPKSEVRA KFKFSLLNAK REETKAMESQ
RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE VSVVQDSVNI SGHTNTNTLK
VPECRLAEDL GNLWENTRFT DCSFFVRGQE FKAHKSVLAA RSPVFNAMFE HEMEESKKNR
VEINDLDPEV FKEMMRFIYT GRAPNLDKMA DNLLAAADKY ALERLKVMCE EALCSNLSVE
NVADTLVLAD LHSAEQLKAQ AIDFINRCSV LRQLGCKDGK NWNSNQATDI METSGWKSMI
QSHPHLVAEA FRALASAQCP QFGIPRKRLK QS

Domain Architecture (From InterPro) ▾

Start	End	Type	Name	InterPro	Source
29	166	Homologous_superfamily	TRAF-like	IPR008974	G3DSA:2.60.210.10
31	161	Domain	MATH/TRAF domain	IPR002083	PS50144
36	142	Domain	MATH/TRAF domain	IPR002083	SM00061
65	161	Domain	MATH/TRAF domain	IPR002083	PF00917
175	291	Homologous_superfamily	SKP1/BTB/POZ domain superfamily	IPR011333	G3DSA:3.30.710.10
180	295	Homologous_superfamily	SKP1/BTB/POZ domain superfamily	IPR011333	SSF54695
192	296	Domain	BTB/POZ domain	IPR000210	PF00651
200	297	Domain	BTB/POZ domain	IPR000210	SM00225
200	262	Domain	BTB/POZ domain	IPR000210	PS50097

Protein functions ▾

GO term	Name	Ontology	Evidence	Reference
GO:0016567	protein ubiquitination	Biological Process	IEA	GO_REF:0000041
GO:0030162	regulation of proteolysis	Biological Process	IBA	GO_REF:0000033
GO:0031397	negative regulation of protein ubiquitination	Biological Process	IMP	PMID:22632832
GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	Biological Process	IBA	GO_REF:0000033
GO:0005634	nucleus	Cellular Component	IEA	GO_REF:0000044
GO:0005737	cytoplasm	Cellular Component	IBA	GO_REF:0000033
GO:0031463	Cul3-RING ubiquitin ligase complex	Cellular Component	IEA	GO_REF:0000117
GO:0005515	protein binding	Molecular Function	IPI	PMID:22632832
GO:0031625	ubiquitin protein ligase binding	Molecular Function	IBA	GO_REF:0000033
GO:0042802	identical protein binding	Molecular Function	IPI	PMID:22632832

Data Usage Statement and License Agreement

Ownership and Copyright

The Database, including all associated datasets, metadata, and documentation, is the intellectual property of the PROXIDRUGs consortium and the InnoDATA project.
The content of the Database is protected under applicable copyright and database protection laws.

Permitted Use

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.
- Modify or build upon the data for academic, educational, or scientific purposes.
- Share derived datasets, analyses, or visualizations with proper citation and explicit acknowledgment of “The Human E3 Ligome” project.

Prohibited Use

Use the Database or any derivative works for commercial purposes without prior written consent from the PROXIDRUGs consortia (InnoDATA PIs).
Redistribute or republish the Database (or substantial parts of it) without proper credit and adherence to the license terms.
Misrepresent the data, alter metadata to mislead, or use it in a way that violates ethical or scientific standards.

Licensing

Unless otherwise stated, the Database is licensed under the Creative Commons Attribution 4.0 International License (CC BY 4.0).
This license allows redistribution and adaptation, provided appropriate credit is given.
Contributions (e.g., data corrections, additions, or scripts) can be made through merge requests on GitLab.
Contributors must agree to license their contributions under the same CC BY 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 et al. (2025, preprint)

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.