Version 5.4
Homo sapiens Protein: UBR7
Summary
InnateDB Protein IDBP-17449.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol UBR7
Protein Name ubiquitin protein ligase E3 component n-recognin 7 (putative)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000013070
InnateDB Gene IDBG-17447 (UBR7)
Protein Structure
UniProt Annotation
Function E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 24 experimentally validated interaction(s) in this database.
Experimentally validated
Total 24 [view]
Protein-Protein 24 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0004842 ubiquitin-protein transferase activity
GO:0008270 zinc ion binding
GO:0016874 ligase activity
Biological Process
GO:0008150 biological_process
GO:0016567 protein ubiquitination
Cellular Component
Protein Structure and Domains
PDB ID
InterPro IPR003126 Zinc finger, N-recognin
IPR011011 Zinc finger, FYVE/PHD-type
IPR013993 Zinc finger, N-recognin, metazoa
PFAM PF02207
PRINTS
PIRSF
SMART SM00396
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8N806
PhosphoSite PhosphoSite-Q8N806
TrEMBL
UniProt Splice Variant
Entrez Gene 55148
UniGene Hs.743356
RefSeq NP_786924
HUGO HGNC:20344
OMIM 613816
CCDS CCDS9909
HPRD 16602
IMGT
EMBL AK001345 AK097477 BC015046 BC051819 BX248249
GenPept AAH15046 AAH51819 BAA91639 BAC05069 CAD62577

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca