Version 5.4
Bos taurus Protein: UBE2J2
Summary
InnateDB Protein IDBP-687106.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol UBE2J2
Protein Name Ubiquitin-conjugating enzyme E2 J2
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000021109
InnateDB Gene IDBG-635280 (UBE2J2)
Protein Structure
UniProt Annotation
Function Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) (By similarity). {ECO:0000255PROSITE-ProRule:PRU00388}.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 11 interaction(s) predicted by orthology.
Predicted by orthology
Total 11 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016881 acid-amino acid ligase activity
Biological Process
GO:0006986 response to unfolded protein
GO:0016567 protein ubiquitination
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID
InterPro IPR000608 Ubiquitin-conjugating enzyme, E2
IPR016135 Ubiquitin-conjugating enzyme/RWD-like
PFAM PF00179
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q2TA03
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 506103
UniGene Bt.32465
RefSeq NP_001033132
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC111185
GenPept AAI11186

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