Version 5.4
Bos taurus Protein: ERLIN2
Summary
InnateDB Protein IDBP-680429.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ERLIN2
Protein Name Erlin-2
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000039591
InnateDB Gene IDBG-629031 (ERLIN2)
Protein Structure
UniProt Annotation
Function Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Also involved in ITPR1 degradation by the ERAD pathway (By similarity). {ECO:0000250}.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane. {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 28 interaction(s) predicted by orthology.
Predicted by orthology
Total 28 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
Biological Process
GO:0030433 ER-associated ubiquitin-dependent protein catabolic process
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0043234 protein complex
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR001107 Band 7 protein
PFAM PF01145
PRINTS
PIRSF
SMART SM00244
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q1RMU4
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 616278
UniGene Bt.1734
RefSeq NP_001040041
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC114707
GenPept AAI14708

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