Version 5.4
Mus musculus Protein: Tmub2
Summary
InnateDB Protein IDBP-212555.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Tmub2
Protein Name transmembrane and ubiquitin-like domain containing 2
Synonyms 2010008E23Rik;
Species Mus musculus
Ensembl Protein ENSMUSP00000047600
InnateDB Gene IDBG-212553 (Tmub2)
Protein Structure
UniProt Annotation
Function
Subcellular Localization Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
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 2 interaction(s) predicted by orthology.
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0005515 protein binding
Biological Process
GO:0008150 biological_process
Cellular Component
GO:0005575 cellular_component
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1919303
InterPro IPR000626 Ubiquitin-like
IPR029071 Ubiquitin-related domain
PFAM PF00240
PF14560
PRINTS
PIRSF
SMART SM00213
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3V209
PhosphoSite PhosphoSite-Q3V209
TrEMBL
UniProt Splice Variant
Entrez Gene 72053
UniGene
RefSeq NP_082352
MGI ID 1WIA
MGI Symbol Tmub2
OMIM
CCDS CCDS25494
HPRD
IMGT
EMBL AK008158 AK132118 AL954730 BC016187 BC029841
GenPept AAH16187 AAH29841 BAB25500 BAE20990 CAM25077

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