Version 5.4
Mus musculus Protein: Otud6a
Summary
InnateDB Protein IDBP-162049.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Otud6a
Protein Name OTU domain containing 6A
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000059861
InnateDB Gene IDBG-162047 (Otud6a)
Protein Structure
UniProt Annotation
Function Deubiquitinating enzyme that hydrolyzes 'Lys-27'-, 'Lys- 29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains (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 0 experimentally validated interaction(s) in this database.
They are also associated with 5 interaction(s) predicted by orthology.
Predicted by orthology
Total 5 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004843 ubiquitin-specific protease activity
Biological Process
GO:0006508 proteolysis
GO:0035523 protein K29-linked deubiquitination
GO:0035871 protein K11-linked deubiquitination
GO:1990167 protein K27-linked deubiquitination
GO:1990168 protein K33-linked deubiquitination
Cellular Component
GO:0005575 cellular_component
Protein Structure and Domains
PDB ID MGI:3644685
InterPro IPR003323 Ovarian tumour, otubain
PFAM PF02338
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q6IE21
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 408193
UniGene Mm.469910
RefSeq NP_001156663
MGI ID
MGI Symbol Otud6a
OMIM
CCDS CCDS53146
HPRD
IMGT
EMBL AL671299 BC153817 BN000372
GenPept AAI53818 CAE51898 CAM19581

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