Version 5.4
Mus musculus Protein: Ttll2
Summary
InnateDB Protein IDBP-248962.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ttll2
Protein Name tubulin tyrosine ligase-like family, member 2
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000111413
InnateDB Gene IDBG-248960 (Ttll2)
Protein Structure
UniProt Annotation
Function Probable tubulin polyglutamylase that forms polyglutamate side chains on tubulin. Probably acts when complexed with other proteins. {ECO:0000269PubMed:17499049}.
Subcellular Localization
Disease Associations
Tissue Specificity Widely expressed with highest levels in brain, kidney, liver and testis. {ECO:0000269PubMed:17499049}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0016874 ligase activity
Biological Process
GO:0006464 cellular protein modification process
GO:0008150 biological_process
Cellular Component
GO:0005575 cellular_component
Protein Structure and Domains
PDB ID MGI:3644030
InterPro IPR004344 Tubulin-tyrosine ligase/Tubulin polyglutamylase
PFAM PF03133
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt A4Q9E4
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 100216474
UniGene Mm.477432
RefSeq NP_001091737
MGI ID
MGI Symbol Ttll2
OMIM
CCDS CCDS49941
HPRD
IMGT
EMBL AM690745
GenPept CAM84322

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