Version 5.4
Mus musculus Protein: Ttll1
Summary
InnateDB Protein IDBP-262295.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ttll1
Protein Name tubulin tyrosine ligase-like 1
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000105106
InnateDB Gene IDBG-168200 (Ttll1)
Protein Structure
UniProt Annotation
Function Catalytic subunit of the neuronal tubulin polyglutamylase complex. Modifies alpha- and beta-tubulin, generating side chains of glutamate on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. {ECO:0000269PubMed:15890843}.
Subcellular Localization Cytoplasm, cytoskeleton {ECO:0000305}.
Disease Associations
Tissue Specificity Widely expressed with highest levels in brain, heart and kidney. {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:0005515 protein binding
GO:0016874 ligase activity
Biological Process
GO:0003351 epithelial cilium movement
GO:0006464 cellular protein modification process
GO:0018095 protein polyglutamylation
GO:0035082 axoneme assembly
GO:0044782 cilium organization
GO:0060271 cilium morphogenesis
Cellular Component
GO:0005575 cellular_component
GO:0005737 cytoplasm
GO:0005874 microtubule
Protein Structure and Domains
PDB ID MGI:2443047
InterPro IPR004344 Tubulin-tyrosine ligase/Tubulin polyglutamylase
PFAM PF03133
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q91V51
PhosphoSite PhosphoSite-
TrEMBL Q8BJG7
UniProt Splice Variant
Entrez Gene 319953
UniGene Mm.427774
RefSeq
MGI ID
MGI Symbol Ttll1
OMIM
CCDS CCDS27702
HPRD
IMGT
EMBL AK031917 AK047046 AK084005 AK140472 AK168786 AK169150 AL583887 AL583889 BC010510
GenPept AAH10510 BAC27603 BAC32947 BAC39092 BAE24404 BAE40620 BAE40929

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