Version 5.4
Homo sapiens Protein: TTL
Summary
InnateDB Protein IDBP-66275.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol TTL
Protein Name tubulin tyrosine ligase
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000233336
InnateDB Gene IDBG-66273 (TTL)
Protein Structure
UniProt Annotation
Function Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin. {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
Experimentally validated
Total 1 [view]
Protein-Protein 0
Protein-DNA 0
Protein-RNA 1 [view]
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0004835 tubulin-tyrosine ligase activity
GO:0005524 ATP binding
Biological Process
GO:0000226 microtubule cytoskeleton organization
GO:0006464 cellular protein modification process
GO:0030516 regulation of axon extension
Cellular Component
Protein Structure and Domains
PDB ID
InterPro IPR004344 Tubulin-tyrosine ligase/Tubulin polyglutamylase
PFAM PF03133
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8NG68
PhosphoSite PhosphoSite-Q8NG68
TrEMBL
UniProt Splice Variant
Entrez Gene 150465
UniGene Hs.620364
RefSeq NP_714923
HUGO HGNC:21586
OMIM 608291
CCDS CCDS2096
HPRD 12206
IMGT
EMBL AB071393 AC012442 BC036819 BX538316 CH471217
GenPept AAH36819 AAX81998 BAC06832 CAD98091 EAW73589

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