Version 5.4
Homo sapiens Protein: TTLL3
Summary
InnateDB Protein IDBP-362003.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol TTLL3
Protein Name tubulin tyrosine ligase-like family, member 3
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000403874
InnateDB Gene IDBG-235749 (TTLL3)
Protein Structure
UniProt Annotation
Function Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. {ECO:0000269PubMed:19524510}.
Subcellular Localization Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, cilium {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 2 experimentally validated interaction(s) in this database.
Experimentally validated
Total 2 [view]
Protein-Protein 1 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0070735 protein-glycine ligase activity
GO:0070736 protein-glycine ligase activity, initiating
Biological Process
GO:0006464 cellular protein modification process
GO:0018094 protein polyglycylation
GO:0035082 axoneme assembly
GO:0042384 cilium assembly
Cellular Component
GO:0005874 microtubule
GO:0005929 cilium
GO:0005930 axoneme
GO:0015630 microtubule cytoskeleton
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 Q9Y4R7
PhosphoSite PhosphoSite-Q9Y4R7
TrEMBL
UniProt Splice Variant
Entrez Gene 26140
UniGene Hs.726435
RefSeq
HUGO HGNC:24483
OMIM
CCDS
HPRD 15585
IMGT
EMBL AC022382 AF078842 AK023960 AL096725 AL833939 BC098298 BC098361 BC099735 BC105638 BX648175
GenPept AAF23353 AAH98298 AAH98361 AAH99735 AAI05639 BAB14741 CAB46375 CAD38794 CAH10554

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