Version 5.4
Homo sapiens Protein: TMOD3
Summary
InnateDB Protein IDBP-12279.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol TMOD3
Protein Name tropomodulin 3 (ubiquitous)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000308753
InnateDB Gene IDBG-12277 (TMOD3)
Protein Structure
UniProt Annotation
Function Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). {ECO:0000250}.
Subcellular Localization Cytoplasm, cytoskeleton {ECO:0000250}.
Disease Associations
Tissue Specificity Ubiquitous. {ECO:0000269PubMed:10662549}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 46 experimentally validated interaction(s) in this database.
They are also associated with 3 interaction(s) predicted by orthology.
Experimentally validated
Total 46 [view]
Protein-Protein 44 [view]
Protein-DNA 2 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 3 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003779 actin binding
GO:0005523 tropomyosin binding
Biological Process
GO:0051694 pointed-end actin filament capping
Cellular Component
GO:0005865 striated muscle thin filament
Protein Structure and Domains
PDB ID
InterPro IPR004934 Tropomodulin
PFAM PF03250
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9NYL9
PhosphoSite PhosphoSite-Q9NYL9
TrEMBL H0YNU8
UniProt Splice Variant
Entrez Gene 29766
UniGene Hs.741713
RefSeq NP_055362
HUGO HGNC:11873
OMIM 605112
CCDS CCDS10145
HPRD 10389
IMGT
EMBL AC090971 AF177171 AF237631 AK312569 AL137543 BC020542
GenPept AAF31670 AAF45299 AAH20542 BAG35464 CAB70801

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