Version 5.4
Homo sapiens Protein: TMOD4
Summary
InnateDB Protein IDBP-102315.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol TMOD4
Protein Name tropomodulin 4 (muscle)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000295314
InnateDB Gene IDBG-102313 (TMOD4)
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.
Subcellular Localization Cytoplasm, cytoskeleton.
Disease Associations
Tissue Specificity Highly expressed in skeletal muscle. {ECO:0000269PubMed:10662549}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 5 experimentally validated interaction(s) in this database.
Experimentally validated
Total 5 [view]
Protein-Protein 5 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003779 actin binding
GO:0005523 tropomyosin binding
Biological Process
GO:0006936 muscle contraction
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 Q9NZQ9
PhosphoSite PhosphoSite-Q9NZQ9
TrEMBL Q5JR82
UniProt Splice Variant
Entrez Gene 29765
UniGene Hs.709681
RefSeq NP_037485
HUGO HGNC:11874
OMIM 605834
CCDS CCDS988
HPRD 16164
IMGT
EMBL AF165217 AF177173 AF321183 AF393375 AL592424 BC017810 CH471121
GenPept AAF01277 AAF31672 AAH17810 AAK06765 AAM73676 CAI16383 EAW53465

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