Version 5.4
Mus musculus Protein: Trrap
Summary
InnateDB Protein IDBP-533941.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Trrap
Protein Name transformation/transcription domain-associated protein
Synonyms AI481500;
Species Mus musculus
Ensembl Protein ENSMUSP00000115917
InnateDB Gene IDBG-208186 (Trrap)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 8 experimentally validated interaction(s) in this database.
They are also associated with 90 interaction(s) predicted by orthology.
Experimentally validated
Total 8 [view]
Protein-Protein 8 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 90 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003713 transcription coactivator activity
Biological Process
GO:0006355 regulation of transcription, DNA-templated
GO:0007093 mitotic cell cycle checkpoint
GO:0016578 histone deubiquitination
GO:0043967 histone H4 acetylation
GO:0043968 histone H2A acetylation
Cellular Component
GO:0000123 histone acetyltransferase complex
GO:0005667 transcription factor complex
GO:0030914 STAGA complex
GO:0033276 transcription factor TFTC complex
GO:0035267 NuA4 histone acetyltransferase complex
Protein Structure and Domains
PDB ID MGI:2153272
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL D3YY11
UniProt Splice Variant
Entrez Gene 100683
UniGene Mm.273570
RefSeq
MGI ID
MGI Symbol Trrap
OMIM
CCDS
HPRD
IMGT
EMBL AC113295 AC131728
GenPept

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