Version 5.4
Mus musculus Protein: Yeats2
Summary
InnateDB Protein IDBP-249352.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Yeats2
Protein Name YEATS domain containing 2
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000111222
InnateDB Gene IDBG-143426 (Yeats2)
Protein Structure
UniProt Annotation
Function Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. {ECO:0000250}.
Subcellular Localization Nucleus {ECO:0000305}.
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 20 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 20 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0017025 TBP-class protein binding
Biological Process
GO:0000122 negative regulation of transcription from RNA polymerase II promoter
GO:0006355 regulation of transcription, DNA-templated
GO:0043966 histone H3 acetylation
GO:0045892 negative regulation of transcription, DNA-templated
Cellular Component
GO:0005634 nucleus
GO:0005671 Ada2/Gcn5/Ada3 transcription activator complex
GO:0072686 mitotic spindle
Protein Structure and Domains
PDB ID MGI:2447762
InterPro IPR005033 YEATS
PFAM PF03366
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3TUF7
PhosphoSite PhosphoSite-Q3TUF7
TrEMBL B9EKJ4
UniProt Splice Variant
Entrez Gene 208146
UniGene Mm.396508
RefSeq NP_001139403
MGI ID
MGI Symbol Yeats2
OMIM
CCDS CCDS49790
HPRD
IMGT
EMBL AK122463 AK160791 BC042768 BC057045 BC150944
GenPept AAH42768 AAH57045 AAI50945 BAC65745 BAE36014

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