Version 5.4
Mus musculus Protein: Kansl2
Summary
InnateDB Protein IDBP-274217.7
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Kansl2
Protein Name RIKEN cDNA 2310037I24 gene
Synonyms 2310037I24Rik; B930009D17;
Species Mus musculus
Ensembl Protein ENSMUSP00000112101
InnateDB Gene IDBG-180403 (Kansl2)
Protein Structure
UniProt Annotation
Function As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. {ECO:0000250}.
Subcellular Localization Nucleus {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 3 experimentally validated interaction(s) in this database.
They are also associated with 2 interaction(s) predicted by orthology.
Experimentally validated
Total 3 [view]
Protein-Protein 3 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0043995 histone acetyltransferase activity (H4-K5 specific)
GO:0043996 histone acetyltransferase activity (H4-K8 specific)
GO:0046972 histone acetyltransferase activity (H4-K16 specific)
Biological Process
GO:0043981 histone H4-K5 acetylation
GO:0043982 histone H4-K8 acetylation
GO:0043984 histone H4-K16 acetylation
Cellular Component
GO:0000123 histone acetyltransferase complex
Protein Structure and Domains
PDB ID MGI:1916862
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8BQR4
PhosphoSite PhosphoSite-Q8BQR4
TrEMBL
UniProt Splice Variant
Entrez Gene 69612
UniGene Mm.470221
RefSeq NP_598475
MGI ID
MGI Symbol Kansl2
OMIM
CCDS CCDS37190
HPRD
IMGT
EMBL AK009662 AK046649 AK046983 AK047269 AK167429 BC003301 BC083325 BC092275 BC125631 BC125633
GenPept AAH03301 AAH83325 AAH92275 AAI25632 AAI25634 BAC25264 BAC32821 BAC32935 BAC33009 BAE39517

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