Version 5.4
Homo sapiens Protein: ELP6
Summary
InnateDB Protein IDBP-31753.7
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ELP6
Protein Name chromosome 3 open reading frame 75
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000296149
InnateDB Gene IDBG-31749 (ELP6)
Protein Structure
UniProt Annotation
Function Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in cell migration.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 6 experimentally validated interaction(s) in this database.
Experimentally validated
Total 6 [view]
Protein-Protein 6 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
Biological Process
GO:0006325 chromatin organization
GO:0006351 transcription, DNA-templated
GO:0006355 regulation of transcription, DNA-templated
GO:0008150 biological_process
GO:0030335 positive regulation of cell migration
Cellular Component
GO:0033588 Elongator holoenzyme complex
Protein Structure and Domains
PDB ID
InterPro IPR018627 Uncharacterised protein family UPF0405
PFAM PF09807
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q0PNE2
PhosphoSite PhosphoSite-Q0PNE2
TrEMBL C9JLH5
UniProt Splice Variant
Entrez Gene 54859
UniGene
RefSeq NP_001026873
HUGO HGNC:25976
OMIM 615020
CCDS CCDS43082
HPRD 07884
IMGT
EMBL AC099778 AK000218 BC000623 BC014204 DQ787088
GenPept AAH00623 AAH14204 ABG79574 BAA91017

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