Version 5.4
Bos taurus Protein: H2AFJ
Summary
InnateDB Protein IDBP-701150.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol H2AFJ
Protein Name Histone H2A.J
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000040641
InnateDB Gene IDBG-648402 (H2AFJ)
Protein Structure
UniProt Annotation
Function Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular Localization Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003677 DNA binding
GO:0043565 sequence-specific DNA binding
GO:0046982 protein heterodimerization activity
Biological Process
GO:0006334 nucleosome assembly
Cellular Component
GO:0000786 nucleosome
GO:0005622 intracellular
GO:0005634 nucleus
GO:0005694 chromosome
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR002119 Histone H2A
IPR003958 Transcription factor CBF/NF-Y/archaeal histone
IPR007125 Histone core
IPR009072 Histone-fold
PFAM PF00808
PF00125
PRINTS PR00620
PIRSF
SMART SM00414
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3ZBX9
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 618489
UniGene Bt.49615
RefSeq NP_001071557
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC103043
GenPept AAI03044

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