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General Information
Symbol
Dmel\His4
Species
D. melanogaster
Name
Histone H4
Annotation Symbol
Feature Type
FlyBase ID
FBgn0001200
Gene Model Status
Stock Availability
Gene Summary
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. (UniProt, P84040)
Contribute a Gene Snapshot for this gene.
Also Known As

H4, histone, core histone, histone 4, H4Ac16

Function
GO Summary Ribbons
Gene Ontology (GO) Annotations (8 terms)
Molecular Function (2 terms)
Terms Based on Experimental Evidence (0 terms)
Terms Based on Predictions or Assertions (2 terms)
CV Term
Evidence
References
enables DNA binding
inferred from electronic annotation with InterPro:IPR001951, InterPro:IPR019809
(assigned by InterPro )
inferred from electronic annotation with InterPro:IPR009072
(assigned by InterPro )
Biological Process (2 terms)
Terms Based on Experimental Evidence (1 term)
CV Term
Evidence
References
inferred from mutant phenotype
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
inferred from electronic annotation with InterPro:IPR004823
(assigned by InterPro )
Cellular Component (4 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
located_in chromosome
inferred from direct assay
inferred from direct assay
part_of RCAF complex
inferred from direct assay
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
part_of nucleosome
traceable author statement
inferred from electronic annotation with InterPro:IPR001951, InterPro:IPR019809
(assigned by InterPro )
Gene Group (FlyBase)
Protein Family (UniProt)
Belongs to the histone H4 family. (P84040)
Summaries
Protein Function (UniProtKB)
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.
(UniProt, P84040)
Summary (Interactive Fly)

Nucleosome component - core histone - acetylation of Histone H4 plays a positive role in promoting access of transcription factors to nucleosomal DNA - depletion of Histone deacetylase 3 antagonizes PI3K-mediated overgrowth through the acetylation of histone H4 at lysine 16 - H4 lysine 20 monomethyl mark, set by PR-Set7 and stabilized by L(3)mbt, is necessary for proper interphase chromatin organization

Gene Model and Products
Number of Transcripts
0
Number of Unique Polypeptides
0
Protein Domains (via Pfam)
Isoform displayed:
Pfam protein domains
InterPro name
classification
start
end
Protein Domains (via SMART)
Isoform displayed:
SMART protein domains
InterPro name
classification
start
end
Comments on Gene Model
Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Additional Transcript Data and Comments
Reported size (kB)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Polypeptides with Identical Sequences

 

Additional Polypeptide Data and Comments
Reported size (kDa)
Comments
External Data
Subunit Structure (UniProtKB)

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

(UniProt, P84040)
Post Translational Modification

Acetylated on Lys-6 and Lys-13 during prophase I of meiosis. Phosphorylation of H2A 'Thr-119' is a prerequisite for H4 Lys-6 acetylation but not for H4 Lys-13 acetylation.

(UniProt, P84040)
Linkouts
Sequences Consistent with the Gene Model
Nucleotide / Polypeptide Records
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\His4 using the Feature Mapper tool.

External Data
Crossreferences
Linkouts
Expression Data
Expression Summary Ribbons
Colored tiles in ribbon indicate that expression data has been curated by FlyBase for that anatomical location. Colorless tiles indicate that there is no curated data for that location.
For complete stage-specific expression data, view the modENCODE Development RNA-Seq section under High-Throughput Expression below.
Transcript Expression
Additional Descriptive Data
Marker for
 
Subcellular Localization
CV Term
Polypeptide Expression
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
organism | anterior

Comment: antibody specific to acylated protein

mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

His4 and His2A that was mono or poly acetylated is detected associated with nuclei of developing spermatids until late stages. During late spermatid development and in mature spermatazoa these proteins can no longer be detected (and are presumably replaced by sperm specific chromatin packaging proteins). However, shortly after fertilization His4 and His2A immunoreactivity reappears associated with the male pronuclear DNA.

Marker for
 
Subcellular Localization
CV Term
Evidence
References
located_in chromosome
inferred from direct assay
inferred from direct assay
part_of RCAF complex
inferred from direct assay
Expression Deduced from Reporters
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\His4 in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Alleles, Insertions, Transgenic Constructs, and Aberrations
Classical and Insertion Alleles ( 4 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 23 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of His4
Transgenic constructs containing regulatory region of His4
Aberrations (Deficiencies and Duplications) ( 3 )
Inferred from experimentation ( 3 )
Gene duplicated in
Inferred from location ( 0 )
    Alleles Representing Disease-Implicated Variants
    Phenotypes
    For more details about a specific phenotype click on the relevant allele symbol.
    Other Phenotypes
    Allele
    Phenotype manifest in
    Allele
    Orthologs
    Human Orthologs (via DIOPT v8.0)
    Homo sapiens (Human) (0)
    No records found.
    Model Organism Orthologs (via DIOPT v8.0)
    Mus musculus (laboratory mouse) (0)
    No records found.
    Rattus norvegicus (Norway rat) (0)
    No records found.
    Xenopus tropicalis (Western clawed frog) (0)
    No records found.
    Danio rerio (Zebrafish) (0)
    No records found.
    Caenorhabditis elegans (Nematode, roundworm) (0)
    No records found.
    Arabidopsis thaliana (thale-cress) (0)
    No records found.
    Saccharomyces cerevisiae (Brewer's yeast) (0)
    No records found.
    Schizosaccharomyces pombe (Fission yeast) (0)
    No records found.
    Ortholog(s) in Drosophila Species (via OrthoDB v9.1) ( None identified )
    No orthologies identified
    Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( None identified )
    No non-Drosophilid orthologies identified
    Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( None identified )
    No non-Dipteran orthologies identified
    Orthologs in non-Insect Arthropods (via OrthoDB v9.1) ( None identified )
    No non-Insect Arthropod orthologies identified
    Orthologs in non-Arthropod Metazoa (via OrthoDB v9.1) ( None identified )
    No non-Arthropod Metazoa orthologies identified
    Paralogs
    Paralogs (via DIOPT v8.0)
    Drosophila melanogaster (Fruit fly) (0)
    No records found.
    Human Disease Associations
    FlyBase Human Disease Model Reports
      Disease Model Summary Ribbon
      Disease Ontology (DO) Annotations
      Models Based on Experimental Evidence ( 0 )
      Allele
      Disease
      Evidence
      References
      Potential Models Based on Orthology ( 0 )
      Human Ortholog
      Disease
      Evidence
      References
      Modifiers Based on Experimental Evidence ( 0 )
      Allele
      Disease
      Interaction
      References
      Disease Associations of Human Orthologs (via DIOPT v8.0 and OMIM)
      Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
      Homo sapiens (Human)
      Gene name
      Score
      OMIM
      OMIM Phenotype
      DO term
      Complementation?
      Transgene?
      Functional Complementation Data
      Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
      Interactions
      Summary of Physical Interactions
      esyN Network Diagram
      Show neighbor-neighbor interactions:
      Select Layout:
      Legend:
      Protein
      RNA
      Selected Interactor(s)
      Interactions Browser

      Please see the Physical Interaction reports below for full details
      protein-protein
      Physical Interaction
      Assay
      References
      Summary of Genetic Interactions
      esyN Network Diagram
      esyN Network Key:
      Suppression
      Enhancement

      Please look at the allele data for full details of the genetic interactions
      Starting gene(s)
      Interaction type
      Interacting gene(s)
      Reference
      Starting gene(s)
      Interaction type
      Interacting gene(s)
      Reference
      External Data
      Subunit Structure (UniProtKB)
      The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
      (UniProt, P84040 )
      Linkouts
      DroID - A comprehensive database of gene and protein interactions.
      Pathways
      Signaling Pathways (FlyBase)
      Metabolic Pathways
      External Data
      Linkouts
      Genomic Location and Detailed Mapping Data
      Chromosome (arm)
      Recombination map
      2-55
      Cytogenetic map
      Sequence location
      FlyBase Computed Cytological Location
      Cytogenetic map
      Evidence for location
      39D3-39E1
      Left limit from in situ hybridisation (FBrf0029738) Right limit from molecular mapping relative to His2A (FBrf0044950)
      Experimentally Determined Cytological Location
      Cytogenetic map
      Notes
      References
      39D-39E
      (determined by in situ hybridisation)
      39D3-39E2
      (determined by in situ hybridisation)
      Experimentally Determined Recombination Data
      Location

      2-55

      Left of (cM)
      Right of (cM)
      Notes
      Stocks and Reagents
      Stocks (20)
      Genomic Clones (0)
       
        cDNA Clones (0)
         

        Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.

        cDNA clones, fully sequenced
        BDGP DGC clones
          Other clones
            Drosophila Genomics Resource Center cDNA clones

            For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.

              cDNA Clones, End Sequenced (ESTs)
              BDGP DGC clones
                Other clones
                  RNAi and Array Information
                  Linkouts
                  Antibody Information
                  Laboratory Generated Antibodies
                  Commercially Available Antibodies
                   
                  Cell Signaling Technology - Commercial vendor for primary antibodies and antibody conjugates.
                  Other Information
                  Relationship to Other Genes
                  Other Comments

                  Disruption of pr-set7 reduces levels of His4 K20 methylation. His4 K20 methylation does not correlate with gene activity.

                  Lysine-20-methylated His4 is localized to chromatin-dense and transcriptionally silent regions. There is an inverse correlation in the number and intensity of bands containing methyl His4-K20 and acetyl His4-K16. Methylation of His4 lysine 20 maintains silent chromatin, in part, by precluding neighbouring acetylation on the His4 tail.

                  Mutations in Iswi affect both cell viability and gene expression during development.

                  Replication-coupling assembly factor (RCAF) is a protein complex that facilitates the assembly of nucleosomes onto newly replicated DNA in vitro. RCAF is comprised of asf1, His3 and His4.

                  In male germ cells, acetylated His4 appears to correlate with the general activity state of the chromosome rather than to an X-specific dosage compensation mechanism. Loss of mle has no detectable effect on expression or localisation of acetylated His4.

                  The majority of replication-dependent histone gene transcripts are not polyadenylated and in addition two types of polyadenylated transcripts can be detected. A small proportion of the histone mRNAs bear a short poly(A) tail which is added to the 3' terminus of a partially degraded stem-loop structure. Polyadenylation signals can be located downstream of the stem-loop structure that can be used to generate mRNAs with a poly(A) tail.

                  The ATPase activity of Iswi is completely inhibited by each of the four histone tails (His2A, His2B, His3 and His4), results indicate a novel role for the flexible histone tails in chromatin remodeling by Iswi.

                  Male-specific lethal (MSL) proteins accumulate in a subregion of male nuclei (the X chromosome) beginning at late blastoderm stage. X chromosomal binding of the MSLs is observed throughout embryonic and larval development in both diploid and polytene tissues. His4 colocalises with the MSLs in embryos.

                  HIS4-Ac16 is bound to the polytene X chromosome, as seen by antibody staining.

                  Immunostaining of embryonic and larval stages demonstrates that His4, msl-1 and msl-3 are associated with the male X chromosome as early as gastrulation, while mle binding is not detected until the late embryonic/late larval stages.

                  His4 is first detected on the X chromosome at stage 8 following msl-2 expression.

                  Expression pattern and localisation of mle, msl-1, msl-2 and His4 proteins are determined and results suggest that the protein associated with the X chromosome and are interdependent since early embryogenesis.

                  Lys5 and Lys12 are utilised during deposition-related His4 diacetylation.

                  The gene products of mle, msl-1 bind to the male X chromosome in an identical pattern, and the binding sites of H4Ac16 acetylated form of the His4 product are largely coincident with the mle/msl-1 binding sites. This localisation of H4Ac16 protein is dependent on the dosage compensation regulatory pathway.

                  Both carnitine and butyrate compounds induce an accumulation of hyperacetylated H4 histones on chromatin.

                  Antisera to H4Ac16 label the euchromatic X chromosome through mitosis, but neither the X heterochromatin nor autosomes.

                  msl-1, like mle and H4Ac16 (an acetylated form of the His4 product), exhibits a wild type male localisation pattern in Sxl- XX nuclei.

                  His4 protein is preferentially acetylated on Lys12 by HatB in vitro.

                  The codon bias of the histone genes from D.melanogaster and D.hydei illustrates that the generalisation that abundantly expressed genes have a high codon bias and low rates of silent substitution does not hold for the histone genes.

                  The position of the homologous histone gene repeats within the nuclei of early embryo cells has been investigated. The two homologous histone gene clusters are distinct and separate through all stages of the cell cycle up to nuclear cycle 13. During interphase of cycle 14, the two clusters colocalise with high frequency, and move from near the midline of the nucleus towards the apical side.

                  TATA complex formation on the Hsp70Bb core promoter shows sequence dependence at the TATA element, at the transcription start site and further downstream. Similar interactions contribute to TATA complexes formed on the Hsp26 and His4 promoters.

                  DNA replication of the 5kb histone gene repeating unit in tissue culture cells (Drosophila Kc cells) initiates at multiple sites located within the repeating unit. Several replication pause sites are located at 5' upstream regions of some histone genes.

                  DNaseI footprinting analysis reveals core histones His2A, His2B, His3 and His4 (but not His1) bind to the kni, Kr and Ubx minimal enhancer elements in a periodic manner.

                  His4 protein isoforms acetylated at lysine residues 5, 8, 12, or 16 have been shown to have distinct patterns of distribution in interphase polytene chromosomes from larvae.

                  The pattern of His4 protein acetylation has been studied.

                  The genomic organisation of the histone genes in D.hydei closely resembles that of D.melanogaster.

                  The D.virilis core histone genes (Dvir\His2B, Dvir\His3, Dvir\His4 and Dvir\His2A), are arranged in the same order and orientation as the D.melanogaster core histone genes (His2B, His3, His4 and His2A). However, the His1 gene that is located between His2B and His3 in D.melanogaster is not found between Dvir\His2B and Dvir\His3 in D.virilis.

                  The expression of HIS-C genes, including His4, during oogenesis has been studied, and compared to periods of DNA synthesis and actin expression during this developmental stage.

                  4.8kb and 5.0kb repeats containing the histone genes His1, His2A, His2B, His3 and His4 are present in all of the more than 20 D.melanogaster strains studied. The strains differ in the relative amounts of the two repeat types, with the 5.0kb repeat always present in equal or greater amounts than the 4.8kb repeat. The strains also differ in a number of far less abundant fragments containing histone gene sequences.

                  Encodes Histone H4. See HIS-C record.

                  Origin and Etymology
                  Discoverer
                  Etymology
                  Identification
                  External Crossreferences and Linkouts ( 14 )
                  Sequence Crossreferences
                  GenBank Nucleotide - A collection of sequences from several sources, including GenBank, RefSeq, TPA, and PDB.
                  GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.
                  UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
                  Linkouts
                  Cell Signaling Technology - Commercial vendor for primary antibodies and antibody conjugates.
                  Cell Signaling Technology - Commercial vendor for primary antibodies and antibody conjugates.
                  DroID - A comprehensive database of gene and protein interactions.
                  FlyCyc Genes - Genes from a BioCyc PGDB for Dmel
                  Interactive Fly - A cyberspace guide to Drosophila development and metazoan evolution
                  Synonyms and Secondary IDs (19)
                  Reported As
                  Symbol Synonym
                  H4
                  (Chaouch and Lasko, 2021, Lu et al., 2021, Vidaurre and Chen, 2021, Arzate-Mejía et al., 2020, Bobkov et al., 2020, Medina-Pritchard et al., 2020, Miwa et al., 2020, Okimune et al., 2020, Samata et al., 2020, Walther et al., 2020, Wooten et al., 2020, Zhang et al., 2020, Chittori et al., 2019, Demirdizen et al., 2019, Morciano et al., 2019, Park et al., 2019, Roure et al., 2019, Thomas et al., 2019, Varga et al., 2019, Yang et al., 2019, Armstrong et al., 2018, Cheetham and Brand, 2018, Horard et al., 2018, Prudêncio et al., 2018, Rust et al., 2018, Šatović et al., 2018, Valsecchi et al., 2018, Zouaz et al., 2018, El-Sharnouby et al., 2017, Khuong et al., 2017, Kitevski-LeBlanc et al., 2017, Kolkhof et al., 2017, Liu and Grosshans, 2017, Ludwigsen et al., 2017, Ramachandran et al., 2017, Rowley et al., 2017, Theofel et al., 2017, Bayona-Feliu et al., 2016, Blasi et al., 2016, Boltengagen et al., 2016, Chlamydas et al., 2016, Doiguchi et al., 2016, Elnfati et al., 2016, Hirano et al., 2016, L Black et al., 2016, Nakashima et al., 2016, Penke et al., 2016, Zhou et al., 2016, Borsos et al., 2015, Comoglio et al., 2015, Edlich-Muth et al., 2015, Fei et al., 2015, Horard and Loppin, 2015, Kok et al., 2015, Liu and Zhang, 2015, Pengelly et al., 2015, Sun et al., 2015, Vlijm et al., 2015, Chen et al., 2014, Emelyanov et al., 2014, Figueiredo et al., 2014, Ho et al., 2014, Klinker et al., 2014, Kusch et al., 2014, Li et al., 2014, Messina et al., 2014, Mohan et al., 2014, Pascual-Garcia et al., 2014, Southall et al., 2014, Thomas et al., 2014, Alfieri et al., 2013, Crona et al., 2013, Ghezzi et al., 2013, Guglielmi et al., 2013, Hunt et al., 2013, Johnson et al., 2013, Kellner et al., 2013, Kockmann et al., 2013, Orsi et al., 2013, Pérez-Montero et al., 2013, Philip and Stenberg, 2013, Salzler et al., 2013, Stein et al., 2013, Sun et al., 2013, Wang et al., 2013, Xing et al., 2013, Yi et al., 2013, Zhou et al., 2013, Alekseyenko et al., 2012, Baradaran-Heravi et al., 2012, Bodai et al., 2012, Conrad et al., 2012, Conrad et al., 2012, Domanitskaya and Schüpbach, 2012, Dunlap et al., 2012, Fabian and Brill, 2012, Feller et al., 2012, Guertin et al., 2012, Hohl et al., 2012, Ito et al., 2012, Larschan et al., 2012, Leser et al., 2012, Lo et al., 2012, Lv et al., 2012, Meier et al., 2012, Petruk et al., 2012, Rincon-Arano et al., 2012, Sakaguchi et al., 2012, Vamos and Boros, 2012, Villar-Garea et al., 2012, Xie et al., 2012, Yang et al., 2012, Zhou et al., 2012, Burgio et al., 2011, Demakov et al., 2011, Dufourt et al., 2011, Egelhofer et al., 2011, Gibert and Karch, 2011, Kharchenko et al., 2011, Kim et al., 2011, Larschan et al., 2011, Li and Arnosti, 2011, Lorbeck et al., 2011, Morra et al., 2011, Nowak et al., 2011, Olszak et al., 2011, Regnard et al., 2011, Schmitges et al., 2011, Siudeja et al., 2011, Strukov et al., 2011, Vatolina et al., 2011, Vatolina et al., 2011, Anderson et al., 2010, Awe and Renkawitz-Pohl, 2010, Bell et al., 2010, Boyles et al., 2010, Deal et al., 2010, Dubruille et al., 2010, Gorchakov et al., 2010, Guertin and Lis, 2010, Huang et al., 2010, Kim et al., 2010, Lee et al., 2010, Lee et al., 2010, Macalpine et al., 2010, modENCODE Consortium et al., 2010, Moore et al., 2010, Orsi et al., 2010, Prestel et al., 2010, Raja et al., 2010, Sawatsubashi et al., 2010, Scheuermann et al., 2010, Schiemann et al., 2010, Spain et al., 2010, Yu et al., 2010, Zhang and Oliver, 2010, Zhang et al., 2010, Ciurciu et al., 2009, Gelbart et al., 2009, Gorchakov et al., 2009, Graham et al., 2009, Grimm et al., 2009, Kolesnikova et al., 2009, Kwon et al., 2009, Landmann et al., 2009, Morciano et al., 2009, Phalke et al., 2009, Plata et al., 2009, Scharf et al., 2009, Schwaiger et al., 2009, Sullivan et al., 2009, Ahlander et al., 2008, Bao et al., 2008, Birchler et al., 2008, Burgio et al., 2008, Cakouros et al., 2008, Ciurciu et al., 2008, Clapier et al., 2008, Deng et al., 2008, Fanti et al., 2008, Font-Burgada et al., 2008, Krajewski, 2008, Kulkarni-Shukla et al., 2008, Li et al., 2008, Liu et al., 2008, Martinez and Arnosti, 2008, Park et al., 2008, Sakaguchi et al., 2008, Song et al., 2008, Yang et al., 2008, Andreyeva et al., 2007, Behm-Ansmant et al., 2007, Beisel et al., 2007, Bell et al., 2007, Bonnefoy et al., 2007, Calvi et al., 2007, Camporeale et al., 2007, Corona et al., 2007, Dalal et al., 2007, Dalal et al., 2007, Demakova et al., 2007, Di Stefano et al., 2007, Fortini, 2007, Grewal and Elgin, 2007, Grimm et al., 2007, Han et al., 2007, Isogai et al., 2007, Jung and Bonini, 2007, Krejci and Bray, 2007, Park et al., 2007, Pindyurin et al., 2007, Pinnola et al., 2007, Prasanth and Spector, 2007, Rathke et al., 2007, Secombe et al., 2007, Tie et al., 2007, Yin and Lin, 2007, Birchler et al., 2006, Brasaemle and Hansen, 2006, Camporeale et al., 2006, Ciurciu et al., 2006, Deng and Meller, 2006, Deng and Meller, 2006, Furuhashi et al., 2006, Furuyama and Henikoff, 2006, Godfrey et al., 2006, Guelman et al., 2006, Guelman et al., 2006, Gunjan et al., 2006, Klymenko et al., 2006, Krishnamoorthy et al., 2006, Liu et al., 2006, Mendjan et al., 2006, Ni et al., 2006, Pal Bhadra et al., 2006, Papp and Muller, 2006, Pickersgill et al., 2006, Santoso and Kadonaga, 2006, Varga-Weisz and Becker, 2006, Wang et al., 2006, Wendt and Shilatifard, 2006, Zhang et al., 2006, Andreyeva et al., 2005, Canudas et al., 2005, Frydrychova et al., 2005, Hamada et al., 2005, Ivanovska et al., 2005, Karachentsev et al., 2005, Lusser et al., 2005, Pankotai et al., 2005, Spada et al., 2005, Spierer et al., 2005, Straub et al., 2005, Straub et al., 2005, Straub et al., 2005, Swaminathan et al., 2005, Aggarwal and Calvi, 2004, Aihara et al., 2004, Ebert et al., 2004, Fu et al., 2004, Gilfillan et al., 2004, Hartl et al., 2004, Karachentsev and Steward, 2004, Kusch et al., 2004, Kusch et al., 2004, Larsson et al., 2004, Lippman and Martienssen, 2004, Morales et al., 2004, Qi et al., 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                  Name Synonyms
                  Bicoid interacting protein 2
                  Secondary FlyBase IDs
                    Datasets (2)
                    Study focus (2)
                    Experimental Role
                    Project
                    Project Type
                    Title
                    • bait_protein
                    Genome-wide localization of histones and their modifications in cell lines by ChIP-chip and ChIP-Seq.
                    • bait_protein
                    Genome-wide localization of histones and their modifications in fly tissues by ChIP-chip and ChIP-Seq.
                    References (593)