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General Information
Symbol
Dmel\His3
Species
D. melanogaster
Name
Histone H3
Annotation Symbol
Feature Type
FlyBase ID
FBgn0001199
Gene Model Status
Stock Availability
Also Known As
H3, histone, PH3, histone 3, Histone3
Function
GO Summary Ribbons
Protein Family (UniProt)
Belongs to the histone H3 family. (P02299)
Molecular Function (GO)
[Detailed GO annotations]
Experimental Evidence
-
Predictions / Assertions
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, P02299)
Summary (Interactive Fly)
Nucleosome component - core histone - Histone H3 Serine 28 is essential for efficient Polycomb-mediated gene repression - transposon silencing is a major developmental function of H3K9 - JIL-1 targets Histone H3 during dosage compensation
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, P02299)
Post Translational Modification
Phosphorylation at Ser-11 by ial/aurora-B during mitosis and meiosis is crucial for chromosome condensation and cell-cycle progression. Phosphorylation at Ser-11 by JIL-1 during interphase is linked to gene activation and restricts the formation of heterochromatin at inappropriate sites. Phosphorylation at Ser-11 is enriched on male X chromosome compared to the autosome. Acetylation is generally linked to gene activation. Acetylated on Lys-15 during prophase I of meiosis. Phosphorylation of H2A 'Thr-119' is a prerequisite for H3 Lys-15 acetylation. Acetylation on Lys-15 is enriched on male X chromosome compared to the autosome. Methylation at Lys-5 or Lys-80 is generally associated with active chromatin. Methylation at Lys-80 by gpp occurs at low levels in specific developmental stages and tissues undergoing active cell division, and at highest levels in epidermal cells undergoing differentiation.
(UniProt, P02299)
Crossreferences
InterPro - A database of protein families, domains and functional sites
Linkouts
Sequences Consistent with the Gene Model
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\His3 using the Feature Mapper tool.

External Data
Crossreferences
Linkouts
Gene Ontology (6 terms)
Molecular Function (2 terms)
Terms Based on Experimental Evidence (0 terms)
Terms Based on Predictions or Assertions (2 terms)
CV Term
Evidence
References
inferred from electronic annotation with InterPro:IPR000164, InterPro:IPR007125
(assigned by InterPro )
inferred from electronic annotation with InterPro:IPR009072
(assigned by InterPro )
Biological Process (0 terms)
Terms Based on Experimental Evidence (0 terms)
Terms Based on Predictions or Assertions (0 terms)
Cellular Component (5 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
colocalizes_with nuclear chromatin
inferred from direct assay
inferred from direct assay
inferred from direct assay
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
traceable author statement
inferred from electronic annotation with InterPro:IPR000164
(assigned by InterPro )
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
Polypeptide Expression
No Assay Recorded
Stage
Tissue/Position (including subcellular localization)
Reference
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
testis | apical

Comment: phosphorylated His3

Additional Descriptive Data
Phosphorylated His3 is observed in single cells close to the hub cell, and in 8-cell clusters displaced from the hub cells in the apical tip of the testis.
Antibodies against His3.3 protein stain uniformly over the polytene chromosomes. His3.3 protein staining is seen in meiotic prophase chromatin of primary spermatocytes. One or two strongly staining foci were observed in each nucleus. The distribution of label coincides with the location of some of the Y-chromosomal lampbrush loops. At this stage His3 protein is observed mainly in the autosomal chromatin. In postmeiotic stages, His3.3 protein is observed in the protein body while the His3 protein is found mainly in the chromatin. During spermatid elongation, His3.3 protein is deposited in chromatin. At subsequent stages no major differences were observed in the distribution of His3 protein and His3.3 protein. In post-elongation spermatid cysts, the pattern of staining changes from an even distribution to a dispersed pattern. In mature sperm, no staining is observed.
Marker for
Subcellular Localization
CV Term
Evidence
References
colocalizes_with nuclear chromatin
inferred from direct assay
inferred from direct assay
inferred from direct assay
Expression Deduced from Reporters
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\His3 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
Linkouts
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
Images
Alleles, Insertions, and Transgenic Constructs
Classical and Insertion Alleles ( 3 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 37 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of His3
Transgenic constructs containing regulatory region of His3
Deletions and Duplications ( 3 )
Phenotypes
Orthologs
Human Orthologs (via DIOPT v7.1)
Homo sapiens (Human) (0)
No records found.
Model Organism Orthologs (via DIOPT v7.1)
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.
Orthologs 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 v7.1)
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
    Comments on Models/Modifiers Based on Experimental Evidence ( 0 )
     
    Disease Associations of Human Orthologs (via DIOPT v7.1 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
    RNA-protein
    Physical Interaction
    Assay
    References
    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, P02299 )
    Linkouts
    DroID - A comprehensive database of gene and protein interactions.
    Pathways
    Gene Group - Pathway Membership (FlyBase)
    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 (16)
    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 sequences
      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
                Source for database identify of
                Source for database merge of
                Source for merge of: His3 anon-WO0118547.10
                Encoded by
                Additional comments
                Source for merge of His3 anon-WO0118547.10 was sequence comparison ( date:051113 ).
                Other Comments
                The canonical "H3.2" histone (His3, present in multiple copies in the genome as part of the repeating histone gene unit) and variant "His3.3" histone (encoded by His3.3A and His3.3B) forms can functionally replace each other. Cells are able to divide and differentiate when H3.2 is entirely absent but is replaced by S phase-expressed His3.3.
                Cells that contain a non-methylatable residue instead of K4 in all canonical and variant H3 genes are competent to respond to major developmental signaling pathways by activating target gene expression, although their proliferative capacity is slowed down relative to wild type.
                Genomic sites of H3K4Me3 and H3K27Me3 assayed in 0-12 hr. embryos; H3K4Me3 also assayed in S2 and Kc cells. See experiments listed under "Samples" at GEO: 16245 (http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE16245).
                Nucleosomes containing His3.3A protein but not His3 protein are specifically assembled in paternal chromatin before the first round of DNA replication in the fertilised egg.
                Extrachromosomal circular DNA (eccDNA) is present throughout the fly's life cycle. The eccDNA population contains circular multimers of tandemly repeated genes, including His3.
                Area matching Drosophila Histone H3 gene, Acc. No. AB003784.
                Methyl-K9 His3 protein and Su(var)205 protein co-localise to the heterochromatic region of polytene chromosomes.
                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.
                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.
                Transcription complexes containing gro may associate with the amino terminus of His3 and these interactions may be propogated along the chromosomes due to the ability of gro to participate in higher order structures.
                RNA polymerase pauses on the Hsp70Bb and His3 promoters in a nuclear extract derived from embryos.
                Distinct specific subsets of lysines are utilised during deposition-related His4 diacetylation.
                The TFIID complex interacts with the promoter of His3 making contacts at the TATA element, initiator, +18 and +28 regions.
                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.
                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.
                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.
                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-3. See HIS-C record.
                Origin and Etymology
                Discoverer
                Etymology
                Identification
                External Crossreferences and Linkouts ( 37 )
                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
                Other crossreferences
                InterPro - A database of protein families, domains and functional sites
                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.
                FLIGHT - Cell culture data for RNAi and other high-throughput technologies
                Interactive Fly - A cyberspace guide to Drosophila development and metazoan evolution
                Synonyms and Secondary IDs (46)
                Reported As
                Symbol Synonym
                H3
                (Arya et al., 2019, Cakouros and Gronthos, 2019, Chen et al., 2019, De et al., 2019, Dorafshan et al., 2019, Lee et al., 2019, Liu et al., 2019, Morciano et al., 2019, Park et al., 2019, Radion et al., 2019, Soffers et al., 2019, Yang et al., 2019, Akulenko et al., 2018, Clémot et al., 2018, De et al., 2018, Fedoseeva et al., 2018, Joos et al., 2018, Li et al., 2018, Lu et al., 2018, Ma et al., 2018, Masuko et al., 2018, Penke et al., 2018, Sadasivam and Huang, 2018, Šatović et al., 2018, Skrajna et al., 2018, Tsui et al., 2018, Wang et al., 2018, Warecki and Sullivan, 2018, Zheng et al., 2018, Berson et al., 2017, Boija et al., 2017, Chan et al., 2017, Colmenares et al., 2017, El-Sharnouby et al., 2017, Fromental-Ramain et al., 2017, Khuong et al., 2017, Kitevski-LeBlanc et al., 2017, Li et al., 2017, Liu and Grosshans, 2017, Morgan et al., 2017, Ramachandran et al., 2017, Rowley et al., 2017, Sen et al., 2017, Tencer et al., 2017, Theofel et al., 2017, Urban et al., 2017, Akan et al., 2016, Basu et al., 2016, Bayona-Feliu et al., 2016, Chlamydas et al., 2016, Elnfati et al., 2016, Gajan et al., 2016, Hirano et al., 2016, Huang et al., 2016, Kahn et al., 2016, Kavi et al., 2016, Kwon et al., 2016, L Black et al., 2016, Nakashima et al., 2016, Ozawa et al., 2016, Peng et al., 2016, Shih et al., 2016, Völker-Albert et al., 2016, Wike et al., 2016, Xia et al., 2016, Zhou et al., 2016, Borsos et al., 2015, Comoglio et al., 2015, Dietz et al., 2015, Edlich-Muth et al., 2015, Eisert et al., 2015, Fei et al., 2015, Gatchalian et al., 2015, Kang et al., 2015, Kok et al., 2015, Lee, 2015, Lindehell et al., 2015, Liu and Zhang, 2015, Merkling et al., 2015, Pengelly et al., 2015, Pu et al., 2015, Stephenson et al., 2015, Vlijm et al., 2015, Welch et al., 2015, Yu et al., 2015, Yung et al., 2015, Zaballos et al., 2015, Afonso et al., 2014, Alekseyenko et al., 2014, Alkhori et al., 2014, Azzaz et al., 2014, Bowman et al., 2014, Chen et al., 2014, Emelyanov et al., 2014, Frost et al., 2014, Garreau-Balandier et al., 2014, Herz et al., 2014, Ho et al., 2014, Huang et al., 2014, Jeibmann et al., 2014, Klinker et al., 2014, Kusch et al., 2014, Lee et al., 2014, Le Thomas et al., 2014, Liang et al., 2014, Li et al., 2014, Liu et al., 2014, Maksimenko et al., 2014, Messina et al., 2014, Mohan et al., 2014, Mohn et al., 2014, Mulvey et al., 2014, Oliva et al., 2014, Ost et al., 2014, Pascual-Garcia et al., 2014, Patel et al., 2014, Satyaki et al., 2014, Seridi et al., 2014, Thomas et al., 2014, Tie et al., 2014, Zaytseva et al., 2014, Zhang et al., 2014, Bonnay et al., 2013, Cane et al., 2013, Chauhan et al., 2013, Chen et al., 2013, Copur and Müller, 2013, Crona et al., 2013, Darbo et al., 2013, Dönertas et al., 2013, Dorighi and Tamkun, 2013, Doyen et al., 2013, Gaur et al., 2013, Guglielmi et al., 2013, He and Noll, 2013, Huang et al., 2013, Hunt et al., 2013, Iovino et al., 2013, Januschke et al., 2013, Kellner et al., 2013, Le Thomas et al., 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2012, Cui et al., 2012, Domanitskaya and Schüpbach, 2012, Dunlap et al., 2012, Fasulo et al., 2012, Fedoseeva et al., 2012, Feller et al., 2012, Gomez et al., 2012, Gurudatta et al., 2012, Gutiérrez et al., 2012, Hallson et al., 2012, Herz et al., 2012, Hohl et al., 2012, Hou et al., 2012, Ito et al., 2012, Jemc et al., 2012, Kim et al., 2012, Larson et al., 2012, Li et al., 2012, Lin et al., 2012, Lloret-Llinares et al., 2012, Maheshwari and Barbash, 2012, Meier et al., 2012, Monk et al., 2012, Moraru et al., 2012, Moshkin et al., 2012, Nakayama et al., 2012, Nowak et al., 2012, Park et al., 2012, Petruk et al., 2012, Poernbacher et al., 2012, Popkova et al., 2012, Pushpavalli et al., 2012, Rincon-Arano et al., 2012, Schneiderman et al., 2012, Schwartz et al., 2012, Sentmanat and Elgin, 2012, Sienski et al., 2012, Stepanik and Harte, 2012, Suyari et al., 2012, Tie et al., 2012, Tran et al., 2012, Ulvklo et al., 2012, Vamos and Boros, 2012, Van Bortle et al., 2012, Venkei et al., 2012, 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                anon-WO0118547.10
                Name Synonyms
                Phospho histone 3
                histone H3
                (Huang et al., 2016, Kavi et al., 2016, Liaw, 2016, Tie et al., 2016, Wike et al., 2016, Borsos et al., 2015, Merkling et al., 2015, Stephenson et al., 2015, Hamada-Kawaguchi et al., 2014, Jeibmann et al., 2014, Roy et al., 2014, Britton et al., 2013, Dorighi and Tamkun, 2013, Rai et al., 2013, Xie et al., 2013, Chauhan et al., 2012, Kellner et al., 2012, Radman-Livaja et al., 2012, Eliazer et al., 2011, Endo et al., 2011, Garcia and Stathopoulos, 2011, Kondo and Perrimon, 2011, Lee et al., 2011, Li and Arnosti, 2011, Li et al., 2011, Moiseeva and Tchurikov, 2011, Schmitges et al., 2011, Viktorin et al., 2011, Wang and Elgin, 2011, Wang et al., 2011, Willecke et al., 2011, Buchon et al., 2010, Bulchand et al., 2010, Chioda et al., 2010, Forero et al., 2010, Gou et al., 2010, Hartman et al., 2010, Li et al., 2010, Meyer et al., 2010, Podhraski et al., 2010, Richardson and Pichaud, 2010, Swaminathan and Pile, 2010, Torras-Llort et al., 2010, Benoit et al., 2009, Buchon et al., 2009, Buszczak et al., 2009, Chatterjee and Ip, 2009, Epstein et al., 2009, Fang et al., 2009, Gambetta et al., 2009, Graham et al., 2009, Insco et al., 2009, Jiang and Edgar, 2009, Khan et al., 2009, Margueron et al., 2009, Patalano et al., 2009, Peng and Karpen, 2009, Romani et al., 2009, Sahota et al., 2009, Yokoyama et al., 2009, Alekseyenko et al., 2008, Bao et al., 2008, Bello et al., 2008, Boone and Doe, 2008, Cakouros et al., 2008, Cheng et al., 2008, Ciurciu et al., 2008, Cryderman et al., 2008, Emberly et al., 2008, Erclik et al., 2008, Fiedler et al., 2008, Gilchrist et al., 2008, Hauenschild et al., 2008, Joshi et al., 2008, Kaplow et al., 2008, Kurzhals et al., 2008, Lagarou et al., 2008, Leatherman and DiNardo, 2008, Lin et al., 2008, Lloret-Llinares et al., 2008, Mehrotra et al., 2008, Nishimura et al., 2008, Petesch and Lis, 2008, Rimkus et al., 2008, Shi et al., 2008, Song et al., 2008, Wen et al., 2008, Abdu et al., 2007, Bhadra et al., 2007, Brunk et al., 2007, Budde, 2007, Calvi et al., 2007, Ferreira et al., 2007, Griffis et al., 2007, Hyllus et al., 2007, Jacquier et al., 2007, Johnston et al., 2007, Klenov et al., 2007, Lipsick et al., 2007, Manak et al., 2007, Moshkin et al., 2007, Ou et al., 2007, Parker et al., 2007, Pindyurin et al., 2007, Rathke et al., 2007, Rathke et al., 2007, Ringrose and Paro, 2007, Schuettengruber et al., 2007, Seum et al., 2007, Seum et al., 2007, Smolik and Jones, 2007, Song et al., 2007, Tie et al., 2007, Aguilar-Fuentes et al., 2006, Axelson, 2006, Bao et al., 2006, Bello et al., 2006, Cavalli, 2006, Chang et al., 2006, Eissenberg, 2006, Ellis, 2006, Foglietti et al., 2006, Guelman et al., 2006, Horner et al., 2006, Johansen and Johansen, 2006, Maeda and Karch, 2006, Muller and Kassis, 2006, Nakayama et al., 2006, Petruk et al., 2006, Pickersgill et al., 2006, Schubeler, 2006, Tenney et al., 2006, Willard et al., 2006, Yasuhara and Wakimoto, 2006, Carre et al., 2005, Caussinus and Gonzalez, 2005, De Lucia et al., 2005, Dunleavy et al., 2005, Jin, 2005, Ketel et al., 2005, Oliveira et al., 2005, Pankotai et al., 2005, Siegrist and Doe, 2005, Zhao et al., 2005, Zhou, 2005, Lanzotti et al., 2004, Lund and van Lohuizen, 2004, McHugh et al., 2004, Pollock et al., 2004, Ringrose et al., 2004, Smith et al., 2004, Azzouz and Schumperli, 2003, Breiling et al., 2003, Carrera et al., 2003, Fischle et al., 2003, Martin and St. Johnston, 2003, Min et al., 2003, Murphy, 2003, Wasser and Chia, 2003, Lanzotti et al., 2002, Moshkin et al., 2002, Odden et al., 2002, Krause et al., 2001, Irion and Leptin, 1999, Houston et al., 1998)
                phospho-Histone H3
                phosphorylated histone H3
                phosphorylated histone-H3
                replication-dependent histone 3
                Secondary FlyBase IDs
                • FBgn0062243
                Datasets (6)
                Study focus (6)
                Experimental Role
                Project
                Project Type
                Title
                • bait_protein
                ChIP-Seq profiling of histone modifications in purified embryonic mesodermal cells.
                • transgene_used
                Protein profiling reveals five principal chromatin types in Drosophila cells.
                • 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.
                • bait_protein
                Genome-wide localization of histone modifications by ChIP-chip and ChIP-Seq.
                • bait_protein
                Genome-wide localization of chromatin factors by ChIP-chip and ChIP-Seq.
                References (1,370)