FB2024_02 , released April 23, 2024
Gene: Dmel\His3
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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
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, P02299)
Contribute a Gene Snapshot for this gene.
Also Known As

H3, histone, PH3, histone 3, dH3

Function
Gene Ontology (GO) Annotations (10 terms)
Molecular Function (5 terms)
Terms Based on Experimental Evidence (1 term)
CV Term
Evidence
References
inferred from physical interaction with UniProtKB:Q9V464
Terms Based on Predictions or Assertions (4 terms)
CV Term
Evidence
References
enables DNA binding
inferred from electronic annotation with InterPro:IPR000164, InterPro:IPR007125
inferred from sequence or structural similarity with UniProtKB:P84243
Biological Process (1 term)
Terms Based on Experimental Evidence (0 terms)
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
inferred from sequence or structural similarity with UniProtKB:P84243
Cellular Component (5 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
part_of chromatin
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
inferred from electronic annotation with InterPro:IPR000164
inferred from sequence or structural similarity with UniProtKB:P84243
Gene Group (FlyBase)
Protein Family (UniProt)
Belongs to the histone H3 family. (P02299)
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
Structure
Protein 3D structure   (Predicted by AlphaFold)   (AlphaFold entry P02299)

If you don't see a structure in the viewer, refresh your browser.
Model Confidence:
  • Very high (pLDDT > 90)
  • Confident (90 > pLDDT > 70)
  • Low (70 > pLDDT > 50)
  • Very low (pLDDT < 50)

AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.

Experimentally Determined Structures
Crossreferences
PDB - An information portal to biological macromolecular structures
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. Interacts (via N-terminus di- or tri-methylated on Lys-10 (H3K9me2/3)) with rhi (via Chromo domain); this interaction is direct (PubMed:24906153, PubMed:25085419).

(UniProt, P02299)
Post Translational Modification

Phosphorylated at Thr-4 (H3T3ph) by Haspin during mitosis and interphase (PubMed:32750047). Phosphorylation at Ser-11 by aurB/ial during mitosis and meiosis is crucial for chromosome condensation and cell-cycle progression (PubMed:11114889, PubMed:11266459, PubMed:11371341, PubMed:12514098, PubMed:15175259). 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 (PubMed:11114889, PubMed:11266459, PubMed:11371341, PubMed:12514098, PubMed:15175259).

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 (PubMed:14732680, PubMed:15175259, PubMed:15371351). Tri-methylation at Lys-10 (H3K9me3) is generally associated with transcriptional repression (Probable). Tri-methylation at Lys-10 (H3K9me3) is partly stimulated at specific chromatin loci by homologous piRNAs (PubMed:25085419). Tri-methylation at Lys-10 (H3K9me3) stimulates recruitment of the Rhino-Deadlock-Cutoff (RDC) complex to promote piRNA biogenesis (PubMed:24906153, PubMed:25085419).

(UniProt, P02299)
Crossreferences
InterPro - A database of protein families, domains and functional sites
PDB - An information portal to biological macromolecular structures
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
Expression Data
Testis-specificity index

The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).

NA

Transcript Expression
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

His3 is strongly expressed in the embryonic anterior midgut at stage 13 and is downregulated by stage 14.

Maternal His3 mRNA is deposited in eggs; most has degraded by embryonic stage 5. Zygotic expression begins at embryonic cycle 14. His3 transcript is expressed in mitotic domains at later stages.

Marker for
Subcellular Localization
CV Term
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
part_of chromatin
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

JBrowse - Visual display of RNA-Seq signals

View Dmel\His3 in JBrowse
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 ( 3 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 68 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of His3
Transgenic constructs containing regulatory region of His3
Aberrations (Deficiencies and Duplications) ( 3 )
Inferred from experimentation ( 3 )
Gene duplicated in
Inferred from location ( 0 )
    Variants
    Variant Molecular Consequences
    Alleles Representing Disease-Implicated Variants
    Phenotypes
    Orthologs
    Human Orthologs (via DIOPT v9.1)
    Species\Gene Symbol
    Score
    Best Score
    Best Reverse Score
    Alignment
    Complementation?
    Transgene?
    Homo sapiens (Human) (0)
    Model Organism Orthologs (via DIOPT v9.1)
    Species\Gene Symbol
    Score
    Best Score
    Best Reverse Score
    Alignment
    Complementation?
    Transgene?
    Rattus norvegicus (Norway rat) (0)
    Mus musculus (laboratory mouse) (0)
    Xenopus tropicalis (Western clawed frog) (0)
    Danio rerio (Zebrafish) (0)
    Caenorhabditis elegans (Nematode, roundworm) (0)
    Anopheles gambiae (African malaria mosquito) (0)
    Arabidopsis thaliana (thale-cress) (0)
    Saccharomyces cerevisiae (Brewer's yeast) (0)
    Schizosaccharomyces pombe (Fission yeast) (0)
    Escherichia coli (enterobacterium) (0)
    Other Organism Orthologs (via OrthoDB)
    Data provided directly from OrthoDB:His3. Refer to their site for version information.
    Paralogs
    Paralogs (via DIOPT v9.1)
    Human Disease Associations
    FlyBase Human Disease Model Reports
      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 v9.1 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:
      Show/hide secondary interactors 
      (data from AllianceMine provided by esyN)
      Select Layout:
      Legend:
      Protein
      RNA
      Selected Interactor(s)
      Interactions Browser

      Please see the Physical Interaction reports below for full details
      MIST Molecular Interaction Search Tool

      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
      Show/hide secondary interactors 
      (data from AllianceMine provided by esyN)
      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. Interacts (via N-terminus di- or tri-methylated on Lys-10 (H3K9me2/3)) with rhi (via Chromo domain); this interaction is direct (PubMed:24906153, PubMed:25085419).
      (UniProt, P02299 )
      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 (22)
      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 JBrowse 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 Line Information
                  Publicly Available Cell Lines
                   
                    Other Stable Cell Lines
                     
                    • New stable cell line derived from S2-unspecified : Stable cell lines expressing GFP-Rz-His3 (Rz is the hammerhead-ribozyme-based mRNA reporter that produces nonstop mRNA fragments) or GFP-His3 were established. A stable cell line that expresses GFP-ptc-His3 under the control of the Act5C promoter was created.

                    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.

                    Relationship to Other Genes
                    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 ).

                    Nomenclature History
                    Source for database identify of
                    Nomenclature comments
                    Etymology
                    Synonyms and Secondary IDs (49)
                    Reported As
                    Symbol Synonym
                    H3
                    (Corcoran and Jacob, 2023, Emerson and Lee, 2023, Erokhin et al., 2023, Erokhin et al., 2023, Gleason and Chen, 2023, Godneeva et al., 2023, Han et al., 2023, Hodkinson et al., 2023, Iki et al., 2023, Jangam et al., 2023, Jin et al., 2023, Lundkvist et al., 2023, Tirgar et al., 2023, Weaver et al., 2023, Wu et al., 2023, Yang et al., 2023, Zhang et al., 2023, Zhang et al., 2023, Zhao et al., 2023, Darnat et al., 2022, Huang et al., 2022, Lan and Liao, 2022, Ranjan and Chen, 2022, Ranjan and Chen, 2022, Richards et al., 2022, Shindo et al., 2022, Torres-Campana et al., 2022, Urban et al., 2022, Wu and Yan, 2022, Akkouche et al., 2021, Aleman et al., 2021, Casale et al., 2021, Cenik and Shilatifard, 2021, Chaouch and Lasko, 2021, Eastwood et al., 2021, Endo et al., 2021, Ghotbi et al., 2021, Kalashnikova et al., 2021, Khan et al., 2021, Llorens-Giralt et al., 2021, Lu et al., 2021, Matsuo, 2021, Nichols and Corces, 2021, Okimune et al., 2021, Onishi et al., 2021, Palmateer et al., 2021, Peterson et al., 2021, Potter-Birriel et al., 2021, Regadas et al., 2021, Schnabl et al., 2021, Torres-Zelada and Weake, 2021, Usik et al., 2021, Vidaurre and Chen, 2021, Adashev et al., 2020, Alabert et al., 2020, Albanese et al., 2020, Arzate-Mejía et al., 2020, Bender, 2020, Bobkov et al., 2020, Cacchione et al., 2020, Carty and Dunleavy, 2020, De et al., 2020, DeLuca et al., 2020, Demakova et al., 2020, Fresán et al., 2020, Fursova et al., 2020, Ghotbi et al., 2020, Heurteau et al., 2020, Koreski et al., 2020, Kuroda et al., 2020, Lepesant et al., 2020, Liu et al., 2020, Meyer-Nava et al., 2020, Miwa et al., 2020, Mugat et al., 2020, Ninova et al., 2020, Ninova et al., 2020, Okimune et al., 2020, Parhad et al., 2020, Park and Kim, 2020, Saint-Leandre et al., 2020, Santana et al., 2020, Sato and Siomi, 2020, Tsai et al., 2020, Vizcaya-Molina et al., 2020, Walther et al., 2020, Wooten et al., 2020, Zhu and Belden, 2020, Zraly et al., 2020, Ahmad and Spens, 2019, Akhtar et al., 2019, Albig et al., 2019, Arya et al., 2019, Boileau et al., 2019, Bonnet et al., 2019, Cakouros and Gronthos, 2019, Chen et al., 2019, Chittori et al., 2019, De et al., 2019, Delandre and Marshall, 2019, Demirdizen et al., 2019, Dorafshan et al., 2019, Kuhn et al., 2019, Lee et al., 2019, Liu et al., 2019, Morciano et al., 2019, Nakamura et al., 2019, Park et al., 2019, Radion et al., 2019, Roure et al., 2019, Senapati et al., 2019, Soffers et al., 2019, Varga et al., 2019, Yang et al., 2019, Akulenko et al., 2018, Armstrong et al., 2018, Clémot et al., 2018, De et al., 2018, Fedoseeva et al., 2018, Joos et al., 2018, Lee et al., 2018, Li et al., 2018, Lu et al., 2018, Ma et al., 2018, Masuko et al., 2018, Penke et al., 2018, Pokholkova et al., 2018, Sadasivam and Huang, 2018, Šatović et al., 2018, Skrajna et al., 2018, Song 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, Janssens et al., 2017, Kang 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, Rickels 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, Lorberbaum et al., 2016, Nakashima et al., 2016, Ozawa et al., 2016, Peng et al., 2016, Penke 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, Mugat et al., 2015, Pengelly et al., 2015, Pu et al., 2015, Stephenson et al., 2015, Sun 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, Dufourt 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, Landais 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., 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Jacobs-Lorena, 1985)
                    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.
                    Study result (0)
                    Result
                    Result Type
                    Title
                    External Crossreferences and Linkouts ( 47 )
                    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/GCRP - The gene-centric reference proteome (GCRP) provides a 1:1 mapping between genes and UniProt accessions in which a single 'canonical' isoform represents the product(s) of each protein-coding gene.
                    UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
                    Other crossreferences
                    AlphaFold DB - AlphaFold provides open access to protein structure predictions for the human proteome and other key proteins of interest, to accelerate scientific research.
                    InterPro - A database of protein families, domains and functional sites
                    PDB - An information portal to biological macromolecular structures
                    Linkouts
                    Cell Signaling Technology - Commercial vendor for primary antibodies and antibody conjugates.
                    DroID - A comprehensive database of gene and protein interactions.
                    Interactive Fly - A cyberspace guide to Drosophila development and metazoan evolution
                    References (1,542)