General Information
Symbol
Dmel\bcd
Species
D. melanogaster
Name
bicoid
Annotation Symbol
CG1034
Feature Type
FlyBase ID
FBgn0000166
Gene Model Status
Stock Availability
Gene Snapshot
Bicoid is a homeodomain-containing transcription factor that forms a concentration gradient to specify the fate map along the anterior-posterior axis of the embryo. [Date last reviewed: 2016-12-01]
Also Known As
bicoid
Genomic Location
Cytogenetic map
Sequence location
3R:6,755,842..6,759,466 [-]
Recombination map
3-48
Sequence
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
GO Summary Ribbons
Families, Domains and Molecular Function
Protein Family (UniProt, Sequence Similarities)
Belongs to the paired homeobox family. Bicoid subfamily. (P09081)
Summaries
Gene Group Membership
HOX-LIKE HOMEOBOX TRANSCRIPTION FACTORS -
HOX-like (HOXL) homeobox transcription factors are sequence-specific DNA binding proteins that regulate transcription. They encompass transcription factors encoded by the Hox genes of the Antennapedia and the Bithorax gene complexes and genes closely related in sequence. HOXL transcription factors are major regulators of animal development. (Adapted from FBrf0232555).
Effectors Negatively Regulated by Torso Signaling Pathway -
Target effectors which are specifically inhibited by the activation of the Torso signaling pathway.
UniProt Contributed Function Data
Segment polarity protein that provides positional cues for the development of head and thoracic segments. Regulates the expression of zygotic genes, possibly through its homeodomain, and inhibits the activity of other maternal gene products. May also bind RNA. Interacts with Bin1 to repress transcription of bicoid target genes in the anterior tip of the embryo; a process known as retraction.
(UniProt, P09081)
Phenotypic Description from the Red Book (Lindsley and Zimm 1992)
bcd: bicoid
Maternal-effect lethal mutations showing defective head and thorax development. Females homozygous for strong alleles produce embryos in which head and thorax are replaced by duplicated telson, including anal plates, tuft, spiracles, and filzkorper; however, no pole cells formed at the anterior end. Deletions and fusions of anterior abdominal segments and occasionally anterior abdominal segments in reversed polarity are also observed. Strong alleles amorphic based on phenotypic similarities of embryos produced by homozygous and hemizygous females. Weak alleles result in pattern defects in heads of embryos; lack only labral derivatives (median tooth, dorsal bridge); intermediate weak genotypes produce reduced head but retain normal thoracic development; intermediate strong produce further reduction of head, deletion of second and third and reduction of first thoracic dentical belts; thoracic segments fused. Partial rescue of embryonic phenotype effected by injection of cytoplasm (5% of volume) from the anterior ends of unfertilized wild-type eggs into the anterior pole of newly fertilized eggs of bcd mothers; injection into ectopic sites stimulates differentiation of anterior structures at site of injection; efficiency proportional to number of bcd+ alleles carried by cytoplasm donor. Phenocopies result from leakage of 5% of egg volume from anterior perforation of normal embryos. The distance of the head fold at gastrulation is proportional to the number of bcd+ alleles in the maternal genotype. bcd mRNA appears as a flattened disc plastered to the anterior extremity of early embryos; by the time of pole cell migration it has become localized to the clear cytoplasm at the periphery, forming a cap over the anterior end of the egg and is distributed in a steeply decreasing gradient such that 90% of the RNA is in the anterior 18% of egg length; by nuclear cycle 14 the RNA begins to disappear and becomes undetectable by midway through cellularization. bcd protein on the other hand forms a shallower gradient in which 57% of protein is in the anterior 18% of egg length, and the gradient doesn't reach baseline until the posterior 30% of egg length; the gradient forms from two to four hours after oviposition in both fertilized and unfertilized eggs, and except during mitosis is concentrated in nuclei; diffusion postulated to account for the establishment of the protein gradient following translation from anteriorly anchored RNA. Protein levels decrease during cellularization, although some nuclear staining persists until the end of germ-band elongation. bcd transcript first detectable in the ovaries of bcd females; forms a ring around the anterior margin of the developing oocyte in stages 5 and 6; in stages 9 and 10 nurse-cell accumulation observed to be localized toward the periphery of the cyst; by stage 12 the nurse cells have emptied their contents into the oocyte and the bcd transcript appears as an anterior cap (St. Johnston, Driever, Berleth, Richstein, and Nusslein-Volhard, 1989, Development Supplement: 13-19). No evidence of translation of bcd protein during oogenesis. Formation of the bcd gradient is regulated by three maternally active genes exu, sww, and stau; exu appears necessary for nurse cell accumulation; sww is required for anterior localization of bcd mRNA in the oocyte; and stau appears to be involved in RNA localization in the embryo. A defect in any of these functions results in little or no gradient of bcd activity. bcd in turn appears to control the activity of anterior gene activity; specifically the anterior pattern of hb expression is not observed and is replaced by a mirror-image posterior hb stripe in bcd- embryos (Tautz, 1988, Nature 332: 281-84; Schroder, Tautz, Seifertz, and Jackle, 1988, EMBO J. 7: 2881-87).
Gene Model and Products
Number of Transcripts
5
Number of Unique Polypeptides
5

Please see the GBrowse view of Dmel\bcd or the JBrowse view of Dmel\bcd for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

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
Gene model reviewed during 5.49
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.50
Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0081664
1479
149
FBtr0081665
2499
489
FBtr0081666
2536
418
FBtr0081667
2521
413
FBtr0081668
2514
494
Additional Transcript Data and Comments
Reported size (kB)
2.4 (unknown)
2.6, 1.6 (northern blot, sequence analsyis)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
FBpp0081164
16.4
149
7.29
FBpp0081165
54.0
489
7.42
FBpp0081166
45.4
418
7.15
FBpp0081167
44.9
413
7.31
FBpp0081168
54.5
494
7.31
Polypeptides with Identical Sequences

None of the polypeptides share 100% sequence identity.

Additional Polypeptide Data and Comments
Comments
Both the cad protein gradient and the hb transcript expression pattern are dependant upon the homeodomain and the PEST domain of bcd protein. Deletions and mutations of PEST sequences in the bcd coding region resulted in an inability to repress cad expression in the anterior region of the embryo. Similar deltions result is a loss of hb expression between 20 and 50% egg length in the anterior expression domain. Thus, the deletional analysis of bcd protein domains shows that the domain that is required for translational represssion of cad is also required for transcriptional activation of hb.
Both the cad protein gradient and the hb transcript expression pattern are dependant upon the homeodomain and the PEST domain of bcd protein. Deletions and mutations of PEST sequences in the bcd coding region resulted in an inability to repress cad expression in the anterior region of the embryo. Similar deltions result is a loss of hb expression between 20 and 50% egg length in the anterior expression domain. Thus, the deletional analysis of bcd protein domains shows that the domain that is required for translational represssion of cad is also required for transcriptional activation of hb.
bcd protein is expressed in yeast under the control of βestradiol in order to control the amount of bcd protein produced. Cooperative binding to bcd response regions on various lacZ reporter constructs was studied with transcription assays, in vitro gel shift assays and foot print analysis. The bcd responsive region of kni was used both in vitro and in vivo to ascertain the strength of bcd binding sites.
bcd protein binds to the BRE (bcd response element) of the cad 3''UTR. Binding of bcd protein to cad transcript facilitates proper cad localization, presumably due to translational repression of cad by bcd.
bcd protein regulates the expression of cad through translational repression by binding to the cad 3''UTR at specific "bicoid binding regions" (BBR). Expression pattern analysis, UV crosslink assays and Schnieder cell co-transfection assays all conclude that the homeodomain of bcd protein is necessary and suffiecient for binding to the BBR of cad transcripts. bcd protein will supress translation of "BBR-containing"mRNAs.
The expression pattern of genes downstream of bcd were analysed after egg ligation at various egg lengths. It was observed that the bcd protein gradient, as well as the cad protein gradient were blocked by egg ligation, and thus, the expression of downstream gap genes were altered. The authors suggest that alteration of the bcd protein gradient, alters the hb expression profile and in turn, through regulation by hb, Kr and kni expression domains are altered, consequently altering the domains of pair-rule gene expression.
CAT assays with bcd protein expressed in Schneider cells show that bcd activates a promoter containing three copies of a bcd consensus sequence. Through studies both in vivo and in vitro it has been shown that the activation of transcription due to bcd is dependant upon the phosphorylation state of bcd protein. Phosphorylated bcd will not activate transcription, and the phosphorylation of bcd is dependant upon tor and phl.
Antibodies recognize a doublet of proteins of 55kD and 57kD. The appearance of two bands is thought to be due to posttranslational modification because the 5aa difference between the two bcd proteins is not enough to account for the 2-3kD size difference.
One of several products generated by alternative splicing.
bcd protein is translated from in vitro transcribed bcd mRNA in wheat germ extract and rabit reticulocyte lysate and is expressed in Drosophila Scheider cells to yeild a 58 kD protein. Exchange of the bcd 5'' UTR for Xenopus beta-globin 5'' UTR yeilds higher protein levels in these translation systems.
The bcd protein was expressed and purified from embryos, Drosophila Schneider cells, and E. coli. The bcd protein produced by embryos and Schneider cells was 58kD, while the protein from E. coli was 53kD,indicating that the protein produced in Drosophila was highly phosphorylated. Indeed, when bcd protein isolated from Drosophila embryos or cells was incubated with phosphatase prior to elecrtophoresis, the protein was resolved at 53kD.
The author compared the sequences of several Drosophila melanogater genes and one human gene with consensus RNA Recognition Motifs (RRM) to bcd protein sequence and identified a putative RRM.
External Data
Subunit Structure (UniProtKB)
Interacts with Bin1; in vitro and yeast cells. Interacts with bin3.
(UniProt, P09081)
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\bcd using the Feature Mapper tool.

External Data
Crossreferences
Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
Linkouts
Gene Ontology (18 terms)
Molecular Function (7 terms)
Terms Based on Experimental Evidence (5 terms)
CV Term
Evidence
References
inferred from mutant phenotype
inferred from physical interaction with FLYBASE:bin3; FB:FBgn0263144
inferred from physical interaction with FLYBASE:Bin1; FB:FBgn0024491
inferred from physical interaction with FLYBASE:fsd; FB:FBgn0033813
inferred from physical interaction with FLYBASE:eIF4EHP; FB:FBgn0053100
Terms Based on Predictions or Assertions (3 terms)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN002518688
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002518688
(assigned by GO_Central )
Biological Process (10 terms)
Terms Based on Experimental Evidence (7 terms)
CV Term
Evidence
References
Terms Based on Predictions or Assertions (4 terms)
CV Term
Evidence
References
Cellular Component (1 term)
Terms Based on Experimental Evidence (0 terms)
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
inferred by curator from GO:0000981
inferred from biological aspect of ancestor with PANTHER:PTN002518688
(assigned by GO_Central )
Expression Data
Transcript Expression
No Assay Recorded
Stage
Tissue/Position (including subcellular localization)
Reference
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
northern blot
Stage
Tissue/Position (including subcellular localization)
Reference

Comment: reference states 0-2 hr AEL

Comment: reference states 2-4 hr AEL

radioisotope in situ
Stage
Tissue/Position (including subcellular localization)
Reference
RT-PCR
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data
bcd transcript expression was assayed at 20oC from embryonic time 0 to 7.25 hours. The authors stated that this was a temperature correction factor of 1.7, therefore, corresponding to 0-3.25 hours of development at 25oC. At time 0 prior to egg activation bcd transcript lacks a poly-A tail. Upon activation the transcript is rapidly poly-adenylated. Maximal polyadenylation corresponds to maximal translation of the bcd protein. At approximately 2 hours post activation at 25oC significant deadenylation is observed which leads to reduced translation of bcd protein and subsequent degradation of bcd transcript.
Following injection of the full length S35 labeled bcd transcript, the transcript becomes tightly localized to the anterior cortex of the embryo, reaching between 5-10% egg length.
bcd transcripts localize as an anterior cap in mature oocytes and are found in a characteristic patchy pattern in nurse cells.
bcd transcript accumulation occurs in 4 phases during oogenesis. Between stages S6 and S9, transcripts accumulate as a ring at the anterior end of the oocyte. In stages S9-S10a follicles, they localize to the apical region of nurse cells. As nurse cells contract in stages S10b-S11, all bcd transcripts localize to the cortex at the anterior end of the oocyte. Between stage S12 and egg deposition they become localized to a spherical dorsally located region at the anterior pole. The distribution of bcd transcripts in nurse cells and the oocyte is altered in exu and swa mutants. In early embryos, bcd transcripts are restricted to the anterior pole. exu and swa mutations lead to nearly uniform distribution of bcd RNA in the early embryo while stau mutations produce a gradient of expression at the anterior pole of the embryo.
The bcd-RB transcript is expressed at very low levels through all stages of development.
During oogenesis bcd transcript is localized to the anterior edges of the oocyte and remains localized throughout oocyte development. bcd transcript is also detected surrounding the nurse cell nuclei. In early embryos bcd transcript is detected in an "anterior cap", with strong signal present in the most anterior part of the embryo. Lower levels of bcd transcript are detected in a gradient up to 80% egg length.
bcd is detected at high levels in nurse cells and in the anterior of oocytes. In embryos undergoing cleavage, an anterior-posterior gradient of bcd expression is apparent. Expression levels subsequently decline, and are undectectable after the cellular blastoderm stage.
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
western blot
Stage
Tissue/Position (including subcellular localization)
Reference
organism

Comment: reference states 0-3.25 hr AEL

Additional Descriptive Data
bcd protein expression was assayed at 20oC from embryonic time 0 to 7.25 hours. The authors stated that this was a temperature correction factor of 1.7, therefore, corresponding to 0-3.25 hours of development at 25oC. bcd protein was detected throughout this period, but began to decrease after 2 hours of development at 25oC, the time at which bcd transcript deadenylation became pronounced.
Although bcd protein is present in the cytoplasm, it is strongly concentrated in the nucleus.
bcd protein is not detected in nosbcd.3UTR embryos.
bcd protein is distributed in an exponential concentration gradient in the early embryo with a maximum at the anterior tip, reaching background levels in the posterior third of the embryo. None is detected in oocytes.
Embryos derived from bcd females carrying one copy of bcdTN3 show wild type bcd protein distribution, where bcd protein is localized to the anterior pole of the embryo.
Marker for
 
Subcellular Localization
CV Term
Evidence
References
Expression Deduced from Reporters
Reporter: P{2xBLE1+}
Stage
Tissue/Position (including subcellular localization)
Reference
Reporter: P{bcd+lacZ}
Stage
Tissue/Position (including subcellular localization)
Reference
Reporter: P{bcdΔ7+lacZ}
Stage
Tissue/Position (including subcellular localization)
Reference
Reporter: P{bcdΔ11+lacZ}
Stage
Tissue/Position (including subcellular localization)
Reference
Reporter: P{bcdΔ14+lacZ}
Stage
Tissue/Position (including subcellular localization)
Reference
Reporter: P{bcdΔ14S-lacZ}
Stage
Tissue/Position (including subcellular localization)
Reference
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\bcd 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
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Flygut - An atlas of the Drosophila adult midgut
Images
FlyExpress - Embryonic expression images (BDGP data)
  • Stages(s) 1-3
  • Stages(s) 4-6
Alleles, Insertions, Transgenic Constructs and Phenotypes
Classical and Insertion Alleles ( 22 )
Transgenic Constructs ( 192 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of bcd
Allele of bcd
Mutagen
Associated Transgenic Construct
Stocks
Transgenic constructs containing regulatory region of bcd
characterization construct
GAL4 construct
Name
Expression Data
vital-reporter construct
Deletions and Duplications ( 13 )
Summary of Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Lethality
Allele
Sterility
Allele
Other Phenotypes
Allele
Phenotype manifest in
Allele
embryonic neuroblast & abdomen
Orthologs
Human Orthologs (via DIOPT v7.1)
Homo sapiens (Human) (2)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
1 of 15
Yes
No
1 of 15
Yes
No
Model Organism Orthologs (via DIOPT v7.1)
Mus musculus (laboratory mouse) (2)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
1 of 15
Yes
No
1 of 15
Yes
No
Rattus norvegicus (Norway rat) (0)
No orthologs reported.
Xenopus tropicalis (Western clawed frog) (0)
No orthologs reported.
Danio rerio (Zebrafish) (0)
No orthologs reported.
Caenorhabditis elegans (Nematode, roundworm) (2)
1 of 15
Yes
No
1 of 15
Yes
Yes
Arabidopsis thaliana (thale-cress) (1)
1 of 9
Yes
Yes
Saccharomyces cerevisiae (Brewer's yeast) (1)
1 of 15
Yes
No
Schizosaccharomyces pombe (Fission yeast) (0)
No orthologs reported.
Orthologs in Drosophila Species (via OrthoDB v9.1) ( EOG09190CD2 )
Organism
Common Name
Gene
AAA Syntenic Ortholog
Multiple Dmel Genes in this Orthologous Group
Drosophila melanogaster
fruit fly
Drosophila simulans
Drosophila sechellia
Drosophila erecta
Drosophila yakuba
Drosophila ananassae
Drosophila pseudoobscura pseudoobscura
Drosophila persimilis
Drosophila willistoni
Drosophila virilis
Drosophila mojavensis
Drosophila grimshawi
Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( EOG091507VJ )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Musca domestica
House fly
Lucilia cuprina
Australian sheep blowfly
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
Human Disease Model Data
FlyBase Human Disease Model Reports
    Alleles Reported to Model Human Disease (Disease Ontology)
    Download
    Models ( 0 )
    Allele
    Disease
    Evidence
    References
    Interactions ( 0 )
    Allele
    Disease
    Interaction
    References
    Comments ( 0 )
     
    Human Orthologs (via DIOPT v7.1)
    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
    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 look at the Interaction Group reports for full details of the physical interactions
    RNA-protein
    Interacting group
    Assay
    References
    protein-protein
    Interacting group
    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)
    Interacts with Bin1; in vitro and yeast cells. Interacts with bin3.
    (UniProt, P09081 )
    Linkouts
    BioGRID - A database of protein and genetic interactions.
    DroID - A comprehensive database of gene and protein interactions.
    InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
    Pathways
    Gene Group - Pathway Membership (FlyBase)
    Effectors Negatively Regulated by Torso Signaling Pathway -
    Target effectors which are specifically inhibited by the activation of the Torso signaling pathway.
    External Data
    Linkouts
    SignaLink - A signaling pathway resource with multi-layered regulatory networks.
    Genomic Location and Detailed Mapping Data
    Chromosome (arm)
    3R
    Recombination map
    3-48
    Cytogenetic map
    Sequence location
    3R:6,755,842..6,759,466 [-]
    FlyBase Computed Cytological Location
    Cytogenetic map
    Evidence for location
    84A5-84A5
    Limits computationally determined from genome sequence between P{PZ}pb04498 and P{lacW}l(3)L2100L2100
    Experimentally Determined Cytological Location
    Cytogenetic map
    Notes
    References
    84A1-84A1
    (determined by in situ hybridisation)
    84A-84A
    (determined by in situ hybridisation)
    Experimentally Determined Recombination Data
    Left of (cM)
    Right of (cM)
    Notes
    Stocks and Reagents
    Stocks (22)
    Genomic Clones (28)
    cDNA Clones (78)
     

    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)
    RNAi and Array Information
    Linkouts
    DRSC - Results frm RNAi screens
    GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
    Antibody Information
    Laboratory Generated Antibodies
    Commercially Available Antibodies
     
    Other Information
    Relationship to Other Genes
    Source for database identify of
    Source for identity of: bcd CG1034
    Source for database merge of
    Additional comments
    Other Comments
    DNA-protein interactions: genome-wide binding profile assayed for bcd protein in Kc167 cells; see Chromatin_types_NKI collection report. Individual protein-binding experiments listed under "Samples" at GEO_GSE22069 (http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE22069).
    A bcd mRNA concentration gradient is formed along the cortex of the embryo by nuclear cycle 10 or the beginning of syncytial blastoderm. The gradient falls off exponentially with distance from the anterior pole and persists unchanged during nuclear cycles 10-13. During the first third of nuclear cycle 14, bcd mRNA is transported to the apical nuclear periplasm where it is degraded rapidly. bcd mRNA and stau protein co-localise and form a similar gradient. Congruence of protein and mRNA gradients at all times implies that the bcd protein gradient may derive from the bcd mRNA gradient.
    DNA-protein interactions: genome-wide binding profile assayed for bcd protein in 2-3 hr embryos; see BDTNP1_TFBS_bcd collection report.
    bcd RNA is transported as particles from nurse cells to the oocyte by a Dhc64C/BicD dependent mechanism distinct from the general flow of cytoplasm from nurse cell to oocyte.
    Localisation of bcd mRNA in late oocytes is maintained by continual active transport on microtubules.
    The bcd protein gradient shows high embryo-to-embryo variability and is not correlated with egg length. In contrast, the hb mRNA and protein profile shows extreme reproducibility from embryo to embryo, and shows a strong correlation with egg length.
    A small domain of the bcd protein located immediately N-terminal to the homeodomain represses its own transcriptional activation activity in Drosophila S2 cells. This domain does not affect the properties of DNA-binding or subcellular distribution of the bcd protein.
    Two distinct domains of bcd mediate its transcriptional down-regulation by the tor pathway.
    Localization of bcd RNA depends on swa : bcd RNA spreads into the oocyte if swa protein is not anteriorly localized at stage 10. swa protein may act as an adaptor for the dynein complex enabling dynein to transport bcd RNA along microtubules to their minus ends at the anterior pole of the oocyte.
    hb is able to specify thoracic segments in the absence of bcd.
    In embryos, prd and bcd gene products bind most strongly to known target elements within a promoter. In addition, they may also bind at significant levels to the majority of genes, as do the selector homeoproteins.
    The bcd gene product contains separable protein domains for transcriptional and translational regulation of target genes.
    The h and bcd gene products bind to conserved sequence blocks in the run 7-stripe region.
    The regulation of bcd target genes by bcd requires the normal function of lwr.
    Study of bcd mRNA decay reveals mRNA stability is developmentally regulated. The mRNA destabilising sequence (BIE, bcd instability element) is contained in the 3' half of the message: 92 nucleotides immediately following the translation termination codon.
    Binding of the bcd 3'UTR by stau protein requires a double stranded conformation of the stems within the bcd RNA localisation signal.
    h stripe 7 activation requires several factors including the cad and bcd proteins.
    exu protein is highly enriched in the sponge bodies, subcellular structures in nurse cells. Neither the accumulation of or level of exu protein is dependent on the amount of bcd mRNA present in the ovaries. Results propose that sponge bodies are structures that, by assembly and transport of included molecules or associated structures, are involved in localisation of mRNAs in oocytes.
    tor does not affect the ability of bcd to bind DNA, but instead directs modification of bcd or of a potential bcd co-factor, which renders the bcd protein unable to activate transcription.
    Regulation of cad by bcd occurs at the level of translation and depends on both the bcd homeodomain and on cis-acting sequences in the 3' untranslated region (UTR) of the cad message. The bcd homeodomain can bind specifically to these cis-acting sequences in vitro. bcd regulates cad expression by blocking translational initiation.
    High levels of bcd morphogen are not required for oc activation.
    Transport and early localisation activities of fs(1)K10, bcd and osk mRNAs are remarkably similar to each other suggesting the mRNAs interact with a common set of microtubule based motor proteins and associated factors.
    cort and grau genes are necessary for bcd protein expression. Mutations in cort impair bcd and other maternal patterning genes mRNA translation by disrupting cytoplasmic polyadenylation. bcd mRNA expression, localisation or processing are not affected.
    The bcd product binds cooperatively to its sites within a hb enhancer element. A less than 4-fold increase in bcd protein concentration is sufficient to achieve an unbound/bound transition in DNA binding.
    In embryos lacking bcd activity, as a result of mutation, the cad gradient fails to form and cad becomes evenly distributed throughout the embryo. This suggests that bcd may act in the region specific control of cad mRNA translation. In vitro studies reveal that bcd binds through its homeodomain to cad mRNA and exerts translational control through a bcd-binding region (BBR) of cad mRNA.
    Most metazoan homeodomains share a preference for the TAAT motif, they can differ from each other in their preference for the bases immediately 3' to this core. This preference is determined, in part, by the identity of amino acid position 50. Because homeodomain sequences have been identified that possess at least 10 different amino acids at position 50 it is investigated whether multiple DNA binding specificities can be conferred by changing this position to a variety of amino acid side chains.
    Regions of bcd that are important for protein-protein interaction and cooperative DNA binding are defined using coimmunoprecipitation analysis. The amino terminal half of bcd interacts with another bcd molecule, but the homeodomain alone fails to interact. Mutations that affect DNA binding do not adversely affect protein-protein interaction function.
    swa function is required to maintain the position of several localised mRNAs and localised ribonucleoprotein (RNP) complexes in the cortex of the oocyte (including bcd and hts mRNA).
    Gene product is known to regulate Kr CD (cis acting control element) expression.
    Early ph-p gene expression is under the control of bcd and en as activators and of osk as an inhibitor.
    Two independent and redundant elements in the kni upstream region depend upon bcd and cad activity. Ecol\lacZ reporter gene analysis demonstrates bcd and cad are necessary to activate kni.
    Nurse cell-specific genes are functional in the pseudonurse cells of otu mutants, but the transport of pum, otu, ovo and bcd RNAs to the cytoplasm is affected.
    An ovarian protein, exl binds to BLE1, an RNA localisation element from bcd mRNA. exl localisation is disrupted in exu mutants suggesting exl and exu proteins interact.
    Several mutations have been isolated that fail to compensate for the fate change caused by the alteration in the bcd gradient.
    In embryos from mothers with extra copies of bcd, the adjustment of the fate map involves inreased apoptosis in the anterior region, allowing the development of a normally proportioned larva.
    Microtubules are necessary for the localisation of bcd RNA to the anterior oocyte margin during oogenesis.
    The bcd product binds DNA cooperatively in vitro with an affinity that is ten fold higher for clustered than for single sites. The cooperativity maps to the homeodomain and flanking sequences. bcd acts as a translational repressor of cad, binding the 3' untranslated region of cad. The RNA binding activity maps to the homeobox.
    cad, a conserved homeodomain protein that forms a posterior to anterior concentration gradient, and the anterior determinant bcd cooperate to form a partly redundant activator system in the posterior region of the embryo.
    The products of the Taf4 and Taf6 loci serve as coactivators to mediate transcriptional activation by the bcd and hb enhancer binding proteins. A quadruple complex containing Tbp, Taf1, Taf4 and Taf6 mediates transcriptional synergism by bcd and hb, whereas triple Tbp-Taf complexes lacking one or other coactivator failed to support synergistic activation. The concerted action of multiple regulators with different coactivators helps to establish the pattern and level of segmentation gene transcription during development.
    Mutagenesis studies in combination with protein binding experiments and reconstituted transcription reactions identified two independent activation domains of bcd that target different coactivator subunits (Taf4 and Taf6). Both coactivators are required for bcd to recruit the Tbp-Taf complex to the promoter and direct synergistic activation of transcription. Contact between multiple activation domains for bcd and different targets within the TfIID complex can mediate transcriptional synergism.
    Embryos with a reduced number of cells in the abdominal primordia have been used to determine whether they can regulate towards the normal during subsequent cell growth, no evidence was found for regulation of cell number.
    Down-regulation of bcd activity depends on the function of Dsor1. Dsor1 acts downstream of phl in the tor pathway and encodes a MAP-kinase kinase (MAPKK). Several clustered consensus sites for MAP kinase phosphorylation can be found in the bcd coding sequence.
    The stau product associates specifically with both osk and bcd mRNAs to mediate their localizations, but at two distinct stages of development. stau protein is required to anchor bcd mRNA at the anterior of the egg, and is transported with osk mRNA during oogenesis.
    sna can repress activation by bcd.
    bcd DNA binding specificity distinguishes among related binding sites by a base-specific contact between recognition helix residue 9 and base pair 7. DNA site specificity is necessary for bcd's action as a morphogen. bcd's ability to activate gene expression depends on the distance between its binding sites.
    bcd product is involved in the directed intercalation of cells during germ band extension. Increasing the dosage of wild type bcd increases the rate of cell intercalation in germ band extension.
    Mutations of Pka-C1 cause similar mislocalisations of bcd and osk RNAs to those observed from N mutations. Mutations also severely disrupt the organisation of microtubules at the posterior of the oocyte at the time of bcd and osk localisation.
    Among Drosophila species there is substantial conservation of components acting in bcd mRNA localization.
    bcd transcription is controlled by Sry-δ. Germline clonal analysis reveals that wild type Sry-δ activity is required for proper oogenesis in addition to bcd transcription.
    Fractionation procedure has been used to examine the cytoskeletal association of localised bcd RNA in egg chambers.
    A PCR based assay has been used to determine whether the encoded mRNAs exhibit changes in poly(A) status upon translational activation.
    hb is required for bcd to execute all its functions. The combined activity of bcd and hb, rather than bcd alone, form the morphogenetic gradient that specifies polarity along the embryonic axis and patterns the embryo.
    Transient overexpression of run alters the expression of the gap genes. A subset of these effects may be due to an antagonistic effect of run on transcriptional activation by the maternal morphogen bcd.
    Distribution of tud protein in mutant embryos has been studied. Maternal genes such as bcd, tor and trk that are necessary for anteroposterior axis formation, but not required for germ cell formation or abdominal segmentation, have no effect on the distribution of tud protein.
    The introduction of a membrane barrier across the embryo by ligation of the egg alters the bcd protein gradient.
    Comparison of bcd and hts transcript distribution in swa, exu and stau mutant embryos indicates different genetic requirements for proper localization of bcd and hts RNAs.
    There is not a simple relationship between the position of the swa protein and the site of its action in bcd RNA localisation.
    The role of bcd in the regulation of run mRNA expression in the early embryo has been investigated.
    Ecol\lacZ reporter gene constructs demonstrate the presence of bcd maternal system cis-acting response elements in the 5' flanking region of tll.
    An essential element, BLE1, which specifically directs the early steps of bcd mRNA localization has been identified. The bcd mRNA localization signal appears to consist of multiple different elements, each responsible for different steps in the localization process.
    In its anterior domain (labral primordia) cnc is activated by bicoid and torso maternal pathways.
    The homologs of Antp, ftz, Scr, Dfd, Ama, bcd, zen, pb and lab, but not zen2 are all present in D.pseudoobscura.pseudoobscura, in the same linear order and similarly spaced along the chromosome as in D.melanogaster.
    An artificial bcd responder gene composed of three bcd consensus binding sites driving Ecol\lacZ expression is activated by bcd and repressed by tor. This repression does not require tll or hkb. Phosphorylation resulting from the tor signal transduction pathway down-regulates transcriptional activation by the bcd morphogen. The normal phosphorylation changes that affect bcd during development do not occur in tor mutant embryos.
    Bicoid sequences were used to mislocalise nanos in experiments that determined that localisation of nanos RNA controls embryonic polarity.
    The 3' untranslated region of bcd contains a conserved motif involved in mRNA localization.
    bcd is responsible for the activation of tll transcription at the anterior pole in terminal mutant embryos and plays a critical role in the formation of the tll stripe.
    The gene products of bcd, hb, Kr and gt all bind within the 480bp region that is necessary and sufficient for the expression of eve stripe 2. Activation depends on cooperative interactions between hb and bcd. Forming the posterior border of the stripe involves a delicate balance between Kr repressor and bcd activator.
    Apical localization of pair-rule transcripts restricts lateral protein diffusion allowing pair-rule proteins to define sharp boundaries and precise spatial domains.
    bcd is involved in the pathway that leads to the activation of Sxl in the anterior region. Embryos carrying four doses of maternal bcd show an expansion of the anterior fate map. If the embryos also lack run activity the anterior domain of Sxl expression extends posteriorly so causing the central domain of Sxl expression to shrink.
    The bcd gradient can only activate the hb gene in the anterior part of the embryo. The anterior domain of gt expression is most likely directly controlled by bcd.
    The interaction of the bcd homeodomain with mutated bcd binding sites has been studied using assays in yeast. Base pair 7 on the bcd recognition helix is important for bcd binding, base pairs 8 and 9 influence recognition.
    gt may be a target for the bcd morphogen in the embryo.
    bcd mRNA localization requires the function of at least three genes, the exu gene acts earliest in the pathway. exu acts in initiating bcd mRNA localization but does not play a persistent role in that process.
    Mutations in maternal anterior class gene bcd interact with RpII140wimp.
    Microtubules are required for establishing and maintaining the position of bcd mRNA in nurse cells and the oocyte. When microtubule inhibitors are removed from the egg chamber bcd mRNA is relocalized. Taxol treatment results in the localization of bcd mRNA at ectopic positions in the oocyte.
    bcd protein directly regulates the expression of eve stripe 2 expression by DNA binding to the stripe 2 promoter element.
    The posterior group gene stau is required for bcd RNA to localize correctly to the anterior pole. By the time the egg is laid, stau protein is concentrated at the anterior pole, in the same region as bcd RNA.
    The eve stripe 2 is lost in bcd- embryos.
    bcd nos response elements (NREs) confer nos sensitivity on maternal hb mRNA.
    bcd does not affect transcription from the mus209 promoter of mus209-Ecol\CAT reporter constructs.
    The effects of an altered nucleocytoplasmic ratio on transcripts that normally undergo changes in transcript pattern in cell cycle 14 is studied. A delay in the degradation of the bcd maternal message is correlated with a decrease in nuclear density and a change in the cell cycle program.
    The bcd mRNA leader sequence is not required for transcript localization nor for the translational block of bcd mRNA during oogenesis. The concentration gradient, not the existence of different forms of bcd protein, is responsible for specifying subregions of the embryo.
    bcd mutants exhibit deletion of the head and thorax, the acron is transformed to the telson.
    Mature follicles are immunologically stained for asymmetric distribution of ecdysteroid-related antigen. During late oogenesis localisation of the antigen changes dramatically suggesting the antigen plays a role in early embryogenesis and, perhaps, in pattern formation.
    Maternal effect mutations disrupt the anteroposterior or dorsoventral pattern of the early embryo. Examination of an allelic series of hypomorphic alleles reveals a graded requirement for bcd activity along the anteroposterior axis. Deletion of anterior head structures is associated with all bcd mutations, further posterior deletions depend on the severity of the mutation. Analysis of a temperature sensitive allele demonstrates the time of bcd function is from pole cell formation to the cellular blastoderm.
    bcd gene function is not required for vas protein localization.
    bcd genes from several Drosophila species were isolated and analyzed to define more precisely the cis-acting bcd mRNA localization signal. Each has the potential to form an extensive, stereotypical secondary structure. These results suggest that the cis-acting element responsible for anterior localization of bcd mRNA is, or is part of, the secondary structure.
    The bcd gene of D.pseudoobscura.pseudoobscura has been cloned and sequenced for use as a tool for identifying important functional domains within the transcription unit.
    Double abdomen induction in bcd is more efficient by genetic methods, within bcd mutant embryos, than removal of anterior cytoplasm.
    bcd protein binds to five sites upstream of the transcription start site of the zygotic gap gene hb. Three of the sites are necessary and sufficient for the activation of zygotic hb expression.
    P-element mediated transformation of high and low affinity bcd binding sites fused to the Hsp70 promoter has been used to demonstrate that the maternally derived gradient of bcd can define more than one domain of zygotic gene expression by variation of binding site affinity.
    Multiple steps are involved in the localization of bcd RNA at the anterior pole of the oocyte.
    bcd gene product binds to distinct sites in the hb gene, its affinity for these sites determines the minimum concentration of bcd protein necessary to activate hb transcription.
    bcd has been cloned, sequenced and transcripts analysed. bcd transcript localisation is affected by mutations in other maternal genes.
    In bcd embryos the anterior anlagen are missing while the posterior pattern is enlarged and spread to the anterior.
    Increases or decreases in bcd protein levels in a given region of the embryo cause a corresponding posterior or anterior shift of anterior anlagen in the embryo.
    The bcd gene product is a 55kD protein translated soon after egg deposition. The distribution of protein in wild type embryos can be explained by models involving local source, diffusion and dispersed decay. Protein is detectable at up to 30% egg length explaining how long range effects can be observed in bcd- embryos.
    bcd activity is essential for the normal expression of the 2.9kb hb transcript.
    bcd RNA localisation in swa- eggs has been analysed.
    Identified on the basis of similarity to a 600bp prd cDNA fragment which codes for the last 205 amino acids of prd.
    Maternal-effect lethal mutations showing defective head and thorax development. Females homozygous for strong alleles produce embryos in which head and thorax are replaced by duplicated telson, including anal plates, tuft, spiracles, and filzkorper; however, no pole cells formed at the anterior end. Deletions and fusions of anterior abdominal segments and occasionally anterior abdominal segments in reversed polarity are also observed. Strong alleles amorphic based on phenotypic similarities of embryos produced by homozygous and hemizygous females. Weak alleles result in pattern defects in heads of embryos; lack only labral derivatives (median tooth, dorsal bridge); intermediate weak genotypes produce reduced head but retain normal thoracic development; intermediate strong produce further reduction of head, deletion of second and third and reduction of first thoracic dentical belts; thoracic segments fused. Partial rescue of embryonic phenotype effected by injection of cytoplasm (5% of volume) from the anterior ends of unfertilized wild-type eggs into the anterior pole of newly fertilized eggs of bcd mothers; injection into ectopic sites stimulates differentiation of anterior structures at site of injection; efficiency proportional to number of bcd+ alleles carried by cytoplasm donor. Phenocopies result from leakage of 5% of egg volume from anterior perforation of normal embryos. The distance of the head fold at gastrulation is proportional to the number of bcd+ alleles in the maternal genotype. bcd mRNA appears as a flattened disc plastered to the anterior extremity of early embryos; by the time of pole cell migration it has become localized to the clear cytoplasm at the periphery, forming a cap over the anterior end of the egg and is distributed in a steeply decreasing gradient such that 90% of the RNA is in the anterior 18% of egg length; by nuclear cycle 14 the RNA begins to disappear and becomes undetectable by midway through cellularization. bcd protein on the other hand forms a shallower gradient in which 57% of protein is in the anterior 18% of egg length and the gradient doesn't reach baseline until the posterior 30% of egg length; the gradient forms from two to four hours after oviposition in both fertilized and unfertilized eggs and except during mitosis is concentrated in nuclei; diffusion postulated to account for the establishment of the protein gradient following translation from anteriorly anchored RNA. Protein levels decrease during cellularization, although some nuclear staining persists until the end of germ-band elongation. bcd transcript first detectable in the ovaries of bcd females; forms a ring around the anterior margin of the developing oocyte in stages 5 and 6; in stages 9 and 10 nurse-cell accumulation observed to be localized toward the periphery of the cyst; by stage 12 the nurse cells have emptied their contents into the oocyte and the bcd transcript appears as an anterior cap (St. Johnston, Driever, Berleth, Richstein and Nusslein-Volhard, 1989). No evidence of translation of bcd protein during oogenesis. Formation of the bcd gradient is regulated by three maternally active genes exu, swa and stau; exu appears necessary for nurse cell accumulation; swa is required for anterior localization of bcd mRNA in the oocyte; and stau appears to be involved in RNA localization in the embryo. A defect in any of these functions results in little or no gradient of bcd activity. bcd in turn appears to control the activity of anterior gene activity; specifically the anterior pattern of hb expression is not observed and is replaced by a mirror-image posterior hb stripe in bcd- embryos (Tautz, 1988; Schroder, Tautz, Seifertz and Jackle, 1988).
    Origin and Etymology
    Discoverer
    Etymology
    Identification
    External Crossreferences and Linkouts ( 106 )
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    Synonyms and Secondary IDs (13)
    Reported As
    Symbol Synonym
    BG:DS00276.7
    Bcd
    (Adhikary et al., 2017, Aguilera-Gomez and Rabouille, 2017, Bentovim et al., 2017, Chertkova et al., 2017, Fradin, 2017, Isakova et al., 2017, Altenhein et al., 2016, Sandler and Stathopoulos, 2016, Vincent et al., 2016, Briscoe and Small, 2015, Naval-Sánchez et al., 2015, Villaverde et al., 2015, Mannervik, 2014, Marjoram et al., 2014, Martinez et al., 2014, Xu et al., 2014, Garcia et al., 2013, Hartmann et al., 2013, Kim et al., 2013, Liu and Ma, 2013, Liu and Ma, 2013, Lucas et al., 2013, McKay and Lieb, 2013, Müller et al., 2013, Rödel et al., 2013, Umulis and Othmer, 2013, Chen et al., 2012, Crombach et al., 2012, Hardway, 2012, He et al., 2012, Nikulova et al., 2012, Tamari and Barkai, 2012, Vazquez-Pianzola and Suter, 2012, Ajuria et al., 2011, Castle et al., 2011, Gursky et al., 2011, Holloway et al., 2011, Kim et al., 2011, Liu and Niranjan, 2011, Nien et al., 2011, Papatsenko and Levine, 2011, Tsurumi et al., 2011, Zhang et al., 2011, Aerts et al., 2010, Bauer et al., 2010, He et al., 2010, Kavousanakis et al., 2010, Mace et al., 2010, Sample and Shvartsman, 2010, He et al., 2009, He et al., 2009, Manu et al., 2009, Manu et al., 2009, Moses, 2009, Okabe-Oho et al., 2009, Papatsenko et al., 2009, Bialek et al., 2008, Holloway et al., 2008, Lopes et al., 2008, Lucchetta et al., 2008, Noyes et al., 2008, Ogawa et al., 2008, Tkacik et al., 2008, Gregor et al., 2007, Baird-Titus et al., 2006, Bandyopadhyay et al., 2006, Jaeger and Reinitz, 2006, Lopes et al., 2006, Lopes et al., 2006, Moorman et al., 2006, Moorman et al., 2006, Perkins et al., 2006, Cho et al., 2005, Fu and Ma, 2005, Gregor et al., 2005, Ma, 2005, Tanda et al., 2000, Torigoi et al., 2000, Comeron and Kreitman, 1998)
    bcd
    (Haines and Eisen, 2018, Lefebvre and Lécuyer, 2018, Myasnikova and Spirov, 2018, Myasnikova and Spirov, 2018, Streichan et al., 2018, Amourda and Saunders, 2017, Barr et al., 2017, Cai et al., 2017, Chambers et al., 2017, Ghodsi et al., 2017, Goldman and Gonsalvez, 2017, Hannon et al., 2017, Hu et al., 2017.6.13, Nieuwburg et al., 2017, Rupprecht et al., 2017, Vazquez-Pianzola et al., 2017, Bürglin and Affolter, 2016, Jermusyk et al., 2016, Lazzaretti et al., 2016, Lim et al., 2016, Na et al., 2016, Quinlan, 2016, Sandler and Stathopoulos, 2016, Sanghavi et al., 2016, Cicin-Sain et al., 2015, Ghodsi et al., 2015, Gula and Samsonov, 2015, Hsu et al., 2015, Kozlov et al., 2015, Liu and Ma, 2015, Schertel et al., 2015, Cheung et al., 2014, Fahmy et al., 2014, Fu et al., 2014, Jiang and Singh, 2014, Sigaut et al., 2014, Sitaram et al., 2014, Spahn et al., 2014, Tanaka et al., 2014, Toshima et al., 2014, Vartiainen et al., 2014, Bischof et al., 2013, Combs and Eisen, 2013, Heffer and Pick, 2013, Kim et al., 2013, Li and Gilmour, 2013, Liu et al., 2013, Liu et al., 2013, McKay and Lieb, 2013, Neckameyer and Argue, 2013, Surkova et al., 2013, Webber et al., 2013, Aswani et al., 2012, Baffet et al., 2012, Crombach et al., 2012, Crombach et al., 2012, Haskel-Ittah et al., 2012, Holderbaum et al., 2012.4.9, Jaeger et al., 2012, Kim et al., 2012, Kvon et al., 2012, Liang et al., 2012, McDermott et al., 2012, Nagel et al., 2012, Reschen et al., 2012, Sokolowski et al., 2012, Vazquez-Pianzola and Suter, 2012, Becalska et al., 2011, Chang et al., 2011, Cheung et al., 2011, Drocco et al., 2011, Dubin-Bar et al., 2011, Fan et al., 2011, Fernandez-Gonzalez and Zallen, 2011, Fowlkes et al., 2011, Gehring, 2011, Gursky et al., 2011, Harrison et al., 2011, Hartmann et al., 2011, Kim et al., 2011, Li et al., 2011, Little et al., 2011, Liu and Ma, 2011, Liu et al., 2011, Mikhaylova and Nurminsky, 2011, Nègre et al., 2011, Pruteanu-Malinici et al., 2011, Roy et al., 2011, Singh et al., 2011, Aswani et al., 2010, Becalska and Gavis, 2010, Deng et al., 2010, Dewar et al., 2010, Dilão and Muraro, 2010, Dilão and Muraro, 2010, Doerflinger et al., 2010, Duchi et al., 2010, Gonsalvez et al., 2010, Grimm and Wieschaus, 2010, He et al., 2010, He et al., 2010, Hueber et al., 2010, Kim et al., 2010, Marques et al., 2010, Morton de Lachapelle and Bergmann, 2010, Porcher et al., 2010, Scheuermann et al., 2010, The modENCODE Consortium, 2010, The modENCODE Consortium, 2010, Umulis et al., 2010, Weil et al., 2010, Ashyraliyev et al., 2009, Benoit et al., 2009, Erdmann et al., 2009, Fernandez-Gonzalez et al., 2009, Fomekong-Nanfack et al., 2009, Fomekong-Nanfack et al., 2009, Kim et al., 2009, Löhr et al., 2009, Lu et al., 2009, Marco et al., 2009, McNeil et al., 2009, Myasnikova et al., 2009, Navarro et al., 2009, Ochoa-Espinosa et al., 2009, Pisarev et al., 2009, Shevelyov et al., 2009, Smith et al., 2009, Snee and Macdonald, 2009, Spirov et al., 2009, Suyama et al., 2009, Tchuraev and Galimzyanov, 2009, Venken et al., 2009, Venken et al., 2009, Benoit et al., 2008, Bergmann et al., 2008, Blanco and Gehring, 2008, Chen et al., 2008, Cui et al., 2008, Cui et al., 2008, de Wit et al., 2008, Gavis et al., 2008, Gervais et al., 2008, Gregor et al., 2008, Hare et al., 2008, He et al., 2008, Kwong et al., 2008, Liang et al., 2008, Lopes et al., 2008, Pope and Harris, 2008, Surkova et al., 2008, Surkova et al., 2008, Tanaka and Nakamura, 2008, Tian and Deng, 2008, Weil et al., 2008, Aerts et al., 2007, Bergmann et al., 2007, Brent et al., 2007, Chicoine et al., 2007, Clark et al., 2007, Coppey et al., 2007, Demuth and Wade, 2007, Geng and MacDonald, 2007, Gregor et al., 2007, Gregor et al., 2007, Irion and St Johnston, 2007, Lecuyer et al., 2007, Lohr et al., 2007, Lopes et al., 2007, Meignin et al., 2007, Mische et al., 2007, Negre and Ruiz, 2007, Ochoa-Espinosa and Small, 2007, Ogishima and Tanaka, 2007, Peretz et al., 2007, Roy et al., 2007, Serbus and Sullivan, 2007, Song et al., 2007, Stevens et al., 2007, Tadros et al., 2007, Abdu et al., 2006, Bartolome and Charlesworth, 2006, Blankenship et al., 2006, Holloway et al., 2006, Janssens et al., 2006, Januschke et al., 2006, Keranen et al., 2006, Lin et al., 2006, Martinez Arias, 2006, McGregor, 2006, Munro et al., 2006, Ochoa-Espinosa and Small, 2006, Perkins et al., 2006, Preall et al., 2006, Shapiro and Anderson, 2006, Vogt et al., 2006, Wratten et al., 2006, Yucel and Small, 2006, Yucel and Small, 2006, Barker et al., 2005, Cho et al., 2005, Hayashi et al., 2005, Lopes et al., 2005, Negre et al., 2005, Norvell et al., 2005, Pearson et al., 2005, Peel et al., 2005, Sage et al., 2005, Snee et al., 2005, Wilhelm et al., 2005, Gurunathan et al., 2004, Motola and Neuman-Silberberg, 2004, Stanyon et al., 2004, Daulny et al., 2003, Fouix et al., 2003, Fu et al., 2003, Nibu et al., 2003, Spirov and Holloway, 2003, Shaw et al., 2002, Gursky et al., 2001, Hayashi and Murakami, 2001, Lee et al., 2001, Schaeffer et al., 2000, Verrotti et al., 1999, Wang et al., 1994)
    mum
    prd4
    Name Synonyms
    Bicoid
    (Baird-Titus et al., 2018, Wang et al., 2018, Amourda and Saunders, 2017, Bentovim et al., 2017, Fradin, 2017, Gilmour et al., 2017, Kong et al., 2017, Ferraro et al., 2016, Boija and Mannervik, 2015, McCarthy et al., 2015, Rebeiz et al., 2015, Li et al., 2014, Vasquez Jaramillo et al., 2014, Villar et al., 2014, Lucas et al., 2013, McKay and Lieb, 2013, Rödel et al., 2013, Hardway, 2012, Haskel-Ittah et al., 2012, He et al., 2012, Holmqvist et al., 2012, Kvon et al., 2012, Morelli et al., 2012, Nakano and Takashima, 2012, Nikulova et al., 2012, Perry et al., 2012, Umulis and Othmer, 2012, Vazquez-Pianzola and Suter, 2012, Ajuria et al., 2011, Cheung et al., 2011, Drocco et al., 2011, Gehring, 2011, Gursky et al., 2011, Holloway et al., 2011, Kim et al., 2011, Li and Arnosti, 2011, Liu et al., 2011, Morishita and Iwasa, 2011, Nègre et al., 2011, Nien et al., 2011, Ogawa and Miyake, 2011, Papatsenko and Levine, 2011, Roth, 2011, Tsurumi et al., 2011, Zhang et al., 2011, Deng et al., 2010, Grimm and Wieschaus, 2010, He et al., 2010, Kim et al., 2010, Kim et al., 2010, Lusk and Eisen, 2010, Morton de Lachapelle and Bergmann, 2010, Porcher et al., 2010, Zhang and Moret, 2010, Hecht et al., 2009, Löhr et al., 2009, MacArthur et al., 2009, Manu et al., 2009, Morishita and Iwasa, 2009, Nie et al., 2009, Papatsenko et al., 2009, Saunders and Howard, 2009, Bergmann et al., 2008, Bialek et al., 2008, Blanco and Gehring, 2008, Coppey et al., 2008, Crocker and Erives, 2008, Dougherty et al., 2008, Hare et al., 2008, He et al., 2008, Holloway et al., 2008, Ishihara and Shibata, 2008, Kim et al., 2008, Lopes et al., 2008, Lucchetta et al., 2008, Tkacik et al., 2008, Brower-Toland et al., 2007, Goering et al., 2007, Gregor et al., 2007, Gregor et al., 2007, Kerszberg and Wolpert, 2007, Lott et al., 2007, Megason and Fraser, 2007, Okumura et al., 2007, Pollard et al., 2007, Zinzen and Papatsenko, 2007, Baird-Titus et al., 2006, Graves and Tamkun, 2006, Hallikas et al., 2006, Jaeger and Reinitz, 2006, Janssens et al., 2006, Moorman et al., 2006, Moorman et al., 2006, Yucel and Small, 2006, Kulkarni and Arnosti, 2005, Cho, 2004, MacArthur and Brookfield, 2004, Beilfuss et al., 2003, Park et al., 2003)
    bicoid
    (Coll et al., 2018, Goldman and Gonsalvez, 2017, Eichhorn et al., 2016, Stegmaier et al., 2016, Xie and Hu, 2016, Cicin-Sain et al., 2015, Gula and Samsonov, 2015, Hales et al., 2015, Kozlov et al., 2015, Peng et al., 2015, Cantera et al., 2014, Cheung et al., 2014, Fahmy et al., 2014, Ghosh et al., 2014, Toshima et al., 2014, Vartiainen et al., 2014, Cui et al., 2013, Laver et al., 2013, McDermott and Davis, 2013, Neckameyer and Argue, 2013, Pinder and Smibert, 2013, Surkova et al., 2013, Conte et al., 2012, Jaeger et al., 2012, Liang et al., 2012, Liu and Niranjan, 2012, Bieler et al., 2011, Chang et al., 2011, Gursky et al., 2011, Hartmann et al., 2011, Little et al., 2011, Liu and Ma, 2011, Liu and Niranjan, 2011, Dewar et al., 2010, Dilão and Muraro, 2010, Dilão and Muraro, 2010, Fernandez-Sanchez et al., 2010, Gonsalvez et al., 2010, Kavousanakis et al., 2010, Lecca et al., 2010, Loiseau et al., 2010, Mace et al., 2010, Marques et al., 2010, Martin et al., 2010, Sample and Shvartsman, 2010, Weil et al., 2010, Benoit et al., 2009, Besse et al., 2009, Fang et al., 2009, Krauss et al., 2009, McNeil et al., 2009, Myasnikova et al., 2009, Pisarev et al., 2009, Smith et al., 2009, Spirov et al., 2009, Suyama et al., 2009, Zamparo and Perkins, 2009, Alexandrov et al., 2008, Cui et al., 2008, Cui et al., 2008, Emberly, 2008, Gavis et al., 2008, Gervais et al., 2008, Gregor et al., 2008, Hartmann et al., 2008, Lemke et al., 2008, Lepzelter and Wang, 2008, Liang et al., 2008, Meignin and Davis, 2008, Pope and Harris, 2008, Scherp and Hasenstein, 2008, Sung et al., 2008, Surkova et al., 2008, Tian and Deng, 2008, Weil et al., 2008, Yucel et al., 2008, Coppey et al., 2007, da Silva and Vincent, 2007, Demuth and Wade, 2007, Friedman and Perrimon, 2007, Ho and Gavis, 2007, Irion and St Johnston, 2007, Lander, 2007, Lohr et al., 2007, Meignin et al., 2007, Mische et al., 2007, Ochoa-Espinosa and Small, 2007, Roy et al., 2007, Rusten and Stenmark, 2007, Stevens et al., 2007, Weil et al., 2007, Abdu et al., 2006, Blankenship et al., 2006, Holloway et al., 2006, Horner et al., 2006, Irion et al., 2006, Januschke et al., 2006, Keranen et al., 2006, Kiebler and Bassell, 2006, Lin et al., 2006, McGregor, 2006, Ochoa-Espinosa and Small, 2006, Veitia, 2006, Verdier et al., 2006, Vogt et al., 2006, Weil et al., 2006, Yucel and Small, 2006, Barker et al., 2005, Lopes et al., 2005, Negre et al., 2005, Schmidt-Ott, 2005, Shav-Tal and Singer, 2005, Snee et al., 2005, Motola and Neuman-Silberberg, 2004, Riede, 2004, Nibu et al., 2003, Gursky et al., 2001, Lee et al., 2001, Holloway and Harrison, 1999, Martin, 1999.1.14)
    multimorph
    Secondary FlyBase IDs
    • FBgn0040059
    • FBgn0014130
    • FBgn0014131
    • FBgn0015909
    • FBgn0015910
    • FBgn0015911
    • FBgn0015912
    Datasets (3)
    Study focus (3)
    Experimental Role
    Project
    Project Type
    Title
    • bait_protein
    ChIP characterization of transcription factor genome binding, Berkeley Drosophila Transcription Factor Network Project.
    • transgene_used
    Protein profiling reveals five principal chromatin types in Drosophila cells.
    • bait_protein
    Genome-wide localization of transcription factors by ChIP-chip and ChIP-Seq.
    References (1,347)